Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 01:05, 17 November 2007 (UTC)
[edit]Proteins without matches (9)
[edit]Proteins with a High Potential Match (10)
[edit]Redirected Proteins (6)
[edit]Manual Inspection (Page not found) (19)
[edit]
Protein Status Grid - Date: 01:05, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 01:05, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on ABO... {November 16, 2007 4:43:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:43:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ABO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lz0.
| PDB = {{PDB2|1lz0}}, {{PDB2|1lz7}}, {{PDB2|1lzi}}, {{PDB2|1lzj}}, {{PDB2|1r7t}}, {{PDB2|1r7u}}, {{PDB2|1r7v}}, {{PDB2|1r7x}}, {{PDB2|1r7y}}, {{PDB2|1r80}}, {{PDB2|1r81}}, {{PDB2|1r82}}, {{PDB2|1wsz}}, {{PDB2|1wt0}}, {{PDB2|1wt1}}, {{PDB2|1wt2}}, {{PDB2|1wt3}}, {{PDB2|1xz6}}, {{PDB2|1zhj}}, {{PDB2|1zi1}}, {{PDB2|1zi3}}, {{PDB2|1zi4}}, {{PDB2|1zi5}}, {{PDB2|1ziz}}, {{PDB2|1zj0}}, {{PDB2|1zj1}}, {{PDB2|1zj2}}, {{PDB2|1zj3}}, {{PDB2|1zjo}}, {{PDB2|1zjp}}, {{PDB2|2a8u}}, {{PDB2|2a8w}}, {{PDB2|2i7b}}, {{PDB2|2o1f}}, {{PDB2|2o1g}}, {{PDB2|2o1h}}
| Name = ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase; transferase B, alpha 1-3-galactosyltransferase)
| HGNCid = 79
| Symbol = ABO
| AltSymbols =; A3GALNT; A3GALT1; GTB; NAGAT
| OMIM = 110300
| ECnumber =
| Homologene = 69306
| MGIid =
| GeneAtlas_image1 = PBB_GE_ABO_214504_at_tn.png
| GeneAtlas_image2 = PBB_GE_ABO_216929_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004380 |text = glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity}} {{GNF_GO|id=GO:0004381 |text = fucosylgalactoside 3-alpha-galactosyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016758 |text = transferase activity, transferring hexosyl groups}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030173 |text = integral to Golgi membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0009058 |text = biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 28
| Hs_Ensembl = ENSG00000175164
| Hs_RefseqProtein = NP_065202
| Hs_RefseqmRNA = NM_020469
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 135120384
| Hs_GenLoc_end = 135140451
| Hs_Uniprot = P16442
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase; transferase B, alpha 1-3-galactosyltransferase)''', also known as '''ABO''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABO ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase; transferase B, alpha 1-3-galactosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ferguson-Smith MA, Aitken DA, Turleau C, de Grouchy J |title=Localisation of the human ABO: Np-1: AK-1 linkage group by regional assignment of AK-1 to 9q34. |journal=Hum. Genet. |volume=34 |issue= 1 |pages= 35-43 |year= 1976 |pmid= 184030 |doi= }}
*{{cite journal | author=Nagai M, Davè V, Kaplan BE, Yoshida A |title=Human blood group glycosyltransferases. I. Purification of n-acetylgalactosaminyltransferase. |journal=J. Biol. Chem. |volume=253 |issue= 2 |pages= 377-9 |year= 1978 |pmid= 618875 |doi= }}
*{{cite journal | author=Takeya A, Hosomi O, Shimoda N, Yazawa S |title=Biosynthesis of the blood group P antigen-like GalNAc beta 1-->3Gal beta 1-->4GlcNAc/Glc structure: a novel N-acetylgalactosaminyltransferase in human blood plasma. |journal=J. Biochem. |volume=112 |issue= 3 |pages= 389-95 |year= 1992 |pmid= 1429528 |doi= }}
*{{cite journal | author=Kominato Y, McNeill PD, Yamamoto M, ''et al.'' |title=Animal histo-blood group ABO genes. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 1 |pages= 154-64 |year= 1992 |pmid= 1449469 |doi= }}
*{{cite journal | author=Yamamoto F, McNeill PD, Hakomori S |title=Human histo-blood group A2 transferase coded by A2 allele, one of the A subtypes, is characterized by a single base deletion in the coding sequence, which results in an additional domain at the carboxyl terminal. |journal=Biochem. Biophys. Res. Commun. |volume=187 |issue= 1 |pages= 366-74 |year= 1992 |pmid= 1520322 |doi= }}
*{{cite journal | author=Clausen H, White T, Takio K, ''et al.'' |title=Isolation to homogeneity and partial characterization of a histo-blood group A defined Fuc alpha 1----2Gal alpha 1----3-N-acetylgalactosaminyltransferase from human lung tissue. |journal=J. Biol. Chem. |volume=265 |issue= 2 |pages= 1139-45 |year= 1990 |pmid= 2104827 |doi= }}
*{{cite journal | author=Yamamoto F, Marken J, Tsuji T, ''et al.'' |title=Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1----2Gal alpha 1----3GalNAc transferase (histo-blood group A transferase) mRNA. |journal=J. Biol. Chem. |volume=265 |issue= 2 |pages= 1146-51 |year= 1990 |pmid= 2104828 |doi= }}
*{{cite journal | author=Yamamoto F, Hakomori S |title=Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions. |journal=J. Biol. Chem. |volume=265 |issue= 31 |pages= 19257-62 |year= 1990 |pmid= 2121736 |doi= }}
*{{cite journal | author=Yamamoto F, Clausen H, White T, ''et al.'' |title=Molecular genetic basis of the histo-blood group ABO system. |journal=Nature |volume=345 |issue= 6272 |pages= 229-33 |year= 1990 |pmid= 2333095 |doi= 10.1038/345229a0 }}
*{{cite journal | author=Whitehead JS, Bella S, Kim YS |title=An N-acetylgalactosaminyltransferase from human blood group A plasma. II. Kinetic and physicochemical properties. |journal=J. Biol. Chem. |volume=249 |issue= 11 |pages= 3448-52 |year= 1974 |pmid= 4831223 |doi= }}
*{{cite journal | author=Whitehead JS, Bella A, Kim YS |title=An N-acetylgalactosaminyltransferase from human blood group A plasma. I. Purification and agarose binding properties. |journal=J. Biol. Chem. |volume=249 |issue= 11 |pages= 442-7 |year= 1974 |pmid= 4831233 |doi= }}
*{{cite journal | author=Kobata A, Ginsburg V |title=Uridine diphosphate-N-acetyl-D-galactosamine: D-galactose alpha-3-N-acetyl-D-galactosaminyltransferase, a product of the gene that determines blood type A in man. |journal=J. Biol. Chem. |volume=245 |issue= 6 |pages= 1484-90 |year= 1970 |pmid= 5442829 |doi= }}
*{{cite journal | author=Yoshida A, Yamaguchi H, Okubo Y |title=Genetic mechanism of cis-AB inheritance. I. A case associated with unequal chromosomal crossing over. |journal=Am. J. Hum. Genet. |volume=32 |issue= 3 |pages= 332-8 |year= 1980 |pmid= 6770676 |doi= }}
*{{cite journal | author=Olsson ML, Thuresson B, Chester MA |title=An Ael allele-specific nucleotide insertion at the blood group ABO locus and its detection using a sequence-specific polymerase chain reaction. |journal=Biochem. Biophys. Res. Commun. |volume=216 |issue= 2 |pages= 642-7 |year= 1995 |pmid= 7488159 |doi= 10.1006/bbrc.1995.2670 }}
*{{cite journal | author=Bennett EP, Steffensen R, Clausen H, ''et al.'' |title=Genomic cloning of the human histo-blood group ABO locus. |journal=Biochem. Biophys. Res. Commun. |volume=206 |issue= 1 |pages= 318-25 |year= 1995 |pmid= 7598760 |doi= }}
*{{cite journal | author=Yamamoto F, McNeill PD, Hakomori S |title=Genomic organization of human histo-blood group ABO genes. |journal=Glycobiology |volume=5 |issue= 1 |pages= 51-8 |year= 1995 |pmid= 7772867 |doi= }}
*{{cite journal | author=Bennett EP, Steffensen R, Clausen H, ''et al.'' |title=Genomic cloning of the human histo-blood group ABO locus. |journal=Biochem. Biophys. Res. Commun. |volume=211 |issue= 1 |pages= 347 |year= 1995 |pmid= 7779106 |doi= }}
*{{cite journal | author=Yamamoto F, McNeill PD, Kominato Y, ''et al.'' |title=Molecular genetic analysis of the ABO blood group system: 2. cis-AB alleles. |journal=Vox Sang. |volume=64 |issue= 2 |pages= 120-3 |year= 1993 |pmid= 8456556 |doi= }}
*{{cite journal | author=Yamamoto F, McNeill PD, Yamamoto M, ''et al.'' |title=Molecular genetic analysis of the ABO blood group system: 3. A(X) and B(A) alleles. |journal=Vox Sang. |volume=64 |issue= 3 |pages= 171-4 |year= 1993 |pmid= 8484250 |doi= }}
*{{cite journal | author=Ogasawara K, Yabe R, Uchikawa M, ''et al.'' |title=Molecular genetic analysis of variant phenotypes of the ABO blood group system. |journal=Blood |volume=88 |issue= 7 |pages= 2732-7 |year= 1996 |pmid= 8839869 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ALK... {November 16, 2007 4:43:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:44:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Anaplastic lymphoma kinase (Ki-1)
| HGNCid = 427
| Symbol = ALK
| AltSymbols =; CD246; TFG/ALK
| OMIM = 105590
| ECnumber =
| Homologene = 68387
| MGIid = 103305
| GeneAtlas_image1 = PBB_GE_ALK_208211_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ALK_208212_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004714 |text = transmembrane receptor protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004716 |text = receptor signaling protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006487 |text = protein amino acid N-linked glycosylation}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007420 |text = brain development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 238
| Hs_Ensembl = ENSG00000171094
| Hs_RefseqProtein = NP_004295
| Hs_RefseqmRNA = NM_004304
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 29269594
| Hs_GenLoc_end = 29997029
| Hs_Uniprot = Q9UM73
| Mm_EntrezGene = 11682
| Mm_Ensembl = ENSMUSG00000055471
| Mm_RefseqmRNA = NM_007439
| Mm_RefseqProtein = NP_031465
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 71774299
| Mm_GenLoc_end = 72508566
| Mm_Uniprot = P97793
}}
}}
'''Anaplastic lymphoma kinase (Ki-1)''', also known as '''ALK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALK anaplastic lymphoma kinase (Ki-1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=238| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 2;5 chromosomal translocation is frequently associated with anaplastic large cell lymphomas (ALCLs). The translocation creates a fusion gene consisting of the ALK (anaplastic lymphoma kinase) gene and the nucleophosmin (NPM) gene: the 3' half of ALK, derived from chromosome 2, is fused to the 5' portion of NPM from chromosome 5. A recent study shows that the product of the NPM-ALK fusion gene is oncogenic. The deduced amino acid sequences reveal that ALK is a novel receptor protein-tyrosine kinase having a putative transmembrane domain and an extracellular domain. These sequences are absent in the product of the transforming NPM-ALK gene. ALK shows the greatest sequence similarity to LTK (leukocyte tyrosine kinase). ALK plays an important role in the development of the brain and exerts its effects on specific neurons in the nervous system.<ref name="entrez">{{cite web | title = Entrez Gene: ALK anaplastic lymphoma kinase (Ki-1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=238| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Benharroch D, Meguerian-Bedoyan Z, Lamant L, ''et al.'' |title=ALK-positive lymphoma: a single disease with a broad spectrum of morphology. |journal=Blood |volume=91 |issue= 6 |pages= 2076-84 |year= 1998 |pmid= 9490693 |doi= }}
*{{cite journal | author=Pulford K, Lamant L, Espinos E, ''et al.'' |title=The emerging normal and disease-related roles of anaplastic lymphoma kinase. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 23 |pages= 2939-53 |year= 2005 |pmid= 15583856 |doi= 10.1007/s00018-004-4275-9 }}
*{{cite journal | author=Morris SW, Kirstein MN, Valentine MB, ''et al.'' |title=Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma. |journal=Science |volume=263 |issue= 5151 |pages= 1281-4 |year= 1994 |pmid= 8122112 |doi= }}
*{{cite journal | author=Fujimoto J, Shiota M, Iwahara T, ''et al.'' |title=Characterization of the transforming activity of p80, a hyperphosphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 9 |pages= 4181-6 |year= 1996 |pmid= 8633037 |doi= }}
*{{cite journal | author=Iwahara T, Fujimoto J, Wen D, ''et al.'' |title=Molecular characterization of ALK, a receptor tyrosine kinase expressed specifically in the nervous system. |journal=Oncogene |volume=14 |issue= 4 |pages= 439-49 |year= 1997 |pmid= 9053841 |doi= 10.1038/sj.onc.1200849 }}
*{{cite journal | author=Morris SW, Naeve C, Mathew P, ''et al.'' |title=ALK, the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin's lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK) |journal=Oncogene |volume=14 |issue= 18 |pages= 2175-88 |year= 1997 |pmid= 9174053 |doi= 10.1038/sj.onc.1201062 }}
*{{cite journal | author=Bai RY, Dieter P, Peschel C, ''et al.'' |title=Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 6951-61 |year= 1998 |pmid= 9819383 |doi= }}
*{{cite journal | author=Hernández L, Pinyol M, Hernández S, ''et al.'' |title=TRK-fused gene (TFG) is a new partner of ALK in anaplastic large cell lymphoma producing two structurally different TFG-ALK translocations. |journal=Blood |volume=94 |issue= 9 |pages= 3265-8 |year= 1999 |pmid= 10556217 |doi= }}
*{{cite journal | author=Souttou B, Carvalho NB, Raulais D, Vigny M |title=Activation of anaplastic lymphoma kinase receptor tyrosine kinase induces neuronal differentiation through the mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9526-31 |year= 2001 |pmid= 11121404 |doi= 10.1074/jbc.M007333200 }}
*{{cite journal | author=Stoica GE, Kuo A, Aigner A, ''et al.'' |title=Identification of anaplastic lymphoma kinase as a receptor for the growth factor pleiotrophin. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 16772-9 |year= 2001 |pmid= 11278720 |doi= 10.1074/jbc.M010660200 }}
*{{cite journal | author=Simonitsch I, Polgar D, Hajek M, ''et al.'' |title=The cytoplasmic truncated receptor tyrosine kinase ALK homodimer immortalizes and cooperates with ras in cellular transformation. |journal=FASEB J. |volume=15 |issue= 8 |pages= 1416-8 |year= 2001 |pmid= 11387242 |doi= }}
*{{cite journal | author=Powers C, Aigner A, Stoica GE, ''et al.'' |title=Pleiotrophin signaling through anaplastic lymphoma kinase is rate-limiting for glioblastoma growth. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14153-8 |year= 2002 |pmid= 11809760 |doi= 10.1074/jbc.M112354200 }}
*{{cite journal | author=Zamo A, Chiarle R, Piva R, ''et al.'' |title=Anaplastic lymphoma kinase (ALK) activates Stat3 and protects hematopoietic cells from cell death. |journal=Oncogene |volume=21 |issue= 7 |pages= 1038-47 |year= 2002 |pmid= 11850821 |doi= 10.1038/sj.onc.1205152 }}
*{{cite journal | author=Passoni L, Scardino A, Bertazzoli C, ''et al.'' |title=ALK as a novel lymphoma-associated tumor antigen: identification of 2 HLA-A2.1-restricted CD8+ T-cell epitopes. |journal=Blood |volume=99 |issue= 6 |pages= 2100-6 |year= 2002 |pmid= 11877285 |doi= }}
*{{cite journal | author=Bonvini P, Gastaldi T, Falini B, Rosolen A |title=Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK(+) CD30(+) lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin. |journal=Cancer Res. |volume=62 |issue= 5 |pages= 1559-66 |year= 2002 |pmid= 11888936 |doi= }}
*{{cite journal | author=Hernández L, Beà S, Bellosillo B, ''et al.'' |title=Diversity of genomic breakpoints in TFG-ALK translocations in anaplastic large cell lymphomas: identification of a new TFG-ALK(XL) chimeric gene with transforming activity. |journal=Am. J. Pathol. |volume=160 |issue= 4 |pages= 1487-94 |year= 2002 |pmid= 11943732 |doi= }}
*{{cite journal | author=ten Berge RL, Meijer CJ, Dukers DF, ''et al.'' |title=Expression levels of apoptosis-related proteins predict clinical outcome in anaplastic large cell lymphoma. |journal=Blood |volume=99 |issue= 12 |pages= 4540-6 |year= 2002 |pmid= 12036886 |doi= }}
*{{cite journal | author=Cools J, Wlodarska I, Somers R, ''et al.'' |title=Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor. |journal=Genes Chromosomes Cancer |volume=34 |issue= 4 |pages= 354-62 |year= 2002 |pmid= 12112524 |doi= 10.1002/gcc.10033 }}
*{{cite journal | author=Dirks WG, Fähnrich S, Lis Y, ''et al.'' |title=Expression and functional analysis of the anaplastic lymphoma kinase (ALK) gene in tumor cell lines. |journal=Int. J. Cancer |volume=100 |issue= 1 |pages= 49-56 |year= 2002 |pmid= 12115586 |doi= 10.1002/ijc.10435 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ANPEP... {November 16, 2007 4:44:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:45:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)
| HGNCid = 500
| Symbol = ANPEP
| AltSymbols =; APN; CD13; LAP1; PEPN; gp150
| OMIM = 151530
| ECnumber =
| Homologene = 68163
| MGIid = 96749
| GeneAtlas_image1 = PBB_GE_ANPEP_202888_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0004179 |text = membrane alanyl aminopeptidase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005793 |text = ER-Golgi intermediate compartment}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 290
| Hs_Ensembl = ENSG00000166825
| Hs_RefseqProtein = NP_001141
| Hs_RefseqmRNA = NM_001150
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 88129131
| Hs_GenLoc_end = 88159072
| Hs_Uniprot = P15144
| Mm_EntrezGene = 16790
| Mm_Ensembl = ENSMUSG00000039062
| Mm_RefseqmRNA = NM_008486
| Mm_RefseqProtein = NP_032512
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 79695323
| Mm_GenLoc_end = 79715831
| Mm_Uniprot = Q3TB69
}}
}}
'''Alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)''', also known as '''ANPEP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ANPEP alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=290| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma.<ref name="entrez">{{cite web | title = Entrez Gene: ANPEP alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=290| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yeager CL, Ashmun RA, Williams RK, ''et al.'' |title=Human aminopeptidase N is a receptor for human coronavirus 229E. |journal=Nature |volume=357 |issue= 6377 |pages= 420-2 |year= 1992 |pmid= 1350662 |doi= 10.1038/357420a0 }}
*{{cite journal | author=Shapiro LH, Ashmun RA, Roberts WM, Look AT |title=Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells. |journal=J. Biol. Chem. |volume=266 |issue= 18 |pages= 11999-2007 |year= 1991 |pmid= 1675638 |doi= }}
*{{cite journal | author=O'Connell PJ, Gerkis V, d'Apice AJ |title=Variable O-glycosylation of CD13 (aminopeptidase N). |journal=J. Biol. Chem. |volume=266 |issue= 7 |pages= 4593-7 |year= 1991 |pmid= 1705556 |doi= }}
*{{cite journal | author=Watt VM, Willard HF |title=The human aminopeptidase N gene: isolation, chromosome localization, and DNA polymorphism analysis. |journal=Hum. Genet. |volume=85 |issue= 6 |pages= 651-4 |year= 1990 |pmid= 1977688 |doi= }}
*{{cite journal | author=Look AT, Peiper SC, Rebentisch MB, ''et al.'' |title=Molecular cloning, expression, and chromosomal localization of the gene encoding a human myeloid membrane antigen (gp150). |journal=J. Clin. Invest. |volume=78 |issue= 4 |pages= 914-21 |year= 1986 |pmid= 2428842 |doi= }}
*{{cite journal | author=Look AT, Ashmun RA, Shapiro LH, Peiper SC |title=Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N. |journal=J. Clin. Invest. |volume=83 |issue= 4 |pages= 1299-307 |year= 1989 |pmid= 2564851 |doi= }}
*{{cite journal | author=Olsen J, Cowell GM, Kønigshøfer E, ''et al.'' |title=Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. |journal=FEBS Lett. |volume=238 |issue= 2 |pages= 307-14 |year= 1988 |pmid= 2901990 |doi= }}
*{{cite journal | author=Kruse TA, Bolund L, Grzeschik KH, ''et al.'' |title=Assignment of the human aminopeptidase N (peptidase E) gene to chromosome 15q13-qter. |journal=FEBS Lett. |volume=239 |issue= 2 |pages= 305-8 |year= 1988 |pmid= 2903074 |doi= }}
*{{cite journal | author=Tokioka-Terao M, Hiwada K, Kokubu T |title=Purification and characterization of aminopeptidase N from human plasma. |journal=Enzyme |volume=32 |issue= 2 |pages= 65-75 |year= 1985 |pmid= 6149934 |doi= }}
*{{cite journal | author=Watanabe Y, Iwaki-Egawa S, Mizukoshi H, Fujimoto Y |title=Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N. |journal=Biol. Chem. Hoppe-Seyler |volume=376 |issue= 7 |pages= 397-400 |year= 1995 |pmid= 7576235 |doi= }}
*{{cite journal | author=Favaloro EJ, Browning T, Facey D |title=CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated. |journal=Exp. Hematol. |volume=21 |issue= 13 |pages= 1695-701 |year= 1993 |pmid= 7902291 |doi= }}
*{{cite journal | author=Núñez L, Amigo L, Rigotti A, ''et al.'' |title=Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids. |journal=FEBS Lett. |volume=329 |issue= 1-2 |pages= 84-8 |year= 1993 |pmid= 8102610 |doi= }}
*{{cite journal | author=Söderberg C, Giugni TD, Zaia JA, ''et al.'' |title=CD13 (human aminopeptidase N) mediates human cytomegalovirus infection. |journal=J. Virol. |volume=67 |issue= 11 |pages= 6576-85 |year= 1993 |pmid= 8105105 |doi= }}
*{{cite journal | author=Kolb AF, Maile J, Heister A, Siddell SG |title=Characterization of functional domains in the human coronavirus HCV 229E receptor. |journal=J. Gen. Virol. |volume=77 ( Pt 10) |issue= |pages= 2515-21 |year= 1996 |pmid= 8887485 |doi= }}
*{{cite journal | author=Norén K, Hansen GH, Clausen H, ''et al.'' |title=Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity. |journal=Exp. Cell Res. |volume=231 |issue= 1 |pages= 112-8 |year= 1997 |pmid= 9056417 |doi= 10.1006/excr.1996.3455 }}
*{{cite journal | author=Kolb AF, Hegyi A, Siddell SG |title=Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N. |journal=J. Gen. Virol. |volume=78 ( Pt 11) |issue= |pages= 2795-802 |year= 1997 |pmid= 9367365 |doi= }}
*{{cite journal | author=Hegyi A, Kolb AF |title=Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N. |journal=J. Gen. Virol. |volume=79 ( Pt 6) |issue= |pages= 1387-91 |year= 1998 |pmid= 9634079 |doi= }}
*{{cite journal | author=Dong X, An B, Salvucci Kierstead L, ''et al.'' |title=Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells. |journal=J. Immunol. |volume=164 |issue= 1 |pages= 129-35 |year= 2000 |pmid= 10605003 |doi= }}
*{{cite journal | author=Pasqualini R, Koivunen E, Kain R, ''et al.'' |title=Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. |journal=Cancer Res. |volume=60 |issue= 3 |pages= 722-7 |year= 2000 |pmid= 10676659 |doi= }}
*{{cite journal | author=Renold A, Cescato R, Beuret N, ''et al.'' |title=Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9290-5 |year= 2000 |pmid= 10734069 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DSP... {November 16, 2007 4:45:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:45:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DSP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lm5.
| PDB = {{PDB2|1lm5}}, {{PDB2|1lm7}}
| Name = Desmoplakin
| HGNCid = 3052
| Symbol = DSP
| AltSymbols =; DPI; DPII
| OMIM = 125647
| ECnumber =
| Homologene = 37922
| MGIid = 109611
| GeneAtlas_image1 = PBB_GE_DSP_200606_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0001533 |text = cornified envelope}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}} {{GNF_GO|id=GO:0005913 |text = cell-cell adherens junction}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0030057 |text = desmosome}}
| Process = {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1832
| Hs_Ensembl = ENSG00000096696
| Hs_RefseqProtein = NP_001008844
| Hs_RefseqmRNA = NM_001008844
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 7486869
| Hs_GenLoc_end = 7531945
| Hs_Uniprot = P15924
| Mm_EntrezGene = 109620
| Mm_Ensembl = ENSMUSG00000054889
| Mm_RefseqmRNA = XM_621314
| Mm_RefseqProtein = XP_621314
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 38203950
| Mm_GenLoc_end = 38206041
| Mm_Uniprot =
}}
}}
'''Desmoplakin''', also known as '''DSP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DSP desmoplakin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1832| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Desmosomes are intercellular junctions that tightly link adjacent cells. Desmoplakin is an obligate component of functional desmosomes that anchors intermediate filaments to desmosomal plaques. The N-terminus of desmoplakin is required for localization to the desmosome and interacts with the N-terminal region of plakophilin 1 and plakoglobin. The C-terminus of desmoplakin binds with intermediate filaments. In the mid-region of desmoplakin, a coiled-coiled rod domain is responsible for homodimerization. Mutations in this gene are the cause of several cardiomyopathies and keratodermas as well as the autoimmune disease paraneoplastic pemphigus.<ref name="entrez">{{cite web | title = Entrez Gene: DSP desmoplakin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1832| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Presland RB, Dale BA |title=Epithelial structural proteins of the skin and oral cavity: function in health and disease. |journal=Crit. Rev. Oral Biol. Med. |volume=11 |issue= 4 |pages= 383-408 |year= 2001 |pmid= 11132762 |doi= }}
*{{cite journal | author=Green KJ, Parry DA, Steinert PM, ''et al.'' |title=Structure of the human desmoplakins. Implications for function in the desmosomal plaque. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2603-12 |year= 1990 |pmid= 1689290 |doi= }}
*{{cite journal | author=Just M, Herbst H, Hummel M, ''et al.'' |title=Undulin is a novel member of the fibronectin-tenascin family of extracellular matrix glycoproteins. |journal=J. Biol. Chem. |volume=266 |issue= 26 |pages= 17326-32 |year= 1991 |pmid= 1716629 |doi= }}
*{{cite journal | author=Virata ML, Wagner RM, Parry DA, Green KJ |title=Molecular structure of the human desmoplakin I and II amino terminus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 2 |pages= 544-8 |year= 1992 |pmid= 1731325 |doi= }}
*{{cite journal | author=Arnemann J, Spurr NK, Wheeler GN, ''et al.'' |title=Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and plakoglobin DPIII (JUP). |journal=Genomics |volume=10 |issue= 3 |pages= 640-5 |year= 1991 |pmid= 1889810 |doi= }}
*{{cite journal | author=Anhalt GJ, Kim SC, Stanley JR, ''et al.'' |title=Paraneoplastic pemphigus. An autoimmune mucocutaneous disease associated with neoplasia. |journal=N. Engl. J. Med. |volume=323 |issue= 25 |pages= 1729-35 |year= 1991 |pmid= 2247105 |doi= }}
*{{cite journal | author=Green KJ, Parry DA, Steinert PM, ''et al.'' |title=Structure of the human desmoplakins. Implications for function in the desmosomal plaque. |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11406-7 |year= 1990 |pmid= 2391353 |doi= }}
*{{cite journal | author=Stappenbeck TS, Lamb JA, Corcoran CM, Green KJ |title=Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks. |journal=J. Biol. Chem. |volume=269 |issue= 47 |pages= 29351-4 |year= 1994 |pmid= 7525582 |doi= }}
*{{cite journal | author=Kouklis PD, Hutton E, Fuchs E |title=Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. |journal=J. Cell Biol. |volume=127 |issue= 4 |pages= 1049-60 |year= 1994 |pmid= 7525601 |doi= }}
*{{cite journal | author=Steinert PM, Marekov LN |title=Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 2021-30 |year= 1997 |pmid= 8999895 |doi= }}
*{{cite journal | author=Meng JJ, Bornslaeger EA, Green KJ, ''et al.'' |title=Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21495-503 |year= 1997 |pmid= 9261168 |doi= }}
*{{cite journal | author=Kowalczyk AP, Bornslaeger EA, Borgwardt JE, ''et al.'' |title=The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes. |journal=J. Cell Biol. |volume=139 |issue= 3 |pages= 773-84 |year= 1997 |pmid= 9348293 |doi= }}
*{{cite journal | author=Olavesen MG, Bentley E, Mason RV, ''et al.'' |title=Fine mapping of 39 ESTs on human chromosome 6p23-p25. |journal=Genomics |volume=46 |issue= 2 |pages= 303-6 |year= 1998 |pmid= 9417921 |doi= 10.1006/geno.1997.5032 }}
*{{cite journal | author=Smith EA, Fuchs E |title=Defining the interactions between intermediate filaments and desmosomes. |journal=J. Cell Biol. |volume=141 |issue= 5 |pages= 1229-41 |year= 1998 |pmid= 9606214 |doi= }}
*{{cite journal | author=Marekov LN, Steinert PM |title=Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope. |journal=J. Biol. Chem. |volume=273 |issue= 28 |pages= 17763-70 |year= 1998 |pmid= 9651377 |doi= }}
*{{cite journal | author=Kowalczyk AP, Navarro P, Dejana E, ''et al.'' |title=VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions. |journal=J. Cell. Sci. |volume=111 ( Pt 20) |issue= |pages= 3045-57 |year= 1998 |pmid= 9739078 |doi= }}
*{{cite journal | author=Suzuki M, Okuyama S, Okamoto S, ''et al.'' |title=A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer. |journal=Oncogene |volume=17 |issue= 7 |pages= 853-65 |year= 1998 |pmid= 9780002 |doi= 10.1038/sj.onc.1202163 }}
*{{cite journal | author=Armstrong DK, McKenna KE, Purkis PE, ''et al.'' |title=Haploinsufficiency of desmoplakin causes a striate subtype of palmoplantar keratoderma. |journal=Hum. Mol. Genet. |volume=8 |issue= 1 |pages= 143-8 |year= 1999 |pmid= 9887343 |doi= }}
*{{cite journal | author=Whittock NV, Ashton GH, Dopping-Hepenstal PJ, ''et al.'' |title=Striate palmoplantar keratoderma resulting from desmoplakin haploinsufficiency. |journal=J. Invest. Dermatol. |volume=113 |issue= 6 |pages= 940-6 |year= 2000 |pmid= 10594734 |doi= 10.1046/j.1523-1747.1999.00783.x }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FANCA... {November 16, 2007 4:45:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:46:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Fanconi anemia, complementation group A
| HGNCid = 3582
| Symbol = FANCA
| AltSymbols =; FA; FA-H; FA1; FAA; FACA; FAH; FANCH; MGC75158
| OMIM = 607139
| ECnumber =
| Homologene = 108
| MGIid = 1341823
| GeneAtlas_image1 = PBB_GE_FANCA_203805_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FANCA_203806_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007140 |text = male meiosis}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0008585 |text = female gonad development}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2175
| Hs_Ensembl = ENSG00000187741
| Hs_RefseqProtein = NP_000126
| Hs_RefseqmRNA = NM_000135
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 88331460
| Hs_GenLoc_end = 88410566
| Hs_Uniprot = O15360
| Mm_EntrezGene = 14087
| Mm_Ensembl = ENSMUSG00000032815
| Mm_RefseqmRNA = NM_016925
| Mm_RefseqProtein = NP_058621
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 126154390
| Mm_GenLoc_end = 126204666
| Mm_Uniprot = Q9CS36
}}
}}
'''Fanconi anemia, complementation group A''', also known as '''FANCA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FANCA Fanconi anemia, complementation group A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2175| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. The previously defined group FANCH is the same as FANCA. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group A. Alternative splicing results in multiple transcript variants encoding different isoforms. Mutations in this gene are the most common cause of Fanconi anemia.<ref name="entrez">{{cite web | title = Entrez Gene: FANCA Fanconi anemia, complementation group A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2175| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Marmo E |title=[Beta-adrenolytic agents in the treatment of hypertension] |journal=La Clinica terapeutica |volume=74 |issue= 3 |pages= 209-29 |year= 1976 |pmid= 6186 |doi= }}
*{{cite journal | author=Pronk JC, Gibson RA, Savoia A, ''et al.'' |title=Localisation of the Fanconi anaemia complementation group A gene to chromosome 16q24.3. |journal=Nat. Genet. |volume=11 |issue= 3 |pages= 338-40 |year= 1995 |pmid= 7581462 |doi= 10.1038/ng1195-338 }}
*{{cite journal | author=Gschwend M, Levran O, Kruglyak L, ''et al.'' |title=A locus for Fanconi anemia on 16q determined by homozygosity mapping. |journal=Am. J. Hum. Genet. |volume=59 |issue= 2 |pages= 377-84 |year= 1996 |pmid= 8755924 |doi= }}
*{{cite journal | author=Lo Ten Foe JR, Rooimans MA, Bosnoyan-Collins L, ''et al.'' |title=Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA. |journal=Nat. Genet. |volume=14 |issue= 3 |pages= 320-3 |year= 1996 |pmid= 8896563 |doi= 10.1038/ng1196-320 }}
*{{cite journal | author= |title=Positional cloning of the Fanconi anaemia group A gene. The Fanconi anaemia/breast cancer consortium. |journal=Nat. Genet. |volume=14 |issue= 3 |pages= 324-8 |year= 1996 |pmid= 8896564 |doi= 10.1038/ng1196-324 }}
*{{cite journal | author=Ianzano L, D'Apolito M, Centra M, ''et al.'' |title=The genomic organization of the Fanconi anemia group A (FAA) gene. |journal=Genomics |volume=41 |issue= 3 |pages= 309-14 |year= 1997 |pmid= 9169126 |doi= 10.1006/geno.1997.4675 }}
*{{cite journal | author=Levran O, Erlich T, Magdalena N, ''et al.'' |title=Sequence variation in the Fanconi anemia gene FAA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 24 |pages= 13051-6 |year= 1998 |pmid= 9371798 |doi= }}
*{{cite journal | author=Joenje H, Oostra AB, Wijker M, ''et al.'' |title=Evidence for at least eight Fanconi anemia genes. |journal=Am. J. Hum. Genet. |volume=61 |issue= 4 |pages= 940-4 |year= 1997 |pmid= 9382107 |doi= }}
*{{cite journal | author=Kupfer GM, Näf D, Suliman A, ''et al.'' |title=The Fanconi anaemia proteins, FAA and FAC, interact to form a nuclear complex. |journal=Nat. Genet. |volume=17 |issue= 4 |pages= 487-90 |year= 1997 |pmid= 9398857 |doi= 10.1038/ng1297-487 }}
*{{cite journal | author=Savino M, Ianzano L, Strippoli P, ''et al.'' |title=Mutations of the Fanconi anemia group A gene (FAA) in Italian patients. |journal=Am. J. Hum. Genet. |volume=61 |issue= 6 |pages= 1246-53 |year= 1998 |pmid= 9399890 |doi= }}
*{{cite journal | author=Levran O, Doggett NA, Auerbach AD |title=Identification of Alu-mediated deletions in the Fanconi anemia gene FAA. |journal=Hum. Mutat. |volume=12 |issue= 3 |pages= 145-52 |year= 1998 |pmid= 9711872 |doi= 10.1002/(SICI)1098-1004(1998)12:3<145::AID-HUMU2>3.0.CO;2-G }}
*{{cite journal | author=Centra M, Memeo E, d'Apolito M, ''et al.'' |title=Fine exon-intron structure of the Fanconi anemia group A (FAA) gene and characterization of two genomic deletions. |journal=Genomics |volume=51 |issue= 3 |pages= 463-7 |year= 1998 |pmid= 9721219 |doi= 10.1006/geno.1998.5353 }}
*{{cite journal | author=Näf D, Kupfer GM, Suliman A, ''et al.'' |title=Functional activity of the fanconi anemia protein FAA requires FAC binding and nuclear localization. |journal=Mol. Cell. Biol. |volume=18 |issue= 10 |pages= 5952-60 |year= 1998 |pmid= 9742112 |doi= }}
*{{cite journal | author=Yamashita T, Kupfer GM, Naf D, ''et al.'' |title=The fanconi anemia pathway requires FAA phosphorylation and FAA/FAC nuclear accumulation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 22 |pages= 13085-90 |year= 1998 |pmid= 9789045 |doi= }}
*{{cite journal | author=Nakamura A, Matsuura S, Tauchi H, ''et al.'' |title=Four novel mutations of the Fanconi anemia group A gene (FAA) in Japanese patients. |journal=J. Hum. Genet. |volume=44 |issue= 1 |pages= 48-51 |year= 1999 |pmid= 9929978 |doi= }}
*{{cite journal | author=Wijker M, Morgan NV, Herterich S, ''et al.'' |title=Heterogeneous spectrum of mutations in the Fanconi anaemia group A gene. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 1 |pages= 52-9 |year= 1999 |pmid= 10094191 |doi= 10.1038/sj.ejhg.5200248 }}
*{{cite journal | author=Kupfer G, Naf D, Garcia-Higuera I, ''et al.'' |title=A patient-derived mutant form of the Fanconi anemia protein, FANCA, is defective in nuclear accumulation. |journal=Exp. Hematol. |volume=27 |issue= 4 |pages= 587-93 |year= 1999 |pmid= 10210316 |doi= }}
*{{cite journal | author=Garcia-Higuera I, Kuang Y, Näf D, ''et al.'' |title=Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a functional nuclear complex. |journal=Mol. Cell. Biol. |volume=19 |issue= 7 |pages= 4866-73 |year= 1999 |pmid= 10373536 |doi= }}
*{{cite journal | author=Jelesko JG, Harper R, Furuya M, Gruissem W |title=Rare germinal unequal crossing-over leading to recombinant gene formation and gene duplication in Arabidopsis thaliana. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 18 |pages= 10302-7 |year= 1999 |pmid= 10468603 |doi= }}
*{{cite journal | author=Waisfisz Q, de Winter JP, Kruyt FA, ''et al.'' |title=A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 18 |pages= 10320-5 |year= 1999 |pmid= 10468606 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GALT... {November 16, 2007 4:46:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:47:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Galactose-1-phosphate uridylyltransferase
| HGNCid = 4135
| Symbol = GALT
| AltSymbols =;
| OMIM = 606999
| ECnumber =
| Homologene = 126
| MGIid = 95638
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008108 |text = UDP-glucose:hexose-1-phosphate uridylyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006012 |text = galactose metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2592
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000146
| Hs_RefseqmRNA = NM_000155
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 14430
| Mm_Ensembl = ENSMUSG00000036073
| Mm_RefseqmRNA = NM_016658
| Mm_RefseqProtein = NP_057867
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 41944037
| Mm_GenLoc_end = 41947191
| Mm_Uniprot = Q3TQJ2
}}
}}
'''Galactose-1-phosphate uridylyltransferase''', also known as '''GALT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GALT galactose-1-phosphate uridylyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2592| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Galactose-1-phosphate uridyl transferase (GALT) catalyzes the second step of the Leloir pathway of galactose metabolism, namely the conversion of UDP-glucose + galactose-1-phosphate to glucose-1-phosphate + UDP-galactose. The absence of this enzyme results in classic galactosemia in humans and can be fatal in the newborn period if lactose is not removed from the diet. The pathophysiology of galactosemia has not been clearly defined.<ref name="entrez">{{cite web | title = Entrez Gene: GALT galactose-1-phosphate uridylyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2592| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Reichardt JK |title=Genetic basis of galactosemia. |journal=Hum. Mutat. |volume=1 |issue= 3 |pages= 190-6 |year= 1993 |pmid= 1301925 |doi= 10.1002/humu.1380010303 }}
*{{cite journal | author=Tyfield L, Reichardt J, Fridovich-Keil J, ''et al.'' |title=Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene. |journal=Hum. Mutat. |volume=13 |issue= 6 |pages= 417-30 |year= 1999 |pmid= 10408771 |doi= 10.1002/(SICI)1098-1004(1999)13:6<417::AID-HUMU1>3.0.CO;2-0 }}
*{{cite journal | author=Reichardt JK, Belmont JW, Levy HL, Woo SL |title=Characterization of two missense mutations in human galactose-1-phosphate uridyltransferase: different molecular mechanisms for galactosemia. |journal=Genomics |volume=12 |issue= 3 |pages= 596-600 |year= 1992 |pmid= 1373122 |doi= }}
*{{cite journal | author=Leslie ND, Immerman EB, Flach JE, ''et al.'' |title=The human galactose-1-phosphate uridyltransferase gene. |journal=Genomics |volume=14 |issue= 2 |pages= 474-80 |year= 1992 |pmid= 1427861 |doi= }}
*{{cite journal | author=Reichardt JK, Levy HL, Woo SL |title=Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase. |journal=Biochemistry |volume=31 |issue= 24 |pages= 5430-3 |year= 1992 |pmid= 1610789 |doi= }}
*{{cite journal | author=Reichardt JK, Packman S, Woo SL |title=Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase. |journal=Am. J. Hum. Genet. |volume=49 |issue= 4 |pages= 860-7 |year= 1991 |pmid= 1897530 |doi= }}
*{{cite journal | author=Reichardt JK, Woo SL |title=Molecular basis of galactosemia: mutations and polymorphisms in the gene encoding human galactose-1-phosphate uridylyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 7 |pages= 2633-7 |year= 1991 |pmid= 2011574 |doi= }}
*{{cite journal | author=Flach JE, Reichardt JK, Elsas LJ |title=Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase. |journal=Mol. Biol. Med. |volume=7 |issue= 4 |pages= 365-9 |year= 1990 |pmid= 2233247 |doi= }}
*{{cite journal | author=Reichardt JK, Berg P |title=Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase. |journal=Mol. Biol. Med. |volume=5 |issue= 2 |pages= 107-22 |year= 1988 |pmid= 2840550 |doi= }}
*{{cite journal | author=Bergren WG, Donnell GN |title=A new variant of galactose-1-phosphate uridyltransferase in man: the Los Angeles variant. |journal=Ann. Hum. Genet. |volume=37 |issue= 1 |pages= 1-8 |year= 1974 |pmid= 4759900 |doi= }}
*{{cite journal | author=Shih LY, Suslak L, Rosin I, ''et al.'' |title=Gene dosage studies supporting localization of the structural gene for galactose-1-phosphate uridyl transferase (GALT) to band p13 of chromosome 9. |journal=Am. J. Med. Genet. |volume=19 |issue= 3 |pages= 539-43 |year= 1985 |pmid= 6095663 |doi= 10.1002/ajmg.1320190316 }}
*{{cite journal | author=Ashino J, Okano Y, Suyama I, ''et al.'' |title=Molecular characterization of galactosemia (type 1) mutations in Japanese. |journal=Hum. Mutat. |volume=6 |issue= 1 |pages= 36-43 |year= 1995 |pmid= 7550229 |doi= 10.1002/humu.1380060108 }}
*{{cite journal | author=Elsas LJ, Langley S, Paulk EM, ''et al.'' |title=A molecular approach to galactosemia. |journal=Eur. J. Pediatr. |volume=154 |issue= 7 Suppl 2 |pages= S21-7 |year= 1995 |pmid= 7671959 |doi= }}
*{{cite journal | author=Elsas LJ, Langley S, Steele E, ''et al.'' |title=Galactosemia: a strategy to identify new biochemical phenotypes and molecular genotypes. |journal=Am. J. Hum. Genet. |volume=56 |issue= 3 |pages= 630-9 |year= 1995 |pmid= 7887416 |doi= }}
*{{cite journal | author=Fridovich-Keil JL, Langley SD, Mazur LA, ''et al.'' |title=Identification and functional analysis of three distinct mutations in the human galactose-1-phosphate uridyltransferase gene associated with galactosemia in a single family. |journal=Am. J. Hum. Genet. |volume=56 |issue= 3 |pages= 640-6 |year= 1995 |pmid= 7887417 |doi= }}
*{{cite journal | author=Davit-Spraul A, Pourci ML, Ng KH, ''et al.'' |title=Regulatory effects of galactose on galactose-1-phosphate uridyltransferase activity on human hepatoblastoma HepG2 cells. |journal=FEBS Lett. |volume=354 |issue= 2 |pages= 232-6 |year= 1994 |pmid= 7957929 |doi= }}
*{{cite journal | author=Lin HC, Kirby LT, Ng WG, Reichardt JK |title=On the molecular nature of the Duarte variant of galactose-1-phosphate uridyl transferase (GALT). |journal=Hum. Genet. |volume=93 |issue= 2 |pages= 167-9 |year= 1994 |pmid= 8112740 |doi= }}
*{{cite journal | author=Elsas LJ, Dembure PP, Langley S, ''et al.'' |title=A common mutation associated with the Duarte galactosemia allele. |journal=Am. J. Hum. Genet. |volume=54 |issue= 6 |pages= 1030-6 |year= 1994 |pmid= 8198125 |doi= }}
*{{cite journal | author=Reichardt JK, Novelli G, Dallapiccola B |title=Molecular characterization of the H319Q galactosemia mutation. |journal=Hum. Mol. Genet. |volume=2 |issue= 3 |pages= 325-6 |year= 1993 |pmid= 8499924 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GAST... {November 16, 2007 4:46:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:46:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Gastrin
| HGNCid = 4164
| Symbol = GAST
| AltSymbols =; GAS
| OMIM = 137250
| ECnumber =
| Homologene = 628
| MGIid = 104768
| GeneAtlas_image1 = PBB_GE_GAST_208138_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006939 |text = smooth muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2520
| Hs_Ensembl = ENSG00000184502
| Hs_RefseqProtein = NP_000796
| Hs_RefseqmRNA = NM_000805
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 37122139
| Hs_GenLoc_end = 37125746
| Hs_Uniprot = P01350
| Mm_EntrezGene = 14459
| Mm_Ensembl = ENSMUSG00000017165
| Mm_RefseqmRNA = NM_010257
| Mm_RefseqProtein = NP_034387
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 100150497
| Mm_GenLoc_end = 100153086
| Mm_Uniprot = Q6GSF5
}}
}}
'''Gastrin''', also known as '''GAST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAST gastrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2520| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Gastrin is a hormone whose main function is to stimulate secretion of hydrochloric acid by the gastric mucosa, which results in gastrin formation inhibition. This hormone also acts as a mitogenic factor for gastrointestinal epithelial cells. Gastrin has two biologically active peptide forms, G34 and G17.<ref name="entrez">{{cite web | title = Entrez Gene: GAST gastrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2520| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rozengurt E, Walsh JH |title=Gastrin, CCK, signaling, and cancer. |journal=Annu. Rev. Physiol. |volume=63 |issue= |pages= 49-76 |year= 2001 |pmid= 11181948 |doi= 10.1146/annurev.physiol.63.1.49 }}
*{{cite journal | author=Dockray GJ |title=Clinical endocrinology and metabolism. Gastrin. |journal=Best Pract. Res. Clin. Endocrinol. Metab. |volume=18 |issue= 4 |pages= 555-68 |year= 2005 |pmid= 15533775 |doi= 10.1016/j.beem.2004.07.003 }}
*{{cite journal | author=Anlauf M, Garbrecht N, Henopp T, ''et al.'' |title=Sporadic versus hereditary gastrinomas of the duodenum and pancreas: distinct clinico-pathological and epidemiological features. |journal=World J. Gastroenterol. |volume=12 |issue= 34 |pages= 5440-6 |year= 2006 |pmid= 17006979 |doi= }}
*{{cite journal | author=Polosatov MV, Klimov PK, Masevich CG, ''et al.'' |title=Interaction of synthetic human big gastrin with blood proteins of man and animals. |journal=Acta hepato-gastroenterologica |volume=26 |issue= 2 |pages= 154-9 |year= 1979 |pmid= 463490 |doi= }}
*{{cite journal | author=Fritsch WP, Hausamen TU, Scholten T |title=[Gastrointestinal hormones. I. Hormones of the gastrin group] |journal=Zeitschrift für Gastroenterologie |volume=15 |issue= 4 |pages= 264-76 |year= 1977 |pmid= 871064 |doi= }}
*{{cite journal | author=Higashimoto Y, Himeno S, Shinomura Y, ''et al.'' |title=Purification and structural determination of urinary NH2-terminal big gastrin fragments. |journal=Biochem. Biophys. Res. Commun. |volume=160 |issue= 3 |pages= 1364-70 |year= 1989 |pmid= 2730647 |doi= }}
*{{cite journal | author=Pauwels S, Najdovski T, Dimaline R, ''et al.'' |title=Degradation of human gastrin and CCK by endopeptidase 24.11: differential behaviour of the sulphated and unsulphated peptides. |journal=Biochim. Biophys. Acta |volume=996 |issue= 1-2 |pages= 82-8 |year= 1989 |pmid= 2736261 |doi= }}
*{{cite journal | author=Lund T, Geurts van Kessel AH, Haun S, Dixon JE |title=The genes for human gastrin and cholecystokinin are located on different chromosomes. |journal=Hum. Genet. |volume=73 |issue= 1 |pages= 77-80 |year= 1986 |pmid= 3011648 |doi= }}
*{{cite journal | author=Kariya Y, Kato K, Hayashizaki Y, ''et al.'' |title=Expression of human gastrin gene in normal and gastrinoma tissues. |journal=Gene |volume=50 |issue= 1-3 |pages= 345-52 |year= 1987 |pmid= 3034736 |doi= }}
*{{cite journal | author=Gregory RA, Tracy HJ, Agarwal KL, Grossman MI |title=Aminoacid constitution of two gastrins isolated from Zollinger-Ellison tumour tissue. |journal=Gut |volume=10 |issue= 8 |pages= 603-8 |year= 1969 |pmid= 5822140 |doi= }}
*{{cite journal | author=Bentley PH, Kenner GW, Sheppard RC |title=Structures of human gastrins I and II. |journal=Nature |volume=209 |issue= 5023 |pages= 583-5 |year= 1967 |pmid= 5921183 |doi= }}
*{{cite journal | author=Ito R, Sato K, Helmer T, ''et al.'' |title=Structural analysis of the gene encoding human gastrin: the large intron contains an Alu sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 15 |pages= 4662-6 |year= 1984 |pmid= 6087340 |doi= }}
*{{cite journal | author=Wiborg O, Berglund L, Boel E, ''et al.'' |title=Structure of a human gastrin gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 4 |pages= 1067-9 |year= 1984 |pmid= 6322186 |doi= }}
*{{cite journal | author=Kato K, Hayashizaki Y, Takahashi Y, ''et al.'' |title=Molecular cloning of the human gastrin gene. |journal=Nucleic Acids Res. |volume=11 |issue= 23 |pages= 8197-203 |year= 1984 |pmid= 6324077 |doi= }}
*{{cite journal | author=Boel E, Vuust J, Norris F, ''et al.'' |title=Molecular cloning of human gastrin cDNA: evidence for evolution of gastrin by gene duplication. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 10 |pages= 2866-9 |year= 1983 |pmid= 6574456 |doi= }}
*{{cite journal | author=Kato K, Himeno S, Takahashi Y, ''et al.'' |title=Molecular cloning of human gastrin precursor cDNA. |journal=Gene |volume=26 |issue= 1 |pages= 53-7 |year= 1984 |pmid= 6689486 |doi= }}
*{{cite journal | author=Koh TJ, Wang TC |title=Molecular cloning and sequencing of the murine gastrin gene. |journal=Biochem. Biophys. Res. Commun. |volume=216 |issue= 1 |pages= 34-41 |year= 1995 |pmid= 7488110 |doi= 10.1006/bbrc.1995.2588 }}
*{{cite journal | author=Rehfeld JF, Hansen CP, Johnsen AH |title=Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism. |journal=EMBO J. |volume=14 |issue= 2 |pages= 389-96 |year= 1995 |pmid= 7530658 |doi= }}
*{{cite journal | author=Rehfeld JF, Johnsen AH |title=Identification of gastrin component I as gastrin-71. The largest possible bioactive progastrin product. |journal=Eur. J. Biochem. |volume=223 |issue= 3 |pages= 765-73 |year= 1994 |pmid= 8055952 |doi= }}
*{{cite journal | author=Varro A, Dockray GJ |title=Post-translational processing of progastrin: inhibition of cleavage, phosphorylation and sulphation by brefeldin A. |journal=Biochem. J. |volume=295 ( Pt 3) |issue= |pages= 813-9 |year= 1993 |pmid= 8240296 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GSTA1... {November 16, 2007 4:47:04 PM PST}
- SEARCH REDIRECT: Control Box Found: GSTA1 {November 16, 2007 4:47:35 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:47:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:47:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:47:36 PM PST}
- UPDATED: Updated protein page: GSTA1 {November 16, 2007 4:47:43 PM PST}
- INFO: Beginning work on GTF2F1... {November 16, 2007 4:47:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:48:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GTF2F1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f3u.
| PDB = {{PDB2|1f3u}}, {{PDB2|1i27}}, {{PDB2|1j2x}}, {{PDB2|1nha}}, {{PDB2|1onv}}
| Name = General transcription factor IIF, polypeptide 1, 74kDa
| HGNCid = 4652
| Symbol = GTF2F1
| AltSymbols =; BTF4; RAP74; TF2F1; TFIIF
| OMIM = 189968
| ECnumber =
| Homologene = 1585
| MGIid = 1923848
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005674 |text = transcription factor TFIIF complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2962
| Hs_Ensembl = ENSG00000125651
| Hs_RefseqProtein = NP_002087
| Hs_RefseqmRNA = NM_002096
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 6235811
| Hs_GenLoc_end = 6344184
| Hs_Uniprot = P35269
| Mm_EntrezGene = 98053
| Mm_Ensembl = ENSMUSG00000002658
| Mm_RefseqmRNA = NM_133801
| Mm_RefseqProtein = NP_598562
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 56688526
| Mm_GenLoc_end = 56696547
| Mm_Uniprot = Q8R5B7
}}
}}
'''General transcription factor IIF, polypeptide 1, 74kDa''', also known as '''GTF2F1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2F1 general transcription factor IIF, polypeptide 1, 74kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2962| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kato H, Sumimoto H, Pognonec P, ''et al.'' |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655-66 |year= 1992 |pmid= 1559613 |doi= }}
*{{cite journal | author=Aso T, Vasavada HA, Kawaguchi T, ''et al.'' |title=Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF. |journal=Nature |volume=355 |issue= 6359 |pages= 461-4 |year= 1992 |pmid= 1734283 |doi= 10.1038/355461a0 }}
*{{cite journal | author=Finkelstein A, Kostrub CF, Li J, ''et al.'' |title=A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II. |journal=Nature |volume=355 |issue= 6359 |pages= 464-7 |year= 1992 |pmid= 1734284 |doi= 10.1038/355464a0 }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Ruppert S, Tjian R |title=Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. |journal=Genes Dev. |volume=9 |issue= 22 |pages= 2747-55 |year= 1995 |pmid= 7590250 |doi= }}
*{{cite journal | author=Hisatake K, Ohta T, Takada R, ''et al.'' |title=Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 18 |pages= 8195-9 |year= 1995 |pmid= 7667268 |doi= }}
*{{cite journal | author=Joliot V, Demma M, Prywes R |title=Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor. |journal=Nature |volume=373 |issue= 6515 |pages= 632-5 |year= 1995 |pmid= 7854423 |doi= 10.1038/373632a0 }}
*{{cite journal | author=Zhu H, Joliot V, Prywes R |title=Role of transcription factor TFIIF in serum response factor-activated transcription. |journal=J. Biol. Chem. |volume=269 |issue= 5 |pages= 3489-97 |year= 1994 |pmid= 8106390 |doi= }}
*{{cite journal | author=Yonaha M, Aso T, Kobayashi Y, ''et al.'' |title=Domain structure of a human general transcription initiation factor, TFIIF. |journal=Nucleic Acids Res. |volume=21 |issue= 2 |pages= 273-9 |year= 1993 |pmid= 8441635 |doi= }}
*{{cite journal | author=Aso T, Tsai P, Kawaguchi T, ''et al.'' |title=Assignment of the human GTF2F1 gene to chromosome 19p13.3. |journal=Genomics |volume=16 |issue= 1 |pages= 252-3 |year= 1993 |pmid= 8486367 |doi= 10.1006/geno.1993.1168 }}
*{{cite journal | author=Dikstein R, Ruppert S, Tjian R |title=TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74. |journal=Cell |volume=84 |issue= 5 |pages= 781-90 |year= 1996 |pmid= 8625415 |doi= }}
*{{cite journal | author=Fang SM, Burton ZF |title=RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding. |journal=J. Biol. Chem. |volume=271 |issue= 20 |pages= 11703-9 |year= 1996 |pmid= 8662660 |doi= }}
*{{cite journal | author=McEwan IJ, Dahlman-Wright K, Ford J, Wright AP |title=Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. |journal=Biochemistry |volume=35 |issue= 29 |pages= 9584-93 |year= 1996 |pmid= 8755740 |doi= 10.1021/bi960793v }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=Scully R, Anderson SF, Chao DM, ''et al.'' |title=BRCA1 is a component of the RNA polymerase II holoenzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5605-10 |year= 1997 |pmid= 9159119 |doi= }}
*{{cite journal | author=McEwan IJ, Gustafsson J |title=Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8485-90 |year= 1997 |pmid= 9238003 |doi= }}
*{{cite journal | author=Newberry EP, Latifi T, Battaile JT, Towler DA |title=Structure-function analysis of Msx2-mediated transcriptional suppression. |journal=Biochemistry |volume=36 |issue= 34 |pages= 10451-62 |year= 1997 |pmid= 9265625 |doi= 10.1021/bi971008x }}
*{{cite journal | author=O'Brien T, Tjian R |title=Functional analysis of the human TAFII250 N-terminal kinase domain. |journal=Mol. Cell |volume=1 |issue= 6 |pages= 905-11 |year= 1998 |pmid= 9660973 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSP90B1... {November 16, 2007 4:53:12 PM PST}
- SEARCH REDIRECT: Control Box Found: HSP90B1 {November 16, 2007 4:53:47 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:53:48 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:53:48 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:53:48 PM PST}
- UPDATED: Updated protein page: HSP90B1 {November 16, 2007 4:53:55 PM PST}
- INFO: Beginning work on HSPA4... {November 16, 2007 4:48:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:48:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Heat shock 70kDa protein 4
| HGNCid = 5237
| Symbol = HSPA4
| AltSymbols =; APG-2; HS24/P52; MGC131852; RY; hsp70; hsp70RY
| OMIM = 601113
| ECnumber =
| Homologene = 1624
| MGIid = 1342292
| GeneAtlas_image1 = PBB_GE_HSPA4_208814_at_tn.png
| GeneAtlas_image2 = PBB_GE_HSPA4_208815_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_HSPA4_211015_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3308
| Hs_Ensembl = ENSG00000170606
| Hs_RefseqProtein = NP_002145
| Hs_RefseqmRNA = NM_002154
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 132415561
| Hs_GenLoc_end = 132468608
| Hs_Uniprot = P34932
| Mm_EntrezGene = 15525
| Mm_Ensembl = ENSMUSG00000020361
| Mm_RefseqmRNA = NM_008300
| Mm_RefseqProtein = NP_032326
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 53103239
| Mm_GenLoc_end = 53143853
| Mm_Uniprot = Q571M2
}}
}}
'''Heat shock 70kDa protein 4''', also known as '''HSPA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSPA4 heat shock 70kDa protein 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3308| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Abravaya K, Myers MP, Murphy SP, Morimoto RI |title=The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. |journal=Genes Dev. |volume=6 |issue= 7 |pages= 1153-64 |year= 1992 |pmid= 1628823 |doi= }}
*{{cite journal | author=Liao J, Lowthert LA, Ghori N, Omary MB |title=The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 915-22 |year= 1995 |pmid= 7529764 |doi= }}
*{{cite journal | author=Furlini G, Vignoli M, Re MC, ''et al.'' |title=Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein. |journal=J. Gen. Virol. |volume=75 ( Pt 1) |issue= |pages= 193-9 |year= 1994 |pmid= 7906708 |doi= }}
*{{cite journal | author=Fathallah DM, Cherif D, Dellagi K, Arnaout MA |title=Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5. |journal=J. Immunol. |volume=151 |issue= 2 |pages= 810-3 |year= 1993 |pmid= 8335910 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Schulte AM, Fischer S, Sachse GE, ''et al.'' |title=Identification and characterization of a novel hsc70-like gene in the human lung tumor cell line HS24. |journal=DNA Cell Biol. |volume=16 |issue= 3 |pages= 257-68 |year= 1997 |pmid= 9115634 |doi= }}
*{{cite journal | author=Kaneko Y, Kimura T, Kishishita M, ''et al.'' |title=Cloning of apg-2 encoding a novel member of heat shock protein 110 family. |journal=Gene |volume=189 |issue= 1 |pages= 19-24 |year= 1997 |pmid= 9161406 |doi= }}
*{{cite journal | author=Bruner KL, Derfoul A, Robertson NM, ''et al.'' |title=The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52. |journal=Receptors & signal transduction |volume=7 |issue= 2 |pages= 85-98 |year= 1998 |pmid= 9392437 |doi= }}
*{{cite journal | author=Satyal SH, Chen D, Fox SG, ''et al.'' |title=Negative regulation of the heat shock transcriptional response by HSBP1. |journal=Genes Dev. |volume=12 |issue= 13 |pages= 1962-74 |year= 1998 |pmid= 9649501 |doi= }}
*{{cite journal | author=Naylor DJ, Stines AP, Hoogenraad NJ, Høj PB |title=Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-like proteins, the Co-chaperones of specific Hsp70 members. |journal=J. Biol. Chem. |volume=273 |issue= 33 |pages= 21169-77 |year= 1998 |pmid= 9694873 |doi= }}
*{{cite journal | author=Melville MW, Tan SL, Wambach M, ''et al.'' |title=The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3797-803 |year= 1999 |pmid= 9920933 |doi= }}
*{{cite journal | author=Ballinger CA, Connell P, Wu Y, ''et al.'' |title=Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4535-45 |year= 1999 |pmid= 10330192 |doi= }}
*{{cite journal | author=Liu H, Vuyyuru VB, Pham CD, ''et al.'' |title=Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association. |journal=Oncogene |volume=18 |issue= 23 |pages= 3461-70 |year= 1999 |pmid= 10376524 |doi= 10.1038/sj.onc.1202699 }}
*{{cite journal | author=Nonoguchi K, Itoh K, Xue JH, ''et al.'' |title=Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110 family, and chromosomal assignment of their genes. |journal=Gene |volume=237 |issue= 1 |pages= 21-8 |year= 1999 |pmid= 10524232 |doi= }}
*{{cite journal | author=O'Keeffe B, Fong Y, Chen D, ''et al.'' |title=Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 279-87 |year= 2000 |pmid= 10617616 |doi= }}
*{{cite journal | author=Agostini I, Popov S, Li J, ''et al.'' |title=Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 398-403 |year= 2000 |pmid= 10964507 |doi= 10.1006/excr.2000.4992 }}
*{{cite journal | author=Kim M, Jiang LH, Wilson HL, ''et al.'' |title=Proteomic and functional evidence for a P2X7 receptor signalling complex. |journal=EMBO J. |volume=20 |issue= 22 |pages= 6347-58 |year= 2002 |pmid= 11707406 |doi= 10.1093/emboj/20.22.6347 }}
*{{cite journal | author=Johnson CA, White DA, Lavender JS, ''et al.'' |title=Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9590-7 |year= 2002 |pmid= 11777905 |doi= 10.1074/jbc.M107942200 }}
*{{cite journal | author=Gurer C, Cimarelli A, Luban J |title=Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. |journal=J. Virol. |volume=76 |issue= 9 |pages= 4666-70 |year= 2002 |pmid= 11932435 |doi= }}
*{{cite journal | author=Freeman BC, Yamamoto KR |title=Disassembly of transcriptional regulatory complexes by molecular chaperones. |journal=Science |volume=296 |issue= 5576 |pages= 2232-5 |year= 2002 |pmid= 12077419 |doi= 10.1126/science.1073051 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on INPP5D... {November 16, 2007 4:48:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:49:19 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Inositol polyphosphate-5-phosphatase, 145kDa
| HGNCid = 6079
| Symbol = INPP5D
| AltSymbols =; MGC104855; MGC142140; MGC142142; SHIP; SHIP1; SIP-145; hp51CN
| OMIM = 601582
| ECnumber =
| Homologene = 4046
| MGIid = 107357
| Function = {{GNF_GO|id=GO:0004437 |text = inositol or phosphatidylinositol phosphatase activity}} {{GNF_GO|id=GO:0004445 |text = inositol-polyphosphate 5-phosphatase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006796 |text = phosphate metabolic process}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3635
| Hs_Ensembl =
| Hs_RefseqProtein = XP_935053
| Hs_RefseqmRNA = XM_929960
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16331
| Mm_Ensembl = ENSMUSG00000026288
| Mm_RefseqmRNA = NM_010566
| Mm_RefseqProtein = NP_034696
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 89451660
| Mm_GenLoc_end = 89549455
| Mm_Uniprot =
}}
}}
'''Inositol polyphosphate-5-phosphatase, 145kDa''', also known as '''INPP5D''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: INPP5D inositol polyphosphate-5-phosphatase, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3635| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and encodes a protein with an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation. At the plasma membrane, the protein hydrolyzes the 5' phosphate from phosphatidylinositol (3,4,5)-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, thereby affecting multiple signaling pathways. Overall, the protein functions as a negative regulator of myeliod cell proliferation and survival. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: INPP5D inositol polyphosphate-5-phosphatase, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3635| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=MacDonald SM, Vonakis BM |title=Association of the Src homology 2 domain-containing inositol 5' phosphatase (SHIP) to releasability in human basophils. |journal=Mol. Immunol. |volume=38 |issue= 16-18 |pages= 1323-7 |year= 2003 |pmid= 12217402 |doi= }}
*{{cite journal | author=Damen JE, Liu L, Rosten P, ''et al.'' |title=The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 4 |pages= 1689-93 |year= 1996 |pmid= 8643691 |doi= }}
*{{cite journal | author=Lioubin MN, Algate PA, Tsai S, ''et al.'' |title=p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. |journal=Genes Dev. |volume=10 |issue= 9 |pages= 1084-95 |year= 1996 |pmid= 8654924 |doi= }}
*{{cite journal | author=Kavanaugh WM, Pot DA, Chin SM, ''et al.'' |title=Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. |journal=Curr. Biol. |volume=6 |issue= 4 |pages= 438-45 |year= 1997 |pmid= 8723348 |doi= }}
*{{cite journal | author=Drayer AL, Pesesse X, De Smedt F, ''et al.'' |title=Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. |journal=Biochem. Biophys. Res. Commun. |volume=225 |issue= 1 |pages= 243-9 |year= 1996 |pmid= 8769125 |doi= 10.1006/bbrc.1996.1161 }}
*{{cite journal | author=Ware MD, Rosten P, Damen JE, ''et al.'' |title=Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. |journal=Blood |volume=88 |issue= 8 |pages= 2833-40 |year= 1996 |pmid= 8874179 |doi= }}
*{{cite journal | author=Geier SJ, Algate PA, Carlberg K, ''et al.'' |title=The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. |journal=Blood |volume=89 |issue= 6 |pages= 1876-85 |year= 1997 |pmid= 9058707 |doi= }}
*{{cite journal | author=Odai H, Sasaki K, Iwamatsu A, ''et al.'' |title=Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl. |journal=Blood |volume=89 |issue= 8 |pages= 2745-56 |year= 1997 |pmid= 9108392 |doi= }}
*{{cite journal | author=Liu L, Damen JE, Ware MD, Krystal G |title=Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 10998-1001 |year= 1997 |pmid= 9110989 |doi= }}
*{{cite journal | author=Giuriato S, Payrastre B, Drayer AL, ''et al.'' |title=Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 26857-63 |year= 1997 |pmid= 9341117 |doi= }}
*{{cite journal | author=Kuroiwa A, Yamashita Y, Inui M, ''et al.'' |title=Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene. |journal=J. Biol. Chem. |volume=273 |issue= 2 |pages= 1070-4 |year= 1998 |pmid= 9422771 |doi= }}
*{{cite journal | author=Liu Q, Shalaby F, Jones J, ''et al.'' |title=The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis. |journal=Blood |volume=91 |issue= 8 |pages= 2753-9 |year= 1998 |pmid= 9531585 |doi= }}
*{{cite journal | author=Zhang S, Broxmeyer HE |title=p85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP, and a tyrosine-phosphorylated 100-kDa protein in Flt3 ligand-stimulated hematopoietic cells. |journal=Biochem. Biophys. Res. Commun. |volume=254 |issue= 2 |pages= 440-5 |year= 1999 |pmid= 9918857 |doi= 10.1006/bbrc.1998.9959 }}
*{{cite journal | author=Mikhalap SV, Shlapatska LM, Berdova AG, ''et al.'' |title=CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis. |journal=J. Immunol. |volume=162 |issue= 10 |pages= 5719-27 |year= 1999 |pmid= 10229804 |doi= }}
*{{cite journal | author=Pumphrey NJ, Taylor V, Freeman S, ''et al.'' |title=Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31. |journal=FEBS Lett. |volume=450 |issue= 1-2 |pages= 77-83 |year= 1999 |pmid= 10350061 |doi= }}
*{{cite journal | author=Mason JM, Beattie BK, Liu Q, ''et al.'' |title=The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4398-406 |year= 2000 |pmid= 10660611 |doi= }}
*{{cite journal | author=Bone H, Welham MJ |title=Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. |journal=Cell. Signal. |volume=12 |issue= 3 |pages= 183-94 |year= 2000 |pmid= 10704825 |doi= }}
*{{cite journal | author=Lemay S, Davidson D, Latour S, Veillette A |title=Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. |journal=Mol. Cell. Biol. |volume=20 |issue= 8 |pages= 2743-54 |year= 2000 |pmid= 10733577 |doi= }}
*{{cite journal | author=Poe JC, Fujimoto M, Jansen PJ, ''et al.'' |title=CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux. |journal=J. Biol. Chem. |volume=275 |issue= 23 |pages= 17420-7 |year= 2000 |pmid= 10748054 |doi= 10.1074/jbc.M001892200 }}
*{{cite journal | author=Dunant NM, Wisniewski D, Strife A, ''et al.'' |title=The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells. |journal=Cell. Signal. |volume=12 |issue= 5 |pages= 317-26 |year= 2000 |pmid= 10822173 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KPNA6... {November 16, 2007 4:56:39 PM PST}
- SEARCH REDIRECT: Control Box Found: KPNA6 {November 16, 2007 4:57:09 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:57:13 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:57:13 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:57:13 PM PST}
- UPDATED: Updated protein page: KPNA6 {November 16, 2007 4:57:20 PM PST}
- INFO: Beginning work on LRP2... {November 16, 2007 4:49:19 PM PST}
- SEARCH REDIRECT: Control Box Found: LRP2 {November 16, 2007 4:49:45 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:49:48 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:49:48 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:49:48 PM PST}
- UPDATED: Updated protein page: LRP2 {November 16, 2007 4:49:54 PM PST}
- INFO: Beginning work on MMP8... {November 16, 2007 4:49:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:50:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MMP8_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a85.
| PDB = {{PDB2|1a85}}, {{PDB2|1a86}}, {{PDB2|1bzs}}, {{PDB2|1i73}}, {{PDB2|1i76}}, {{PDB2|1jan}}, {{PDB2|1jao}}, {{PDB2|1jap}}, {{PDB2|1jaq}}, {{PDB2|1jh1}}, {{PDB2|1jj9}}, {{PDB2|1kbc}}, {{PDB2|1mmb}}, {{PDB2|1mnc}}, {{PDB2|1zp5}}, {{PDB2|1zs0}}, {{PDB2|1zvx}}, {{PDB2|2oy2}}, {{PDB2|2oy4}}
| Name = Matrix metallopeptidase 8 (neutrophil collagenase)
| HGNCid = 7175
| Symbol = MMP8
| AltSymbols =; CLG1; HNC; PMNL-CL
| OMIM = 120355
| ECnumber =
| Homologene = 22482
| MGIid = 1202395
| GeneAtlas_image1 = PBB_GE_MMP8_207329_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0004232 |text = interstitial collagenase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008130 |text = neutrophil collagenase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000270 |text = peptidoglycan metabolic process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4317
| Hs_Ensembl = ENSG00000118113
| Hs_RefseqProtein = NP_002415
| Hs_RefseqmRNA = NM_002424
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 102088599
| Hs_GenLoc_end = 102100868
| Hs_Uniprot = P22894
| Mm_EntrezGene = 17394
| Mm_Ensembl = ENSMUSG00000005800
| Mm_RefseqmRNA = NM_008611
| Mm_RefseqProtein = NP_032637
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 7558456
| Mm_GenLoc_end = 7568486
| Mm_Uniprot = Q3TAV4
}}
}}
'''Matrix metallopeptidase 8 (neutrophil collagenase)''', also known as '''MMP8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MMP8 matrix metallopeptidase 8 (neutrophil collagenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4317| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.<ref name="entrez">{{cite web | title = Entrez Gene: MMP8 matrix metallopeptidase 8 (neutrophil collagenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4317| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chandler S, Miller KM, Clements JM, ''et al.'' |title=Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview. |journal=J. Neuroimmunol. |volume=72 |issue= 2 |pages= 155-61 |year= 1997 |pmid= 9042108 |doi= }}
*{{cite journal | author=Massova I, Kotra LP, Fridman R, Mobashery S |title=Matrix metalloproteinases: structures, evolution, and diversification. |journal=FASEB J. |volume=12 |issue= 12 |pages= 1075-95 |year= 1998 |pmid= 9737711 |doi= }}
*{{cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491-4 |year= 1999 |pmid= 10419448 |doi= }}
*{{cite journal | author=Bläser J, Triebel S, Reinke H, Tschesche H |title=Formation of a covalent Hg-Cys-bond during mercurial activation of PMNL procollagenase gives evidence of a cysteine-switch mechanism. |journal=FEBS Lett. |volume=313 |issue= 1 |pages= 59-61 |year= 1992 |pmid= 1330697 |doi= }}
*{{cite journal | author=Devarajan P, Mookhtiar K, Van Wart H, Berliner N |title=Structure and expression of the cDNA encoding human neutrophil collagenase. |journal=Blood |volume=77 |issue= 12 |pages= 2731-8 |year= 1991 |pmid= 1646048 |doi= }}
*{{cite journal | author=Bläser J, Knäuper V, Osthues A, ''et al.'' |title=Mercurial activation of human polymorphonuclear leucocyte procollagenase. |journal=Eur. J. Biochem. |volume=202 |issue= 3 |pages= 1223-30 |year= 1992 |pmid= 1662606 |doi= }}
*{{cite journal | author=Knäuper V, Krämer S, Reinke H, Tschesche H |title=Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. |journal=Eur. J. Biochem. |volume=189 |issue= 2 |pages= 295-300 |year= 1990 |pmid= 2159879 |doi= }}
*{{cite journal | author=Hasty KA, Pourmotabbed TF, Goldberg GI, ''et al.'' |title=Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. |journal=J. Biol. Chem. |volume=265 |issue= 20 |pages= 11421-4 |year= 1990 |pmid= 2164002 |doi= }}
*{{cite journal | author=Knäuper V, Krämer S, Reinke H, Tschesche H |title=Partial amino acid sequence of human PMN leukocyte procollagenase. |journal=Biol. Chem. Hoppe-Seyler |volume=371 Suppl |issue= |pages= 295-304 |year= 1990 |pmid= 2169256 |doi= }}
*{{cite journal | author=Knäuper V, Krämer S, Reinke H, Tschesche H |title=Partial amino-acid sequence of human PMN leukocyte procollagenase. |journal=Biol. Chem. Hoppe-Seyler |volume=371 |issue= 8 |pages= 733 |year= 1990 |pmid= 2169766 |doi= }}
*{{cite journal | author=Mallya SK, Mookhtiar KA, Gao Y, ''et al.'' |title=Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase. |journal=Biochemistry |volume=29 |issue= 47 |pages= 10628-34 |year= 1991 |pmid= 2176876 |doi= }}
*{{cite journal | author=Stams T, Spurlino JC, Smith DL, ''et al.'' |title=Structure of human neutrophil collagenase reveals large S1' specificity pocket. |journal=Nat. Struct. Biol. |volume=1 |issue= 2 |pages= 119-23 |year= 1995 |pmid= 7656015 |doi= }}
*{{cite journal | author=Fosang AJ, Last K, Neame PJ, ''et al.'' |title=Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan. |journal=Biochem. J. |volume=304 ( Pt 2) |issue= |pages= 347-51 |year= 1995 |pmid= 7998967 |doi= }}
*{{cite journal | author=Bode W, Reinemer P, Huber R, ''et al.'' |title=The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. |journal=EMBO J. |volume=13 |issue= 6 |pages= 1263-9 |year= 1994 |pmid= 8137810 |doi= }}
*{{cite journal | author=Fosang AJ, Last K, Knäuper V, ''et al.'' |title=Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain. |journal=Biochem. J. |volume=295 ( Pt 1) |issue= |pages= 273-6 |year= 1993 |pmid= 8216228 |doi= }}
*{{cite journal | author=Reinemer P, Grams F, Huber R, ''et al.'' |title=Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study. |journal=FEBS Lett. |volume=338 |issue= 2 |pages= 227-33 |year= 1994 |pmid= 8307185 |doi= }}
*{{cite journal | author=Thomas DB, Davies M, Peters JR, Williams JD |title=Tamm Horsfall protein binds to a single class of carbohydrate specific receptors on human neutrophils. |journal=Kidney Int. |volume=44 |issue= 2 |pages= 423-9 |year= 1993 |pmid= 8397318 |doi= }}
*{{cite journal | author=Cole AA, Chubinskaya S, Schumacher B, ''et al.'' |title=Chondrocyte matrix metalloproteinase-8. Human articular chondrocytes express neutrophil collagenase. |journal=J. Biol. Chem. |volume=271 |issue= 18 |pages= 11023-6 |year= 1996 |pmid= 8631924 |doi= }}
*{{cite journal | author=Nakahara Y, Miyata T, Hamuro T, ''et al.'' |title=Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: one N-and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2. |journal=Biochemistry |volume=35 |issue= 20 |pages= 6450-9 |year= 1996 |pmid= 8639592 |doi= 10.1021/bi9524880 }}
*{{cite journal | author=Pendás AM, Santamaría I, Alvarez MV, ''et al.'' |title=Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3. |journal=Genomics |volume=37 |issue= 2 |pages= 266-8 |year= 1997 |pmid= 8921407 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NPHS1... {November 16, 2007 4:50:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:50:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Nephrosis 1, congenital, Finnish type (nephrin)
| HGNCid = 7908
| Symbol = NPHS1
| AltSymbols =; CNF; NPHN
| OMIM = 602716
| ECnumber =
| Homologene = 20974
| MGIid = 1859637
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007588 |text = excretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4868
| Hs_Ensembl =
| Hs_RefseqProtein = NP_004637
| Hs_RefseqmRNA = NM_004646
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 54631
| Mm_Ensembl = ENSMUSG00000006649
| Mm_RefseqmRNA = NM_019459
| Mm_RefseqProtein = NP_062332
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 30168485
| Mm_GenLoc_end = 30195968
| Mm_Uniprot = Q925S5
}}
}}
'''Nephrosis 1, congenital, Finnish type (nephrin)''', also known as '''NPHS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NPHS1 nephrosis 1, congenital, Finnish type (nephrin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4868| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Nephrin is a kidney glomerular filtration barrier protein that is an essential component of the interpodocyte-spanning slit diaphragm. Mutations in the nephrin gene are associated with congenital nephrotic syndrome (NPHS1; MIM 256300).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NPHS1 nephrosis 1, congenital, Finnish type (nephrin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4868| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tryggvason K |title=Nephrin: role in normal kidney and in disease. |journal=Adv. Nephrol. Necker Hosp. |volume=31 |issue= |pages= 221-34 |year= 2002 |pmid= 11692461 |doi= }}
*{{cite journal | author=Kestilä M, Lenkkeri U, Männikkö M, ''et al.'' |title=Positionally cloned gene for a novel glomerular protein--nephrin--is mutated in congenital nephrotic syndrome. |journal=Mol. Cell |volume=1 |issue= 4 |pages= 575-82 |year= 1998 |pmid= 9660941 |doi= }}
*{{cite journal | author=Lenkkeri U, Männikkö M, McCready P, ''et al.'' |title=Structure of the gene for congenital nephrotic syndrome of the finnish type (NPHS1) and characterization of mutations. |journal=Am. J. Hum. Genet. |volume=64 |issue= 1 |pages= 51-61 |year= 1999 |pmid= 9915943 |doi= }}
*{{cite journal | author=Ruotsalainen V, Ljungberg P, Wartiovaara J, ''et al.'' |title=Nephrin is specifically located at the slit diaphragm of glomerular podocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 14 |pages= 7962-7 |year= 1999 |pmid= 10393930 |doi= }}
*{{cite journal | author=Holthöfer H, Ahola H, Solin ML, ''et al.'' |title=Nephrin localizes at the podocyte filtration slit area and is characteristically spliced in the human kidney. |journal=Am. J. Pathol. |volume=155 |issue= 5 |pages= 1681-7 |year= 1999 |pmid= 10550324 |doi= }}
*{{cite journal | author=Bolk S, Puffenberger EG, Hudson J, ''et al.'' |title=Elevated frequency and allelic heterogeneity of congenital nephrotic syndrome, Finnish type, in the old order Mennonites. |journal=Am. J. Hum. Genet. |volume=65 |issue= 6 |pages= 1785-90 |year= 2000 |pmid= 10577936 |doi= }}
*{{cite journal | author=Aya K, Tanaka H, Seino Y |title=Novel mutation in the nephrin gene of a Japanese patient with congenital nephrotic syndrome of the Finnish type. |journal=Kidney Int. |volume=57 |issue= 2 |pages= 401-4 |year= 2000 |pmid= 10652016 |doi= 10.1046/j.1523-1755.2000.00859.x }}
*{{cite journal | author=Li C, Ruotsalainen V, Tryggvason K, ''et al.'' |title=CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere. |journal=Am. J. Physiol. Renal Physiol. |volume=279 |issue= 4 |pages= F785-92 |year= 2000 |pmid= 10997929 |doi= }}
*{{cite journal | author=Huber TB, Kottgen M, Schilling B, ''et al.'' |title=Interaction with podocin facilitates nephrin signaling. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 41543-6 |year= 2001 |pmid= 11562357 |doi= 10.1074/jbc.C100452200 }}
*{{cite journal | author=Palmén T, Ahola H, Palgi J, ''et al.'' |title=Nephrin is expressed in the pancreatic beta cells. |journal=Diabetologia |volume=44 |issue= 10 |pages= 1274-80 |year= 2002 |pmid= 11692176 |doi= }}
*{{cite journal | author=Schwarz K, Simons M, Reiser J, ''et al.'' |title=Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin. |journal=J. Clin. Invest. |volume=108 |issue= 11 |pages= 1621-9 |year= 2002 |pmid= 11733557 |doi= }}
*{{cite journal | author=Koziell A, Grech V, Hussain S, ''et al.'' |title=Genotype/phenotype correlations of NPHS1 and NPHS2 mutations in nephrotic syndrome advocate a functional inter-relationship in glomerular filtration. |journal=Hum. Mol. Genet. |volume=11 |issue= 4 |pages= 379-88 |year= 2002 |pmid= 11854170 |doi= }}
*{{cite journal | author=Yan K, Khoshnoodi J, Ruotsalainen V, Tryggvason K |title=N-linked glycosylation is critical for the plasma membrane localization of nephrin. |journal=J. Am. Soc. Nephrol. |volume=13 |issue= 5 |pages= 1385-9 |year= 2002 |pmid= 11961028 |doi= }}
*{{cite journal | author=Shimizu J, Tanaka H, Aya K, ''et al.'' |title=A missense mutation in the nephrin gene impairs membrane targeting. |journal=Am. J. Kidney Dis. |volume=40 |issue= 4 |pages= 697-703 |year= 2002 |pmid= 12324903 |doi= 10.1053/ajkd.2002.35676 }}
*{{cite journal | author=Saleem MA, Ni L, Witherden I, ''et al.'' |title=Co-localization of nephrin, podocin, and the actin cytoskeleton: evidence for a role in podocyte foot process formation. |journal=Am. J. Pathol. |volume=161 |issue= 4 |pages= 1459-66 |year= 2002 |pmid= 12368218 |doi= }}
*{{cite journal | author=Kim BK, Hong HK, Kim JH, Lee HS |title=Differential expression of nephrin in acquired human proteinuric diseases. |journal=Am. J. Kidney Dis. |volume=40 |issue= 5 |pages= 964-73 |year= 2002 |pmid= 12407641 |doi= 10.1053/ajkd.2002.36328 }}
*{{cite journal | author=Langham RG, Kelly DJ, Cox AJ, ''et al.'' |title=Proteinuria and the expression of the podocyte slit diaphragm protein, nephrin, in diabetic nephropathy: effects of angiotensin converting enzyme inhibition. |journal=Diabetologia |volume=45 |issue= 11 |pages= 1572-6 |year= 2003 |pmid= 12436341 |doi= 10.1007/s00125-002-0946-y }}
*{{cite journal | author=Gigante M, Monno F, Roberto R, ''et al.'' |title=Congenital nephrotic syndrome of the Finnish type in Italy: a molecular approach. |journal=J. Nephrol. |volume=15 |issue= 6 |pages= 696-702 |year= 2003 |pmid= 12495287 |doi= }}
*{{cite journal | author=Pettersson-Fernholm K, Forsblom C, Perola M, ''et al.'' |title=Polymorphisms in the nephrin gene and diabetic nephropathy in type 1 diabetic patients. |journal=Kidney Int. |volume=63 |issue= 4 |pages= 1205-10 |year= 2003 |pmid= 12631336 |doi= 10.1046/j.1523-1755.2003.00855.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PBEF1... {November 16, 2007 4:55:07 PM PST}
- SEARCH REDIRECT: Control Box Found: PBEF1 {November 16, 2007 4:55:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:55:56 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:55:56 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:55:56 PM PST}
- UPDATED: Updated protein page: PBEF1 {November 16, 2007 4:56:01 PM PST}
- INFO: Beginning work on POR... {November 16, 2007 4:50:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:51:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_POR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1amo.
| PDB = {{PDB2|1amo}}, {{PDB2|1b1c}}, {{PDB2|1j9z}}, {{PDB2|1ja0}}, {{PDB2|1ja1}}
| Name = P450 (cytochrome) oxidoreductase
| HGNCid = 9208
| Symbol = POR
| AltSymbols =; CPR; CYPOR; DKFZp686G04235; FLJ26468; P450R
| OMIM = 124015
| ECnumber =
| Homologene = 725
| MGIid = 97744
| GeneAtlas_image1 = PBB_GE_POR_208928_at_tn.png
| Function = {{GNF_GO|id=GO:0003958 |text = NADPH-hemoprotein reductase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0010181 |text = FMN binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5447
| Hs_Ensembl = ENSG00000127948
| Hs_RefseqProtein = NP_000932
| Hs_RefseqmRNA = NM_000941
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 75382409
| Hs_GenLoc_end = 75454108
| Hs_Uniprot = P16435
| Mm_EntrezGene = 18984
| Mm_Ensembl = ENSMUSG00000005514
| Mm_RefseqmRNA = NM_008898
| Mm_RefseqProtein = NP_032924
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 135973785
| Mm_GenLoc_end = 136019952
| Mm_Uniprot = Q05DV1
}}
}}
'''P450 (cytochrome) oxidoreductase''', also known as '''POR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: POR P450 (cytochrome) oxidoreductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5447| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an endoplasmic reticulum membrane oxidoreductase with an FAD-binding domain and a flavodoxin-like domain. The protein binds two cofactors, FAD and FMN, which allow it to donate electrons directly from NADPH to all microsomal P450 enzymes. Mutations in this gene have been associated with various diseases, including apparent combined P450C17 and P450C21 deficiency, amenorrhea and disordered steroidogenesis, congenital adrenal hyperplasia and Antley-Bixler syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: POR P450 (cytochrome) oxidoreductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5447| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Miller WL, Geller DH, Auchus RJ |title=The molecular basis of isolated 17,20 lyase deficiency. |journal=Endocr. Res. |volume=24 |issue= 3-4 |pages= 817-25 |year= 1999 |pmid= 9888582 |doi= }}
*{{cite journal | author=Backes WL, Kelley RW |title=Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. |journal=Pharmacol. Ther. |volume=98 |issue= 2 |pages= 221-33 |year= 2003 |pmid= 12725870 |doi= }}
*{{cite journal | author=Miller WL, Huang N, Pandey AV, ''et al.'' |title=P450 oxidoreductase deficiency: a new disorder of steroidogenesis. |journal=Ann. N. Y. Acad. Sci. |volume=1061 |issue= |pages= 100-8 |year= 2006 |pmid= 16467261 |doi= 10.1196/annals.1336.012 }}
*{{cite journal | author=Shephard EA, Palmer CN, Segall HJ, Phillips IR |title=Quantification of cytochrome P450 reductase gene expression in human tissues. |journal=Arch. Biochem. Biophys. |volume=294 |issue= 1 |pages= 168-72 |year= 1992 |pmid= 1550342 |doi= }}
*{{cite journal | author=Haniu M, McManus ME, Birkett DJ, ''et al.'' |title=Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. |journal=Biochemistry |volume=28 |issue= 21 |pages= 8639-45 |year= 1990 |pmid= 2513880 |doi= }}
*{{cite journal | author=Shephard EA, Phillips IR, Santisteban I, ''et al.'' |title=Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2. |journal=Ann. Hum. Genet. |volume=53 |issue= Pt 4 |pages= 291-301 |year= 1990 |pmid= 2516426 |doi= }}
*{{cite journal | author=Wilks A, Black SM, Miller WL, Ortiz de Montellano PR |title=Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase. |journal=Biochemistry |volume=34 |issue= 13 |pages= 4421-7 |year= 1995 |pmid= 7703255 |doi= }}
*{{cite journal | author=Bhamre S, Anandatheerathavarada HK, Shankar SK, ''et al.'' |title=Purification of multiple forms of cytochrome P450 from a human brain and reconstitution of catalytic activities. |journal=Arch. Biochem. Biophys. |volume=301 |issue= 2 |pages= 251-5 |year= 1993 |pmid= 8460938 |doi= 10.1006/abbi.1993.1141 }}
*{{cite journal | author=Patterson LH, Jones S, Gescher A |title=Generation of a free radical from calphostin C by microsomal cytochrome P450 reductase in rat and human liver. |journal=Biochem. Pharmacol. |volume=51 |issue= 5 |pages= 599-603 |year= 1996 |pmid= 8615895 |doi= }}
*{{cite journal | author=Zhao Q, Smith G, Modi S, ''et al.'' |title=Crystallization and preliminary X-ray diffraction studies of human cytochrome P450 reductase. |journal=J. Struct. Biol. |volume=116 |issue= 2 |pages= 320-5 |year= 1996 |pmid= 8812989 |doi= 10.1006/jsbi.1996.0048 }}
*{{cite journal | author=Barsukov I, Modi S, Lian LY, ''et al.'' |title=1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase. |journal=J. Biomol. NMR |volume=10 |issue= 1 |pages= 63-75 |year= 1998 |pmid= 9335117 |doi= }}
*{{cite journal | author=Guengerich FP, Johnson WW |title=Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14741-50 |year= 1998 |pmid= 9398194 |doi= 10.1021/bi9719399 }}
*{{cite journal | author=Bridges A, Gruenke L, Chang YT, ''et al.'' |title=Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase. |journal=J. Biol. Chem. |volume=273 |issue= 27 |pages= 17036-49 |year= 1998 |pmid= 9642268 |doi= }}
*{{cite journal | author=Kruyt FA, Hoshino T, Liu JM, ''et al.'' |title=Abnormal microsomal detoxification implicated in Fanconi anemia group C by interaction of the FAC protein with NADPH cytochrome P450 reductase. |journal=Blood |volume=92 |issue= 9 |pages= 3050-6 |year= 1998 |pmid= 9787138 |doi= }}
*{{cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Zhao Q, Modi S, Smith G, ''et al.'' |title=Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. |journal=Protein Sci. |volume=8 |issue= 2 |pages= 298-306 |year= 1999 |pmid= 10048323 |doi= }}
*{{cite journal | author=López de Cerain A, Marín A, Idoate MA, ''et al.'' |title=Carbonyl reductase and NADPH cytochrome P450 reductase activities in human tumoral versus normal tissues. |journal=Eur. J. Cancer |volume=35 |issue= 2 |pages= 320-4 |year= 1999 |pmid= 10448278 |doi= }}
*{{cite journal | author=Brimer C, Dalton JT, Zhu Z, ''et al.'' |title=Creation of polarized cells coexpressing CYP3A4, NADPH cytochrome P450 reductase and MDR1/P-glycoprotein. |journal=Pharm. Res. |volume=17 |issue= 7 |pages= 803-10 |year= 2001 |pmid= 10990198 |doi= }}
*{{cite journal | author=Shimada T, Tsumura F, Gillam EM, ''et al.'' |title=Roles of NADPH-P450 reductase in the O-deethylation of 7-ethoxycoumarin by recombinant human cytochrome P450 1B1 variants in Escherichia coli. |journal=Protein Expr. Purif. |volume=20 |issue= 1 |pages= 73-80 |year= 2000 |pmid= 11035953 |doi= 10.1006/prep.2000.1302 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPBP... {November 16, 2007 4:51:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:52:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PPBP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f9p.
| PDB = {{PDB2|1f9p}}, {{PDB2|1nap}}, {{PDB2|1tvx}}
| Name = Pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)
| HGNCid = 9240
| Symbol = PPBP
| AltSymbols =; PBP; B-TG1; Beta-TG; CTAP-III; CTAP3; CTAPIII; CXCL7; LA-PF4; LDGF; MDGF; NAP-2; SCYB7; TC1; TC2; TGB; TGB1; THBGB; THBGB1
| OMIM = 121010
| ECnumber =
| Homologene = 48122
| MGIid = 1888712
| GeneAtlas_image1 = PBB_GE_PPBP_214146_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005355 |text = glucose transmembrane transporter activity}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0015758 |text = glucose transport}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5473
| Hs_Ensembl = ENSG00000163736
| Hs_RefseqProtein = NP_002695
| Hs_RefseqmRNA = NM_002704
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 75071622
| Hs_GenLoc_end = 75072764
| Hs_Uniprot = P02775
| Mm_EntrezGene = 57349
| Mm_Ensembl = ENSMUSG00000029372
| Mm_RefseqmRNA = NM_023785
| Mm_RefseqProtein = NP_076274
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 91843718
| Mm_GenLoc_end = 91845263
| Mm_Uniprot =
}}
}}
'''Pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)''', also known as '''PPBP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPBP pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5473| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a platelet-derived growth factor that belongs to the CXC chemokine family. This growth factor is a potent chemoattractant and activator of neutrophils. It has been shown to stimulate various cellular processes including DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and sythesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by synovial cells.<ref name="entrez">{{cite web | title = Entrez Gene: PPBP pro-platelet basic protein (chemokine (C-X-C motif) ligand 7)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5473| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Begg GS, Pepper DS, Chesterman CN, Morgan FJ |title=Complete covalent structure of human beta-thromboglobulin. |journal=Biochemistry |volume=17 |issue= 9 |pages= 1739-44 |year= 1978 |pmid= 77677 |doi= }}
*{{cite journal | author=Kaplan KL, Broekman MJ, Chernoff A, ''et al.'' |title=Platelet alpha-granule proteins: studies on release and subcellular localization. |journal=Blood |volume=53 |issue= 4 |pages= 604-18 |year= 1979 |pmid= 426909 |doi= }}
*{{cite journal | author=Tunnacliffe A, Majumdar S, Yan B, Poncz M |title=Genes for beta-thromboglobulin and platelet factor 4 are closely linked and form part of a cluster of related genes on chromosome 4. |journal=Blood |volume=79 |issue= 11 |pages= 2896-900 |year= 1992 |pmid= 1316786 |doi= }}
*{{cite journal | author=Cohen AB, Stevens MD, Miller EJ, ''et al.'' |title=Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets. |journal=Am. J. Physiol. |volume=263 |issue= 2 Pt 1 |pages= L249-56 |year= 1992 |pmid= 1387511 |doi= }}
*{{cite journal | author=Morris SW, Nelson N, Valentine MB, ''et al.'' |title=Assignment of the genes encoding human interleukin-8 receptor types 1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35. |journal=Genomics |volume=14 |issue= 3 |pages= 685-91 |year= 1992 |pmid= 1427896 |doi= }}
*{{cite journal | author=Majumdar S, Gonder D, Koutsis B, Poncz M |title=Characterization of the human beta-thromboglobulin gene. Comparison with the gene for platelet factor 4. |journal=J. Biol. Chem. |volume=266 |issue= 9 |pages= 5785-9 |year= 1991 |pmid= 1826003 |doi= }}
*{{cite journal | author=Wenger RH, Hameister H, Clemetson KJ |title=Human platelet basic protein/connective tissue activating peptide-III maps in a gene cluster on chromosome 4q12-q13 along with other genes of the beta-thromboglobulin superfamily. |journal=Hum. Genet. |volume=87 |issue= 3 |pages= 367-8 |year= 1991 |pmid= 1830861 |doi= }}
*{{cite journal | author=Hjemdahl P, Perneby C, Theodorsson E, ''et al.'' |title=A new assay for beta-thromboglobulin in urine. |journal=Thromb. Res. |volume=64 |issue= 1 |pages= 33-43 |year= 1992 |pmid= 1837963 |doi= }}
*{{cite journal | author=Brandt E, Van Damme J, Flad HD |title=Neutrophils can generate their activator neutrophil-activating peptide 2 by proteolytic cleavage of platelet-derived connective tissue-activating peptide III. |journal=Cytokine |volume=3 |issue= 4 |pages= 311-21 |year= 1991 |pmid= 1873479 |doi= }}
*{{cite journal | author=Clark-Lewis I, Moser B, Walz A, ''et al.'' |title=Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide. |journal=Biochemistry |volume=30 |issue= 12 |pages= 3128-35 |year= 1991 |pmid= 2007144 |doi= }}
*{{cite journal | author=Walz A, Baggiolini M |title=Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases. |journal=J. Exp. Med. |volume=171 |issue= 2 |pages= 449-54 |year= 1990 |pmid= 2406364 |doi= }}
*{{cite journal | author=Holt JC, Harris ME, Holt AM, ''et al.'' |title=Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin. |journal=Biochemistry |volume=25 |issue= 8 |pages= 1988-96 |year= 1986 |pmid= 2423119 |doi= }}
*{{cite journal | author=Walz A, Baggiolini M |title=A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils. |journal=Biochem. Biophys. Res. Commun. |volume=159 |issue= 3 |pages= 969-75 |year= 1989 |pmid= 2522778 |doi= }}
*{{cite journal | author=Wenger RH, Wicki AN, Walz A, ''et al.'' |title=Cloning of cDNA coding for connective tissue activating peptide III from a human platelet-derived lambda gt11 expression library. |journal=Blood |volume=73 |issue= 6 |pages= 1498-503 |year= 1989 |pmid= 2713489 |doi= }}
*{{cite journal | author=Castor CW, Walz DA, Ragsdale CG, ''et al.'' |title=Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets. |journal=Biochem. Biophys. Res. Commun. |volume=163 |issue= 2 |pages= 1071-8 |year= 1989 |pmid= 2783111 |doi= }}
*{{cite journal | author=Holt JC, Rabellino EM, Gewirtz AM, ''et al.'' |title=Occurrence of platelet basic protein, a precursor of low affinity platelet factor 4 and beta-thromboglobulin, in human platelets and megakaryocytes. |journal=Exp. Hematol. |volume=16 |issue= 4 |pages= 302-6 |year= 1988 |pmid= 2966071 |doi= }}
*{{cite journal | author=Castor CW, Furlong AM, Carter-Su C |title=Connective tissue activation: stimulation of glucose transport by connective tissue activating peptide III. |journal=Biochemistry |volume=24 |issue= 7 |pages= 1762-7 |year= 1985 |pmid= 4005226 |doi= }}
*{{cite journal | author=McLaren KM, Pepper DS |title=Immunological localisation of beta-thromboglobulin and platelet factor 4 in human megakaryocytes and platelets. |journal=J. Clin. Pathol. |volume=35 |issue= 11 |pages= 1227-31 |year= 1983 |pmid= 6183294 |doi= }}
*{{cite journal | author=Castor CW, Miller JW, Walz DA |title=Structural and biological characteristics of connective tissue activating peptide (CTAP-III), a major human platelet-derived growth factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 3 |pages= 765-9 |year= 1983 |pmid= 6572368 |doi= }}
*{{cite journal | author=Malkowski MG, Wu JY, Lazar JB, ''et al.'' |title=The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7077-87 |year= 1995 |pmid= 7706245 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC40A1... {November 16, 2007 4:57:20 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:57:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 40 (iron-regulated transporter), member 1
| HGNCid = 10909
| Symbol = SLC40A1
| AltSymbols =; FPN1; HFE4; IREG1; MST079; MSTP079; MTP1; SLC11A3
| OMIM = 604653
| ECnumber =
| Homologene = 40959
| MGIid = 1315204
| Function = {{GNF_GO|id=GO:0005381 |text = iron ion transmembrane transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006826 |text = iron ion transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 30061
| Hs_Ensembl = ENSG00000138449
| Hs_RefseqProtein = NP_055400
| Hs_RefseqmRNA = NM_014585
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 190133563
| Hs_GenLoc_end = 190153858
| Hs_Uniprot = Q9NP59
| Mm_EntrezGene = 53945
| Mm_Ensembl = ENSMUSG00000025993
| Mm_RefseqmRNA = NM_016917
| Mm_RefseqProtein = NP_058613
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 45852630
| Mm_GenLoc_end = 45870079
| Mm_Uniprot = Q3TJ33
}}
}}
'''Solute carrier family 40 (iron-regulated transporter), member 1''', also known as '''SLC40A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC40A1 solute carrier family 40 (iron-regulated transporter), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=30061| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pietrangelo A |title=The ferroportin disease. |journal=Blood Cells Mol. Dis. |volume=32 |issue= 1 |pages= 131-8 |year= 2004 |pmid= 14757427 |doi= }}
*{{cite journal | author=Robson KJ, Merryweather-Clarke AT, Cadet E, ''et al.'' |title=Recent advances in understanding haemochromatosis: a transition state. |journal=J. Med. Genet. |volume=41 |issue= 10 |pages= 721-30 |year= 2005 |pmid= 15466004 |doi= 10.1136/jmg.2004.020644 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Donovan A, Brownlie A, Zhou Y, ''et al.'' |title=Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. |journal=Nature |volume=403 |issue= 6771 |pages= 776-81 |year= 2000 |pmid= 10693807 |doi= 10.1038/35001596 }}
*{{cite journal | author=Abboud S, Haile DJ |title=A novel mammalian iron-regulated protein involved in intracellular iron metabolism. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19906-12 |year= 2000 |pmid= 10747949 |doi= 10.1074/jbc.M000713200 }}
*{{cite journal | author=Haile DJ |title=Assignment of Slc11a3 to mouse chromosome 1 band 1B and SLC11A3 to human chromosome 2q32 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 3-4 |pages= 328-9 |year= 2000 |pmid= 10828623 |doi= }}
*{{cite journal | author=McKie AT, Marciani P, Rolfs A, ''et al.'' |title=A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation. |journal=Mol. Cell |volume=5 |issue= 2 |pages= 299-309 |year= 2000 |pmid= 10882071 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Njajou OT, Vaessen N, Joosse M, ''et al.'' |title=A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis. |journal=Nat. Genet. |volume=28 |issue= 3 |pages= 213-4 |year= 2001 |pmid= 11431687 |doi= 10.1038/90038 }}
*{{cite journal | author=Montosi G, Donovan A, Totaro A, ''et al.'' |title=Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene. |journal=J. Clin. Invest. |volume=108 |issue= 4 |pages= 619-23 |year= 2001 |pmid= 11518736 |doi= }}
*{{cite journal | author=Press RD |title=Hemochromatosis caused by mutations in the iron-regulatory proteins ferroportin and H ferritin. |journal=Mol. Diagn. |volume=6 |issue= 4 |pages= 347 |year= 2002 |pmid= 11774199 |doi= }}
*{{cite journal | author=Lee PL, Gelbart T, West C, ''et al.'' |title=A study of genes that may modulate the expression of hereditary hemochromatosis: transferrin receptor-1, ferroportin, ceruloplasmin, ferritin light and heavy chains, iron regulatory proteins (IRP)-1 and -2, and hepcidin. |journal=Blood Cells Mol. Dis. |volume=27 |issue= 5 |pages= 783-802 |year= 2003 |pmid= 11783942 |doi= 10.1006/bcmd.2001.0445 }}
*{{cite journal | author=Rolfs A, Bonkovsky HL, Kohlroser JG, ''et al.'' |title=Intestinal expression of genes involved in iron absorption in humans. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=282 |issue= 4 |pages= G598-607 |year= 2002 |pmid= 11897618 |doi= 10.1152/ajpgi.00371.2001 }}
*{{cite journal | author=Thomas C, Oates PS |title=IEC-6 cells are an appropriate model of intestinal iron absorption in rats. |journal=J. Nutr. |volume=132 |issue= 4 |pages= 680-7 |year= 2002 |pmid= 11925460 |doi= }}
*{{cite journal | author=Wallace DF, Pedersen P, Dixon JL, ''et al.'' |title=Novel mutation in ferroportin1 is associated with autosomal dominant hemochromatosis. |journal=Blood |volume=100 |issue= 2 |pages= 692-4 |year= 2002 |pmid= 12091366 |doi= }}
*{{cite journal | author=Devalia V, Carter K, Walker AP, ''et al.'' |title=Autosomal dominant reticuloendothelial iron overload associated with a 3-base pair deletion in the ferroportin 1 gene (SLC11A3). |journal=Blood |volume=100 |issue= 2 |pages= 695-7 |year= 2002 |pmid= 12091367 |doi= 10.1182/blood-2001-11-0132 }}
*{{cite journal | author=Roetto A, Merryweather-Clarke AT, Daraio F, ''et al.'' |title=A valine deletion of ferroportin 1: a common mutation in hemochromastosis type 4. |journal=Blood |volume=100 |issue= 2 |pages= 733-4 |year= 2002 |pmid= 12123233 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SPTB... {November 16, 2007 4:52:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:52:49 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SPTB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1s35.
| PDB = {{PDB2|1s35}}
| Name = Spectrin, beta, erythrocytic (includes spherocytosis, clinical type I)
| HGNCid = 11274
| Symbol = SPTB
| AltSymbols =; HSpTB1
| OMIM = 182870
| ECnumber =
| Homologene = 295
| MGIid = 98387
| GeneAtlas_image1 = PBB_GE_SPTB_208416_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SPTB_214145_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0008091 |text = spectrin}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6710
| Hs_Ensembl = ENSG00000070182
| Hs_RefseqProtein = NP_000338
| Hs_RefseqmRNA = NM_000347
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 64284778
| Hs_GenLoc_end = 64416354
| Hs_Uniprot = P11277
| Mm_EntrezGene = 20741
| Mm_Ensembl = ENSMUSG00000021061
| Mm_RefseqmRNA = NM_013675
| Mm_RefseqProtein = NP_038703
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 77499328
| Mm_GenLoc_end = 77629387
| Mm_Uniprot = Q149M1
}}
}}
'''Spectrin, beta, erythrocytic (includes spherocytosis, clinical type I)''', also known as '''SPTB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPTB spectrin, beta, erythrocytic (includes spherocytosis, clinical type I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6710| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bennett V, Baines AJ |title=Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. |journal=Physiol. Rev. |volume=81 |issue= 3 |pages= 1353-92 |year= 2001 |pmid= 11427698 |doi= }}
*{{cite journal | author=Kanzaki A, Rabodonirina M, Yawata Y, ''et al.'' |title=A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216). |journal=Blood |volume=80 |issue= 8 |pages= 2115-21 |year= 1992 |pmid= 1391962 |doi= }}
*{{cite journal | author=Speicher DW, Weglarz L, DeSilva TM |title=Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. |journal=J. Biol. Chem. |volume=267 |issue= 21 |pages= 14775-82 |year= 1992 |pmid= 1634521 |doi= }}
*{{cite journal | author=Gallagher PG, Tse WT, Costa F, ''et al.'' |title=A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15154-9 |year= 1991 |pmid= 1840591 |doi= }}
*{{cite journal | author=Tse WT, Lecomte MC, Costa FF, ''et al.'' |title=Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association. |journal=J. Clin. Invest. |volume=86 |issue= 3 |pages= 909-16 |year= 1990 |pmid= 1975598 |doi= }}
*{{cite journal | author=Yoon SH, Kentros CG, Prchal JT |title=Identification of an unusual deletion within homologous repeats of human reticulocyte beta-spectrin and probable peptide polymorphism. |journal=Gene |volume=91 |issue= 2 |pages= 297-302 |year= 1990 |pmid= 1976574 |doi= }}
*{{cite journal | author=Garbarz M, Tse WT, Gallagher PG, ''et al.'' |title=Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation. |journal=J. Clin. Invest. |volume=88 |issue= 1 |pages= 76-81 |year= 1991 |pmid= 2056132 |doi= }}
*{{cite journal | author=Tse WT, Gallagher PG, Pothier B, ''et al.'' |title=An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216). |journal=Blood |volume=78 |issue= 2 |pages= 517-23 |year= 1991 |pmid= 2070088 |doi= }}
*{{cite journal | author=Winkelmann JC, Chang JG, Tse WT, ''et al.'' |title=Full-length sequence of the cDNA for human erythroid beta-spectrin. |journal=J. Biol. Chem. |volume=265 |issue= 20 |pages= 11827-32 |year= 1990 |pmid= 2195026 |doi= }}
*{{cite journal | author=Fukushima Y, Byers MG, Watkins PC, ''et al.'' |title=Assignment of the gene for beta-spectrin (SPTB) to chromosome 14q23----q24.2 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 232-3 |year= 1990 |pmid= 2209094 |doi= }}
*{{cite journal | author=Winkelmann JC, Costa FF, Linzie BL, Forget BG |title=Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus. |journal=J. Biol. Chem. |volume=265 |issue= 33 |pages= 20449-54 |year= 1990 |pmid= 2243099 |doi= }}
*{{cite journal | author=Coetzer T, Palek J, Lawler J, ''et al.'' |title=Structural and functional heterogeneity of alpha spectrin mutations involving the spectrin heterodimer self-association site: relationships to hematologic expression of homozygous hereditary elliptocytosis and hereditary pyropoikilocytosis. |journal=Blood |volume=75 |issue= 11 |pages= 2235-44 |year= 1990 |pmid= 2346784 |doi= }}
*{{cite journal | author=Winkelmann JC, Leto TL, Watkins PC, ''et al.'' |title=Molecular cloning of the cDNA for human erythrocyte beta-spectrin. |journal=Blood |volume=72 |issue= 1 |pages= 328-34 |year= 1988 |pmid= 3390609 |doi= }}
*{{cite journal | author=Prchal JT, Morley BJ, Yoon SH, ''et al.'' |title=Isolation and characterization of cDNA clones for human erythrocyte beta-spectrin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7468-72 |year= 1987 |pmid= 3478706 |doi= }}
*{{cite journal | author=Pothier B, Morlé L, Alloisio N, ''et al.'' |title=Spectrin Nice (beta 220/216): a shortened beta-chain variant associated with an increase of the alpha I/74 fragment in a case of elliptocytosis. |journal=Blood |volume=69 |issue= 6 |pages= 1759-65 |year= 1987 |pmid= 3580577 |doi= }}
*{{cite journal | author=Wolfe LC, John KM, Falcone JC, ''et al.'' |title=A genetic defect in the binding of protein 4.1 to spectrin in a kindred with hereditary spherocytosis. |journal=N. Engl. J. Med. |volume=307 |issue= 22 |pages= 1367-74 |year= 1982 |pmid= 6215583 |doi= }}
*{{cite journal | author=Speicher DW, Marchesi VT |title=Erythrocyte spectrin is comprised of many homologous triple helical segments. |journal=Nature |volume=311 |issue= 5982 |pages= 177-80 |year= 1984 |pmid= 6472478 |doi= }}
*{{cite journal | author=Carlier MF, Simon C, Cassoly R, Pradel LA |title=Interaction between microtubule-associated protein tau and spectrin. |journal=Biochimie |volume=66 |issue= 4 |pages= 305-11 |year= 1984 |pmid= 6743699 |doi= }}
*{{cite journal | author=Goodman SR, Shiffer KA, Casoria LA, Eyster ME |title=Identification of the molecular defect in the erythrocyte membrane skeleton of some kindreds with hereditary spherocytosis. |journal=Blood |volume=60 |issue= 3 |pages= 772-84 |year= 1982 |pmid= 7104494 |doi= }}
*{{cite journal | author=Schischmanoff PO, Winardi R, Discher DE, ''et al.'' |title=Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding. |journal=J. Biol. Chem. |volume=270 |issue= 36 |pages= 21243-50 |year= 1995 |pmid= 7673158 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TBXA2R... {November 16, 2007 4:52:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:53:12 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Thromboxane A2 receptor
| HGNCid = 11608
| Symbol = TBXA2R
| AltSymbols =; TXA2-R
| OMIM = 188070
| ECnumber =
| Homologene = 825
| MGIid = 98496
| GeneAtlas_image1 = PBB_GE_TBXA2R_336_at_tn.png
| GeneAtlas_image2 = PBB_GE_TBXA2R_207554_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TBXA2R_211590_x_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004960 |text = thromboxane receptor activity}} {{GNF_GO|id=GO:0004961 |text = thromboxane A2 receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6915
| Hs_Ensembl = ENSG00000006638
| Hs_RefseqProtein = NP_001051
| Hs_RefseqmRNA = NM_001060
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 3545778
| Hs_GenLoc_end = 3557658
| Hs_Uniprot = P21731
| Mm_EntrezGene = 21390
| Mm_Ensembl = ENSMUSG00000034881
| Mm_RefseqmRNA = NM_009325
| Mm_RefseqProtein = NP_033351
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 80731957
| Mm_GenLoc_end = 80738300
| Mm_Uniprot = Q5FW61
}}
}}
'''Thromboxane A2 receptor''', also known as '''TBXA2R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TBXA2R thromboxane A2 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6915| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Namba T, Narumiya S |title=[Thromboxane A2 receptor; structure, function and tissue distribution] |journal=Nippon Rinsho |volume=51 |issue= 1 |pages= 233-40 |year= 1993 |pmid= 8433523 |doi= }}
*{{cite journal | author=Murugappan S, Shankar H, Kunapuli SP |title=Platelet receptors for adenine nucleotides and thromboxane A2. |journal=Semin. Thromb. Hemost. |volume=30 |issue= 4 |pages= 411-8 |year= 2005 |pmid= 15354262 |doi= 10.1055/s-2004-833476 }}
*{{cite journal | author=Hirata M, Hayashi Y, Ushikubi F, ''et al.'' |title=Cloning and expression of cDNA for a human thromboxane A2 receptor. |journal=Nature |volume=349 |issue= 6310 |pages= 617-20 |year= 1991 |pmid= 1825698 |doi= 10.1038/349617a0 }}
*{{cite journal | author=Raychowdhury MK, Yukawa M, Collins LJ, ''et al.'' |title=Alternative splicing produces a divergent cytoplasmic tail in the human endothelial thromboxane A2 receptor. |journal=J. Biol. Chem. |volume=270 |issue= 12 |pages= 7011 |year= 1995 |pmid= 7896853 |doi= }}
*{{cite journal | author=Hirata T, Kakizuka A, Ushikubi F, ''et al.'' |title=Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly inherited bleeding disorder. |journal=J. Clin. Invest. |volume=94 |issue= 4 |pages= 1662-7 |year= 1994 |pmid= 7929844 |doi= }}
*{{cite journal | author=D'Angelo DD, Davis MG, Ali S, Dorn GW |title=Cloning and pharmacologic characterization of a thromboxane A2 receptor from K562 (human chronic myelogenous leukemia) cells. |journal=J. Pharmacol. Exp. Ther. |volume=271 |issue= 2 |pages= 1034-41 |year= 1994 |pmid= 7965765 |doi= }}
*{{cite journal | author=Raychowdhury MK, Yukawa M, Collins LJ, ''et al.'' |title=Alternative splicing produces a divergent cytoplasmic tail in the human endothelial thromboxane A2 receptor. |journal=J. Biol. Chem. |volume=269 |issue= 30 |pages= 19256-61 |year= 1994 |pmid= 8034687 |doi= }}
*{{cite journal | author=Borg C, Lim CT, Yeomans DC, ''et al.'' |title=Purification of rat brain, rabbit aorta, and human platelet thromboxane A2/prostaglandin H2 receptors by immunoaffinity chromatography employing anti-peptide and anti-receptor antibodies. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 6109-16 |year= 1994 |pmid= 8119956 |doi= }}
*{{cite journal | author=Nüsing RM, Hirata M, Kakizuka A, ''et al.'' |title=Characterization and chromosomal mapping of the human thromboxane A2 receptor gene. |journal=J. Biol. Chem. |volume=268 |issue= 33 |pages= 25253-9 |year= 1993 |pmid= 8227091 |doi= }}
*{{cite journal | author=Funk CD, Furci L, Moran N, Fitzgerald GA |title=Point mutation in the seventh hydrophobic domain of the human thromboxane A2 receptor allows discrimination between agonist and antagonist binding sites. |journal=Mol. Pharmacol. |volume=44 |issue= 5 |pages= 934-9 |year= 1994 |pmid= 8246916 |doi= }}
*{{cite journal | author=Schwengel DA, Nouri N, Meyers DA, Levitt RC |title=Linkage mapping of the human thromboxane A2 receptor (TBXA2R) to chromosome 19p13.3 using transcribed 3' untranslated DNA sequence polymorphisms. |journal=Genomics |volume=18 |issue= 2 |pages= 212-5 |year= 1994 |pmid= 8288221 |doi= 10.1006/geno.1993.1457 }}
*{{cite journal | author=Offermanns S, Laugwitz KL, Spicher K, Schultz G |title=G proteins of the G12 family are activated via thromboxane A2 and thrombin receptors in human platelets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 2 |pages= 504-8 |year= 1994 |pmid= 8290554 |doi= }}
*{{cite journal | author=Hirata T, Ushikubi F, Kakizuka A, ''et al.'' |title=Two thromboxane A2 receptor isoforms in human platelets. Opposite coupling to adenylyl cyclase with different sensitivity to Arg60 to Leu mutation. |journal=J. Clin. Invest. |volume=97 |issue= 4 |pages= 949-56 |year= 1996 |pmid= 8613548 |doi= }}
*{{cite journal | author=Kinsella BT, O'Mahony DJ, Fitzgerald GA |title=The human thromboxane A2 receptor alpha isoform (TP alpha) functionally couples to the G proteins Gq and G11 in vivo and is activated by the isoprostane 8-epi prostaglandin F2 alpha. |journal=J. Pharmacol. Exp. Ther. |volume=281 |issue= 2 |pages= 957-64 |year= 1997 |pmid= 9152406 |doi= }}
*{{cite journal | author=Becker KP, Garnovskaya M, Gettys T, Halushka PV |title=Coupling of thromboxane A2 receptor isoforms to Galpha13: effects on ligand binding and signalling. |journal=Biochim. Biophys. Acta |volume=1450 |issue= 3 |pages= 288-96 |year= 1999 |pmid= 10395940 |doi= }}
*{{cite journal | author=Barr CL, Wigg KG, Pakstis AJ, ''et al.'' |title=Genome scan for linkage to Gilles de la Tourette syndrome. |journal=Am. J. Med. Genet. |volume=88 |issue= 4 |pages= 437-45 |year= 1999 |pmid= 10402514 |doi= }}
*{{cite journal | author=Zhou H, Yan F, Tai HH |title=Phosphorylation and desensitization of the human thromboxane receptor-alpha by G protein-coupled receptor kinases. |journal=J. Pharmacol. Exp. Ther. |volume=298 |issue= 3 |pages= 1243-51 |year= 2001 |pmid= 11504827 |doi= }}
*{{cite journal | author=Vezza R, Mezzasoma AM, Venditti G, Gresele P |title=Prostaglandin endoperoxides and thromboxane A2 activate the same receptor isoforms in human platelets. |journal=Thromb. Haemost. |volume=87 |issue= 1 |pages= 114-21 |year= 2002 |pmid= 11848439 |doi= }}
*{{cite journal | author=Turek JW, Halmos T, Sullivan NL, ''et al.'' |title=Mapping of a ligand-binding site for the human thromboxane A2 receptor protein. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16791-7 |year= 2002 |pmid= 11877412 |doi= 10.1074/jbc.M105872200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on U2AF2... {November 16, 2007 4:56:01 PM PST}
- SEARCH REDIRECT: Control Box Found: U2AF2 {November 16, 2007 4:56:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:56:33 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:56:33 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:56:33 PM PST}
- UPDATED: Updated protein page: U2AF2 {November 16, 2007 4:56:39 PM PST}
- INFO: Beginning work on UBE3A... {November 16, 2007 4:53:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:54:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_UBE3A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c4z.
| PDB = {{PDB2|1c4z}}, {{PDB2|1d5f}}
| Name = Ubiquitin protein ligase E3A (human papilloma virus E6-associated protein, Angelman syndrome)
| HGNCid = 12496
| Symbol = UBE3A
| AltSymbols =; ANCR; AS; E6-AP; EPVE6AP; FLJ26981; HPVE6A
| OMIM = 601623
| ECnumber =
| Homologene = 7988
| MGIid = 105098
| GeneAtlas_image1 = PBB_GE_UBE3A_211285_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE3A_211575_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_UBE3A_213128_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007420 |text = brain development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7337
| Hs_Ensembl = ENSG00000114062
| Hs_RefseqProtein = NP_000453
| Hs_RefseqmRNA = NM_000462
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 23133489
| Hs_GenLoc_end = 23235221
| Hs_Uniprot = Q05086
| Mm_EntrezGene = 22215
| Mm_Ensembl = ENSMUSG00000025326
| Mm_RefseqmRNA = NM_001033962
| Mm_RefseqProtein = NP_001029134
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 59096621
| Mm_GenLoc_end = 59174596
| Mm_Uniprot = Q3TPQ9
}}
}}
'''Ubiquitin protein ligase E3A (human papilloma virus E6-associated protein, Angelman syndrome)''', also known as '''UBE3A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE3A ubiquitin protein ligase E3A (human papilloma virus E6-associated protein, Angelman syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7337| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an E3 ubiquitin-protein ligase, part of the ubiquitin protein degradation system. This imprinted gene is maternally expressed in brain and biallelically expressed in other tissues. Maternally inherited deletion of this gene causes Angelman Syndrome, characterized by severe motor and intellectual retardation, ataxia, hypotonia, epilepsy, absence of speech, and characteristic facies. The protein also interacts with the E6 protein of human papillomavirus types 16 and 18, resulting in ubiquitination and proteolysis of tumor protein p53. Alternative splicing of this gene results in three transcript variants encoding three isoforms with different N-termini. Additional transcript variants have been described, but their full length nature has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: UBE3A ubiquitin protein ligase E3A (human papilloma virus E6-associated protein, Angelman syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7337| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Scheffner M, Huibregtse JM, Vierstra RD, Howley PM |title=The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. |journal=Cell |volume=75 |issue= 3 |pages= 495-505 |year= 1993 |pmid= 8221889 |doi= }}
*{{cite journal | author=Huibregtse JM, Scheffner M, Howley PM |title=Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53. |journal=Mol. Cell. Biol. |volume=13 |issue= 2 |pages= 775-84 |year= 1993 |pmid= 8380895 |doi= }}
*{{cite journal | author=Nuber U, Schwarz S, Kaiser P, ''et al.'' |title=Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2795-800 |year= 1996 |pmid= 8576257 |doi= }}
*{{cite journal | author=Kishino T, Lalande M, Wagstaff J |title=UBE3A/E6-AP mutations cause Angelman syndrome. |journal=Nat. Genet. |volume=15 |issue= 1 |pages= 70-3 |year= 1997 |pmid= 8988171 |doi= 10.1038/ng0197-70 }}
*{{cite journal | author=Matsuura T, Sutcliffe JS, Fang P, ''et al.'' |title=De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome. |journal=Nat. Genet. |volume=15 |issue= 1 |pages= 74-7 |year= 1997 |pmid= 8988172 |doi= 10.1038/ng0197-74 }}
*{{cite journal | author=Yamamoto Y, Huibregtse JM, Howley PM |title=The human E6-AP gene (UBE3A) encodes three potential protein isoforms generated by differential splicing. |journal=Genomics |volume=41 |issue= 2 |pages= 263-6 |year= 1997 |pmid= 9143503 |doi= 10.1006/geno.1997.4617 }}
*{{cite journal | author=Kumar S, Kao WH, Howley PM |title=Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13548-54 |year= 1997 |pmid= 9153201 |doi= }}
*{{cite journal | author=Vu TH, Hoffman AR |title=Imprinting of the Angelman syndrome gene, UBE3A, is restricted to brain. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 12-3 |year= 1997 |pmid= 9288087 |doi= 10.1038/ng0997-12 }}
*{{cite journal | author=Rougeulle C, Glatt H, Lalande M |title=The Angelman syndrome candidate gene, UBE3A/E6-AP, is imprinted in brain. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 14-5 |year= 1997 |pmid= 9288088 |doi= 10.1038/ng0997-14 }}
*{{cite journal | author=Daniels PR, Sanders CM, Coulson P, Maitland NJ |title=Molecular analysis of the interaction between HPV type 16 E6 and human E6-associated protein. |journal=FEBS Lett. |volume=416 |issue= 1 |pages= 6-10 |year= 1997 |pmid= 9369221 |doi= }}
*{{cite journal | author=Kishino T, Wagstaff J |title=Genomic organization of the UBE3A/E6-AP gene and related pseudogenes. |journal=Genomics |volume=47 |issue= 1 |pages= 101-7 |year= 1998 |pmid= 9465301 |doi= 10.1006/geno.1997.5093 }}
*{{cite journal | author=Malzac P, Webber H, Moncla A, ''et al.'' |title=Mutation analysis of UBE3A in Angelman syndrome patients. |journal=Am. J. Hum. Genet. |volume=62 |issue= 6 |pages= 1353-60 |year= 1998 |pmid= 9585605 |doi= }}
*{{cite journal | author=Nuber U, Schwarz SE, Scheffner M |title=The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate. |journal=Eur. J. Biochem. |volume=254 |issue= 3 |pages= 643-9 |year= 1998 |pmid= 9688277 |doi= }}
*{{cite journal | author=Tsai TF, Raas-Rothschild A, Ben-Neriah Z, Beaudet AL |title=Prenatal diagnosis and carrier detection for a point mutation in UBE3A causing Angelman syndrome. |journal=Am. J. Hum. Genet. |volume=63 |issue= 5 |pages= 1561-3 |year= 1998 |pmid= 9792887 |doi= }}
*{{cite journal | author=Kühne C, Banks L |title=E3-ubiquitin ligase/E6-AP links multicopy maintenance protein 7 to the ubiquitination pathway by a novel motif, the L2G box. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34302-9 |year= 1999 |pmid= 9852095 |doi= }}
*{{cite journal | author=Nawaz Z, Lonard DM, Smith CL, ''et al.'' |title=The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily. |journal=Mol. Cell. Biol. |volume=19 |issue= 2 |pages= 1182-9 |year= 1999 |pmid= 9891052 |doi= }}
*{{cite journal | author=Anan T, Nagata Y, Koga H, ''et al.'' |title=Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes. |journal=Genes Cells |volume=3 |issue= 11 |pages= 751-63 |year= 1999 |pmid= 9990509 |doi= }}
*{{cite journal | author=Nuber U, Scheffner M |title=Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. |journal=J. Biol. Chem. |volume=274 |issue= 11 |pages= 7576-82 |year= 1999 |pmid= 10066826 |doi= }}
*{{cite journal | author=Oda H, Kumar S, Howley PM |title=Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 17 |pages= 9557-62 |year= 1999 |pmid= 10449731 |doi= }}
*{{cite journal | author=Scanlan MJ, Gordan JD, Williamson B, ''et al.'' |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma. |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456-64 |year= 1999 |pmid= 10508479 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ZFP36... {November 16, 2007 4:54:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:55:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ZFP36_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m9o.
| PDB = {{PDB2|1m9o}}
| Name = Zinc finger protein 36, C3H type, homolog (mouse)
| HGNCid = 12862
| Symbol = ZFP36
| AltSymbols =; G0S24; GOS24; NUP475; RNF162A; TIS11; TTP
| OMIM = 190700
| ECnumber =
| Homologene = 2558
| MGIid = 99180
| GeneAtlas_image1 = PBB_GE_ZFP36_201531_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003727 |text = single-stranded RNA binding}} {{GNF_GO|id=GO:0003729 |text = mRNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006402 |text = mRNA catabolic process}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}} {{GNF_GO|id=GO:0043488 |text = regulation of mRNA stability}} {{GNF_GO|id=GO:0045638 |text = negative regulation of myeloid cell differentiation}} {{GNF_GO|id=GO:0050728 |text = negative regulation of inflammatory response}} {{GNF_GO|id=GO:0050779 |text = RNA destabilization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7538
| Hs_Ensembl = ENSG00000128016
| Hs_RefseqProtein = NP_003398
| Hs_RefseqmRNA = NM_003407
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 44589293
| Hs_GenLoc_end = 44591853
| Hs_Uniprot = P26651
| Mm_EntrezGene = 22695
| Mm_Ensembl = ENSMUSG00000044786
| Mm_RefseqmRNA = NM_011756
| Mm_RefseqProtein = NP_035886
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 28085544
| Mm_GenLoc_end = 28087988
| Mm_Uniprot = Q3TW34
}}
}}
'''Zinc finger protein 36, C3H type, homolog (mouse)''', also known as '''ZFP36''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ZFP36 zinc finger protein 36, C3H type, homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7538| accessdate = }}</ref>
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{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Blackshear PJ |title=Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover. |journal=Biochem. Soc. Trans. |volume=30 |issue= Pt 6 |pages= 945-52 |year= 2003 |pmid= 12440952 |doi= 10.1042/ }}
*{{cite journal | author=Carrick DM, Lai WS, Blackshear PJ |title=The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis. |journal=Arthritis Res. Ther. |volume=6 |issue= 6 |pages= 248-64 |year= 2005 |pmid= 15535838 |doi= 10.1186/ar1441 }}
*{{cite journal | author=Makar AB, McMartin KE, Palese M, Tephly TR |title=Formate assay in body fluids: application in methanol poisoning. |journal=Biochemical medicine |volume=13 |issue= 2 |pages= 117-26 |year= 1976 |pmid= 1 |doi= }}
*{{cite journal | author=DuBois RN, McLane MW, Ryder K, ''et al.'' |title=A growth factor-inducible nuclear protein with a novel cysteine/histidine repetitive sequence. |journal=J. Biol. Chem. |volume=265 |issue= 31 |pages= 19185-91 |year= 1990 |pmid= 1699942 |doi= }}
*{{cite journal | author=Taylor GA, Lai WS, Oakey RJ, ''et al.'' |title=The human TTP protein: sequence, alignment with related proteins, and chromosomal localization of the mouse and human genes. |journal=Nucleic Acids Res. |volume=19 |issue= 12 |pages= 3454 |year= 1991 |pmid= 2062660 |doi= }}
*{{cite journal | author=Lai WS, Stumpo DJ, Blackshear PJ |title=Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein. |journal=J. Biol. Chem. |volume=265 |issue= 27 |pages= 16556-63 |year= 1990 |pmid= 2204625 |doi= }}
*{{cite journal | author=Taylor GA, Thompson MJ, Lai WS, Blackshear PJ |title=Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13341-7 |year= 1995 |pmid= 7768935 |doi= }}
*{{cite journal | author=Heximer SP, Forsdyke DR |title=A human putative lymphocyte G0/G1 switch gene homologous to a rodent gene encoding a zinc-binding potential transcription factor. |journal=DNA Cell Biol. |volume=12 |issue= 1 |pages= 73-88 |year= 1993 |pmid= 8422274 |doi= }}
*{{cite journal | author=Huebner K, Druck T, LaForgia S, ''et al.'' |title=Chromosomal localization of four human zinc finger cDNAs. |journal=Hum. Genet. |volume=91 |issue= 3 |pages= 217-22 |year= 1993 |pmid= 8478004 |doi= }}
*{{cite journal | author=Carballo E, Lai WS, Blackshear PJ |title=Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. |journal=Science |volume=281 |issue= 5379 |pages= 1001-5 |year= 1998 |pmid= 9703499 |doi= }}
*{{cite journal | author=Lai WS, Carballo E, Thorn JM, ''et al.'' |title=Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA. |journal=J. Biol. Chem. |volume=275 |issue= 23 |pages= 17827-37 |year= 2000 |pmid= 10751406 |doi= 10.1074/jbc.M001696200 }}
*{{cite journal | author=Dintilhac A, Bernués J |title=HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7021-8 |year= 2002 |pmid= 11748221 |doi= 10.1074/jbc.M108417200 }}
*{{cite journal | author=Lai WS, Kennington EA, Blackshear PJ |title=Interactions of CCCH zinc finger proteins with mRNA: non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9606-13 |year= 2002 |pmid= 11782475 |doi= 10.1074/jbc.M110395200 }}
*{{cite journal | author=Johnson BA, Stehn JR, Yaffe MB, Blackwell TK |title=Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 18029-36 |year= 2002 |pmid= 11886850 |doi= 10.1074/jbc.M110465200 }}
*{{cite journal | author=Brooks SA, Connolly JE, Diegel RJ, ''et al.'' |title=Analysis of the function, expression, and subcellular distribution of human tristetraprolin. |journal=Arthritis Rheum. |volume=46 |issue= 5 |pages= 1362-70 |year= 2002 |pmid= 12115244 |doi= 10.1002/art.10235 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Amann BT, Worthington MT, Berg JM |title=A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure. |journal=Biochemistry |volume=42 |issue= 1 |pages= 217-21 |year= 2003 |pmid= 12515557 |doi= 10.1021/bi026988m }}
*{{cite journal | author=Yu H, Stasinopoulos S, Leedman P, Medcalf RL |title=Inherent instability of plasminogen activator inhibitor type 2 mRNA is regulated by tristetraprolin. |journal=J. Biol. Chem. |volume=278 |issue= 16 |pages= 13912-8 |year= 2003 |pmid= 12578825 |doi= 10.1074/jbc.M213027200 }}
*{{cite journal | author=Sawaoka H, Dixon DA, Oates JA, Boutaud O |title=Tristetraprolin binds to the 3'-untranslated region of cyclooxygenase-2 mRNA. A polyadenylation variant in a cancer cell line lacks the binding site. |journal=J. Biol. Chem. |volume=278 |issue= 16 |pages= 13928-35 |year= 2003 |pmid= 12578839 |doi= 10.1074/jbc.M300016200 }}
}}
{{refend}}
{{protein-stub}}
end log.
