Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 06:43, 19 November 2007 (UTC)[edit]
Proteins without matches (11)[edit]
Proteins with a High Potential Match (8)[edit]
Redirected Proteins (6)[edit]
Manual Inspection (Page not found) (19)[edit]
Updated (6)[edit]
Protein Status Grid - Date: 06:43, 19 November 2007 (UTC)[edit]
Vebose Log - Date: 06:43, 19 November 2007 (UTC)[edit]
- INFO: Beginning work on BTG2... {November 18, 2007 10:32:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:33:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = 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 = BTG family, member 2
| HGNCid = 1131
| Symbol = BTG2
| AltSymbols =; PC3; MGC126063; MGC126064; TIS21
| OMIM = 601597
| ECnumber =
| Homologene = 31406
| MGIid = 108384
| GeneAtlas_image1 = PBB_GE_BTG2_201236_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BTG2_201235_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006479 |text = protein amino acid methylation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009952 |text = anterior/posterior pattern formation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7832
| Hs_Ensembl = ENSG00000159388
| Hs_RefseqProtein = NP_006754
| Hs_RefseqmRNA = NM_006763
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 201541242
| Hs_GenLoc_end = 201545353
| Hs_Uniprot = P78543
| Mm_EntrezGene = 12227
| Mm_Ensembl = ENSMUSG00000020423
| Mm_RefseqmRNA = NM_007570
| Mm_RefseqProtein = NP_031596
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 135891276
| Mm_GenLoc_end = 135895566
| Mm_Uniprot = Q3TF68
}}
}}
'''BTG family, member 2''', also known as '''BTG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BTG2 BTG family, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7832| 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 member of the BTG/Tob family. This family has structurally related proteins that appear to have antiproliferative properties. This encoded protein is involved in the regulation of the G1/S transition of the cell cycle.<ref name="entrez">{{cite web | title = Entrez Gene: BTG2 BTG family, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7832| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Puisieux A, Magaud JP |title=[Mechanisms of BTG2 activity, a transcriptional target of p53: evidences and hypothesis.] |journal=Bulletin du cancer |volume=86 |issue= 4 |pages= 358-64 |year= 1999 |pmid= 10341341 |doi= }}
*{{cite journal | author=Tirone F |title=The gene PC3(TIS21/BTG2), prototype member of the PC3/BTG/TOB family: regulator in control of cell growth, differentiation, and DNA repair? |journal=J. Cell. Physiol. |volume=187 |issue= 2 |pages= 155-65 |year= 2001 |pmid= 11267995 |doi= 10.1002/jcp.1062 }}
*{{cite journal | author=Matsuda S, Rouault J, Magaud J, Berthet C |title=In search of a function for the TIS21/PC3/BTG1/TOB family. |journal=FEBS Lett. |volume=497 |issue= 2-3 |pages= 67-72 |year= 2001 |pmid= 11377414 |doi= }}
*{{cite journal | author=Fletcher BS, Lim RW, Varnum BC, ''et al.'' |title=Structure and expression of TIS21, a primary response gene induced by growth factors and tumor promoters. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14511-8 |year= 1991 |pmid= 1713584 |doi= }}
*{{cite journal | author=Lin WJ, Gary JD, Yang MC, ''et al.'' |title=The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15034-44 |year= 1996 |pmid= 8663146 |doi= }}
*{{cite journal | author=Montagnoli A, Guardavaccaro D, Starace G, Tirone F |title=Overexpression of the nerve growth factor-inducible PC3 immediate early gene is associated with growth inhibition. |journal=Cell Growth Differ. |volume=7 |issue= 10 |pages= 1327-36 |year= 1997 |pmid= 8891336 |doi= }}
*{{cite journal | author=Rouault JP, Falette N, Guéhenneux F, ''et al.'' |title=Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway. |journal=Nat. Genet. |volume=14 |issue= 4 |pages= 482-6 |year= 1997 |pmid= 8944033 |doi= 10.1038/ng1296-482 }}
*{{cite journal | author=Rouault JP, Prévôt D, Berthet C, ''et al.'' |title=Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22563-9 |year= 1998 |pmid= 9712883 |doi= }}
*{{cite journal | author=Walden PD, Lefkowitz GK, Ficazzola M, ''et al.'' |title=Identification of genes associated with stromal hyperplasia and glandular atrophy of the prostate by mRNA differential display. |journal=Exp. Cell Res. |volume=245 |issue= 1 |pages= 19-26 |year= 1999 |pmid= 9828097 |doi= 10.1006/excr.1998.4237 }}
*{{cite journal | author=Iacopetti P, Michelini M, Stuckmann I, ''et al.'' |title=Expression of the antiproliferative gene TIS21 at the onset of neurogenesis identifies single neuroepithelial cells that switch from proliferative to neuron-generating division. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 8 |pages= 4639-44 |year= 1999 |pmid= 10200315 |doi= }}
*{{cite journal | author=Prévôt D, Voeltzel T, Birot AM, ''et al.'' |title=The leukemia-associated protein Btg1 and the p53-regulated protein Btg2 interact with the homeoprotein Hoxb9 and enhance its transcriptional activation. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 147-53 |year= 2000 |pmid= 10617598 |doi= }}
*{{cite journal | author=Guardavaccaro D, Corrente G, Covone F, ''et al.'' |title=Arrest of G(1)-S progression by the p53-inducible gene PC3 is Rb dependent and relies on the inhibition of cyclin D1 transcription. |journal=Mol. Cell. Biol. |volume=20 |issue= 5 |pages= 1797-815 |year= 2000 |pmid= 10669755 |doi= }}
*{{cite journal | author=Prévôt D, Morel AP, Voeltzel T, ''et al.'' |title=Relationships of the antiproliferative proteins BTG1 and BTG2 with CAF1, the human homolog of a component of the yeast CCR4 transcriptional complex: involvement in estrogen receptor alpha signaling pathway. |journal=J. Biol. Chem. |volume=276 |issue= 13 |pages= 9640-8 |year= 2001 |pmid= 11136725 |doi= 10.1074/jbc.M008201200 }}
*{{cite journal | author=Lin WJ, Chang YF, Wang WL, Huang CY |title=Mitogen-stimulated TIS21 protein interacts with a protein-kinase-Calpha-binding protein rPICK1. |journal=Biochem. J. |volume=354 |issue= Pt 3 |pages= 635-43 |year= 2001 |pmid= 11237868 |doi= }}
*{{cite journal | author=Yoshida Y, Hosoda E, Nakamura T, Yamamoto T |title=Association of ANA, a member of the antiproliferative Tob family proteins, with a Caf1 component of the CCR4 transcriptional regulatory complex. |journal=Jpn. J. Cancer Res. |volume=92 |issue= 6 |pages= 592-6 |year= 2001 |pmid= 11429045 |doi= }}
*{{cite journal | author=Ficazzola MA, Fraiman M, Gitlin J, ''et al.'' |title=Antiproliferative B cell translocation gene 2 protein is down-regulated post-transcriptionally as an early event in prostate carcinogenesis. |journal=Carcinogenesis |volume=22 |issue= 8 |pages= 1271-9 |year= 2001 |pmid= 11470758 |doi= }}
*{{cite journal | author=Duriez C, Falette N, Audoynaud C, ''et al.'' |title=The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene. |journal=Gene |volume=282 |issue= 1-2 |pages= 207-14 |year= 2002 |pmid= 11814693 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on C1S... {November 18, 2007 10:19:55 PM PST}
- SEARCH REDIRECT: Control Box Found: C1S {November 18, 2007 10:20:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:20:19 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:20:19 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:20:19 PM PST}
- UPDATED: Updated protein page: C1S {November 18, 2007 10:20:25 PM PST}
- INFO: Beginning work on CALCR... {November 18, 2007 10:20:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:20:51 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 = Calcitonin receptor
| HGNCid = 1440
| Symbol = CALCR
| AltSymbols =; CRT; CTR; CTR1
| OMIM = 114131
| ECnumber =
| Homologene = 1320
| MGIid = 101950
| GeneAtlas_image1 = PBB_GE_CALCR_207886_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CALCR_207887_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004930 |text = G-protein coupled receptor activity}} {{GNF_GO|id=GO:0004948 |text = calcitonin receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{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:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0007202 |text = phospholipase C activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 799
| Hs_Ensembl = ENSG00000004948
| Hs_RefseqProtein = NP_001733
| Hs_RefseqmRNA = NM_001742
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 92891735
| Hs_GenLoc_end = 93041686
| Hs_Uniprot = P30988
| Mm_EntrezGene = 12311
| Mm_Ensembl = ENSMUSG00000023964
| Mm_RefseqmRNA = NM_001042725
| Mm_RefseqProtein = NP_001036190
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 3637395
| Mm_GenLoc_end = 3672973
| Mm_Uniprot = Q790U4
}}
}}
'''Calcitonin receptor''', also known as '''CALCR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CALCR calcitonin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=799| 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=Pondel M |title=Calcitonin and calcitonin receptors: bone and beyond. |journal=International journal of experimental pathology |volume=81 |issue= 6 |pages= 405-22 |year= 2001 |pmid= 11298188 |doi= }}
*{{cite journal | author=Gorn AH, Lin HY, Yamin M, ''et al.'' |title=Cloning, characterization, and expression of a human calcitonin receptor from an ovarian carcinoma cell line. |journal=J. Clin. Invest. |volume=90 |issue= 5 |pages= 1726-35 |year= 1992 |pmid= 1331173 |doi= }}
*{{cite journal | author=Albrandt K, Brady EM, Moore CX, ''et al.'' |title=Molecular cloning and functional expression of a third isoform of the human calcitonin receptor and partial characterization of the calcitonin receptor gene. |journal=Endocrinology |volume=136 |issue= 12 |pages= 5377-84 |year= 1995 |pmid= 7588285 |doi= }}
*{{cite journal | author=Egerton M, Needham M, Evans S, ''et al.'' |title=Identification of multiple human calcitonin receptor isoforms: heterologous expression and pharmacological characterization. |journal=J. Mol. Endocrinol. |volume=14 |issue= 2 |pages= 179-89 |year= 1995 |pmid= 7619207 |doi= }}
*{{cite journal | author=Nussenzveig DR, Mathew S, Gershengorn MC |title=Alternative splicing of a 48-nucleotide exon generates two isoforms of the human calcitonin receptor. |journal=Endocrinology |volume=136 |issue= 5 |pages= 2047-51 |year= 1995 |pmid= 7720653 |doi= }}
*{{cite journal | author=Nakamura M, Hashimoto T, Nakajima T, ''et al.'' |title=A new type of human calcitonin receptor isoform generated by alternative splicing. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 2 |pages= 744-51 |year= 1995 |pmid= 7733946 |doi= }}
*{{cite journal | author=Pérez Jurado LA, Li X, Francke U |title=The human calcitonin receptor gene (CALCR) at 7q21.3 is outside the deletion associated with the Williams syndrome. |journal=Cytogenet. Cell Genet. |volume=70 |issue= 3-4 |pages= 246-9 |year= 1995 |pmid= 7789182 |doi= }}
*{{cite journal | author=Nussenzveig DR, Thaw CN, Gershengorn MC |title=Inhibition of inositol phosphate second messenger formation by intracellular loop one of a human calcitonin receptor. Expression and mutational analysis of synthetic receptor genes. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 28123-9 |year= 1994 |pmid= 7961748 |doi= }}
*{{cite journal | author=Kuestner RE, Elrod RD, Grant FJ, ''et al.'' |title=Cloning and characterization of an abundant subtype of the human calcitonin receptor. |journal=Mol. Pharmacol. |volume=46 |issue= 2 |pages= 246-55 |year= 1994 |pmid= 8078488 |doi= }}
*{{cite journal | author=Frendo JL, Pichaud F, Mourroux RD, ''et al.'' |title=An isoform of the human calcitonin receptor is expressed in TT cells and in medullary carcinoma of the thyroid. |journal=FEBS Lett. |volume=342 |issue= 2 |pages= 214-6 |year= 1994 |pmid= 8143880 |doi= }}
*{{cite journal | author=Masi L, Becherini L, Gennari L, ''et al.'' |title=Allelic variants of human calcitonin receptor: distribution and association with bone mass in postmenopausal Italian women. |journal=Biochem. Biophys. Res. Commun. |volume=245 |issue= 2 |pages= 622-6 |year= 1998 |pmid= 9571205 |doi= 10.1006/bbrc.1998.8445 }}
*{{cite journal | author=Taboulet J, Frenkian M, Frendo JL, ''et al.'' |title=Calcitonin receptor polymorphism is associated with a decreased fracture risk in post-menopausal women. |journal=Hum. Mol. Genet. |volume=7 |issue= 13 |pages= 2129-33 |year= 1999 |pmid= 9817931 |doi= }}
*{{cite journal | author=Christopoulos G, Perry KJ, Morfis M, ''et al.'' |title=Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. |journal=Mol. Pharmacol. |volume=56 |issue= 1 |pages= 235-42 |year= 1999 |pmid= 10385705 |doi= }}
*{{cite journal | author=Nishikawa T, Ishikawa H, Yamamoto S, Koshihara Y |title=A novel calcitonin receptor gene in human osteoclasts from normal bone marrow. |journal=FEBS Lett. |volume=458 |issue= 3 |pages= 409-14 |year= 2000 |pmid= 10570950 |doi= }}
*{{cite journal | author=Beaudreuil J, Taboulet J, Orcel P, ''et al.'' |title=Calcitonin receptor mRNA in mononuclear leucocytes from postmenopausal women: decrease during osteoporosis and link to bone markers with specific isoform involvement. |journal=Bone |volume=27 |issue= 1 |pages= 161-8 |year= 2000 |pmid= 10865224 |doi= }}
*{{cite journal | author=Wada S, Yasuda S, Nagai T, ''et al.'' |title=Regulation of calcitonin receptor by glucocorticoid in human osteoclast-like cells prepared in vitro using receptor activator of nuclear factor-kappaB ligand and macrophage colony-stimulating factor. |journal=Endocrinology |volume=142 |issue= 4 |pages= 1471-8 |year= 2001 |pmid= 11250927 |doi= }}
*{{cite journal | author=Ogden CA, deCathelineau A, Hoffmann PR, ''et al.'' |title=C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. |journal=J. Exp. Med. |volume=194 |issue= 6 |pages= 781-95 |year= 2001 |pmid= 11560994 |doi= }}
*{{cite journal | author=Nosaka Y, Tachi Y, Shimpuku H, ''et al.'' |title=Association of calcitonin receptor gene polymorphism with early marginal bone loss around endosseous implants. |journal=The International journal of oral & maxillofacial implants |volume=17 |issue= 1 |pages= 38-43 |year= 2002 |pmid= 11858573 |doi= }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CALD1... {November 18, 2007 10:20:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:21:36 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 =
| image_source =
| PDB =
| Name = Caldesmon 1
| HGNCid = 1441
| Symbol = CALD1
| AltSymbols =; CDM; H-CAD; L-CAD; MGC21352; NAG22
| OMIM = 114213
| ECnumber =
| Homologene = 69531
| MGIid =
| GeneAtlas_image1 = PBB_GE_CALD1_201616_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CALD1_201615_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CALD1_201617_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005523 |text = tropomyosin binding}} {{GNF_GO|id=GO:0017022 |text = myosin binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0030478 |text = actin cap}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 800
| Hs_Ensembl = ENSG00000122786
| Hs_RefseqProtein = NP_004333
| Hs_RefseqmRNA = NM_004342
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 134114711
| Hs_GenLoc_end = 134306010
| Hs_Uniprot = Q05682
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Caldesmon 1''', also known as '''CALD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CALD1 caldesmon 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=800| 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 a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca(2+)-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca(2+)-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: CALD1 caldesmon 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=800| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Huber PA |title=Caldesmon. |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 8-9 |pages= 1047-51 |year= 1998 |pmid= 9415999 |doi= }}
*{{cite journal | author=Gusev NB |title=Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation. |journal=Biochemistry Mosc. |volume=66 |issue= 10 |pages= 1112-21 |year= 2002 |pmid= 11736632 |doi= }}
*{{cite journal | author=Wang CL |title=Caldesmon and smooth-muscle regulation. |journal=Cell Biochem. Biophys. |volume=35 |issue= 3 |pages= 275-88 |year= 2002 |pmid= 11894847 |doi= }}
*{{cite journal | author=Mani RS, McCubbin WD, Kay CM |title=Calcium-dependent regulation of caldesmon by an 11-kDa smooth muscle calcium-binding protein, caltropin. |journal=Biochemistry |volume=31 |issue= 47 |pages= 11896-901 |year= 1992 |pmid= 1445920 |doi= }}
*{{cite journal | author=Hayashi K, Yano H, Hashida T, ''et al.'' |title=Genomic structure of the human caldesmon gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 24 |pages= 12122-6 |year= 1993 |pmid= 1465449 |doi= }}
*{{cite journal | author=Humphrey MB, Herrera-Sosa H, Gonzalez G, ''et al.'' |title=Cloning of cDNAs encoding human caldesmons. |journal=Gene |volume=112 |issue= 2 |pages= 197-204 |year= 1992 |pmid= 1555769 |doi= }}
*{{cite journal | author=Adam LP, Gapinski CJ, Hathaway DR |title=Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas. |journal=FEBS Lett. |volume=302 |issue= 3 |pages= 223-6 |year= 1992 |pmid= 1601129 |doi= }}
*{{cite journal | author=Novy RE, Lin JL, Lin JJ |title=Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells. |journal=J. Biol. Chem. |volume=266 |issue= 25 |pages= 16917-24 |year= 1991 |pmid= 1885618 |doi= }}
*{{cite journal | author=Horiuchi KY, Chacko S |title=Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin. |journal=Biochemistry |volume=27 |issue= 22 |pages= 8388-93 |year= 1989 |pmid= 3242591 |doi= }}
*{{cite journal | author=der Terrossian E, Deprette C, Lebbar I, Cassoly R |title=Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane. |journal=Eur. J. Biochem. |volume=219 |issue= 1-2 |pages= 503-11 |year= 1994 |pmid= 8307018 |doi= }}
*{{cite journal | author=Surgucheva I, Bryan J |title=Over-expression of smooth muscle caldesmon in mouse fibroblasts. |journal=Cell Motil. Cytoskeleton |volume=32 |issue= 3 |pages= 233-43 |year= 1996 |pmid= 8581978 |doi= 10.1002/cm.970320307 }}
*{{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=Graether SP, Heinonen TY, Raharjo WH, ''et al.'' |title=Tryptophan residues in caldesmon are major determinants for calmodulin binding. |journal=Biochemistry |volume=36 |issue= 2 |pages= 364-9 |year= 1997 |pmid= 9003189 |doi= 10.1021/bi962008k }}
*{{cite journal | author=Wang Z, Danielsen AJ, Maihle NJ, McManus MJ |title=Tyrosine phosphorylation of caldesmon is required for binding to the Shc.Grb2 complex. |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33807-13 |year= 1999 |pmid= 10559276 |doi= }}
*{{cite journal | author=Adam L, Vadlamudi R, Mandal M, ''et al.'' |title=Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1. |journal=J. Biol. Chem. |volume=275 |issue= 16 |pages= 12041-50 |year= 2000 |pmid= 10766836 |doi= }}
*{{cite journal | author=Hall SM, Hislop AA, Pierce CM, Haworth SG |title=Prenatal origins of human intrapulmonary arteries: formation and smooth muscle maturation. |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 2 |pages= 194-203 |year= 2000 |pmid= 10919986 |doi= }}
*{{cite journal | author=Nimmrich I, Erdmann S, Melchers U, ''et al.'' |title=Seven genes that are differentially transcribed in colorectal tumor cell lines. |journal=Cancer Lett. |volume=160 |issue= 1 |pages= 37-43 |year= 2000 |pmid= 11098082 |doi= }}
*{{cite journal | author=Hisaoka M, Wei-Qi S, Jian W, ''et al.'' |title=Specific but variable expression of h-caldesmon in leiomyosarcomas: an immunohistochemical reassessment of a novel myogenic marker. |journal=Appl. Immunohistochem. Mol. Morphol. |volume=9 |issue= 4 |pages= 302-8 |year= 2003 |pmid= 11759055 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAMK4... {November 18, 2007 10:21:36 PM PST}
- SEARCH REDIRECT: Control Box Found: CAMK4 {November 18, 2007 10:22:08 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:22:11 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:22:11 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:22:11 PM PST}
- UPDATED: Updated protein page: CAMK4 {November 18, 2007 10:22:17 PM PST}
- INFO: Beginning work on CD151... {November 18, 2007 10:22:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:22:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = 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 = CD151 molecule (Raph blood group)
| HGNCid = 1630
| Symbol = CD151
| AltSymbols =; GP27; MER2; PETA-3; RAPH; SFA1; TSPAN24
| OMIM = 602243
| ECnumber =
| Homologene = 20916
| MGIid = 1096360
| GeneAtlas_image1 = PBB_GE_CD151_204306_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 977
| Hs_Ensembl = ENSG00000177697
| Hs_RefseqProtein = NP_001034579
| Hs_RefseqmRNA = NM_001039490
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 822961
| Hs_GenLoc_end = 828830
| Hs_Uniprot = P48509
| Mm_EntrezGene = 12476
| Mm_Ensembl = ENSMUSG00000025510
| Mm_RefseqmRNA = NM_009842
| Mm_RefseqProtein = NP_033972
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 141320142
| Mm_GenLoc_end = 141322788
| Mm_Uniprot = Q921J7
}}
}}
'''CD151 molecule (Raph blood group)''', also known as '''CD151''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD151 CD151 molecule (Raph blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=977| 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 member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins and other transmembrane 4 superfamily proteins. It is involved in cellular processes including cell adhesion and may regulate integrin trafficking and/or function. This protein enhances cell motility, invasion and metastasis of cancer cells. Multiple alternatively spliced transcript variants that encode the same protein have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CD151 CD151 molecule (Raph blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=977| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Ashman LK |title=CD151. |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 3 |pages= 223-6 |year= 2003 |pmid= 12456024 |doi= }}
*{{cite journal | author=Ashman LK, Aylett GW, Mehrabani PA, ''et al.'' |title=The murine monoclonal antibody, 14A2.H1, identifies a novel platelet surface antigen. |journal=Br. J. Haematol. |volume=79 |issue= 2 |pages= 263-70 |year= 1992 |pmid= 1958484 |doi= }}
*{{cite journal | author=Fitter S, Tetaz TJ, Berndt MC, Ashman LK |title=Molecular cloning of cDNA encoding a novel platelet-endothelial cell tetra-span antigen, PETA-3. |journal=Blood |volume=86 |issue= 4 |pages= 1348-55 |year= 1995 |pmid= 7632941 |doi= }}
*{{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=Hasegawa H, Utsunomiya Y, Kishimoto K, ''et al.'' |title=SFA-1, a novel cellular gene induced by human T-cell leukemia virus type 1, is a member of the transmembrane 4 superfamily. |journal=J. Virol. |volume=70 |issue= 5 |pages= 3258-63 |year= 1996 |pmid= 8627808 |doi= }}
*{{cite journal | author=Hasegawa H, Kishimoto K, Yanagisawa K, ''et al.'' |title=Assignment of SFA-1 (PETA-3), a member of the transmembrane 4 superfamily, to human chromosome 11p15.5 by fluorescence in situ hybridization. |journal=Genomics |volume=40 |issue= 1 |pages= 193-6 |year= 1997 |pmid= 9070943 |doi= 10.1006/geno.1996.4563 }}
*{{cite journal | author=Sincock PM, Mayrhofer G, Ashman LK |title=Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. |journal=J. Histochem. Cytochem. |volume=45 |issue= 4 |pages= 515-25 |year= 1997 |pmid= 9111230 |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=Fitter S, Seldin MF, Ashman LK |title=Characterisation of the mouse homologue of CD151 (PETA-3/SFA-1); genomic structure, chromosomal localisation and identification of 2 novel splice forms. |journal=Biochim. Biophys. Acta |volume=1398 |issue= 1 |pages= 75-85 |year= 1998 |pmid= 9602068 |doi= }}
*{{cite journal | author=Sincock PM, Fitter S, Parton RG, ''et al.'' |title=PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function. |journal=J. Cell. Sci. |volume=112 ( Pt 6) |issue= |pages= 833-44 |year= 1999 |pmid= 10036233 |doi= }}
*{{cite journal | author=Serru V, Le Naour F, Billard M, ''et al.'' |title=Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. |journal=Biochem. J. |volume=340 ( Pt 1) |issue= |pages= 103-11 |year= 1999 |pmid= 10229664 |doi= }}
*{{cite journal | author=Testa JE, Brooks PC, Lin JM, Quigley JP |title=Eukaryotic expression cloning with an antimetastatic monoclonal antibody identifies a tetraspanin (PETA-3/CD151) as an effector of human tumor cell migration and metastasis. |journal=Cancer Res. |volume=59 |issue= 15 |pages= 3812-20 |year= 1999 |pmid= 10447000 |doi= }}
*{{cite journal | author=Sterk LM, Geuijen CA, Oomen LC, ''et al.'' |title=The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes. |journal=J. Cell Biol. |volume=149 |issue= 4 |pages= 969-82 |year= 2000 |pmid= 10811835 |doi= }}
*{{cite journal | author=Whittock NV, McLean WH |title=Genomic organization, amplification, fine mapping, and intragenic polymorphisms of the human hemidesmosomal tetraspanin CD151 gene. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 2 |pages= 425-30 |year= 2001 |pmid= 11181065 |doi= 10.1006/bbrc.2001.4384 }}
*{{cite journal | author=Charrin S, Le Naour F, Oualid M, ''et al.'' |title=The major CD9 and CD81 molecular partner. Identification and characterization of the complexes. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14329-37 |year= 2001 |pmid= 11278880 |doi= 10.1074/jbc.M011297200 }}
*{{cite journal | author=Suzuki Y, Tsunoda T, Sese J, ''et al.'' |title=Identification and characterization of the potential promoter regions of 1031 kinds of human genes. |journal=Genome Res. |volume=11 |issue= 5 |pages= 677-84 |year= 2001 |pmid= 11337467 |doi= 10.1101/gr.164001 }}
*{{cite journal | author=Kohno M, Hasegawa H, Miyake M, ''et al.'' |title=CD151 enhances cell motility and metastasis of cancer cells in the presence of focal adhesion kinase. |journal=Int. J. Cancer |volume=97 |issue= 3 |pages= 336-43 |year= 2002 |pmid= 11774285 |doi= }}
*{{cite journal | author=Zhang XA, Kazarov AR, Yang X, ''et al.'' |title=Function of the tetraspanin CD151-alpha6beta1 integrin complex during cellular morphogenesis. |journal=Mol. Biol. Cell |volume=13 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11809818 |doi= 10.1091/mbc.01-10-0481 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CXCL11... {November 18, 2007 10:24:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:24:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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_CXCL11_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rjt.
| PDB = {{PDB2|1rjt}}
| Name = Chemokine (C-X-C motif) ligand 11
| HGNCid = 10638
| Symbol = CXCL11
| AltSymbols =; H174; I-TAC; IP-9; IP9; MGC102770; SCYB11; SCYB9B; b-R1
| OMIM = 604852
| ECnumber =
| Homologene = 3944
| MGIid = 1860203
| GeneAtlas_image1 = PBB_GE_CXCL11_210163_at_tn.png
| GeneAtlas_image2 = PBB_GE_CXCL11_211122_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6373
| Hs_Ensembl = ENSG00000169248
| Hs_RefseqProtein = NP_005400
| Hs_RefseqmRNA = NM_005409
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 77173975
| Hs_GenLoc_end = 77176376
| Hs_Uniprot = O14625
| Mm_EntrezGene = 56066
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_019494
| Mm_RefseqProtein = NP_062367
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Chemokine (C-X-C motif) ligand 11''', also known as '''CXCL11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CXCL11 chemokine (C-X-C motif) ligand 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6373| 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 = Chemokines are a group of small (approximately 8 to 14 kD), mostly basic, structurally related molecules that regulate cell trafficking of various types of leukocytes through interactions with a subset of 7-transmembrane, G protein-coupled receptors. Chemokines also play fundamental roles in the development, homeostasis, and function of the immune system, and they have effects on cells of the central nervous system as well as on endothelial cells involved in angiogenesis or angiostasis. Chemokines are divided into 2 major subfamilies, CXC and CC. This gene is a CXC member of the chemokine superfamily. Its encoded protein induces a chemotactic response in activated T-cells and is the dominant ligand for CXC receptor-3. The gene encoding this protein contains 4 exons and at least three polyadenylation signals which might reflect cell-specific regulation of expression. IFN-gamma is a potent inducer of transcription of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CXCL11 chemokine (C-X-C motif) ligand 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6373| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rani MR, Foster GR, Leung S, ''et al.'' |title=Characterization of beta-R1, a gene that is selectively induced by interferon beta (IFN-beta) compared with IFN-alpha. |journal=J. Biol. Chem. |volume=271 |issue= 37 |pages= 22878-84 |year= 1996 |pmid= 8798467 |doi= }}
*{{cite journal | author=Jacobs KA, Collins-Racie LA, Colbert M, ''et al.'' |title=A genetic selection for isolating cDNAs encoding secreted proteins. |journal=Gene |volume=198 |issue= 1-2 |pages= 289-96 |year= 1997 |pmid= 9370294 |doi= }}
*{{cite journal | author=Cole KE, Strick CA, Paradis TJ, ''et al.'' |title=Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3. |journal=J. Exp. Med. |volume=187 |issue= 12 |pages= 2009-21 |year= 1998 |pmid= 9625760 |doi= }}
*{{cite journal | author=Erdel M, Laich A, Utermann G, ''et al.'' |title=The human gene encoding SCYB9B, a putative novel CXC chemokine, maps to human chromosome 4q21 like the closely related genes for MIG (SCYB9) and INP10 (SCYB10). |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 271-2 |year= 1998 |pmid= 9730616 |doi= }}
*{{cite journal | author=Luo Y, Kim R, Gabuzda D, ''et al.'' |title=The CXC-chemokine, H174: expression in the central nervous system. |journal=J. Neurovirol. |volume=4 |issue= 6 |pages= 575-85 |year= 1999 |pmid= 10065899 |doi= }}
*{{cite journal | author=Tensen CP, Flier J, Van Der Raaij-Helmer EM, ''et al.'' |title=Human IP-9: A keratinocyte-derived high affinity CXC-chemokine ligand for the IP-10/Mig receptor (CXCR3). |journal=J. Invest. Dermatol. |volume=112 |issue= 5 |pages= 716-22 |year= 1999 |pmid= 10233762 |doi= 10.1046/j.1523-1747.1999.00581.x }}
*{{cite journal | author=Laich A, Meyer M, Werner ER, Werner-Felmayer G |title=Structure and expression of the human small cytokine B subfamily member 11 (SCYB11/formerly SCYB9B, alias I-TAC) gene cloned from IFN-gamma-treated human monocytes (THP-1). |journal=J. Interferon Cytokine Res. |volume=19 |issue= 5 |pages= 505-13 |year= 1999 |pmid= 10386863 |doi= 10.1089/107999099313956 }}
*{{cite journal | author=Tensen CP, Flier J, Rampersad SS, ''et al.'' |title=Genomic organization, sequence and transcriptional regulation of the human CXCL 11(1) gene. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 1-2 |pages= 167-72 |year= 1999 |pmid= 10395932 |doi= }}
*{{cite journal | author=Loetscher P, Pellegrino A, Gong JH, ''et al.'' |title=The ligands of CXC chemokine receptor 3, I-TAC, Mig, and IP10, are natural antagonists for CCR3. |journal=J. Biol. Chem. |volume=276 |issue= 5 |pages= 2986-91 |year= 2001 |pmid= 11110785 |doi= 10.1074/jbc.M005652200 }}
*{{cite journal | author=Lambeir AM, Proost P, Durinx C, ''et al.'' |title=Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29839-45 |year= 2001 |pmid= 11390394 |doi= 10.1074/jbc.M103106200 }}
*{{cite journal | author=Hensbergen PJ, van der Raaij-Helmer EM, Dijkman R, ''et al.'' |title=Processing of natural and recombinant CXCR3-targeting chemokines and implications for biological activity. |journal=Eur. J. Biochem. |volume=268 |issue= 18 |pages= 4992-9 |year= 2001 |pmid= 11559369 |doi= }}
*{{cite journal | author=Mohan K, Ding Z, Hanly J, Issekutz TB |title=IFN-gamma-inducible T cell alpha chemoattractant is a potent stimulator of normal human blood T lymphocyte transendothelial migration: differential regulation by IFN-gamma and TNF-alpha. |journal=J. Immunol. |volume=168 |issue= 12 |pages= 6420-8 |year= 2002 |pmid= 12055261 |doi= }}
*{{cite journal | author=Basu S, Schaefer TM, Ghosh M, ''et al.'' |title=Molecular cloning and sequencing of 25 different rhesus macaque chemokine cDNAs reveals evolutionary conservation among C, CC, CXC, AND CX3C families of chemokines. |journal=Cytokine |volume=18 |issue= 3 |pages= 140-8 |year= 2003 |pmid= 12126650 |doi= }}
*{{cite journal | author=Salmaggi A, Gelati M, Dufour A, ''et al.'' |title=Expression and modulation of IFN-gamma-inducible chemokines (IP-10, Mig, and I-TAC) in human brain endothelium and astrocytes: possible relevance for the immune invasion of the central nervous system and the pathogenesis of multiple sclerosis. |journal=J. Interferon Cytokine Res. |volume=22 |issue= 6 |pages= 631-40 |year= 2003 |pmid= 12162873 |doi= 10.1089/10799900260100114 }}
*{{cite journal | author=Rani MR, Hibbert L, Sizemore N, ''et al.'' |title=Requirement of phosphoinositide 3-kinase and Akt for interferon-beta-mediated induction of the beta-R1 (SCYB11) gene. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38456-61 |year= 2002 |pmid= 12169689 |doi= 10.1074/jbc.M203204200 }}
*{{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=Kao J, Kobashigawa J, Fishbein MC, ''et al.'' |title=Elevated serum levels of the CXCR3 chemokine ITAC are associated with the development of transplant coronary artery disease. |journal=Circulation |volume=107 |issue= 15 |pages= 1958-61 |year= 2003 |pmid= 12695288 |doi= 10.1161/01.CIR.0000069270.16498.75 }}
*{{cite journal | author=Satish L, Yager D, Wells A |title=Glu-Leu-Arg-negative CXC chemokine interferon gamma inducible protein-9 as a mediator of epidermal-dermal communication during wound repair. |journal=J. Invest. Dermatol. |volume=120 |issue= 6 |pages= 1110-7 |year= 2003 |pmid= 12787142 |doi= 10.1046/j.1523-1747.2003.12230.x }}
*{{cite journal | author=Klunker S, Trautmann A, Akdis M, ''et al.'' |title=A second step of chemotaxis after transendothelial migration: keratinocytes undergoing apoptosis release IFN-gamma-inducible protein 10, monokine induced by IFN-gamma, and IFN-gamma-inducible alpha-chemoattractant for T cell chemotaxis toward epidermis in atopic dermatitis. |journal=J. Immunol. |volume=171 |issue= 2 |pages= 1078-84 |year= 2003 |pmid= 12847282 |doi= }}
*{{cite journal | author=Xanthou G, Duchesnes CE, Williams TJ, Pease JE |title=CCR3 functional responses are regulated by both CXCR3 and its ligands CXCL9, CXCL10 and CXCL11. |journal=Eur. J. Immunol. |volume=33 |issue= 8 |pages= 2241-50 |year= 2003 |pmid= 12884299 |doi= 10.1002/eji.200323787 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CXCL5... {November 18, 2007 10:24:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:25:24 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 = Chemokine (C-X-C motif) ligand 5
| HGNCid = 10642
| Symbol = CXCL5
| AltSymbols =; ENA-78; SCYB5
| OMIM = 600324
| ECnumber =
| Homologene = 88672
| MGIid =
| GeneAtlas_image1 = PBB_GE_CXCL5_214974_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_CXCL5_215101_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6374
| Hs_Ensembl = ENSG00000163735
| Hs_RefseqProtein = NP_002985
| Hs_RefseqmRNA = NM_002994
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 75080224
| Hs_GenLoc_end = 75083280
| Hs_Uniprot = P42830
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Chemokine (C-X-C motif) ligand 5''', also known as '''CXCL5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CXCL5 chemokine (C-X-C motif) ligand 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6374| 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 an inflammatory chemokine that belongs to the CXC chemokine family. This chemokine is produced concomitantly with interleukin-8 (IL8) in response to stimulation with either interleukin-1 (IL1) or tumor necrosis factor-alpha (TNFA). This chemokine is a potent chemotaxin involved in neutrophil activation.<ref name="entrez">{{cite web | title = Entrez Gene: CXCL5 chemokine (C-X-C motif) ligand 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6374| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Walz A, Schmutz P, Mueller C, Schnyder-Candrian S |title=Regulation and function of the CXC chemokine ENA-78 in monocytes and its role in disease. |journal=J. Leukoc. Biol. |volume=62 |issue= 5 |pages= 604-11 |year= 1997 |pmid= 9365115 |doi= }}
*{{cite journal | author=Struyf S, Proost P, Van Damme J |title=Regulation of the immune response by the interaction of chemokines and proteases. |journal=Adv. Immunol. |volume=81 |issue= |pages= 1-44 |year= 2004 |pmid= 14711052 |doi= }}
*{{cite journal | author=Walz A, Burgener R, Car B, ''et al.'' |title=Structure and neutrophil-activating properties of a novel inflammatory peptide (ENA-78) with homology to interleukin 8. |journal=J. Exp. Med. |volume=174 |issue= 6 |pages= 1355-62 |year= 1992 |pmid= 1744577 |doi= }}
*{{cite journal | author=Power CA, Furness RB, Brawand C, Wells TN |title=Cloning of a full-length cDNA encoding the neutrophil-activating peptide ENA-78 from human platelets. |journal=Gene |volume=151 |issue= 1-2 |pages= 333-4 |year= 1995 |pmid= 7828901 |doi= }}
*{{cite journal | author=Chang MS, McNinch J, Basu R, Simonet S |title=Cloning and characterization of the human neutrophil-activating peptide (ENA-78) gene. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25277-82 |year= 1994 |pmid= 7929219 |doi= }}
*{{cite journal | author=Corbett MS, Schmitt I, Riess O, Walz A |title=Characterization of the gene for human neutrophil-activating peptide 78 (ENA-78). |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 612-7 |year= 1995 |pmid= 7999089 |doi= 10.1006/bbrc.1994.2709 }}
*{{cite journal | author=Koch AE, Kunkel SL, Harlow LA, ''et al.'' |title=Epithelial neutrophil activating peptide-78: a novel chemotactic cytokine for neutrophils in arthritis. |journal=J. Clin. Invest. |volume=94 |issue= 3 |pages= 1012-8 |year= 1994 |pmid= 8083342 |doi= }}
*{{cite journal | author=Power CA, Clemetson JM, Clemetson KJ, Wells TN |title=Chemokine and chemokine receptor mRNA expression in human platelets. |journal=Cytokine |volume=7 |issue= 6 |pages= 479-82 |year= 1996 |pmid= 8580362 |doi= 10.1006/cyto.1995.0065 }}
*{{cite journal | author=Ahuja SK, Murphy PM |title=The CXC chemokines growth-regulated oncogene (GRO) alpha, GRObeta, GROgamma, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20545-50 |year= 1996 |pmid= 8702798 |doi= }}
*{{cite journal | author=Keates S, Keates AC, Mizoguchi E, ''et al.'' |title=Enterocytes are the primary source of the chemokine ENA-78 in normal colon and ulcerative colitis. |journal=Am. J. Physiol. |volume=273 |issue= 1 Pt 1 |pages= G75-82 |year= 1997 |pmid= 9252512 |doi= }}
*{{cite journal | author=Wuyts A, Proost P, Lenaerts JP, ''et al.'' |title=Differential usage of the CXC chemokine receptors 1 and 2 by interleukin-8, granulocyte chemotactic protein-2 and epithelial-cell-derived neutrophil attractant-78. |journal=Eur. J. Biochem. |volume=255 |issue= 1 |pages= 67-73 |year= 1998 |pmid= 9692902 |doi= }}
*{{cite journal | author=Wyrick PB, Knight ST, Paul TR, ''et al.'' |title=Persistent chlamydial envelope antigens in antibiotic-exposed infected cells trigger neutrophil chemotaxis. |journal=J. Infect. Dis. |volume=179 |issue= 4 |pages= 954-66 |year= 1999 |pmid= 10068592 |doi= }}
*{{cite journal | author=Wuyts A, Govaerts C, Struyf S, ''et al.'' |title=Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from tumor cells and leukocytes reveals NH2-terminal heterogeneity. Functional comparison of different natural isoforms. |journal=Eur. J. Biochem. |volume=260 |issue= 2 |pages= 421-9 |year= 1999 |pmid= 10095777 |doi= }}
*{{cite journal | author=Hogaboam CM, Bone-Larson CL, Steinhauser ML, ''et al.'' |title=Novel CXCR2-dependent liver regenerative qualities of ELR-containing CXC chemokines. |journal=FASEB J. |volume=13 |issue= 12 |pages= 1565-74 |year= 1999 |pmid= 10463948 |doi= }}
*{{cite journal | author=Luu NT, Rainger GE, Nash GB |title=Differential ability of exogenous chemotactic agents to disrupt transendothelial migration of flowing neutrophils. |journal=J. Immunol. |volume=164 |issue= 11 |pages= 5961-9 |year= 2000 |pmid= 10820279 |doi= }}
*{{cite journal | author=Crane IJ, Wallace CA, McKillop-Smith S, Forrester JV |title=Control of chemokine production at the blood-retina barrier. |journal=Immunology |volume=101 |issue= 3 |pages= 426-33 |year= 2000 |pmid= 11106948 |doi= }}
*{{cite journal | author=Zhang C, Thornton MA, Kowalska MA, ''et al.'' |title=Localization of distal regulatory domains in the megakaryocyte-specific platelet basic protein/platelet factor 4 gene locus. |journal=Blood |volume=98 |issue= 3 |pages= 610-7 |year= 2001 |pmid= 11468158 |doi= }}
*{{cite journal | author=Chandrasekar B, Melby PC, Sarau HM, ''et al.'' |title=Chemokine-cytokine cross-talk. The ELR+ CXC chemokine LIX (CXCL5) amplifies a proinflammatory cytokine response via a phosphatidylinositol 3-kinase-NF-kappa B pathway. |journal=J. Biol. Chem. |volume=278 |issue= 7 |pages= 4675-86 |year= 2003 |pmid= 12468547 |doi= 10.1074/jbc.M207006200 }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FOXP2... {November 18, 2007 10:35:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:36:12 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_FOXP2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2a07.
| PDB = {{PDB2|2a07}}, {{PDB2|2as5}}
| Name = Forkhead box P2
| HGNCid = 13875
| Symbol = FOXP2
| AltSymbols =; CAGH44; DKFZp686H1726; SPCH1; TNRC10
| OMIM = 605317
| ECnumber =
| Homologene = 33482
| MGIid = 2148705
| GeneAtlas_image1 = PBB_GE_FOXP2_gnf1h09377_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0021757 |text = caudate nucleus development}} {{GNF_GO|id=GO:0021758 |text = putamen development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 93986
| Hs_Ensembl = ENSG00000128573
| Hs_RefseqProtein = NP_055306
| Hs_RefseqmRNA = NM_014491
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 113842288
| Hs_GenLoc_end = 114117219
| Hs_Uniprot = O15409
| Mm_EntrezGene = 114142
| Mm_Ensembl = ENSMUSG00000029563
| Mm_RefseqmRNA = NM_053242
| Mm_RefseqProtein = NP_444472
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 15135506
| Mm_GenLoc_end = 15391977
| Mm_Uniprot = Q8BQ27
}}
}}
'''Forkhead box P2''', also known as '''FOXP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FOXP2 forkhead box P2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=93986| 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 evolutionarily conserved transcription factor expressed in fetal and adult brain. This transcription factor is a member of the forkhead/winged-helix (FOX) family of transcription factors, and contains a FOX DNA-binding domain and a large polyglutamine tract. Members of the FOX family of transcription factors are regulators of embryogenesis. The product of this gene is thought to be required for proper development of speech and language regions of the brain during embryogenesis. Although a point mutation in this gene has been associated with the KE pedigree segregating developmental verbal dyspraxia, no association between mutations in this gene and another speech disorder, autism, has been found. Four alternative transcripts encoding three different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: FOXP2 forkhead box P2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=93986| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vargha-Khadem F, Gadian DG, Copp A, Mishkin M |title=FOXP2 and the neuroanatomy of speech and language. |journal=Nat. Rev. Neurosci. |volume=6 |issue= 2 |pages= 131-8 |year= 2005 |pmid= 15685218 |doi= 10.1038/nrn1605 }}
*{{cite journal | author=Benítez-Burraco A |title=[FOXP2: from the specific disorder to the molecular biology of language. I. Aetiological, neuroanatomical, neurophysiological and molecular aspects] |journal=Revista de neurologia |volume=40 |issue= 11 |pages= 671-82 |year= 2005 |pmid= 15948071 |doi= }}
*{{cite journal | author=Lennon PA, Cooper ML, Peiffer DA, ''et al.'' |title=Deletion of 7q31.1 supports involvement of FOXP2 in language impairment: clinical report and review. |journal=Am. J. Med. Genet. A |volume=143 |issue= 8 |pages= 791-8 |year= 2007 |pmid= 17330859 |doi= 10.1002/ajmg.a.31632 }}
*{{cite journal | author=Hurst JA, Baraitser M, Auger E, ''et al.'' |title=An extended family with a dominantly inherited speech disorder. |journal=Developmental medicine and child neurology |volume=32 |issue= 4 |pages= 352-5 |year= 1990 |pmid= 2332125 |doi= }}
*{{cite journal | author=Margolis RL, Abraham MR, Gatchell SB, ''et al.'' |title=cDNAs with long CAG trinucleotide repeats from human brain. |journal=Hum. Genet. |volume=100 |issue= 1 |pages= 114-22 |year= 1997 |pmid= 9225980 |doi= }}
*{{cite journal | author=Vargha-Khadem F, Watkins KE, Price CJ, ''et al.'' |title=Neural basis of an inherited speech and language disorder. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 21 |pages= 12695-700 |year= 1998 |pmid= 9770548 |doi= }}
*{{cite journal | author=Lai CS, Fisher SE, Hurst JA, ''et al.'' |title=The SPCH1 region on human 7q31: genomic characterization of the critical interval and localization of translocations associated with speech and language disorder. |journal=Am. J. Hum. Genet. |volume=67 |issue= 2 |pages= 357-68 |year= 2000 |pmid= 10880297 |doi= }}
*{{cite journal | author=Shu W, Yang H, Zhang L, ''et al.'' |title=Characterization of a new subfamily of winged-helix/forkhead (Fox) genes that are expressed in the lung and act as transcriptional repressors. |journal=J. Biol. Chem. |volume=276 |issue= 29 |pages= 27488-97 |year= 2001 |pmid= 11358962 |doi= 10.1074/jbc.M100636200 }}
*{{cite journal | author=Lai CS, Fisher SE, Hurst JA, ''et al.'' |title=A forkhead-domain gene is mutated in a severe speech and language disorder. |journal=Nature |volume=413 |issue= 6855 |pages= 519-23 |year= 2001 |pmid= 11586359 |doi= 10.1038/35097076 }}
*{{cite journal | author=Bishop DV |title=Putting language genes in perspective. |journal=Trends Genet. |volume=18 |issue= 2 |pages= 57-9 |year= 2002 |pmid= 11818129 |doi= }}
*{{cite journal | author=Harasty J, Hodges JR |title=Towards the elucidation of the genetic and brain bases of developmental speech and language disorders. |journal=Brain |volume=125 |issue= Pt 3 |pages= 449-51 |year= 2002 |pmid= 11872603 |doi= }}
*{{cite journal | author=Watkins KE, Vargha-Khadem F, Ashburner J, ''et al.'' |title=MRI analysis of an inherited speech and language disorder: structural brain abnormalities. |journal=Brain |volume=125 |issue= Pt 3 |pages= 465-78 |year= 2002 |pmid= 11872605 |doi= }}
*{{cite journal | author=Newbury DF, Bonora E, Lamb JA, ''et al.'' |title=FOXP2 is not a major susceptibility gene for autism or specific language impairment. |journal=Am. J. Hum. Genet. |volume=70 |issue= 5 |pages= 1318-27 |year= 2002 |pmid= 11894222 |doi= }}
*{{cite journal | author=Meaburn E, Dale PS, Craig IW, Plomin R |title=Language-impaired children: No sign of the FOXP2 mutation. |journal=Neuroreport |volume=13 |issue= 8 |pages= 1075-7 |year= 2002 |pmid= 12060812 |doi= }}
*{{cite journal | author=Wassink TH, Piven J, Vieland VJ, ''et al.'' |title=Evaluation of FOXP2 as an autism susceptibility gene. |journal=Am. J. Med. Genet. |volume=114 |issue= 5 |pages= 566-9 |year= 2002 |pmid= 12116195 |doi= 10.1002/ajmg.10415 }}
*{{cite journal | author=Felsenfeld S |title=Finding susceptibility genes for developmental disorders of speech: the long and winding road. |journal=Journal of communication disorders |volume=35 |issue= 4 |pages= 329-45 |year= 2003 |pmid= 12160352 |doi= }}
*{{cite journal | author=Bruce HA, Margolis RL |title=FOXP2: novel exons, splice variants, and CAG repeat length stability. |journal=Hum. Genet. |volume=111 |issue= 2 |pages= 136-44 |year= 2002 |pmid= 12189486 |doi= 10.1007/s00439-002-0768-5 }}
*{{cite journal | author=Enard W, Przeworski M, Fisher SE, ''et al.'' |title=Molecular evolution of FOXP2, a gene involved in speech and language. |journal=Nature |volume=418 |issue= 6900 |pages= 869-72 |year= 2002 |pmid= 12192408 |doi= 10.1038/nature01025 }}
*{{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=Zhang J, Webb DM, Podlaha O |title=Accelerated protein evolution and origins of human-specific features: Foxp2 as an example. |journal=Genetics |volume=162 |issue= 4 |pages= 1825-35 |year= 2003 |pmid= 12524352 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GAB2... {November 18, 2007 10:34:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:34:45 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 = GRB2-associated binding protein 2
| HGNCid = 14458
| Symbol = GAB2
| AltSymbols =; KIAA0571
| OMIM = 606203
| ECnumber =
| Homologene = 69067
| MGIid = 1333854
| GeneAtlas_image1 = PBB_GE_GAB2_203853_s_at_tn.png
| Function =
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9846
| Hs_Ensembl = ENSG00000033327
| Hs_RefseqProtein = NP_036428
| Hs_RefseqmRNA = NM_012296
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 77603990
| Hs_GenLoc_end = 77806414
| Hs_Uniprot = Q9UQC2
| Mm_EntrezGene = 14389
| Mm_Ensembl = ENSMUSG00000004508
| Mm_RefseqmRNA = NM_010248
| Mm_RefseqProtein = NP_034378
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 96956943
| Mm_GenLoc_end = 97180228
| Mm_Uniprot = Q3ZB56
}}
}}
'''GRB2-associated binding protein 2''', also known as '''GAB2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAB2 GRB2-associated binding protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9846| 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 GRB2-associated binding protein (GAB) gene family and is similar to the GAB1 gene. These proteins contain pleckstrin homology (PH) domain, and bind SHP2 tyrosine phosphatase and GRB2 adapter protein. They act as adapters for transmitting various signals in response to stimuli through cytokine and growth factor receptors, and T- and B-cell antigen receptors. The protein encoded by this gene is the principal activator of phosphatidylinositol-3 kinase in response to activation of the high affinity IgE receptor. Two alternatively spliced transcripts encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: GAB2 GRB2-associated binding protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9846| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hibi M, Hirano T |title=Gab-family adapter molecules in signal transduction of cytokine and growth factor receptors, and T and B cell antigen receptors. |journal=Leuk. Lymphoma |volume=37 |issue= 3-4 |pages= 299-307 |year= 2000 |pmid= 10752981 |doi= }}
*{{cite journal | author=Gold MR, Ingham RJ, McLeod SJ, ''et al.'' |title=Targets of B-cell antigen receptor signaling: the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase-3 signaling pathway and the Rap1 GTPase. |journal=Immunol. Rev. |volume=176 |issue= |pages= 47-68 |year= 2001 |pmid= 11043767 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
*{{cite journal | author=Nishida K, Yoshida Y, Itoh M, ''et al.'' |title=Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors. |journal=Blood |volume=93 |issue= 6 |pages= 1809-16 |year= 1999 |pmid= 10068651 |doi= }}
*{{cite journal | author=Zhao C, Yu DH, Shen R, Feng GS |title=Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1. |journal=J. Biol. Chem. |volume=274 |issue= 28 |pages= 19649-54 |year= 1999 |pmid= 10391903 |doi= }}
*{{cite journal | author=Wickrema A, Uddin S, Sharma A, ''et al.'' |title=Engagement of Gab1 and Gab2 in erythropoietin signaling. |journal=J. Biol. Chem. |volume=274 |issue= 35 |pages= 24469-74 |year= 1999 |pmid= 10455108 |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=Liu Y, Jenkins B, Shin JL, Rohrschneider LR |title=Scaffolding protein Gab2 mediates differentiation signaling downstream of Fms receptor tyrosine kinase. |journal=Mol. Cell. Biol. |volume=21 |issue= 9 |pages= 3047-56 |year= 2001 |pmid= 11287610 |doi= 10.1128/MCB.21.9.3047-3056.2001 }}
*{{cite journal | author=Crouin C, Arnaud M, Gesbert F, ''et al.'' |title=A yeast two-hybrid study of human p97/Gab2 interactions with its SH2 domain-containing binding partners. |journal=FEBS Lett. |volume=495 |issue= 3 |pages= 148-53 |year= 2001 |pmid= 11334882 |doi= }}
*{{cite journal | author=Bouscary D, Lecoq-Lafon C, Chrétien S, ''et al.'' |title=Role of Gab proteins in phosphatidylinositol 3-kinase activation by thrombopoietin (Tpo). |journal=Oncogene |volume=20 |issue= 18 |pages= 2197-204 |year= 2001 |pmid= 11402314 |doi= 10.1038/sj.onc.1204317 }}
*{{cite journal | author=Wu C, Lai CF, Mobley WC |title=Nerve growth factor activates persistent Rap1 signaling in endosomes. |journal=J. Neurosci. |volume=21 |issue= 15 |pages= 5406-16 |year= 2001 |pmid= 11466412 |doi= }}
*{{cite journal | author=Yamasaki S, Nishida K, Hibi M, ''et al.'' |title=Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules. |journal=J. Biol. Chem. |volume=276 |issue= 48 |pages= 45175-83 |year= 2002 |pmid= 11572860 |doi= 10.1074/jbc.M105384200 }}
*{{cite journal | author=Yamada K, Nishida K, Hibi M, ''et al.'' |title=Comparative FISH mapping of Gab1 and Gab2 genes in human, mouse and rat. |journal=Cytogenet. Cell Genet. |volume=94 |issue= 1-2 |pages= 39-42 |year= 2001 |pmid= 11701952 |doi= }}
*{{cite journal | author=Lynch DK, Daly RJ |title=PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2. |journal=EMBO J. |volume=21 |issue= 1-2 |pages= 72-82 |year= 2002 |pmid= 11782427 |doi= }}
*{{cite journal | author=Wheadon H, Paling NR, Welham MJ |title=Molecular interactions of SHP1 and SHP2 in IL-3-signalling. |journal=Cell. Signal. |volume=14 |issue= 3 |pages= 219-29 |year= 2002 |pmid= 11812650 |doi= }}
*{{cite journal | author=Dorsey JF, Cunnick JM, Mane SM, Wu J |title=Regulation of the Erk2-Elk1 signaling pathway and megakaryocytic differentiation of Bcr-Abl(+) K562 leukemic cells by Gab2. |journal=Blood |volume=99 |issue= 4 |pages= 1388-97 |year= 2002 |pmid= 11830491 |doi= }}
*{{cite journal | author=Hill RJ, Zozulya S, Lu YL, ''et al.'' |title=The lymphoid protein tyrosine phosphatase Lyp interacts with the adaptor molecule Grb2 and functions as a negative regulator of T-cell activation. |journal=Exp. Hematol. |volume=30 |issue= 3 |pages= 237-44 |year= 2002 |pmid= 11882361 |doi= }}
*{{cite journal | author=Yu WM, Hawley TS, Hawley RG, Qu CK |title=Role of the docking protein Gab2 in beta(1)-integrin signaling pathway-mediated hematopoietic cell adhesion and migration. |journal=Blood |volume=99 |issue= 7 |pages= 2351-9 |year= 2002 |pmid= 11895767 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPS6KA2... {November 18, 2007 10:22:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:23:44 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 = Ribosomal protein S6 kinase, 90kDa, polypeptide 2
| HGNCid = 10431
| Symbol = RPS6KA2
| AltSymbols =; HU-2; RSK; MAPKAPK1C; RSK3; S6K-alpha; S6K-alpha2; p90-RSK3; pp90RSK3
| OMIM = 601685
| ECnumber =
| Homologene = 36318
| MGIid = 1342290
| GeneAtlas_image1 = PBB_GE_RPS6KA2_204906_at_tn.png
| GeneAtlas_image2 = PBB_GE_RPS6KA2_212912_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6196
| Hs_Ensembl = ENSG00000071242
| Hs_RefseqProtein = NP_001006933
| Hs_RefseqmRNA = NM_001006932
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 166742844
| Hs_GenLoc_end = 167195791
| Hs_Uniprot = Q15349
| Mm_EntrezGene = 20112
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_489703
| Mm_RefseqProtein = XP_489703
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ribosomal protein S6 kinase, 90kDa, polypeptide 2''', also known as '''RPS6KA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6196| 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 a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6196| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Zhao Y, Bjørbaek C, Weremowicz S, ''et al.'' |title=RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation. |journal=Mol. Cell. Biol. |volume=15 |issue= 8 |pages= 4353-63 |year= 1995 |pmid= 7623830 |doi= }}
*{{cite journal | author=Moller DE, Xia CH, Tang W, ''et al.'' |title=Human rsk isoforms: cloning and characterization of tissue-specific expression. |journal=Am. J. Physiol. |volume=266 |issue= 2 Pt 1 |pages= C351-9 |year= 1994 |pmid= 8141249 |doi= }}
*{{cite journal | author=Wong EV, Schaefer AW, Landreth G, Lemmon V |title=Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18217-23 |year= 1996 |pmid= 8663493 |doi= }}
*{{cite journal | author=Xing J, Ginty DD, Greenberg ME |title=Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. |journal=Science |volume=273 |issue= 5277 |pages= 959-63 |year= 1996 |pmid= 8688081 |doi= }}
*{{cite journal | author=Zhao Y, Bjorbaek C, Moller DE |title=Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 47 |pages= 29773-9 |year= 1997 |pmid= 8939914 |doi= }}
*{{cite journal | author=Fukunaga R, Hunter T |title=MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. |journal=EMBO J. |volume=16 |issue= 8 |pages= 1921-33 |year= 1997 |pmid= 9155018 |doi= 10.1093/emboj/16.8.1921 }}
*{{cite journal | author=del Peso L, González-García M, Page C, ''et al.'' |title=Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. |journal=Science |volume=278 |issue= 5338 |pages= 687-9 |year= 1997 |pmid= 9381178 |doi= }}
*{{cite journal | author=Deak M, Clifton AD, Lucocq LM, Alessi DR |title=Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. |journal=EMBO J. |volume=17 |issue= 15 |pages= 4426-41 |year= 1998 |pmid= 9687510 |doi= 10.1093/emboj/17.15.4426 }}
*{{cite journal | author=Du K, Montminy M |title=CREB is a regulatory target for the protein kinase Akt/PKB. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32377-9 |year= 1999 |pmid= 9829964 |doi= }}
*{{cite journal | author=Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW |title=Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo. |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 2893-8 |year= 1999 |pmid= 9915826 |doi= }}
*{{cite journal | author=Jensen CJ, Buch MB, Krag TO, ''et al.'' |title=90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 27168-76 |year= 1999 |pmid= 10480933 |doi= }}
*{{cite journal | author=Schimenti JC |title=ORFless, intronless, and mutant transcription units in the mouse t complex responder (Tcr) locus. |journal=Mamm. Genome |volume=10 |issue= 10 |pages= 969-76 |year= 2000 |pmid= 10501965 |doi= }}
*{{cite journal | author=Scheid MP, Schubert KM, Duronio V |title=Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 31108-13 |year= 1999 |pmid= 10521512 |doi= }}
*{{cite journal | author=Tan Y, Demeter MR, Ruan H, Comb MJ |title=BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25865-9 |year= 2000 |pmid= 10837486 |doi= 10.1074/jbc.M004199200 }}
*{{cite journal | author=Lizcano JM, Morrice N, Cohen P |title=Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. |journal=Biochem. J. |volume=349 |issue= Pt 2 |pages= 547-57 |year= 2001 |pmid= 10880354 |doi= }}
*{{cite journal | author=Datta SR, Katsov A, Hu L, ''et al.'' |title=14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. |journal=Mol. Cell |volume=6 |issue= 1 |pages= 41-51 |year= 2000 |pmid= 10949026 |doi= }}
*{{cite journal | author=Gudi T, Casteel DE, Vinson C, ''et al.'' |title=NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation. |journal=Oncogene |volume=19 |issue= 54 |pages= 6324-33 |year= 2001 |pmid= 11175347 |doi= 10.1038/sj.onc.1204007 }}
*{{cite journal | author=Willard FS, Crouch MF |title=MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: a role for the MAP kinase pathway in regulating mitotic exit. |journal=Cell. Signal. |volume=13 |issue= 9 |pages= 653-64 |year= 2001 |pmid= 11495723 |doi= }}
*{{cite journal | author=Schinelli S, Zanassi P, Paolillo M, ''et al.'' |title=Stimulation of endothelin B receptors in astrocytes induces cAMP response element-binding protein phosphorylation and c-fos expression via multiple mitogen-activated protein kinase signaling pathways. |journal=J. Neurosci. |volume=21 |issue= 22 |pages= 8842-53 |year= 2001 |pmid= 11698596 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on S100A6... {November 18, 2007 10:23:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:24:16 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 = PBB_Protein_S100A6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a03.
| PDB = {{PDB2|1a03}}, {{PDB2|1cnp}}, {{PDB2|1jwd}}, {{PDB2|1k8u}}, {{PDB2|1k96}}, {{PDB2|1k9k}}, {{PDB2|1k9p}}, {{PDB2|2cnp}}
| Name = S100 calcium binding protein A6
| HGNCid = 10496
| Symbol = S100A6
| AltSymbols =; 2A9; 5B10; CABP; CACY; PRA
| OMIM = 114110
| ECnumber =
| Homologene = 7925
| MGIid = 1339467
| GeneAtlas_image1 = PBB_GE_S100A6_217728_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0048154 |text = S100 beta binding}} {{GNF_GO|id=GO:0048306 |text = calcium-dependent protein binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007409 |text = axonogenesis}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0048146 |text = positive regulation of fibroblast proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6277
| Hs_Ensembl = ENSG00000197956
| Hs_RefseqProtein = NP_055439
| Hs_RefseqmRNA = NM_014624
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 151773699
| Hs_GenLoc_end = 151775344
| Hs_Uniprot = P06703
| Mm_EntrezGene = 20200
| Mm_Ensembl = ENSMUSG00000001025
| Mm_RefseqmRNA = NM_011313
| Mm_RefseqProtein = NP_035443
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 90699108
| Mm_GenLoc_end = 90700341
| Mm_Uniprot = Q545I9
}}
}}
'''S100 calcium binding protein A6''', also known as '''S100A6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: S100A6 S100 calcium binding protein A6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6277| 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 member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-dependent insulin release, stimulation of prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of this gene have been implicated in melanoma.<ref name="entrez">{{cite web | title = Entrez Gene: S100A6 S100 calcium binding protein A6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6277| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schäfer BW, Heizmann CW |title=The S100 family of EF-hand calcium-binding proteins: functions and pathology. |journal=Trends Biochem. Sci. |volume=21 |issue= 4 |pages= 134-40 |year= 1996 |pmid= 8701470 |doi= }}
*{{cite journal | author=Minami H, Tokumitsu H, Mizutani A, ''et al.'' |title=Specific binding of CAP-50 to calcyclin. |journal=FEBS Lett. |volume=305 |issue= 3 |pages= 217-9 |year= 1993 |pmid= 1299619 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Erne P, Heizmann CW |title=S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart. |journal=Biochemistry |volume=31 |issue= 42 |pages= 10258-64 |year= 1992 |pmid= 1384693 |doi= }}
*{{cite journal | author=Tomida Y, Terasawa M, Kobayashi R, Hidaka H |title=Calcyclin and calvasculin exist in human platelets. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 3 |pages= 1310-6 |year= 1993 |pmid= 1482346 |doi= }}
*{{cite journal | author=Filipek A, Gerke V, Weber K, Kuźnicki J |title=Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography. |journal=Eur. J. Biochem. |volume=195 |issue= 3 |pages= 795-800 |year= 1991 |pmid= 1999197 |doi= }}
*{{cite journal | author=Murphy LC, Murphy LJ, Tsuyuki D, ''et al.'' |title=Cloning and characterization of a cDNA encoding a highly conserved, putative calcium binding protein, identified by an anti-prolactin receptor antiserum. |journal=J. Biol. Chem. |volume=263 |issue= 5 |pages= 2397-401 |year= 1988 |pmid= 2448309 |doi= }}
*{{cite journal | author=Gabius HJ, Bardosi A, Gabius S, ''et al.'' |title=Identification of a cell cycle-dependent gene product as a sialic acid-binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=163 |issue= 1 |pages= 506-12 |year= 1989 |pmid= 2775283 |doi= }}
*{{cite journal | author=Ferrari S, Calabretta B, deRiel JK, ''et al.'' |title=Structural and functional analysis of a growth-regulated gene, the human calcyclin. |journal=J. Biol. Chem. |volume=262 |issue= 17 |pages= 8325-32 |year= 1987 |pmid= 3036810 |doi= }}
*{{cite journal | author=Calabretta B, Battini R, Kaczmarek L, ''et al.'' |title=Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein. |journal=J. Biol. Chem. |volume=261 |issue= 27 |pages= 12628-32 |year= 1986 |pmid= 3755724 |doi= }}
*{{cite journal | author=Schäfer BW, Wicki R, Engelkamp D, ''et al.'' |title=Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family. |journal=Genomics |volume=25 |issue= 3 |pages= 638-43 |year= 1995 |pmid= 7759097 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Mattei MG, ''et al.'' |title=Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6547-51 |year= 1993 |pmid= 8341667 |doi= }}
*{{cite journal | author=Filipek A, Wojda U |title=p30, a novel protein target of mouse calcyclin (S100A6). |journal=Biochem. J. |volume=320 ( Pt 2) |issue= |pages= 585-7 |year= 1997 |pmid= 8973570 |doi= }}
*{{cite journal | author=Kordowska J, Stafford WF, Wang CL |title=Ca2+ and Zn2+ bind to different sites and induce different conformational changes in human calcyclin. |journal=Eur. J. Biochem. |volume=253 |issue= 1 |pages= 57-66 |year= 1998 |pmid= 9578461 |doi= }}
*{{cite journal | author=Yang Q, O'Hanlon D, Heizmann CW, Marks A |title=Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma. |journal=Exp. Cell Res. |volume=246 |issue= 2 |pages= 501-9 |year= 1999 |pmid= 9925766 |doi= 10.1006/excr.1998.4314 }}
*{{cite journal | author=Sudo T, Hidaka H |title=Characterization of the calcyclin (S100A6) binding site of annexin XI-A by site-directed mutagenesis. |journal=FEBS Lett. |volume=444 |issue= 1 |pages= 11-4 |year= 1999 |pmid= 10037139 |doi= }}
*{{cite journal | author=Deloulme JC, Assard N, Mbele GO, ''et al.'' |title=S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35302-10 |year= 2001 |pmid= 10913138 |doi= 10.1074/jbc.M003943200 }}
*{{cite journal | author=Li Y, Yang L, Cui JT, ''et al.'' |title=Construction of cDNA representational difference analysis based on two cDNA libraries and identification of garlic inducible expression genes in human gastric cancer cells. |journal=World J. Gastroenterol. |volume=8 |issue= 2 |pages= 208-12 |year= 2002 |pmid= 11925593 |doi= }}
*{{cite journal | author=Otterbein LR, Kordowska J, Witte-Hoffmann C, ''et al.'' |title=Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution. |journal=Structure |volume=10 |issue= 4 |pages= 557-67 |year= 2002 |pmid= 11937060 |doi= }}
*{{cite journal | author=Filipek A, Jastrzebska B, Nowotny M, Kuznicki J |title=CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28848-52 |year= 2002 |pmid= 12042313 |doi= 10.1074/jbc.M203602200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SFRP1... {November 18, 2007 10:25:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:26:06 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
}}
<!-- 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 = Secreted frizzled-related protein 1
| HGNCid = 10776
| Symbol = SFRP1
| AltSymbols =; FRP1; FRP; FRP-1; FrzA; SARP2
| OMIM = 604156
| ECnumber =
| Homologene = 2266
| MGIid = 892014
| GeneAtlas_image1 = PBB_GE_SFRP1_202037_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SFRP1_202035_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SFRP1_202036_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001756 |text = somitogenesis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6422
| Hs_Ensembl = ENSG00000104332
| Hs_RefseqProtein = NP_003003
| Hs_RefseqmRNA = NM_003012
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 41238640
| Hs_GenLoc_end = 41286149
| Hs_Uniprot = Q8N474
| Mm_EntrezGene = 20377
| Mm_Ensembl = ENSMUSG00000031548
| Mm_RefseqmRNA = NM_013834
| Mm_RefseqProtein = NP_038862
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 24877063
| Mm_GenLoc_end = 24915179
| Mm_Uniprot = Q505A2
}}
}}
'''Secreted frizzled-related protein 1''', also known as '''SFRP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SFRP1 secreted frizzled-related protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6422| 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 = Secreted frizzled-related protein 1 (SFRP1) is a member of the SFRP family that contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs act as soluble modulators of Wnt signaling. SFRP1 and SFRP5 may be involved in determining the polarity of photoreceptor cells in the retina. SFRP1 is expressed in several human tissues, with the highest levels in heart.<ref name="entrez">{{cite web | title = Entrez Gene: SFRP1 secreted frizzled-related protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6422| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ohgimoto S, Tabata N, Suga S, ''et al.'' |title=Molecular characterization of fusion regulatory protein-1 (FRP-1) that induces multinucleated giant cell formation of monocytes and HIV gp160-mediated cell fusion. FRP-1 and 4F2/CD98 are identical molecules. |journal=J. Immunol. |volume=155 |issue= 7 |pages= 3585-92 |year= 1995 |pmid= 7561057 |doi= }}
*{{cite journal | author=Ohgimoto S, Tabata N, Suga S, ''et al.'' |title=Regulation of human immunodeficiency virus gp160-mediated cell fusion by antibodies against fusion regulatory protein 1. |journal=J. Gen. Virol. |volume=77 ( Pt 11) |issue= |pages= 2747-56 |year= 1996 |pmid= 8922468 |doi= }}
*{{cite journal | author=Rattner A, Hsieh JC, Smallwood PM, ''et al.'' |title=A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 7 |pages= 2859-63 |year= 1997 |pmid= 9096311 |doi= }}
*{{cite journal | author=Suga S, Tsurudome M, Ito M, ''et al.'' |title=Human immunodeficiency virus type-1 envelope glycoprotein gp120 induces expression of fusion regulatory protein (FRP)-1/CD98 on CD4+ T cells: a possible regulatory mechanism of HIV-induced syncytium formation. |journal=Med. Microbiol. Immunol. |volume=185 |issue= 4 |pages= 237-43 |year= 1997 |pmid= 9138296 |doi= }}
*{{cite journal | author=Finch PW, He X, Kelley MJ, ''et al.'' |title=Purification and molecular cloning of a secreted, Frizzled-related antagonist of Wnt action. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 13 |pages= 6770-5 |year= 1997 |pmid= 9192640 |doi= }}
*{{cite journal | author=Melkonyan HS, Chang WC, Shapiro JP, ''et al.'' |title=SARPs: a family of secreted apoptosis-related proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 25 |pages= 13636-41 |year= 1998 |pmid= 9391078 |doi= }}
*{{cite journal | author=Tabata N, Ido M, Suga S, ''et al.'' |title=Protein tyrosine kinase activation provides an early and obligatory signal in anti-FRP-1/CD98/4F2 monoclonal antibody induced cell fusion mediated by HIV gp160. |journal=Med. Microbiol. Immunol. |volume=186 |issue= 2-3 |pages= 115-23 |year= 1998 |pmid= 9403839 |doi= }}
*{{cite journal | author=Zhou Z, Wang J, Han X, ''et al.'' |title=Up-regulation of human secreted frizzled homolog in apoptosis and its down-regulation in breast tumors. |journal=Int. J. Cancer |volume=78 |issue= 1 |pages= 95-9 |year= 1998 |pmid= 9724099 |doi= }}
*{{cite journal | author=Bafico A, Gazit A, Pramila T, ''et al.'' |title=Interaction of frizzled related protein (FRP) with Wnt ligands and the frizzled receptor suggests alternative mechanisms for FRP inhibition of Wnt signaling. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 16180-7 |year= 1999 |pmid= 10347172 |doi= }}
*{{cite journal | author=Uren A, Reichsman F, Anest V, ''et al.'' |title=Secreted frizzled-related protein-1 binds directly to Wingless and is a biphasic modulator of Wnt signaling. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4374-82 |year= 2000 |pmid= 10660608 |doi= }}
*{{cite journal | author=Yoshino K, Rubin JS, Higinbotham KG, ''et al.'' |title=Secreted Frizzled-related proteins can regulate metanephric development. |journal=Mech. Dev. |volume=102 |issue= 1-2 |pages= 45-55 |year= 2001 |pmid= 11287180 |doi= }}
*{{cite journal | author=Ugolini F, Charafe-Jauffret E, Bardou VJ, ''et al.'' |title=WNT pathway and mammary carcinogenesis: loss of expression of candidate tumor suppressor gene SFRP1 in most invasive carcinomas except of the medullary type. |journal=Oncogene |volume=20 |issue= 41 |pages= 5810-7 |year= 2001 |pmid= 11593386 |doi= 10.1038/sj.onc.1204706 }}
*{{cite journal | author=Chong JM, Uren A, Rubin JS, Speicher DW |title=Disulfide bond assignments of secreted Frizzled-related protein-1 provide insights about Frizzled homology and netrin modules. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5134-44 |year= 2002 |pmid= 11741940 |doi= 10.1074/jbc.M108533200 }}
*{{cite journal | author=Fukuhara K, Kariya M, Kita M, ''et al.'' |title=Secreted frizzled related protein 1 is overexpressed in uterine leiomyomas, associated with a high estrogenic environment and unrelated to proliferative activity. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 4 |pages= 1729-36 |year= 2002 |pmid= 11932307 |doi= }}
*{{cite journal | author=Ko J, Ryu KS, Lee YH, ''et al.'' |title=Human secreted frizzled-related protein is down-regulated and induces apoptosis in human cervical cancer. |journal=Exp. Cell Res. |volume=280 |issue= 2 |pages= 280-7 |year= 2002 |pmid= 12413893 |doi= }}
*{{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=Mori K, Nishimura M, Tsurudome M, ''et al.'' |title=The functional interaction between CD98 and CD147 in regulation of virus-induced cell fusion and osteoclast formation. |journal=Med. Microbiol. Immunol. |volume=193 |issue= 4 |pages= 155-62 |year= 2005 |pmid= 12925876 |doi= 10.1007/s00430-003-0191-0 }}
*{{cite journal | author=Han X, Amar S |title=Secreted frizzled-related protein 1 (SFRP1) protects fibroblasts from ceramide-induced apoptosis. |journal=J. Biol. Chem. |volume=279 |issue= 4 |pages= 2832-40 |year= 2004 |pmid= 14581477 |doi= 10.1074/jbc.M308102200 }}
*{{cite journal | author=Caldwell GM, Jones C, Gensberg K, ''et al.'' |title=The Wnt antagonist sFRP1 in colorectal tumorigenesis. |journal=Cancer Res. |volume=64 |issue= 3 |pages= 883-8 |year= 2004 |pmid= 14871816 |doi= }}
*{{cite journal | author=Garcia-Hoyos M, Cantalapiedra D, Arroyo C, ''et al.'' |title=Evaluation of SFRP1 as a candidate for human retinal dystrophies. |journal=Mol. Vis. |volume=10 |issue= |pages= 426-31 |year= 2004 |pmid= 15235574 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SILV... {November 18, 2007 10:26:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:26:40 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 = Silver homolog (mouse)
| HGNCid = 10880
| Symbol = SILV
| AltSymbols =; SI; D12S53E; ME20; PMEL17; SIL; gp100
| OMIM = 155550
| ECnumber =
| Homologene = 5048
| MGIid = 98301
| GeneAtlas_image1 = PBB_GE_SILV_209848_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006583 |text = melanin biosynthetic process from tyrosine}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6490
| Hs_Ensembl = ENSG00000185664
| Hs_RefseqProtein = NP_008859
| Hs_RefseqmRNA = NM_006928
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 54634157
| Hs_GenLoc_end = 54646765
| Hs_Uniprot = P40967
| Mm_EntrezGene = 20431
| Mm_Ensembl = ENSMUSG00000025359
| Mm_RefseqmRNA = NM_021882
| Mm_RefseqProtein = NP_068682
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 128109207
| Mm_GenLoc_end = 128123073
| Mm_Uniprot = Q60696
}}
}}
'''Silver homolog (mouse)''', also known as '''SILV''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SILV silver homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6490| 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=Aplan PD, Lombardi DP, Kirsch IR |title=Structural characterization of SIL, a gene frequently disrupted in T-cell acute lymphoblastic leukemia. |journal=Mol. Cell. Biol. |volume=11 |issue= 11 |pages= 5462-9 |year= 1991 |pmid= 1922059 |doi= }}
*{{cite journal | author=Kwon BS, Chintamaneni C, Kozak CA, ''et al.'' |title=A melanocyte-specific gene, Pmel 17, maps near the silver coat color locus on mouse chromosome 10 and is in a syntenic region on human chromosome 12. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 20 |pages= 9228-32 |year= 1991 |pmid= 1924386 |doi= }}
*{{cite journal | author=Brown L, Cheng JT, Chen Q, ''et al.'' |title=Site-specific recombination of the tal-1 gene is a common occurrence in human T cell leukemia. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3343-51 |year= 1990 |pmid= 2209547 |doi= }}
*{{cite journal | author=Aplan PD, Lombardi DP, Ginsberg AM, ''et al.'' |title=Disruption of the human SCL locus by "illegitimate" V-(D)-J recombinase activity. |journal=Science |volume=250 |issue= 4986 |pages= 1426-9 |year= 1991 |pmid= 2255914 |doi= }}
*{{cite journal | author=Adema GJ, de Boer AJ, Vogel AM, ''et al.'' |title=Molecular characterization of the melanocyte lineage-specific antigen gp100. |journal=J. Biol. Chem. |volume=269 |issue= 31 |pages= 20126-33 |year= 1994 |pmid= 7519602 |doi= }}
*{{cite journal | author=Kawakami Y, Eliyahu S, Delgado CH, ''et al.'' |title=Identification of a human melanoma antigen recognized by tumor-infiltrating lymphocytes associated with in vivo tumor rejection. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6458-62 |year= 1994 |pmid= 8022805 |doi= }}
*{{cite journal | author=Maresh GA, Marken JS, Neubauer M, ''et al.'' |title=Cloning and expression of the gene for the melanoma-associated ME20 antigen. |journal=DNA Cell Biol. |volume=13 |issue= 2 |pages= 87-95 |year= 1994 |pmid= 8179825 |doi= }}
*{{cite journal | author=Bailin T, Lee ST, Spritz RA |title=Genomic organization and sequence of D12S53E (Pmel 17), the human homologue of the mouse silver (si) locus. |journal=J. Invest. Dermatol. |volume=106 |issue= 1 |pages= 24-7 |year= 1996 |pmid= 8592076 |doi= }}
*{{cite journal | author=Chakraborty AK, Platt JT, Kim KK, ''et al.'' |title=Polymerization of 5,6-dihydroxyindole-2-carboxylic acid to melanin by the pmel 17/silver locus protein. |journal=Eur. J. Biochem. |volume=236 |issue= 1 |pages= 180-8 |year= 1996 |pmid= 8617263 |doi= }}
*{{cite journal | author=Kim KK, Youn BS, Heng HH, ''et al.'' |title=Genomic organization and FISH mapping of human Pmel 17, the putative silver locus. |journal=Pigment Cell Res. |volume=9 |issue= 1 |pages= 42-8 |year= 1996 |pmid= 8739560 |doi= }}
*{{cite journal | author=Chi DD, Merchant RE, Rand R, ''et al.'' |title=Molecular detection of tumor-associated antigens shared by human cutaneous melanomas and gliomas. |journal=Am. J. Pathol. |volume=150 |issue= 6 |pages= 2143-52 |year= 1997 |pmid= 9176405 |doi= }}
*{{cite journal | author=Wagner SN, Wagner C, Schultewolter T, Goos M |title=Analysis of Pmel17/gp100 expression in primary human tissue specimens: implications for melanoma immuno- and gene-therapy. |journal=Cancer Immunol. Immunother. |volume=44 |issue= 4 |pages= 239-47 |year= 1997 |pmid= 9222283 |doi= }}
*{{cite journal | author=Curry BJ, Myers K, Hersey P |title=Polymerase chain reaction detection of melanoma cells in the circulation: relation to clinical stage, surgical treatment, and recurrence from melanoma. |journal=J. Clin. Oncol. |volume=16 |issue= 5 |pages= 1760-9 |year= 1998 |pmid= 9586889 |doi= }}
*{{cite journal | author=Lupetti R, Pisarra P, Verrecchia A, ''et al.'' |title=Translation of a retained intron in tyrosinase-related protein (TRP) 2 mRNA generates a new cytotoxic T lymphocyte (CTL)-defined and shared human melanoma antigen not expressed in normal cells of the melanocytic lineage. |journal=J. Exp. Med. |volume=188 |issue= 6 |pages= 1005-16 |year= 1998 |pmid= 9743519 |doi= }}
*{{cite journal | author=Lukowsky A, Bellmann B, Ringk A, ''et al.'' |title=Detection of melanoma micrometastases in the sentinel lymph node and in nonsentinel nodes by tyrosinase polymerase chain reaction. |journal=J. Invest. Dermatol. |volume=113 |issue= 4 |pages= 554-9 |year= 1999 |pmid= 10504440 |doi= 10.1046/j.1523-1747.1999.00719.x }}
*{{cite journal | author=Raposo G, Tenza D, Murphy DM, ''et al.'' |title=Distinct protein sorting and localization to premelanosomes, melanosomes, and lysosomes in pigmented melanocytic cells. |journal=J. Cell Biol. |volume=152 |issue= 4 |pages= 809-24 |year= 2001 |pmid= 11266471 |doi= }}
*{{cite journal | author=Virador V, Matsunaga N, Matsunaga J, ''et al.'' |title=Production of melanocyte-specific antibodies to human melanosomal proteins: expression patterns in normal human skin and in cutaneous pigmented lesions. |journal=Pigment Cell Res. |volume=14 |issue= 4 |pages= 289-97 |year= 2002 |pmid= 11549113 |doi= }}
*{{cite journal | author=Berson JF, Harper DC, Tenza D, ''et al.'' |title=Pmel17 initiates premelanosome morphogenesis within multivesicular bodies. |journal=Mol. Biol. Cell |volume=12 |issue= 11 |pages= 3451-64 |year= 2002 |pmid= 11694580 |doi= }}
*{{cite journal | author=Sensi M, Pellegatta S, Vegetti C, ''et al.'' |title=Identification of a novel gp100/pMel17 peptide presented by HLA-A*6801 and recognized on human melanoma by cytolytic T cell clones. |journal=Tissue Antigens |volume=59 |issue= 4 |pages= 273-9 |year= 2003 |pmid= 12135425 |doi= }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC3A1... {November 18, 2007 10:26:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:27:16 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 = Solute carrier family 3 (cystine, dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral amino acid transport), member 1
| HGNCid = 11025
| Symbol = SLC3A1
| AltSymbols =; ATR1; CSNU1; D2H; FLJ34681; NBAT; RBAT
| OMIM = 104614
| ECnumber =
| Homologene = 37289
| MGIid = 1195264
| GeneAtlas_image1 = PBB_GE_SLC3A1_205799_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0015174 |text = basic amino acid transmembrane transporter activity}} {{GNF_GO|id=GO:0015184 |text = L-cystine transmembrane transporter activity}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0015802 |text = basic amino acid transport}} {{GNF_GO|id=GO:0015811 |text = L-cystine transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6519
| Hs_Ensembl = ENSG00000138079
| Hs_RefseqProtein = NP_000332
| Hs_RefseqmRNA = NM_000341
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 44356103
| Hs_GenLoc_end = 44402137
| Hs_Uniprot = Q07837
| Mm_EntrezGene = 20532
| Mm_Ensembl = ENSMUSG00000024131
| Mm_RefseqmRNA = XM_001003828
| Mm_RefseqProtein = XP_001003828
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 84936702
| Mm_GenLoc_end = 84972562
| Mm_Uniprot =
}}
}}
'''Solute carrier family 3 (cystine, dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral amino acid transport), member 1''', also known as '''SLC3A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC3A1 solute carrier family 3 (cystine, dibasic and neutral amino acid transporters, activator of cystine, dibasic and neutral amino acid transport), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6519| 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=Pras E, Raben N, Golomb E, ''et al.'' |title=Mutations in the SLC3A1 transporter gene in cystinuria. |journal=Am. J. Hum. Genet. |volume=56 |issue= 6 |pages= 1297-303 |year= 1995 |pmid= 7539209 |doi= }}
*{{cite journal | author=Calonge MJ, Volpini V, Bisceglia L, ''et al.'' |title=Genetic heterogeneity in cystinuria: the SLC3A1 gene is linked to type I but not to type III cystinuria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9667-71 |year= 1995 |pmid= 7568194 |doi= }}
*{{cite journal | author=Gasparini P, Calonge MJ, Bisceglia L, ''et al.'' |title=Molecular genetics of cystinuria: identification of four new mutations and seven polymorphisms, and evidence for genetic heterogeneity. |journal=Am. J. Hum. Genet. |volume=57 |issue= 4 |pages= 781-8 |year= 1995 |pmid= 7573036 |doi= }}
*{{cite journal | author=Miyamoto K, Katai K, Tatsumi S, ''et al.'' |title=Mutations of the basic amino acid transporter gene associated with cystinuria. |journal=Biochem. J. |volume=310 ( Pt 3) |issue= |pages= 951-5 |year= 1995 |pmid= 7575432 |doi= }}
*{{cite journal | author=Bertran J, Werner A, Chillarón J, ''et al.'' |title=Expression cloning of a human renal cDNA that induces high affinity transport of L-cystine shared with dibasic amino acids in Xenopus oocytes. |journal=J. Biol. Chem. |volume=268 |issue= 20 |pages= 14842-9 |year= 1993 |pmid= 7686906 |doi= }}
*{{cite journal | author=Calonge MJ, Nadal M, Calvano S, ''et al.'' |title=Assignment of the gene responsible for cystinuria (rBAT) and of markers D2S119 and D2S177 to 2p16 by fluorescence in situ hybridization. |journal=Hum. Genet. |volume=95 |issue= 6 |pages= 633-6 |year= 1995 |pmid= 7789946 |doi= }}
*{{cite journal | author=Calonge MJ, Gasparini P, Chillarón J, ''et al.'' |title=Cystinuria caused by mutations in rBAT, a gene involved in the transport of cystine. |journal=Nat. Genet. |volume=6 |issue= 4 |pages= 420-5 |year= 1994 |pmid= 8054986 |doi= 10.1038/ng0494-420 }}
*{{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=Lee WS, Wells RG, Sabbag RV, ''et al.'' |title=Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport. |journal=J. Clin. Invest. |volume=91 |issue= 5 |pages= 1959-63 |year= 1993 |pmid= 8486766 |doi= }}
*{{cite journal | author=Miyamoto K, Segawa H, Tatsumi S, ''et al.'' |title=Effects of truncation of the COOH-terminal region of a Na+-independent neutral and basic amino acid transporter on amino acid transport in Xenopus oocytes. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16758-63 |year= 1996 |pmid= 8663184 |doi= }}
*{{cite journal | author=Endsley JK, Phillips JA, Hruska KA, ''et al.'' |title=Genomic organization of a human cystine transporter gene (SLC3A1) and identification of novel mutations causing cystinuria. |journal=Kidney Int. |volume=51 |issue= 6 |pages= 1893-9 |year= 1997 |pmid= 9186880 |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=Rossier G, Meier C, Bauch C, ''et al.'' |title=LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. |journal=J. Biol. Chem. |volume=274 |issue= 49 |pages= 34948-54 |year= 2000 |pmid= 10574970 |doi= }}
*{{cite journal | author=Pfeiffer R, Loffing J, Rossier G, ''et al.'' |title=Luminal heterodimeric amino acid transporter defective in cystinuria. |journal=Mol. Biol. Cell |volume=10 |issue= 12 |pages= 4135-47 |year= 2000 |pmid= 10588648 |doi= }}
*{{cite journal | author=Rajan DP, Huang W, Kekuda R, ''et al.'' |title=Differential influence of the 4F2 heavy chain and the protein related to b(0,+) amino acid transport on substrate affinity of the heteromeric b(0,+) amino acid transporter. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14331-5 |year= 2000 |pmid= 10799513 |doi= }}
*{{cite journal | author=Mizoguchi K, Cha SH, Chairoungdua A, ''et al.'' |title=Human cystinuria-related transporter: localization and functional characterization. |journal=Kidney Int. |volume=59 |issue= 5 |pages= 1821-33 |year= 2001 |pmid= 11318953 |doi= 10.1046/j.1523-1755.2001.0590051821.x }}
*{{cite journal | author=Harnevik L, Fjellstedt E, Molbaek A, ''et al.'' |title=Identification of 12 novel mutations in the SLC3A1 gene in Swedish cystinuria patients. |journal=Hum. Mutat. |volume=18 |issue= 6 |pages= 516-25 |year= 2002 |pmid= 11748844 |doi= 10.1002/humu.1228 }}
*{{cite journal | author=Bauch C, Verrey F |title=Apical heterodimeric cystine and cationic amino acid transporter expressed in MDCK cells. |journal=Am. J. Physiol. Renal Physiol. |volume=283 |issue= 1 |pages= F181-9 |year= 2002 |pmid= 12060600 |doi= 10.1152/ajprenal.00212.2001 }}
*{{cite journal | author=Fernández E, Carrascal M, Rousaud F, ''et al.'' |title=rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for cystine in the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=283 |issue= 3 |pages= F540-8 |year= 2002 |pmid= 12167606 |doi= 10.1152/ajprenal.00071.2002 }}
*{{cite journal | author=Botzenhart E, Vester U, Schmidt C, ''et al.'' |title=Cystinuria in children: distribution and frequencies of mutations in the SLC3A1 and SLC7A9 genes. |journal=Kidney Int. |volume=62 |issue= 4 |pages= 1136-42 |year= 2003 |pmid= 12234283 |doi= 10.1111/j.1523-1755.2002.kid552.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC9A3R2... {November 18, 2007 10:33:28 PM PST}
- SEARCH REDIRECT: Control Box Found: Sodium-hydrogen exchange regulatory cofactor 2 {November 18, 2007 10:34:13 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:34:14 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 18, 2007 10:34:14 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:34:14 PM PST}
- UPDATED: Updated protein page: Sodium-hydrogen exchange regulatory cofactor 2 {November 18, 2007 10:34:21 PM PST}
- INFO: Beginning work on STX4... {November 18, 2007 10:27:49 PM PST}
- SEARCH REDIRECT: Control Box Found: STX4 {November 18, 2007 10:28:12 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:28:15 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:28:15 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:28:15 PM PST}
- UPDATED: Updated protein page: STX4 {November 18, 2007 10:28:21 PM PST}
- INFO: Beginning work on SULT2A1... {November 18, 2007 10:28:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:29:01 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_SULT2A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1efh.
| PDB = {{PDB2|1efh}}, {{PDB2|1j99}}, {{PDB2|1ov4}}
| Name = Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
| HGNCid = 11458
| Symbol = SULT2A1
| AltSymbols =; HST; ST2; DHEA-ST; ST2A3; STD; hSTa
| OMIM = 125263
| ECnumber =
| Homologene = 37741
| MGIid = 3690091
| GeneAtlas_image1 = PBB_GE_SULT2A1_206292_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SULT2A1_206293_at_tn.png
| Function = {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0047704 |text = bile-salt sulfotransferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0030573 |text = bile acid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6822
| Hs_Ensembl = ENSG00000105398
| Hs_RefseqProtein = NP_003158
| Hs_RefseqmRNA = NM_003167
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 53065682
| Hs_GenLoc_end = 53081405
| Hs_Uniprot = Q06520
| Mm_EntrezGene = 20865
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_987548
| Mm_RefseqProtein = XP_992642
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1''', also known as '''SULT2A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SULT2A1 sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6822| 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 = Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene is primarily expressed in liver and adrenal tissues where the encoded protein sulfates steroids and bile acids.<ref name="entrez">{{cite web | title = Entrez Gene: SULT2A1 sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6822| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weinshilboum RM, Otterness DM, Aksoy IA, ''et al.'' |title=Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes. |journal=FASEB J. |volume=11 |issue= 1 |pages= 3-14 |year= 1997 |pmid= 9034160 |doi= }}
*{{cite journal | author=Glatt H, Engelke CE, Pabel U, ''et al.'' |title=Sulfotransferases: genetics and role in toxicology. |journal=Toxicol. Lett. |volume=112-113 |issue= |pages= 341-8 |year= 2000 |pmid= 10720750 |doi= }}
*{{cite journal | author=Glatt H, Boeing H, Engelke CE, ''et al.'' |title=Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects. |journal=Mutat. Res. |volume=482 |issue= 1-2 |pages= 27-40 |year= 2001 |pmid= 11535246 |doi= }}
*{{cite journal | author=Kong AN, Yang L, Ma M, ''et al.'' |title=Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver. |journal=Biochem. Biophys. Res. Commun. |volume=187 |issue= 1 |pages= 448-54 |year= 1992 |pmid= 1520333 |doi= }}
*{{cite journal | author=Comer KA, Falany CN |title=Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal. |journal=Mol. Pharmacol. |volume=41 |issue= 4 |pages= 645-51 |year= 1992 |pmid= 1569919 |doi= }}
*{{cite journal | author=Otterness DM, Wieben ED, Wood TC, ''et al.'' |title=Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA. |journal=Mol. Pharmacol. |volume=41 |issue= 5 |pages= 865-72 |year= 1992 |pmid= 1588921 |doi= }}
*{{cite journal | author=Radominska A, Comer KA, Zimniak P, ''et al.'' |title=Human liver steroid sulphotransferase sulphates bile acids. |journal=Biochem. J. |volume=272 |issue= 3 |pages= 597-604 |year= 1991 |pmid= 2268288 |doi= }}
*{{cite journal | author=Forbes KJ, Hagen M, Glatt H, ''et al.'' |title=Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. |journal=Mol. Cell. Endocrinol. |volume=112 |issue= 1 |pages= 53-60 |year= 1995 |pmid= 7589785 |doi= }}
*{{cite journal | author=Luu-The V, Dufort I, Paquet N, ''et al.'' |title=Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene. |journal=DNA Cell Biol. |volume=14 |issue= 6 |pages= 511-8 |year= 1995 |pmid= 7598806 |doi= }}
*{{cite journal | author=Comer KA, Falany JL, Falany CN |title=Cloning and expression of human liver dehydroepiandrosterone sulphotransferase. |journal=Biochem. J. |volume=289 ( Pt 1) |issue= |pages= 233-40 |year= 1993 |pmid= 7678732 |doi= }}
*{{cite journal | author=Otterness DM, Her C, Aksoy S, ''et al.'' |title=Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization. |journal=DNA Cell Biol. |volume=14 |issue= 4 |pages= 331-41 |year= 1995 |pmid= 7710689 |doi= }}
*{{cite journal | author=Otterness DM, Mohrenweiser HW, Brandriff BF, Weinshilboum RM |title=Dehydroepiandrosterone sulfotransferase gene (STD): localization to human chromosome band 19q13.3. |journal=Cytogenet. Cell Genet. |volume=70 |issue= 1-2 |pages= 45-7 |year= 1995 |pmid= 7736787 |doi= }}
*{{cite journal | author=Falany CN, Wheeler J, Oh TS, Falany JL |title=Steroid sulfation by expressed human cytosolic sulfotransferases. |journal=J. Steroid Biochem. Mol. Biol. |volume=48 |issue= 4 |pages= 369-75 |year= 1994 |pmid= 8142314 |doi= }}
*{{cite journal | author=Barker EV, Hume R, Hallas A, Coughtrie WH |title=Dehydroepiandrosterone sulfotransferase in the developing human fetus: quantitative biochemical and immunological characterization of the hepatic, renal, and adrenal enzymes. |journal=Endocrinology |volume=134 |issue= 2 |pages= 982-9 |year= 1994 |pmid= 8299591 |doi= }}
*{{cite journal | author=Durocher F, Morissette J, Dufort I, ''et al.'' |title=Genetic linkage mapping of the dehydroepiandrosterone sulfotransferase (STD) gene on the chromosome 19q13.3 region. |journal=Genomics |volume=29 |issue= 3 |pages= 781-3 |year= 1996 |pmid= 8575776 |doi= 10.1006/geno.1995.9935 }}
*{{cite journal | author=Rubin GL, Harrold AJ, Mills JA, ''et al.'' |title=Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy. |journal=Mol. Hum. Reprod. |volume=5 |issue= 11 |pages= 995-1002 |year= 1999 |pmid= 10541560 |doi= }}
*{{cite journal | author=Tashiro A, Sasano H, Nishikawa T, ''et al.'' |title=Expression and activity of dehydroepiandrosterone sulfotransferase in human gastric mucosa. |journal=J. Steroid Biochem. Mol. Biol. |volume=72 |issue= 3-4 |pages= 149-54 |year= 2000 |pmid= 10775806 |doi= }}
*{{cite journal | author=Pedersen LC, Petrotchenko EV, Negishi M |title=Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase. |journal=FEBS Lett. |volume=475 |issue= 1 |pages= 61-4 |year= 2000 |pmid= 10854859 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SUMO2... {November 18, 2007 10:27:16 PM PST}
- SEARCH REDIRECT: Control Box Found: SUMO2 {November 18, 2007 10:27:42 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:27:43 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:27:43 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:27:43 PM PST}
- UPDATED: Updated protein page: SUMO2 {November 18, 2007 10:27:49 PM PST}
- INFO: Beginning work on TBXAS1... {November 18, 2007 10:29:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:29:44 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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<!-- 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 A synthase 1 (platelet, cytochrome P450, family 5, subfamily A)
| HGNCid = 11609
| Symbol = TBXAS1
| AltSymbols =; TS; CYP5; CYP5A1; THAS; TXAS; TXS
| OMIM = 274180
| ECnumber =
| Homologene = 55549
| MGIid = 98497
| GeneAtlas_image1 = PBB_GE_TBXAS1_208130_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004796 |text = thromboxane-A synthase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016712 |text = oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001516 |text = prostaglandin biosynthetic process}} {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6916
| Hs_Ensembl = ENSG00000059377
| Hs_RefseqProtein = NP_001052
| Hs_RefseqmRNA = NM_001061
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 139124668
| Hs_GenLoc_end = 139366560
| Hs_Uniprot = P24557
| Mm_EntrezGene = 21391
| Mm_Ensembl = ENSMUSG00000029925
| Mm_RefseqmRNA = NM_011539
| Mm_RefseqProtein = NP_035669
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 38848593
| Mm_GenLoc_end = 39014194
| Mm_Uniprot = Q3UTF0
}}
}}
'''Thromboxane A synthase 1 (platelet, cytochrome P450, family 5, subfamily A)''', also known as '''TBXAS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TBXAS1 thromboxane A synthase 1 (platelet, cytochrome P450, family 5, subfamily A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6916| 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 a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. However, this protein is considered a member of the cytochrome P450 superfamily on the basis of sequence similarity rather than functional similarity. This endoplasmic reticulum membrane protein catalyzes the conversion of prostglandin H2 to thromboxane A2, a potent vasoconstrictor and inducer of platelet aggregation. The enzyme plays a role in several pathophysiological processes including hemostasis, cardiovascular disease, and stroke. The gene expresses two transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: TBXAS1 thromboxane A synthase 1 (platelet, cytochrome P450, family 5, subfamily A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6916| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Shen RF, Tai HH |title=Thromboxanes: synthase and receptors. |journal=J. Biomed. Sci. |volume=5 |issue= 3 |pages= 153-72 |year= 1998 |pmid= 9678486 |doi= }}
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Wang LH, Kulmacz RJ |title=Thromboxane synthase: structure and function of protein and gene. |journal=Prostaglandins Other Lipid Mediat. |volume=68-69 |issue= |pages= 409-22 |year= 2003 |pmid= 12432933 |doi= }}
*{{cite journal | author=Itoh S, Yanagimoto T, Tagawa S, ''et al.'' |title=Genomic organization of human fetal specific P-450IIIA7 (cytochrome P-450HFLa)-related gene(s) and interaction of transcriptional regulatory factor with its DNA element in the 5' flanking region. |journal=Biochim. Biophys. Acta |volume=1130 |issue= 2 |pages= 133-8 |year= 1992 |pmid= 1562592 |doi= }}
*{{cite journal | author=Yokoyama C, Miyata A, Ihara H, ''et al.'' |title=Molecular cloning of human platelet thromboxane A synthase. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 3 |pages= 1479-84 |year= 1991 |pmid= 1714723 |doi= }}
*{{cite journal | author=Ohashi K, Ruan KH, Kulmacz RJ, ''et al.'' |title=Primary structure of human thromboxane synthase determined from the cDNA sequence. |journal=J. Biol. Chem. |volume=267 |issue= 2 |pages= 789-93 |year= 1992 |pmid= 1730669 |doi= }}
*{{cite journal | author=Jones DA, Fitzpatrick FA, Malcolm KC |title=Thromboxane A2 synthesis in human erythroleukemia cells. |journal=Biochem. Biophys. Res. Commun. |volume=180 |issue= 1 |pages= 8-14 |year= 1991 |pmid= 1930241 |doi= }}
*{{cite journal | author=Wang LH, Ohashi K, Wu KK |title=Isolation of partial complementary DNA encoding human thromboxane synthase. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 1 |pages= 286-91 |year= 1991 |pmid= 2043115 |doi= }}
*{{cite journal | author=Nüsing R, Schneider-Voss S, Ullrich V |title=Immunoaffinity purification of human thromboxane synthase. |journal=Arch. Biochem. Biophys. |volume=280 |issue= 2 |pages= 325-30 |year= 1990 |pmid= 2195994 |doi= }}
*{{cite journal | author=Mestel F, Oetliker O, Beck E, ''et al.'' |title=Severe bleeding associated with defective thromboxane synthetase. |journal=Lancet |volume=1 |issue= 8160 |pages= 157 |year= 1980 |pmid= 6101498 |doi= }}
*{{cite journal | author=Miyata A, Yokoyama C, Ihara H, ''et al.'' |title=Characterization of the human gene (TBXAS1) encoding thromboxane synthase. |journal=Eur. J. Biochem. |volume=224 |issue= 2 |pages= 273-9 |year= 1994 |pmid= 7925341 |doi= }}
*{{cite journal | author=Wang LH, Tazawa R, Lang AQ, Wu KK |title=Alternate splicing of human thromboxane synthase mRNA. |journal=Arch. Biochem. Biophys. |volume=315 |issue= 2 |pages= 273-8 |year= 1995 |pmid= 7986068 |doi= 10.1006/abbi.1994.1500 }}
*{{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=Lee KD, Baek SJ, Shen RF |title=Cloning and characterization of the human thromboxane synthase gene promoter. |journal=Biochem. Biophys. Res. Commun. |volume=201 |issue= 1 |pages= 379-87 |year= 1994 |pmid= 8198598 |doi= 10.1006/bbrc.1994.1712 }}
*{{cite journal | author=Chase MB, Baek SJ, Purtell DC, ''et al.'' |title=Mapping of the human thromboxane synthase gene (TBXAS1) to chromosome 7q34-q35 by two-color fluorescence in situ hybridization. |journal=Genomics |volume=16 |issue= 3 |pages= 771-3 |year= 1993 |pmid= 8325653 |doi= 10.1006/geno.1993.1264 }}
*{{cite journal | author=Ruan KH, Wang LH, Wu KK, Kulmacz RJ |title=Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=268 |issue= 26 |pages= 19483-90 |year= 1993 |pmid= 8366093 |doi= }}
*{{cite journal | author=Tazawa R, Green ED, Ohashi K, ''et al.'' |title=Characterization of the complete genomic structure of human thromboxane synthase gene and functional analysis of its promoter. |journal=Arch. Biochem. Biophys. |volume=334 |issue= 2 |pages= 349-56 |year= 1996 |pmid= 8900410 |doi= 10.1006/abbi.1996.0464 }}
*{{cite journal | author=Baek SJ, Lee KD, Shen RF |title=Genomic structure and polymorphism of the human thromboxane synthase-encoding gene. |journal=Gene |volume=173 |issue= 2 |pages= 251-6 |year= 1996 |pmid= 8964509 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TFF2... {November 18, 2007 10:29:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:30:17 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = 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 = Trefoil factor 2 (spasmolytic protein 1)
| HGNCid = 11756
| Symbol = TFF2
| AltSymbols =; SML1; SP
| OMIM = 182590
| ECnumber =
| Homologene = 3956
| MGIid = 1306805
| GeneAtlas_image1 = PBB_GE_TFF2_214476_at_tn.png
| Function =
| Component =
| Process = {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007586 |text = digestion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7032
| Hs_Ensembl = ENSG00000160181
| Hs_RefseqProtein = NP_005414
| Hs_RefseqmRNA = NM_005423
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 42639538
| Hs_GenLoc_end = 42644176
| Hs_Uniprot = Q03403
| Mm_EntrezGene = 21785
| Mm_Ensembl = ENSMUSG00000024028
| Mm_RefseqmRNA = NM_009363
| Mm_RefseqProtein = NP_033389
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 30868938
| Mm_GenLoc_end = 30871294
| Mm_Uniprot = Q80YV5
}}
}}
'''Trefoil factor 2 (spasmolytic protein 1)''', also known as '''TFF2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TFF2 trefoil factor 2 (spasmolytic protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7032| 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 = Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. They are stable secretory proteins expressed in gastrointestinal mucosa. Their functions are not defined, but they may protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium. The encoded protein inhibits gastric acid secretion. This gene and two other related trefoil family member genes are found in a cluster on chromosome 21.<ref name="entrez">{{cite web | title = Entrez Gene: TFF2 trefoil factor 2 (spasmolytic protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7032| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Advenier C, Lagente V, Boichot E |title=The role of tachykinin receptor antagonists in the prevention of bronchial hyperresponsiveness, airway inflammation and cough. |journal=Eur. Respir. J. |volume=10 |issue= 8 |pages= 1892-906 |year= 1997 |pmid= 9272936 |doi= }}
*{{cite journal | author=Langer G, Jagla W, Behrens-Baumann W, ''et al.'' |title=Ocular TFF-peptides: new mucus-associated secretory products of conjunctival goblet cells. |journal=Adv. Exp. Med. Biol. |volume=506 |issue= Pt A |pages= 313-6 |year= 2003 |pmid= 12613926 |doi= }}
*{{cite journal | author=Tomasetto C, Rockel N, Mattei MG, ''et al.'' |title=The gene encoding the human spasmolytic protein (SML1/hSP) is in 21q 22.3, physically linked to the homologous breast cancer marker gene BCEI/pS2. |journal=Genomics |volume=13 |issue= 4 |pages= 1328-30 |year= 1992 |pmid= 1505966 |doi= }}
*{{cite journal | author=Tomasetto C, Rio MC, Gautier C, ''et al.'' |title=hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinoma. |journal=EMBO J. |volume=9 |issue= 2 |pages= 407-14 |year= 1990 |pmid= 2303034 |doi= }}
*{{cite journal | author=Bhogal N, Donnelly D, Findlay JB |title=The ligand binding site of the neurokinin 2 receptor. Site-directed mutagenesis and identification of neurokinin A binding residues in the human neurokinin 2 receptor. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27269-74 |year= 1994 |pmid= 7961636 |doi= }}
*{{cite journal | author=Hanby AM, Poulsom R, Singh S, ''et al.'' |title=Spasmolytic polypeptide is a major antral peptide: distribution of the trefoil peptides human spasmolytic polypeptide and pS2 in the stomach. |journal=Gastroenterology |volume=105 |issue= 4 |pages= 1110-6 |year= 1993 |pmid= 8405856 |doi= }}
*{{cite journal | author=Itoh H, Tomita M, Uchino H, ''et al.'' |title=cDNA cloning of rat pS2 peptide and expression of trefoil peptides in acetic acid-induced colitis. |journal=Biochem. J. |volume=318 ( Pt 3) |issue= |pages= 939-44 |year= 1996 |pmid= 8836141 |doi= }}
*{{cite journal | author=Gött P, Beck S, Machado JC, ''et al.'' |title=Human trefoil peptides: genomic structure in 21q22.3 and coordinated expression. |journal=Eur. J. Hum. Genet. |volume=4 |issue= 6 |pages= 308-15 |year= 1997 |pmid= 9043862 |doi= }}
*{{cite journal | author=May FE, Westley BR |title=Close physical linkage of the genes encoding the pNR-2/pS2 protein and human spasmolytic protein (hSP). |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 303-7 |year= 1997 |pmid= 9050913 |doi= }}
*{{cite journal | author=Seib T, Blin N, Hilgert K, ''et al.'' |title=The three human trefoil genes TFF1, TFF2, and TFF3 are located within a region of 55 kb on chromosome 21q22.3. |journal=Genomics |volume=40 |issue= 1 |pages= 200-2 |year= 1997 |pmid= 9070946 |doi= 10.1006/geno.1996.4511 }}
*{{cite journal | author=Kayademir T, Silva Edos S, Pusch C, ''et al.'' |title=A novel 25 bp tandem repeat within the human trefoil peptide gene TFF2 in 21q22.3: polymorphism and mammalian evolution. |journal=Eur. J. Hum. Genet. |volume=6 |issue= 2 |pages= 121-8 |year= 1998 |pmid= 9781055 |doi= 10.1038/sj.ejhg.5200166 }}
*{{cite journal | author=Brunelleschi S, Bordin G, Colangelo D, Viano I |title=Tachykinin receptors on human monocytes: their involvement in rheumatoid arthritis. |journal=Neuropeptides |volume=32 |issue= 3 |pages= 215-23 |year= 1999 |pmid= 10189055 |doi= }}
*{{cite journal | author=May FE, Semple JI, Newton JL, Westley BR |title=The human two domain trefoil protein, TFF2, is glycosylated in vivo in the stomach. |journal=Gut |volume=46 |issue= 4 |pages= 454-9 |year= 2000 |pmid= 10716671 |doi= }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Berry A, Scott HS, Kudoh J, ''et al.'' |title=Refined localization of autosomal recessive nonsyndromic deafness DFNB10 locus using 34 novel microsatellite markers, genomic structure, and exclusion of six known genes in the region. |journal=Genomics |volume=68 |issue= 1 |pages= 22-9 |year= 2001 |pmid= 10950923 |doi= 10.1006/geno.2000.6253 }}
*{{cite journal | author=Bulitta CJ, Fleming JV, Raychowdhury R, ''et al.'' |title=Autoinduction of the trefoil factor 2 (TFF2) promoter requires an upstream cis-acting element. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 366-74 |year= 2002 |pmid= 12054609 |doi= 10.1016/S0006-291X(02)00199-7 }}
*{{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=Hu GY, Yu BP, Dong WG, ''et al.'' |title=Expression of TFF2 and Helicobacter pylori infection in carcinogenesis of gastric mucosa. |journal=World J. Gastroenterol. |volume=9 |issue= 5 |pages= 910-4 |year= 2003 |pmid= 12717829 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGFBR3... {November 18, 2007 10:30:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:30:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| update_page = 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 = Transforming growth factor, beta receptor III
| HGNCid = 11774
| Symbol = TGFBR3
| AltSymbols =; BGCAN; betaglycan
| OMIM = 600742
| ECnumber =
| Homologene = 2436
| MGIid = 104637
| GeneAtlas_image1 = PBB_GE_TGFBR3_204731_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005539 |text = glycosaminoglycan binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7049
| Hs_Ensembl = ENSG00000069702
| Hs_RefseqProtein = NP_003234
| Hs_RefseqmRNA = NM_003243
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 91918488
| Hs_GenLoc_end = 92144147
| Hs_Uniprot = Q03167
| Mm_EntrezGene = 21814
| Mm_Ensembl = ENSMUSG00000029287
| Mm_RefseqmRNA = NM_011578
| Mm_RefseqProtein = NP_035708
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 107346872
| Mm_GenLoc_end = 107529822
| Mm_Uniprot = Q3TM82
}}
}}
'''Transforming growth factor, beta receptor III''', also known as '''TGFBR3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGFBR3 transforming growth factor, beta receptor III| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7049| 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=Massagué J |title=Receptors for the TGF-beta family. |journal=Cell |volume=69 |issue= 7 |pages= 1067-70 |year= 1992 |pmid= 1319842 |doi= }}
*{{cite journal | author=Border WA, Noble NA |title=Transforming growth factor beta in tissue fibrosis. |journal=N. Engl. J. Med. |volume=331 |issue= 19 |pages= 1286-92 |year= 1994 |pmid= 7935686 |doi= }}
*{{cite journal | author=Morén A, Ichijo H, Miyazono K |title=Molecular cloning and characterization of the human and porcine transforming growth factor-beta type III receptors. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 1 |pages= 356-62 |year= 1992 |pmid= 1333192 |doi= }}
*{{cite journal | author=López-Casillas F, Cheifetz S, Doody J, ''et al.'' |title=Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system. |journal=Cell |volume=67 |issue= 4 |pages= 785-95 |year= 1991 |pmid= 1657406 |doi= }}
*{{cite journal | author=Wang XF, Lin HY, Ng-Eaton E, ''et al.'' |title=Expression cloning and characterization of the TGF-beta type III receptor. |journal=Cell |volume=67 |issue= 4 |pages= 797-805 |year= 1991 |pmid= 1657407 |doi= }}
*{{cite journal | author=Lin HY, Moustakas A, Knaus P, ''et al.'' |title=The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. |journal=J. Biol. Chem. |volume=270 |issue= 6 |pages= 2747-54 |year= 1995 |pmid= 7852346 |doi= }}
*{{cite journal | author=López-Casillas F, Payne HM, Andres JL, Massagué J |title=Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites. |journal=J. Cell Biol. |volume=124 |issue= 4 |pages= 557-68 |year= 1994 |pmid= 8106553 |doi= }}
*{{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=Johnson DW, Qumsiyeh M, Benkhalifa M, Marchuk DA |title=Assignment of human transforming growth factor-beta type I and type III receptor genes (TGFBR1 and TGFBR3) to 9q33-q34 and 1p32-p33, respectively. |journal=Genomics |volume=28 |issue= 2 |pages= 356-7 |year= 1996 |pmid= 8530052 |doi= 10.1006/geno.1995.1157 }}
*{{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=Brown CB, Boyer AS, Runyan RB, Barnett JV |title=Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart. |journal=Science |volume=283 |issue= 5410 |pages= 2080-2 |year= 1999 |pmid= 10092230 |doi= }}
*{{cite journal | author=Gao J, Symons AL, Bartold PM |title=Expression of transforming growth factor-beta receptors types II and III within various cells in the rat periodontium. |journal=J. Periodont. Res. |volume=34 |issue= 2 |pages= 113-22 |year= 1999 |pmid= 10207840 |doi= }}
*{{cite journal | author=Lewis KA, Gray PC, Blount AL, ''et al.'' |title=Betaglycan binds inhibin and can mediate functional antagonism of activin signalling. |journal=Nature |volume=404 |issue= 6776 |pages= 411-4 |year= 2000 |pmid= 10746731 |doi= 10.1038/35006129 }}
*{{cite journal | author=Zippert R, Bässler A, Holmer SR, ''et al.'' |title=Eleven single nucleotide polymorphisms and one triple nucleotide insertion of the human TGF-beta III receptor gene. |journal=J. Hum. Genet. |volume=45 |issue= 4 |pages= 250-3 |year= 2000 |pmid= 10944857 |doi= }}
*{{cite journal | author=Rotzer D, Roth M, Lutz M, ''et al.'' |title=Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor. |journal=EMBO J. |volume=20 |issue= 3 |pages= 480-90 |year= 2001 |pmid= 11157754 |doi= 10.1093/emboj/20.3.480 }}
*{{cite journal | author=Blobe GC, Schiemann WP, Pepin MC, ''et al.'' |title=Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 24627-37 |year= 2001 |pmid= 11323414 |doi= 10.1074/jbc.M100188200 }}
*{{cite journal | author=De Crescenzo G, Grothe S, Zwaagstra J, ''et al.'' |title=Real-time monitoring of the interactions of transforming growth factor-beta (TGF-beta ) isoforms with latency-associated protein and the ectodomains of the TGF-beta type II and III receptors reveals different kinetic models and stoichiometries of binding. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29632-43 |year= 2001 |pmid= 11382746 |doi= 10.1074/jbc.M009765200 }}
*{{cite journal | author=Blobe GC, Liu X, Fang SJ, ''et al.'' |title=A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 39608-17 |year= 2001 |pmid= 11546783 |doi= 10.1074/jbc.M106831200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TK1... {November 18, 2007 10:30:45 PM PST}
- SEARCH REDIRECT: Control Box Found: Thymidine kinase 1 {November 18, 2007 10:31:49 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:31:50 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:31:50 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:31:50 PM PST}
- UPDATED: Updated protein page: Thymidine kinase 1 {November 18, 2007 10:31:57 PM PST}
- INFO: Beginning work on USF2... {November 18, 2007 10:31:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:32:56 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 = Upstream transcription factor 2, c-fos interacting
| HGNCid = 12594
| Symbol = USF2
| AltSymbols =; FIP
| OMIM = 600390
| ECnumber =
| Homologene = 2527
| MGIid = 99961
| GeneAtlas_image1 = PBB_GE_USF2_202152_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_USF2_214879_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_USF2_215737_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007595 |text = lactation}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7392
| Hs_Ensembl = ENSG00000105698
| Hs_RefseqProtein = NP_003358
| Hs_RefseqmRNA = NM_003367
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 40451721
| Hs_GenLoc_end = 40462558
| Hs_Uniprot = Q15853
| Mm_EntrezGene = 22282
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001001413
| Mm_RefseqProtein = XP_001001413
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Upstream transcription factor 2, c-fos interacting''', also known as '''USF2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: USF2 upstream transcription factor 2, c-fos interacting| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7392| 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 a member of the basic helix-loop-helix leucine zipper family, and can function as a cellular transcription factor. The encoded protein can activate transcription through pyrimidine-rich initiator (Inr) elements and E-box motifs. Two transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: USF2 upstream transcription factor 2, c-fos interacting| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7392| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Corre S, Galibert MD |title=[USF as a key regulatory element of gene expression] |journal=Med Sci (Paris) |volume=22 |issue= 1 |pages= 62-7 |year= 2006 |pmid= 16386222 |doi= }}
*{{cite journal | author=Sirito M, Walker S, Lin Q, ''et al.'' |title=Members of the USF family of helix-loop-helix proteins bind DNA as homo- as well as heterodimers. |journal=Gene Expr. |volume=2 |issue= 3 |pages= 231-40 |year= 1993 |pmid= 1450663 |doi= }}
*{{cite journal | author=Blanar MA, Rutter WJ |title=Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos. |journal=Science |volume=256 |issue= 5059 |pages= 1014-8 |year= 1992 |pmid= 1589769 |doi= }}
*{{cite journal | author=Viollet B, Lefrançois-Martinez AM, Henrion A, ''et al.'' |title=Immunochemical characterization and transacting properties of upstream stimulatory factor isoforms. |journal=J. Biol. Chem. |volume=271 |issue= 3 |pages= 1405-15 |year= 1996 |pmid= 8576131 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Groenen PM, Garcia E, Debeer P, ''et al.'' |title=Structure, sequence, and chromosome 19 localization of human USF2 and its rearrangement in a patient with multicystic renal dysplasia. |journal=Genomics |volume=38 |issue= 2 |pages= 141-8 |year= 1997 |pmid= 8954795 |doi= }}
*{{cite journal | author=Ghosh AK, Datta PK, Jacob ST |title=The dual role of helix-loop--helix-zipper protein USF in ribosomal RNA gene transcription in vivo. |journal=Oncogene |volume=14 |issue= 5 |pages= 589-94 |year= 1997 |pmid= 9053857 |doi= 10.1038/sj.onc.1200866 }}
*{{cite journal | author=Kurschner C, Morgan JI |title=USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its bHLH domain and inhibits c-Maf DNA binding activity. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 2 |pages= 333-9 |year= 1997 |pmid= 9070273 |doi= 10.1006/bbrc.1997.6097 }}
*{{cite journal | author=Breen GA, Jordan EM |title=Regulation of the nuclear gene that encodes the alpha-subunit of the mitochondrial F0F1-ATP synthase complex. Activation by upstream stimulatory factor 2. |journal=J. Biol. Chem. |volume=272 |issue= 16 |pages= 10538-42 |year= 1997 |pmid= 9099698 |doi= }}
*{{cite journal | author=Nechushtan H, Zhang Z, Razin E |title=Microphthalmia (mi) in murine mast cells: regulation of its stimuli-mediated expression on the translational level. |journal=Blood |volume=89 |issue= 8 |pages= 2999-3008 |year= 1997 |pmid= 9108421 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Breen GA, Jordan EM |title=Transcriptional activation of the F(1)F(0) ATP synthase alpha-subunit initiator element by USF2 is mediated by p300. |journal=Biochim. Biophys. Acta |volume=1428 |issue= 2-3 |pages= 169-76 |year= 1999 |pmid= 10434034 |doi= }}
*{{cite journal | author=Kumari D, Usdin K |title=Interaction of the transcription factors USF1, USF2, and alpha -Pal/Nrf-1 with the FMR1 promoter. Implications for Fragile X mental retardation syndrome. |journal=J. Biol. Chem. |volume=276 |issue= 6 |pages= 4357-64 |year= 2001 |pmid= 11058604 |doi= 10.1074/jbc.M009629200 }}
*{{cite journal | author=Kolonics A, Apáti A, Nahajevszky S, ''et al.'' |title=Unregulated activation of STAT-5, ERK1/2 and c-Fos may contribute to the phenotypic transformation from myelodysplastic syndrome to acute leukaemia. |journal=Haematologia (Budap) |volume=31 |issue= 2 |pages= 125-38 |year= 2002 |pmid= 11583024 |doi= }}
*{{cite journal | author=Bengtsson SH, Madeyski-Bengtson K, Nilsson J, Bjursell G |title=Transcriptional regulation of the human carboxyl ester lipase gene in THP-1 monocytes: an E-box required for activation binds upstream stimulatory factors 1 and 2. |journal=Biochem. J. |volume=365 |issue= Pt 2 |pages= 481-8 |year= 2002 |pmid= 11945176 |doi= 10.1042/BJ20020223 }}
*{{cite journal | author=Villavicencio EH, Yoon JW, Frank DJ, ''et al.'' |title=Cooperative E-box regulation of human GLI1 by TWIST and USF. |journal=Genesis |volume=32 |issue= 4 |pages= 247-58 |year= 2002 |pmid= 11948912 |doi= }}
*{{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=Moore ML, Park EA, McMillin JB |title=Upstream stimulatory factor represses the induction of carnitine palmitoyltransferase-Ibeta expression by PGC-1. |journal=J. Biol. Chem. |volume=278 |issue= 19 |pages= 17263-8 |year= 2003 |pmid= 12611894 |doi= 10.1074/jbc.M210486200 }}
*{{cite journal | author=Pickwell GV, Shih H, Quattrochi LC |title=Interaction of upstream stimulatory factor proteins with an E-box located within the human CYP1A2 5'-flanking gene contributes to basal transcriptional gene activation. |journal=Biochem. Pharmacol. |volume=65 |issue= 7 |pages= 1087-96 |year= 2003 |pmid= 12663044 |doi= }}
*{{cite journal | author=Zhu J, Giannola DM, Zhang Y, ''et al.'' |title=NF-Y cooperates with USF1/2 to induce the hematopoietic expression of HOXB4. |journal=Blood |volume=102 |issue= 7 |pages= 2420-7 |year= 2003 |pmid= 12791656 |doi= 10.1182/blood-2003-01-0251 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on WNK1... {November 18, 2007 10:34:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:35:29 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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_WNK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1t4h.
| PDB = {{PDB2|1t4h}}
| Name = WNK lysine deficient protein kinase 1
| HGNCid = 14540
| Symbol = WNK1
| AltSymbols =; KDP; KIAA0344; PHA2C; PRKWNK1
| OMIM = 605232
| ECnumber =
| Homologene = 14253
| MGIid = 2442092
| GeneAtlas_image1 = PBB_GE_WNK1_211992_at_tn.png
| GeneAtlas_image2 = PBB_GE_WNK1_211993_at_tn.png
| GeneAtlas_image3 = PBB_GE_WNK1_211994_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004860 |text = protein kinase inhibitor 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:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0042598 |text = vesicular fraction}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}} {{GNF_GO|id=GO:0050794 |text = regulation of cellular process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 65125
| Hs_Ensembl = ENSG00000060237
| Hs_RefseqProtein = NP_061852
| Hs_RefseqmRNA = NM_018979
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 732993
| Hs_GenLoc_end = 888219
| Hs_Uniprot = Q9H4A3
| Mm_EntrezGene = 232341
| Mm_Ensembl = ENSMUSG00000045962
| Mm_RefseqmRNA = XM_001004362
| Mm_RefseqProtein = XP_001004362
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 119889590
| Mm_GenLoc_end = 120004226
| Mm_Uniprot = Q3TU87
}}
}}
'''WNK lysine deficient protein kinase 1''', also known as '''WNK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: WNK1 WNK lysine deficient protein kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65125| 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 WNK1 gene encodes a cytoplasmic serine-threonine kinase expressed in distal nephron.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: WNK1 WNK lysine deficient protein kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65125| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hart GW, Haltiwanger RS, Holt GD, Kelly WG |title=Nucleoplasmic and cytoplasmic glycoproteins. |journal=Ciba Found. Symp. |volume=145 |issue= |pages= 102-12, discussion 112-8 |year= 1989 |pmid= 2507249 |doi= }}
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Xu BE, Lee BH, Min X, ''et al.'' |title=WNK1: analysis of protein kinase structure, downstream targets, and potential roles in hypertension. |journal=Cell Res. |volume=15 |issue= 1 |pages= 6-10 |year= 2005 |pmid= 15686619 |doi= 10.1038/sj.cr.7290256 }}
*{{cite journal | author=Subramanya AR, Yang CL, McCormick JA, Ellison DH |title=WNK kinases regulate sodium chloride and potassium transport by the aldosterone-sensitive distal nephron. |journal=Kidney Int. |volume=70 |issue= 4 |pages= 630-4 |year= 2006 |pmid= 16820787 |doi= 10.1038/sj.ki.5001634 }}
*{{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=Nagase T, Ishikawa K, Nakajima D, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=4 |issue= 2 |pages= 141-50 |year= 1997 |pmid= 9205841 |doi= }}
*{{cite journal | author=Moore TM, Garg R, Johnson C, ''et al.'' |title=PSK, a novel STE20-like kinase derived from prostatic carcinoma that activates the c-Jun N-terminal kinase mitogen-activated protein kinase pathway and regulates actin cytoskeletal organization. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4311-22 |year= 2000 |pmid= 10660600 |doi= }}
*{{cite journal | author=Disse-Nicodème S, Achard JM, Desitter I, ''et al.'' |title=A new locus on chromosome 12p13.3 for pseudohypoaldosteronism type II, an autosomal dominant form of hypertension. |journal=Am. J. Hum. Genet. |volume=67 |issue= 2 |pages= 302-10 |year= 2000 |pmid= 10869238 |doi= }}
*{{cite journal | author=Wilson FH, Disse-Nicodème S, Choate KA, ''et al.'' |title=Human hypertension caused by mutations in WNK kinases. |journal=Science |volume=293 |issue= 5532 |pages= 1107-12 |year= 2001 |pmid= 11498583 |doi= 10.1126/science.1062844 }}
*{{cite journal | author=Veríssimo F, Jordan P |title=WNK kinases, a novel protein kinase subfamily in multi-cellular organisms. |journal=Oncogene |volume=20 |issue= 39 |pages= 5562-9 |year= 2001 |pmid= 11571656 |doi= 10.1038/sj.onc.1204726 }}
*{{cite journal | author=Xu BE, Min X, Stippec S, ''et al.'' |title=Regulation of WNK1 by an autoinhibitory domain and autophosphorylation. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48456-62 |year= 2003 |pmid= 12374799 |doi= 10.1074/jbc.M207917200 }}
*{{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=Vitari AC, Deak M, Collins BJ, ''et al.'' |title=WNK1, the kinase mutated in an inherited high-blood-pressure syndrome, is a novel PKB (protein kinase B)/Akt substrate. |journal=Biochem. J. |volume=378 |issue= Pt 1 |pages= 257-68 |year= 2004 |pmid= 14611643 |doi= 10.1042/BJ20031692 }}
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*{{cite journal | author=Xu BE, Stippec S, Lenertz L, ''et al.'' |title=WNK1 activates ERK5 by an MEKK2/3-dependent mechanism. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 7826-31 |year= 2004 |pmid= 14681216 |doi= 10.1074/jbc.M313465200 }}
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*{{cite journal | author=Lee BH, Min X, Heise CJ, ''et al.'' |title=WNK1 phosphorylates synaptotagmin 2 and modulates its membrane binding. |journal=Mol. Cell |volume=15 |issue= 5 |pages= 741-51 |year= 2004 |pmid= 15350218 |doi= 10.1016/j.molcel.2004.07.018 }}
}}
{{refend}}
{{protein-stub}}
end log.
