Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:11, 19 November 2007 (UTC)[edit]
Proteins without matches (7)[edit]
Proteins with a High Potential Match (3)[edit]
Redirected Proteins (15)[edit]
Manual Inspection (Page not found) (10)[edit]
Updated (15)[edit]
Protein Status Grid - Date: 19:11, 19 November 2007 (UTC)[edit]
Vebose Log - Date: 19:11, 19 November 2007 (UTC)[edit]
- INFO: Beginning work on BDKRB1... {November 19, 2007 10:44:31 AM PST}
- SEARCH REDIRECT: Control Box Found: BDKRB1 {November 19, 2007 10:45:07 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:45:10 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:45:10 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:45:10 AM PST}
- UPDATED: Updated protein page: BDKRB1 {November 19, 2007 10:45:17 AM PST}
- INFO: Beginning work on BMP1... {November 19, 2007 10:45:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:46:22 AM 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 = Bone morphogenetic protein 1
| HGNCid = 1067
| Symbol = BMP1
| AltSymbols =; FLJ44432; PCOLC; PCP; TLD
| OMIM = 112264
| ECnumber =
| Homologene = 55955
| MGIid = 88176
| GeneAtlas_image1 = PBB_GE_BMP1_207595_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BMP1_205574_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_BMP1_206725_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008533 |text = astacin activity}} {{GNF_GO|id=GO:0017026 |text = procollagen C-endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001502 |text = cartilage condensation}} {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 649
| Hs_Ensembl = ENSG00000168487
| Hs_RefseqProtein = NP_001190
| Hs_RefseqmRNA = NM_001199
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 22078376
| Hs_GenLoc_end = 22125784
| Hs_Uniprot = P13497
| Mm_EntrezGene = 12153
| Mm_Ensembl = ENSMUSG00000022098
| Mm_RefseqmRNA = NM_009755
| Mm_RefseqProtein = NP_033885
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 69209636
| Mm_GenLoc_end = 69255268
| Mm_Uniprot = Q6P550
}}
}}
'''Bone morphogenetic protein 1''', also known as '''BMP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BMP1 bone morphogenetic protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=649| 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 BMP1 locus encodes a protein that is capable of inducing formation of cartilage in vivo. Although other bone morphogenetic proteins are members of the TGF-beta superfamily, BMP1 encodes a protein that is not closely related to other known growth factors. BMP1 protein and procollagen C proteinase (PCP), a secreted metalloprotease requiring calcium and needed for cartilage and bone formation, are identical. PCP or BMP1 protein cleaves the C-terminal propeptides of procollagen I, II, and III and its activity is increased by the procollagen C-endopeptidase enhancer protein. The BMP1 gene is expressed as alternatively spliced variants that share an N-terminal protease domain but differ in their C-terminal region<ref name="entrez">{{cite web | title = Entrez Gene: BMP1 bone morphogenetic protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=649| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tabas JA, Zasloff M, Wasmuth JJ, ''et al.'' |title=Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3. |journal=Genomics |volume=9 |issue= 2 |pages= 283-9 |year= 1991 |pmid= 2004778 |doi= }}
*{{cite journal | author=Wozney JM, Rosen V, Celeste AJ, ''et al.'' |title=Novel regulators of bone formation: molecular clones and activities. |journal=Science |volume=242 |issue= 4885 |pages= 1528-34 |year= 1989 |pmid= 3201241 |doi= }}
*{{cite journal | author=Takahara K, Lyons GE, Greenspan DS |title=Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32572-8 |year= 1995 |pmid= 7798260 |doi= }}
*{{cite journal | author=Yoshiura K, Tamura T, Hong HS, ''et al.'' |title=Mapping of the bone morphogenetic protein 1 gene (BMP1) to 8p21: removal of BMP1 from candidacy for the bone disorder in Langer-Giedion syndrome. |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3-4 |pages= 208-9 |year= 1993 |pmid= 8404039 |doi= }}
*{{cite journal | author=Takahara K, Lee S, Wood S, Greenspan DS |title=Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene. |journal=Genomics |volume=29 |issue= 1 |pages= 9-15 |year= 1996 |pmid= 8530106 |doi= 10.1006/geno.1995.1209 }}
*{{cite journal | author=Kessler E, Takahara K, Biniaminov L, ''et al.'' |title=Bone morphogenetic protein-1: the type I procollagen C-proteinase. |journal=Science |volume=271 |issue= 5247 |pages= 360-2 |year= 1996 |pmid= 8553073 |doi= }}
*{{cite journal | author=Li SW, Sieron AL, Fertala A, ''et al.'' |title=The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 5127-30 |year= 1996 |pmid= 8643539 |doi= }}
*{{cite journal | author=Janitz M, Heiser V, Böttcher U, ''et al.'' |title=Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein-1. |journal=J. Mol. Med. |volume=76 |issue= 2 |pages= 141-6 |year= 1998 |pmid= 9500680 |doi= }}
*{{cite journal | author=Scott IC, Blitz IL, Pappano WN, ''et al.'' |title=Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis. |journal=Dev. Biol. |volume=213 |issue= 2 |pages= 283-300 |year= 1999 |pmid= 10479448 |doi= 10.1006/dbio.1999.9383 }}
*{{cite journal | author=Amano S, Scott IC, Takahara K, ''et al.'' |title=Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 22728-35 |year= 2000 |pmid= 10806203 |doi= 10.1074/jbc.M002345200 }}
*{{cite journal | author=Scott IC, Blitz IL, Pappano WN, ''et al.'' |title=Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling. |journal=Nature |volume=410 |issue= 6827 |pages= 475-8 |year= 2001 |pmid= 11260715 |doi= 10.1038/35068572 }}
*{{cite journal | author=Garrigue-Antar L, Barker C, Kadler KE |title=Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26237-42 |year= 2001 |pmid= 11283002 |doi= 10.1074/jbc.M010814200 }}
*{{cite journal | author=Unsöld C, Pappano WN, Imamura Y, ''et al.'' |title=Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5596-602 |year= 2002 |pmid= 11741999 |doi= 10.1074/jbc.M110003200 }}
*{{cite journal | author=Rattenholl A, Pappano WN, Koch M, ''et al.'' |title=Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen. |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26372-8 |year= 2002 |pmid= 11986329 |doi= 10.1074/jbc.M203247200 }}
*{{cite journal | author=Garrigue-Antar L, Hartigan N, Kadler KE |title=Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 43327-34 |year= 2003 |pmid= 12218058 |doi= 10.1074/jbc.M207342200 }}
*{{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=Hartigan N, Garrigue-Antar L, Kadler KE |title=Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity. |journal=J. Biol. Chem. |volume=278 |issue= 20 |pages= 18045-9 |year= 2003 |pmid= 12637537 |doi= 10.1074/jbc.M211448200 }}
*{{cite journal | author=Leighton M, Kadler KE |title=Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 in the trans-Golgi network. |journal=J. Biol. Chem. |volume=278 |issue= 20 |pages= 18478-84 |year= 2003 |pmid= 12637569 |doi= 10.1074/jbc.M213021200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DCLRE1C... {November 19, 2007 11:02:28 AM PST}
- SEARCH REDIRECT: Control Box Found: DCLRE1C {November 19, 2007 11:03:39 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:03:41 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:03:41 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:03:41 AM PST}
- UPDATED: Updated protein page: DCLRE1C {November 19, 2007 11:03:47 AM PST}
- INFO: Beginning work on FOXL2... {November 19, 2007 10:46:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:47:03 AM 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 = Forkhead box L2
| HGNCid = 1092
| Symbol = FOXL2
| AltSymbols =; BPES; BPES1; PFRK; PINTO; POF3
| OMIM = 605597
| ECnumber =
| Homologene = 74992
| MGIid = 1349428
| GeneAtlas_image1 = PBB_GE_FOXL2_220102_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043028 |text = caspase regulator activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0002074 |text = extraocular skeletal muscle development}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0019101 |text = female somatic sex determination}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0042703 |text = menstruation}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}} {{GNF_GO|id=GO:0043280 |text = positive regulation of caspase activity}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 668
| Hs_Ensembl = ENSG00000183770
| Hs_RefseqProtein = XP_001131060
| Hs_RefseqmRNA = XM_001131060
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 140147124
| Hs_GenLoc_end = 140148254
| Hs_Uniprot = P58012
| Mm_EntrezGene = 26927
| Mm_Ensembl = ENSMUSG00000050397
| Mm_RefseqmRNA = XM_976602
| Mm_RefseqProtein = XP_981696
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 98765013
| Mm_GenLoc_end = 98766140
| Mm_Uniprot = Q2TVT7
}}
}}
'''Forkhead box L2''', also known as '''FOXL2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FOXL2 forkhead box L2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=668| 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=de Die-Smulders CE, Engelen JJ, Donk JM, Fryns JP |title=Further evidence for the location of the BPES gene at 3q2. |journal=J. Med. Genet. |volume=28 |issue= 10 |pages= 725 |year= 1991 |pmid= 1941972 |doi= }}
*{{cite journal | author=Vaiman D, Schibler L, Oustry-Vaiman A, ''et al.'' |title=High-resolution human/goat comparative map of the goat polled/intersex syndrome (PIS): the human homologue is contained in a human YAC from HSA3q23. |journal=Genomics |volume=56 |issue= 1 |pages= 31-9 |year= 1999 |pmid= 10036183 |doi= 10.1006/geno.1998.5691 }}
*{{cite journal | author=Kaestner KH, Knochel W, Martinez DE |title=Unified nomenclature for the winged helix/forkhead transcription factors. |journal=Genes Dev. |volume=14 |issue= 2 |pages= 142-6 |year= 2000 |pmid= 10702024 |doi= }}
*{{cite journal | author=Crisponi L, Deiana M, Loi A, ''et al.'' |title=The putative forkhead transcription factor FOXL2 is mutated in blepharophimosis/ptosis/epicanthus inversus syndrome. |journal=Nat. Genet. |volume=27 |issue= 2 |pages= 159-66 |year= 2001 |pmid= 11175783 |doi= 10.1038/84781 }}
*{{cite journal | author=De Baere E, Dixon MJ, Small KW, ''et al.'' |title=Spectrum of FOXL2 gene mutations in blepharophimosis-ptosis-epicanthus inversus (BPES) families demonstrates a genotype--phenotype correlation. |journal=Hum. Mol. Genet. |volume=10 |issue= 15 |pages= 1591-600 |year= 2001 |pmid= 11468277 |doi= }}
*{{cite journal | author=Dollfus H, Kumaramanickavel G, Biswas P, ''et al.'' |title=Identification of a new TWIST mutation (7p21) with variable eyelid manifestations supports locus homogeneity of BPES at 3q22. |journal=J. Med. Genet. |volume=38 |issue= 7 |pages= 470-2 |year= 2001 |pmid= 11474656 |doi= }}
*{{cite journal | author=Yamada T, Hayasaka S, Matsumoto M, ''et al.'' |title=Heterozygous 17-bp deletion in the forkhead transcription factor gene, FOXL2, in a Japanese family with blepharophimosis-ptosis-epicanthus inversus syndrome. |journal=J. Hum. Genet. |volume=46 |issue= 12 |pages= 733-6 |year= 2002 |pmid= 11776388 |doi= }}
*{{cite journal | author=Kosaki K, Ogata T, Kosaki R, ''et al.'' |title=A novel mutation in the FOXL2 gene in a patient with blepharophimosis syndrome: differential role of the polyalanine tract in the development of the ovary and the eyelid. |journal=Ophthalmic Genet. |volume=23 |issue= 1 |pages= 43-7 |year= 2002 |pmid= 11910558 |doi= }}
*{{cite journal | author=Bell R, Murday VA, Patton MA, Jeffery S |title=Two families with blepharophimosis/ptosis/epicanthus inversus syndrome have mutations in the putative forkhead transcription factor FOXL2. |journal=Genet. Test. |volume=5 |issue= 4 |pages= 335-8 |year= 2002 |pmid= 11960581 |doi= 10.1089/109065701753617499 }}
*{{cite journal | author=Harris SE, Chand AL, Winship IM, ''et al.'' |title=Identification of novel mutations in FOXL2 associated with premature ovarian failure. |journal=Mol. Hum. Reprod. |volume=8 |issue= 8 |pages= 729-33 |year= 2003 |pmid= 12149404 |doi= }}
*{{cite journal | author=De Baere E, Lemercier B, Christin-Maitre S, ''et al.'' |title=FOXL2 mutation screening in a large panel of POF patients and XX males. |journal=J. Med. Genet. |volume=39 |issue= 8 |pages= e43 |year= 2002 |pmid= 12161610 |doi= }}
*{{cite journal | author=Ramírez-Castro JL, Pineda-Trujillo N, Valencia AV, ''et al.'' |title=Mutations in FOXL2 underlying BPES (types 1 and 2) in Colombian families. |journal=Am. J. Med. Genet. |volume=113 |issue= 1 |pages= 47-51 |year= 2003 |pmid= 12400065 |doi= 10.1002/ajmg.10741 }}
*{{cite journal | author=Cocquet J, Pailhoux E, Jaubert F, ''et al.'' |title=Evolution and expression of FOXL2. |journal=J. Med. Genet. |volume=39 |issue= 12 |pages= 916-21 |year= 2003 |pmid= 12471206 |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=De Baere E, Beysen D, Oley C, ''et al.'' |title=FOXL2 and BPES: mutational hotspots, phenotypic variability, and revision of the genotype-phenotype correlation. |journal=Am. J. Hum. Genet. |volume=72 |issue= 2 |pages= 478-87 |year= 2003 |pmid= 12529855 |doi= }}
*{{cite journal | author=Mazumdar A, Kumar R |title=Estrogen regulation of Pak1 and FKHR pathways in breast cancer cells. |journal=FEBS Lett. |volume=535 |issue= 1-3 |pages= 6-10 |year= 2003 |pmid= 12560069 |doi= }}
*{{cite journal | author=Fokstuen S, Antonarakis SE, Blouin JL |title=FOXL2-mutations in blepharophimosis-ptosis-epicanthus inversus syndrome (BPES); challenges for genetic counseling in female patients. |journal=Am. J. Med. Genet. A |volume=117 |issue= 2 |pages= 143-6 |year= 2003 |pmid= 12567411 |doi= 10.1002/ajmg.a.10024 }}
*{{cite journal | author=Dollfus H, Stoetzel C, Riehm S, ''et al.'' |title=Sporadic and familial blepharophimosis -ptosis-epicanthus inversus syndrome: FOXL2 mutation screen and MRI study of the superior levator eyelid muscle. |journal=Clin. Genet. |volume=63 |issue= 2 |pages= 117-20 |year= 2003 |pmid= 12630957 |doi= }}
*{{cite journal | author=Udar N, Yellore V, Chalukya M, ''et al.'' |title=Comparative analysis of the FOXL2 gene and characterization of mutations in BPES patients. |journal=Hum. Mutat. |volume=22 |issue= 3 |pages= 222-8 |year= 2003 |pmid= 12938087 |doi= 10.1002/humu.10251 }}
*{{cite journal | author=Crisponi L, Uda M, Deiana M, ''et al.'' |title=FOXL2 inactivation by a translocation 171 kb away: analysis of 500 kb of chromosome 3 for candidate long-range regulatory sequences. |journal=Genomics |volume=83 |issue= 5 |pages= 757-64 |year= 2004 |pmid= 15081106 |doi= 10.1016/j.ygeno.2003.11.010 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITSN1... {November 19, 2007 10:59:23 AM PST}
- SEARCH REDIRECT: Control Box Found: ITSN1 {November 19, 2007 10:59:58 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:59:59 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:59:59 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:59:59 AM PST}
- UPDATED: Updated protein page: ITSN1 {November 19, 2007 11:00:05 AM PST}
- INFO: Beginning work on LCP1... {November 19, 2007 10:47:03 AM PST}
- SEARCH REDIRECT: Control Box Found: LCP1 {November 19, 2007 10:48:06 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:48:07 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:48:07 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:48:07 AM PST}
- UPDATED: Updated protein page: LCP1 {November 19, 2007 10:48:14 AM PST}
- INFO: Beginning work on LMO2... {November 19, 2007 10:48:14 AM PST}
- SEARCH REDIRECT: Control Box Found: LMO2 {November 19, 2007 10:48:46 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:48:49 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:48:49 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:48:49 AM PST}
- UPDATED: Updated protein page: LMO2 {November 19, 2007 10:48:56 AM PST}
- INFO: Beginning work on MAP3K3... {November 19, 2007 10:48:57 AM PST}
- SEARCH REDIRECT: Control Box Found: MAP3K3 {November 19, 2007 10:49:34 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:49:37 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:49:37 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:49:37 AM PST}
- UPDATED: Updated protein page: MAP3K3 {November 19, 2007 10:49:43 AM PST}
- INFO: Beginning work on MFI2... {November 19, 2007 10:49:43 AM PST}
- SEARCH REDIRECT: Control Box Found: MFI2 {November 19, 2007 10:50:20 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:50:23 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:50:23 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:50:23 AM PST}
- UPDATED: Updated protein page: MFI2 {November 19, 2007 10:50:29 AM PST}
- INFO: Beginning work on MTR... {November 19, 2007 10:50:29 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:50:59 AM 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_MTR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2o2k.
| PDB = {{PDB2|2o2k}}
| Name = 5-methyltetrahydrofolate-homocysteine methyltransferase
| HGNCid = 7468
| Symbol = MTR
| AltSymbols =; FLJ45386
| OMIM = 156570
| ECnumber =
| Homologene = 37280
| MGIid = 894292
| GeneAtlas_image1 = PBB_GE_MTR_203774_at_tn.png
| Function = {{GNF_GO|id=GO:0004156 |text = dihydropteroate synthase activity}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008705 |text = methionine synthase activity}} {{GNF_GO|id=GO:0008898 |text = homocysteine S-methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0031419 |text = cobalamin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050897 |text = cobalt ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}} {{GNF_GO|id=GO:0009086 |text = methionine biosynthetic process}} {{GNF_GO|id=GO:0009396 |text = folic acid and derivative biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4548
| Hs_Ensembl = ENSG00000116984
| Hs_RefseqProtein = NP_000245
| Hs_RefseqmRNA = NM_000254
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 235025233
| Hs_GenLoc_end = 235133904
| Hs_Uniprot = Q99707
| Mm_EntrezGene = 238505
| Mm_Ensembl = ENSMUSG00000021311
| Mm_RefseqmRNA = XM_138431
| Mm_RefseqProtein = XP_138431
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 12266633
| Mm_GenLoc_end = 12312446
| Mm_Uniprot =
}}
}}
'''5-methyltetrahydrofolate-homocysteine methyltransferase''', also known as '''MTR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MTR 5-methyltetrahydrofolate-homocysteine methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4548| 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 = MTR encodes the enzyme 5-methyltetrahydrofolate-homocysteine methyltransferase. This enzyme, also known as cobalamin-dependent methionine synthase, catalyzes the final step in methionine biosynthesis. Mutations in MTR have been identified as the underlying cause of methylcobalamin deficiency complementation group G.<ref name="entrez">{{cite web | title = Entrez Gene: MTR 5-methyltetrahydrofolate-homocysteine methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4548| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Banerjee RV, Matthews RG |title=Cobalamin-dependent methionine synthase. |journal=FASEB J. |volume=4 |issue= 5 |pages= 1450-9 |year= 1990 |pmid= 2407589 |doi= }}
*{{cite journal | author=Ludwig ML, Matthews RG |title=Structure-based perspectives on B12-dependent enzymes. |journal=Annu. Rev. Biochem. |volume=66 |issue= |pages= 269-313 |year= 1997 |pmid= 9242908 |doi= 10.1146/annurev.biochem.66.1.269 }}
*{{cite journal | author=Matthews RG, Sheppard C, Goulding C |title=Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology. |journal=Eur. J. Pediatr. |volume=157 Suppl 2 |issue= |pages= S54-9 |year= 1998 |pmid= 9587027 |doi= }}
*{{cite journal | author=Garovic-Kocic V, Rosenblatt DS |title=Methionine auxotrophy in inborn errors of cobalamin metabolism. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=15 |issue= 4 |pages= 395-400 |year= 1992 |pmid= 1516297 |doi= }}
*{{cite journal | author=O'Connor DL, Moriarty P, Picciano MF |title=The impact of iron deficiency on the flux of folates within the mammary gland. |journal=International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition |volume=62 |issue= 2 |pages= 173-80 |year= 1992 |pmid= 1517041 |doi= }}
*{{cite journal | author=Everman BW, Koblin DD |title=Aging, chronic administration of ethanol, and acute exposure to nitrous oxide: effects on vitamin B12 and folate status in rats. |journal=Mech. Ageing Dev. |volume=62 |issue= 3 |pages= 229-43 |year= 1992 |pmid= 1583909 |doi= }}
*{{cite journal | author=Vassiliadis A, Rosenblatt DS, Cooper BA, Bergeron JJ |title=Lysosomal cobalamin accumulation in fibroblasts from a patient with an inborn error of cobalamin metabolism (cblF complementation group): visualization by electron microscope radioautography. |journal=Exp. Cell Res. |volume=195 |issue= 2 |pages= 295-302 |year= 1991 |pmid= 2070814 |doi= }}
*{{cite journal | author=Li YN, Gulati S, Baker PJ, ''et al.'' |title=Cloning, mapping and RNA analysis of the human methionine synthase gene. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 1851-8 |year= 1997 |pmid= 8968735 |doi= }}
*{{cite journal | author=Gulati S, Baker P, Li YN, ''et al.'' |title=Defects in human methionine synthase in cblG patients. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 1859-65 |year= 1997 |pmid= 8968736 |doi= }}
*{{cite journal | author=Leclerc D, Campeau E, Goyette P, ''et al.'' |title=Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 1867-74 |year= 1997 |pmid= 8968737 |doi= }}
*{{cite journal | author=Chen LH, Liu ML, Hwang HY, ''et al.'' |title=Human methionine synthase. cDNA cloning, gene localization, and expression. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3628-34 |year= 1997 |pmid= 9013615 |doi= }}
*{{cite journal | author=Wilson A, Leclerc D, Saberi F, ''et al.'' |title=Functionally null mutations in patients with the cblG-variant form of methionine synthase deficiency. |journal=Am. J. Hum. Genet. |volume=63 |issue= 2 |pages= 409-14 |year= 1998 |pmid= 9683607 |doi= }}
*{{cite journal | author=Salomon O, Rosenberg N, Zivelin A, ''et al.'' |title=Methionine synthase A2756G and methylenetetrahydrofolate reductase A1298C polymorphisms are not risk factors for idiopathic venous thromboembolism. |journal=Hematol. J. |volume=2 |issue= 1 |pages= 38-41 |year= 2002 |pmid= 11920232 |doi= 10.1038/sj/thj/6200078 }}
*{{cite journal | author=Watkins D, Ru M, Hwang HY, ''et al.'' |title=Hyperhomocysteinemia due to methionine synthase deficiency, cblG: structure of the MTR gene, genotype diversity, and recognition of a common mutation, P1173L. |journal=Am. J. Hum. Genet. |volume=71 |issue= 1 |pages= 143-53 |year= 2002 |pmid= 12068375 |doi= }}
*{{cite journal | author=De Marco P, Calevo MG, Moroni A, ''et al.'' |title=Study of MTHFR and MS polymorphisms as risk factors for NTD in the Italian population. |journal=J. Hum. Genet. |volume=47 |issue= 6 |pages= 319-24 |year= 2002 |pmid= 12111380 |doi= 10.1007/s100380200043 }}
*{{cite journal | author=Doolin MT, Barbaux S, McDonnell M, ''et al.'' |title=Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. |journal=Am. J. Hum. Genet. |volume=71 |issue= 5 |pages= 1222-6 |year= 2003 |pmid= 12375236 |doi= }}
*{{cite journal | author=Zhu H, Wicker NJ, Shaw GM, ''et al.'' |title=Homocysteine remethylation enzyme polymorphisms and increased risks for neural tube defects. |journal=Mol. Genet. Metab. |volume=78 |issue= 3 |pages= 216-21 |year= 2004 |pmid= 12649067 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MTRR... {November 19, 2007 10:50:59 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:51:26 AM 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 = 5-methyltetrahydrofolate-homocysteine methyltransferase reductase
| HGNCid = 7473
| Symbol = MTRR
| AltSymbols =; MGC129643; MSR
| OMIM = 602568
| ECnumber =
| Homologene = 11419
| MGIid = 1891037
| GeneAtlas_image1 = PBB_GE_MTRR_203200_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MTRR_203199_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0010181 |text = FMN binding}} {{GNF_GO|id=GO:0030586 |text = [methionine synthase] reductase activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}} {{GNF_GO|id=GO:0009086 |text = methionine biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4552
| Hs_Ensembl = ENSG00000124275
| Hs_RefseqProtein = NP_002445
| Hs_RefseqmRNA = NM_002454
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 7922217
| Hs_GenLoc_end = 7954237
| Hs_Uniprot = Q9UBK8
| Mm_EntrezGene = 210009
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_990861
| Mm_RefseqProtein = XP_995955
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''5-methyltetrahydrofolate-homocysteine methyltransferase reductase''', also known as '''MTRR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MTRR 5-methyltetrahydrofolate-homocysteine methyltransferase reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4552| 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 = Methionine is an essential amino acid required for protein synthesis and one carbon metabolism. Its synthesis is catalyzed by the enzyme methionine synthase. Methionine synthase eventually becomes inactive due to the oxidation of its cob(I)alamin cofactor. The protein encoded by this gene regenerates a functional methionine synthase via reductive methylation. It is a member of the ferredoxin-NADP(+) reductase (FNR) family of electron transferases. Patients of the cbl-E complementation group of disorders of folate/cobalamin metabolism are defective in reductive activation of methionine synthase. This gene produces two transcripts.<ref name="entrez">{{cite web | title = Entrez Gene: MTRR 5-methyltetrahydrofolate-homocysteine methyltransferase reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4552| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Leclerc D, Wilson A, Dumas R, ''et al.'' |title=Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 6 |pages= 3059-64 |year= 1998 |pmid= 9501215 |doi= }}
*{{cite journal | author=Wilson A, Platt R, Wu Q, ''et al.'' |title=A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. |journal=Mol. Genet. Metab. |volume=67 |issue= 4 |pages= 317-23 |year= 1999 |pmid= 10444342 |doi= 10.1006/mgme.1999.2879 }}
*{{cite journal | author=Wilson A, Leclerc D, Rosenblatt DS, Gravel RA |title=Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. |journal=Hum. Mol. Genet. |volume=8 |issue= 11 |pages= 2009-16 |year= 1999 |pmid= 10484769 |doi= }}
*{{cite journal | author=James SJ, Pogribna M, Pogribny IP, ''et al.'' |title=Abnormal folate metabolism and mutation in the methylenetetrahydrofolate reductase gene may be maternal risk factors for Down syndrome. |journal=Am. J. Clin. Nutr. |volume=70 |issue= 4 |pages= 495-501 |year= 1999 |pmid= 10500018 |doi= }}
*{{cite journal | author=Leclerc D, Odièvre M, Wu Q, ''et al.'' |title=Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene. |journal=Gene |volume=240 |issue= 1 |pages= 75-88 |year= 2000 |pmid= 10564814 |doi= }}
*{{cite journal | author=Doolin MT, Barbaux S, McDonnell M, ''et al.'' |title=Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. |journal=Am. J. Hum. Genet. |volume=71 |issue= 5 |pages= 1222-6 |year= 2003 |pmid= 12375236 |doi= }}
*{{cite journal | author=Olteanu H, Munson T, Banerjee R |title=Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase. |journal=Biochemistry |volume=41 |issue= 45 |pages= 13378-85 |year= 2002 |pmid= 12416982 |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=Zavadakova P, Fowler B, Zeman J, ''et al.'' |title=CblE type of homocystinuria due to methionine synthase reductase deficiency: clinical and molecular studies and prenatal diagnosis in two families. |journal=J. Inherit. Metab. Dis. |volume=25 |issue= 6 |pages= 461-76 |year= 2003 |pmid= 12555939 |doi= }}
*{{cite journal | author=Pietrzyk JJ, Bik-Multanowski M, Sanak M, Twardowska M |title=Polymorphisms of the 5,10-methylenetetrahydrofolate and the methionine synthase reductase genes as independent risk factors for spina bifida. |journal=J. Appl. Genet. |volume=44 |issue= 1 |pages= 111-3 |year= 2003 |pmid= 12590188 |doi= }}
*{{cite journal | author=Zhu H, Wicker NJ, Shaw GM, ''et al.'' |title=Homocysteine remethylation enzyme polymorphisms and increased risks for neural tube defects. |journal=Mol. Genet. Metab. |volume=78 |issue= 3 |pages= 216-21 |year= 2004 |pmid= 12649067 |doi= }}
*{{cite journal | author=Brilakis ES, Berger PB, Ballman KV, Rozen R |title=Methylenetetrahydrofolate reductase (MTHFR) 677C>T and methionine synthase reductase (MTRR) 66A>G polymorphisms: association with serum homocysteine and angiographic coronary artery disease in the era of flour products fortified with folic acid. |journal=Atherosclerosis |volume=168 |issue= 2 |pages= 315-22 |year= 2003 |pmid= 12801615 |doi= }}
*{{cite journal | author=Sliwerska E, Szpecht-Potocka A |title=[Mutations of MTHFR, MTR, MTRR genes as high risk factors for neural tube defects] |journal=Medycyna wieku rozwojowego |volume=6 |issue= 4 |pages= 371-82 |year= 2003 |pmid= 12810988 |doi= }}
*{{cite journal | author=Beyer K, Lao JI, Latorre P, ''et al.'' |title=Methionine synthase polymorphism is a risk factor for Alzheimer disease. |journal=Neuroreport |volume=14 |issue= 10 |pages= 1391-4 |year= 2003 |pmid= 12876480 |doi= 10.1097/01.wnr.0000073683.00308.0e }}
*{{cite journal | author=Bosco P, Guéant-Rodriguez RM, Anello G, ''et al.'' |title=Methionine synthase (MTR) 2756 (A --> G) polymorphism, double heterozygosity methionine synthase 2756 AG/methionine synthase reductase (MTRR) 66 AG, and elevated homocysteinemia are three risk factors for having a child with Down syndrome. |journal=Am. J. Med. Genet. A |volume=121 |issue= 3 |pages= 219-24 |year= 2003 |pmid= 12923861 |doi= 10.1002/ajmg.a.20234 }}
*{{cite journal | author=Olteanu H, Wolthers KR, Munro AW, ''et al.'' |title=Kinetic and thermodynamic characterization of the common polymorphic variants of human methionine synthase reductase. |journal=Biochemistry |volume=43 |issue= 7 |pages= 1988-97 |year= 2004 |pmid= 14967039 |doi= 10.1021/bi035910i }}
*{{cite journal | author=Gemmati D, Ongaro A, Scapoli GL, ''et al.'' |title=Common gene polymorphisms in the metabolic folate and methylation pathway and the risk of acute lymphoblastic leukemia and non-Hodgkin's lymphoma in adults. |journal=Cancer Epidemiol. Biomarkers Prev. |volume=13 |issue= 5 |pages= 787-94 |year= 2004 |pmid= 15159311 |doi= }}
*{{cite journal | author=Leal NA, Olteanu H, Banerjee R, Bobik TA |title=Human ATP:Cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase. |journal=J. Biol. Chem. |volume=279 |issue= 46 |pages= 47536-42 |year= 2005 |pmid= 15347655 |doi= 10.1074/jbc.M405449200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Vaughn JD, Bailey LB, Shelnutt KP, ''et al.'' |title=Methionine synthase reductase 66A->G polymorphism is associated with increased plasma homocysteine concentration when combined with the homozygous methylenetetrahydrofolate reductase 677C->T variant. |journal=J. Nutr. |volume=134 |issue= 11 |pages= 2985-90 |year= 2004 |pmid= 15514263 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MYO5A... {November 19, 2007 10:51:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:52:46 AM 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_MYO5A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1oe9.
| PDB = {{PDB2|1oe9}}, {{PDB2|1w7i}}, {{PDB2|1w7j}}, {{PDB2|1w8j}}, {{PDB2|2ix7}}
| Name = Myosin VA (heavy chain 12, myoxin)
| HGNCid = 7602
| Symbol = MYO5A
| AltSymbols =; GS1; MYH12; MYO5; MYOXIN; MYR12; myosin V; myosin Va
| OMIM = 160777
| ECnumber =
| Homologene = 20100
| MGIid = 105976
| GeneAtlas_image1 = PBB_GE_MYO5A_204527_at_tn.png
| Function = {{GNF_GO|id=GO:0000146 |text = microfilament motor activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016459 |text = myosin complex}} {{GNF_GO|id=GO:0030426 |text = growth cone}} {{GNF_GO|id=GO:0043005 |text = neuron projection}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0030048 |text = actin filament-based movement}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4644
| Hs_Ensembl = ENSG00000197535
| Hs_RefseqProtein = NP_000250
| Hs_RefseqmRNA = NM_000259
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 50392602
| Hs_GenLoc_end = 50608539
| Hs_Uniprot = Q9Y4I1
| Mm_EntrezGene = 17918
| Mm_Ensembl = ENSMUSG00000034593
| Mm_RefseqmRNA = NM_010864
| Mm_RefseqProtein = NP_034994
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 74902095
| Mm_GenLoc_end = 75003902
| Mm_Uniprot = Q99104
}}
}}
'''Myosin VA (heavy chain 12, myoxin)''', also known as '''MYO5A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYO5A myosin VA (heavy chain 12, myoxin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4644| 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=Moore KJ, Testa JR, Francke U, ''et al.'' |title=Cloning and regional assignment of the human myosin heavy chain 12 (MYH12) gene to chromosome band 15q21. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 1-2 |pages= 53-8 |year= 1995 |pmid= 7835087 |doi= }}
*{{cite journal | author=Bement WM, Hasson T, Wirth JA, ''et al.'' |title=Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6549-53 |year= 1994 |pmid= 8022818 |doi= }}
*{{cite journal | author=Engle LJ, Kennett RH |title=Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene. |journal=Genomics |volume=19 |issue= 3 |pages= 407-16 |year= 1994 |pmid= 8188282 |doi= 10.1006/geno.1994.1088 }}
*{{cite journal | author=Pastural E, Barrat FJ, Dufourcq-Lagelouse R, ''et al.'' |title=Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene. |journal=Nat. Genet. |volume=16 |issue= 3 |pages= 289-92 |year= 1997 |pmid= 9207796 |doi= 10.1038/ng0797-289 }}
*{{cite journal | author=Lambert J, Naeyaert JM, Callens T, ''et al.'' |title=Human myosin V gene produces different transcripts in a cell type-specific manner. |journal=Biochem. Biophys. Res. Commun. |volume=252 |issue= 2 |pages= 329-33 |year= 1998 |pmid= 9826529 |doi= 10.1006/bbrc.1998.9644 }}
*{{cite journal | author=Buss F, Kendrick-Jones J, Lionne C, ''et al.'' |title=The localization of myosin VI at the golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. |journal=J. Cell Biol. |volume=143 |issue= 6 |pages= 1535-45 |year= 1999 |pmid= 9852149 |doi= }}
*{{cite journal | author=El-Husseini AE, Vincent SR |title=Cloning and characterization of a novel RING finger protein that interacts with class V myosins. |journal=J. Biol. Chem. |volume=274 |issue= 28 |pages= 19771-7 |year= 1999 |pmid= 10391919 |doi= }}
*{{cite journal | author=Mehta AD, Rock RS, Rief M, ''et al.'' |title=Myosin-V is a processive actin-based motor. |journal=Nature |volume=400 |issue= 6744 |pages= 590-3 |year= 1999 |pmid= 10448864 |doi= 10.1038/23072 }}
*{{cite journal | author=Edgar AJ, Bennett JP |title=Inhibition of dendrite formation in mouse melanocytes transiently transfected with antisense DNA to myosin Va. |journal=J. Anat. |volume=195 ( Pt 2) |issue= |pages= 173-84 |year= 1999 |pmid= 10529054 |doi= }}
*{{cite journal | author=Pastural E, Ersoy F, Yalman N, ''et al.'' |title=Two genes are responsible for Griscelli syndrome at the same 15q21 locus. |journal=Genomics |volume=63 |issue= 3 |pages= 299-306 |year= 2000 |pmid= 10704277 |doi= 10.1006/geno.1999.6081 }}
*{{cite journal | author=Lambert J, Naeyaert JM, De Paepe A, ''et al.'' |title=arg-cys substitution at codon 1246 of the human myosin Va gene is not associated with Griscelli syndrome. |journal=J. Invest. Dermatol. |volume=114 |issue= 4 |pages= 731-3 |year= 2000 |pmid= 10733681 |doi= 10.1046/j.1523-1747.2000.00933.x }}
*{{cite journal | author=Naisbitt S, Valtschanoff J, Allison DW, ''et al.'' |title=Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. |journal=J. Neurosci. |volume=20 |issue= 12 |pages= 4524-34 |year= 2000 |pmid= 10844022 |doi= }}
*{{cite journal | author=Lo KW, Naisbitt S, Fan JS, ''et al.'' |title=The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14059-66 |year= 2001 |pmid= 11148209 |doi= 10.1074/jbc.M010320200 }}
*{{cite journal | author=Ohkawa N, Kokura K, Matsu-Ura T, ''et al.'' |title=Molecular cloning and characterization of neural activity-related RING finger protein (NARF): a new member of the RBCC family is a candidate for the partner of myosin V. |journal=J. Neurochem. |volume=78 |issue= 1 |pages= 75-87 |year= 2001 |pmid= 11432975 |doi= }}
*{{cite journal | author=Fukuda M, Kuroda TS, Mikoshiba K |title=Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12432-6 |year= 2002 |pmid= 11856727 |doi= 10.1074/jbc.C200005200 }}
*{{cite journal | author=Rodriguez OC, Cheney RE |title=Human myosin-Vc is a novel class V myosin expressed in epithelial cells. |journal=J. Cell. Sci. |volume=115 |issue= Pt 5 |pages= 991-1004 |year= 2002 |pmid= 11870218 |doi= }}
*{{cite journal | author=Strom M, Hume AN, Tarafder AK, ''et al.'' |title=A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25423-30 |year= 2002 |pmid= 11980908 |doi= 10.1074/jbc.M202574200 }}
*{{cite journal | author=Wu X, Wang F, Rao K, ''et al.'' |title=Rab27a is an essential component of melanosome receptor for myosin Va. |journal=Mol. Biol. Cell |volume=13 |issue= 5 |pages= 1735-49 |year= 2002 |pmid= 12006666 |doi= 10.1091/mbc.01-12-0595 }}
*{{cite journal | author=Anikster Y, Huizing M, Anderson PD, ''et al.'' |title=Evidence that Griscelli syndrome with neurological involvement is caused by mutations in RAB27A, not MYO5A. |journal=Am. J. Hum. Genet. |volume=71 |issue= 2 |pages= 407-14 |year= 2002 |pmid= 12058346 |doi= }}
*{{cite journal | author=Nagashima K, Torii S, Yi Z, ''et al.'' |title=Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. |journal=FEBS Lett. |volume=517 |issue= 1-3 |pages= 233-8 |year= 2002 |pmid= 12062444 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MYO6... {November 19, 2007 10:52:47 AM PST}
- SEARCH REDIRECT: Control Box Found: MYO6 {November 19, 2007 10:53:22 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:53:23 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:53:23 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:53:23 AM PST}
- UPDATED: Updated protein page: MYO6 {November 19, 2007 10:53:29 AM PST}
- INFO: Beginning work on NFKBIB... {November 19, 2007 10:53:30 AM PST}
- SEARCH REDIRECT: Control Box Found: NFKBIB {November 19, 2007 10:54:02 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:54:05 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:54:05 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:54:05 AM PST}
- UPDATED: Updated protein page: NFKBIB {November 19, 2007 10:54:11 AM PST}
- INFO: Beginning work on NKX3-1... {November 19, 2007 10:54:11 AM PST}
- SEARCH REDIRECT: Control Box Found: NKX3-1 {November 19, 2007 10:54:45 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:54:48 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:54:48 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:54:48 AM PST}
- UPDATED: Updated protein page: NKX3-1 {November 19, 2007 10:54:55 AM PST}
- INFO: Beginning work on PAM... {November 19, 2007 10:54:55 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:55:35 AM 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_PAM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1opm.
| PDB = {{PDB2|1opm}}, {{PDB2|1phm}}, {{PDB2|1sdw}}, {{PDB2|1yi9}}, {{PDB2|1yip}}, {{PDB2|1yjk}}, {{PDB2|1yjl}}, {{PDB2|3phm}}
| Name = Peptidylglycine alpha-amidating monooxygenase
| HGNCid = 8596
| Symbol = PAM
| AltSymbols =; PAL; PHM
| OMIM = 170270
| ECnumber =
| Homologene = 37369
| MGIid = 97475
| GeneAtlas_image1 = PBB_GE_PAM_202336_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PAM_212958_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PAM_214620_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004504 |text = peptidylglycine monooxygenase activity}} {{GNF_GO|id=GO:0004598 |text = peptidylamidoglycolate lyase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0031418 |text = L-ascorbic acid binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000790 |text = nuclear chromatin}} {{GNF_GO|id=GO:0000793 |text = condensed chromosome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030141 |text = secretory granule}}
| Process = {{GNF_GO|id=GO:0001519 |text = peptide amidation}} {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006518 |text = peptide metabolic process}} {{GNF_GO|id=GO:0007076 |text = mitotic chromosome condensation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5066
| Hs_Ensembl = ENSG00000145730
| Hs_RefseqProtein = NP_000910
| Hs_RefseqmRNA = NM_000919
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 102229422
| Hs_GenLoc_end = 102394708
| Hs_Uniprot = P19021
| Mm_EntrezGene = 18484
| Mm_Ensembl = ENSMUSG00000026335
| Mm_RefseqmRNA = NM_013626
| Mm_RefseqProtein = NP_038654
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 99651500
| Mm_GenLoc_end = 99925919
| Mm_Uniprot = Q8BQ31
}}
}}
'''Peptidylglycine alpha-amidating monooxygenase''', also known as '''PAM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5066| 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 multifunctional protein. It has two enzymatically active domains with catalytic activities - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These catalytic domains work sequentially to catalyze neuroendocrine peptides to active alpha-amidated products. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene but some of their full length sequences are not yet known.<ref name="entrez">{{cite web | title = Entrez Gene: PAM peptidylglycine alpha-amidating monooxygenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5066| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pittner RA, Albrandt K, Beaumont K, ''et al.'' |title=Molecular physiology of amylin. |journal=J. Cell. Biochem. |volume=55 Suppl |issue= |pages= 19-28 |year= 1994 |pmid= 7929615 |doi= }}
*{{cite journal | author=Eipper BA, Milgram SL, Husten EJ, ''et al.'' |title=Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains. |journal=Protein Sci. |volume=2 |issue= 4 |pages= 489-97 |year= 1993 |pmid= 8518727 |doi= }}
*{{cite journal | author=Ouafik LH, Stoffers DA, Campbell TA, ''et al.'' |title=The multifunctional peptidylglycine alpha-amidating monooxygenase gene: exon/intron organization of catalytic, processing, and routing domains. |journal=Mol. Endocrinol. |volume=6 |issue= 10 |pages= 1571-84 |year= 1992 |pmid= 1448112 |doi= }}
*{{cite journal | author=Maltese JY, Eipper BA |title=Developmental expression of peptidylglycine alpha-amidating monooxygenase (PAM) in primary cultures of neonatal rat cardiocytes: a model for studying regulation of PAM expression in the rat heart. |journal=Mol. Endocrinol. |volume=6 |issue= 12 |pages= 1998-2008 |year= 1993 |pmid= 1491686 |doi= }}
*{{cite journal | author=Braas KM, Harakall SA, Ouafik L, ''et al.'' |title=Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study. |journal=Endocrinology |volume=130 |issue= 5 |pages= 2778-88 |year= 1992 |pmid= 1572293 |doi= }}
*{{cite journal | author=Glauder J, Ragg H, Rauch J, Engels JW |title=Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells. |journal=Biochem. Biophys. Res. Commun. |volume=169 |issue= 2 |pages= 551-8 |year= 1990 |pmid= 2357221 |doi= }}
*{{cite journal | author=Roberts AN, Leighton B, Todd JA, ''et al.'' |title=Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 24 |pages= 9662-6 |year= 1990 |pmid= 2690069 |doi= }}
*{{cite journal | author=Vos MD, Jones JE, Treston AM |title=Human peptidylglycine alpha-amidating monooxygenase transcripts derived by alternative mRNA splicing of an unreported exon. |journal=Gene |volume=163 |issue= 2 |pages= 307-11 |year= 1995 |pmid= 7590286 |doi= }}
*{{cite journal | author=Tsukamoto T, Noguchi M, Kayama H, ''et al.'' |title=Increased peptidylglycine alpha-amidating monooxygenase activity in cerebrospinal fluid of patients with multiple sclerosis. |journal=Intern. Med. |volume=34 |issue= 4 |pages= 229-32 |year= 1995 |pmid= 7606087 |doi= }}
*{{cite journal | author=Yun HY, Johnson RC, Mains RE, Eipper BA |title=Topological switching of the COOH-terminal domain of peptidylglycine alpha-amidating monooxygenase by alternative RNA splicing. |journal=Arch. Biochem. Biophys. |volume=301 |issue= 1 |pages= 77-84 |year= 1993 |pmid= 7680192 |doi= 10.1006/abbi.1993.1117 }}
*{{cite journal | author=Mains RE, Milgram SL, Keutmann HT, Eipper BA |title=The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins. |journal=Mol. Endocrinol. |volume=9 |issue= 1 |pages= 3-13 |year= 1995 |pmid= 7760848 |doi= }}
*{{cite journal | author=Tateishi K, Arakawa F, Misumi Y, ''et al.'' |title=Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 282-90 |year= 1995 |pmid= 7999037 |doi= 10.1006/bbrc.1994.2662 }}
*{{cite journal | author=Martínez A, Montuenga LM, Springall DR, ''et al.'' |title=Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas. |journal=J. Histochem. Cytochem. |volume=41 |issue= 3 |pages= 375-80 |year= 1993 |pmid= 8094086 |doi= }}
*{{cite journal | author=Kapuscinski M, Green M, Sinha SN, ''et al.'' |title=Peptide alpha-amidation activity in human plasma: relationship to gastrin processing. |journal=Clin. Endocrinol. (Oxf) |volume=39 |issue= 1 |pages= 51-8 |year= 1993 |pmid= 8102327 |doi= }}
*{{cite journal | author=Yun HY, Keutmann HT, Eipper BA |title=Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. |journal=J. Biol. Chem. |volume=269 |issue= 14 |pages= 10946-55 |year= 1994 |pmid= 8144680 |doi= }}
*{{cite journal | author=Ouafik LH, Mattei MG, Giraud P, ''et al.'' |title=Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21. |journal=Genomics |volume=18 |issue= 2 |pages= 319-21 |year= 1994 |pmid= 8288234 |doi= }}
*{{cite journal | author=Husten EJ, Tausk FA, Keutmann HT, Eipper BA |title=Use of endoproteases to identify catalytic domains, linker regions, and functional interactions in soluble peptidylglycine alpha-amidating monooxygenase. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9709-17 |year= 1993 |pmid= 8486658 |doi= }}
*{{cite journal | author=Yun HY, Milgram SL, Keutmann HT, Eipper BA |title=Phosphorylation of the cytosolic domain of peptidylglycine alpha-amidating monooxygenase. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 30075-83 |year= 1996 |pmid= 8530412 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PDCD1... {November 19, 2007 10:55:35 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:56:14 AM 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 = Programmed cell death 1
| HGNCid = 8760
| Symbol = PDCD1
| AltSymbols =; CD279; PD1; SLEB2; hPD-1; hPD-l
| OMIM = 600244
| ECnumber =
| Homologene = 3681
| MGIid = 104879
| GeneAtlas_image1 = PBB_GE_PDCD1_207634_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0004872 |text = receptor activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5133
| Hs_Ensembl = ENSG00000188389
| Hs_RefseqProtein = NP_005009
| Hs_RefseqmRNA = NM_005018
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 242440711
| Hs_GenLoc_end = 242449731
| Hs_Uniprot = Q15116
| Mm_EntrezGene = 18566
| Mm_Ensembl = ENSMUSG00000026285
| Mm_RefseqmRNA = NM_008798
| Mm_RefseqProtein = NP_032824
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 95868708
| Mm_GenLoc_end = 95882959
| Mm_Uniprot = Q544F3
}}
}}
'''Programmed cell death 1''', also known as '''PDCD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PDCD1 programmed cell death 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5133| 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 cell surface membrane protein of the immunoglobulin superfamily. This protein is expressed in pro-B-cells and is thought to play a role in their differentiation. In mice, expression of this gene is induced in the thymus when anti-CD3 antibodies are injected and large numbers of thymocytes undergo apoptosis. Mice deficient for this gene bred on a BALB/c background developed dilated cardiomyopathy and died from congestive heart failure. These studies suggest that this gene product may also be important in T cell function and contribute to the prevention of autoimmune diseases.<ref name="entrez">{{cite web | title = Entrez Gene: PDCD1 programmed cell death 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5133| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ishida Y, Agata Y, Shibahara K, Honjo T |title=Induced expression of PD-1, a novel member of the immunoglobulin gene superfamily, upon programmed cell death. |journal=EMBO J. |volume=11 |issue= 11 |pages= 3887-95 |year= 1992 |pmid= 1396582 |doi= }}
*{{cite journal | author=Shinohara T, Taniwaki M, Ishida Y, ''et al.'' |title=Structure and chromosomal localization of the human PD-1 gene (PDCD1). |journal=Genomics |volume=23 |issue= 3 |pages= 704-6 |year= 1995 |pmid= 7851902 |doi= 10.1006/geno.1994.1562 }}
*{{cite journal | author=Vibhakar R, Juan G, Traganos F, ''et al.'' |title=Activation-induced expression of human programmed death-1 gene in T-lymphocytes. |journal=Exp. Cell Res. |volume=232 |issue= 1 |pages= 25-8 |year= 1997 |pmid= 9141617 |doi= 10.1006/excr.1997.3493 }}
*{{cite journal | author=Finger LR, Pu J, Wasserman R, ''et al.'' |title=The human PD-1 gene: complete cDNA, genomic organization, and developmentally regulated expression in B cell progenitors. |journal=Gene |volume=197 |issue= 1-2 |pages= 177-87 |year= 1997 |pmid= 9332365 |doi= }}
*{{cite journal | author=Iwai Y, Okazaki T, Nishimura H, ''et al.'' |title=Microanatomical localization of PD-1 in human tonsils. |journal=Immunol. Lett. |volume=83 |issue= 3 |pages= 215-20 |year= 2003 |pmid= 12095712 |doi= }}
*{{cite journal | author=Prokunina L, Castillejo-López C, Oberg F, ''et al.'' |title=A regulatory polymorphism in PDCD1 is associated with susceptibility to systemic lupus erythematosus in humans. |journal=Nat. Genet. |volume=32 |issue= 4 |pages= 666-9 |year= 2003 |pmid= 12402038 |doi= 10.1038/ng1020 }}
*{{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=Bennett F, Luxenberg D, Ling V, ''et al.'' |title=Program death-1 engagement upon TCR activation has distinct effects on costimulation and cytokine-driven proliferation: attenuation of ICOS, IL-4, and IL-21, but not CD28, IL-7, and IL-15 responses. |journal=J. Immunol. |volume=170 |issue= 2 |pages= 711-8 |year= 2003 |pmid= 12517932 |doi= }}
*{{cite journal | author=Wang S, Bajorath J, Flies DB, ''et al.'' |title=Molecular modeling and functional mapping of B7-H1 and B7-DC uncouple costimulatory function from PD-1 interaction. |journal=J. Exp. Med. |volume=197 |issue= 9 |pages= 1083-91 |year= 2003 |pmid= 12719480 |doi= 10.1084/jem.20021752 }}
*{{cite journal | author=Youngnak P, Kozono Y, Kozono H, ''et al.'' |title=Differential binding properties of B7-H1 and B7-DC to programmed death-1. |journal=Biochem. Biophys. Res. Commun. |volume=307 |issue= 3 |pages= 672-7 |year= 2003 |pmid= 12893276 |doi= }}
*{{cite journal | author=Nielsen C, Hansen D, Husby S, ''et al.'' |title=Association of a putative regulatory polymorphism in the PD-1 gene with susceptibility to type 1 diabetes. |journal=Tissue Antigens |volume=62 |issue= 6 |pages= 492-7 |year= 2004 |pmid= 14617032 |doi= }}
*{{cite journal | author=Prokunina L, Gunnarsson I, Sturfelt G, ''et al.'' |title=The systemic lupus erythematosus-associated PDCD1 polymorphism PD1.3A in lupus nephritis. |journal=Arthritis Rheum. |volume=50 |issue= 1 |pages= 327-8 |year= 2004 |pmid= 14730631 |doi= 10.1002/art.11442 }}
*{{cite journal | author=Lin SC, Yen JH, Tsai JJ, ''et al.'' |title=Association of a programmed death 1 gene polymorphism with the development of rheumatoid arthritis, but not systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=50 |issue= 3 |pages= 770-5 |year= 2004 |pmid= 15022318 |doi= 10.1002/art.20040 }}
*{{cite journal | author=Prokunina L, Padyukov L, Bennet A, ''et al.'' |title=Association of the PD-1.3A allele of the PDCD1 gene in patients with rheumatoid arthritis negative for rheumatoid factor and the shared epitope. |journal=Arthritis Rheum. |volume=50 |issue= 6 |pages= 1770-3 |year= 2004 |pmid= 15188352 |doi= 10.1002/art.20280 }}
*{{cite journal | author=Sanghera DK, Manzi S, Bontempo F, ''et al.'' |title=Role of an intronic polymorphism in the PDCD1 gene with the risk of sporadic systemic lupus erythematosus and the occurrence of antiphospholipid antibodies. |journal=Hum. Genet. |volume=115 |issue= 5 |pages= 393-8 |year= 2004 |pmid= 15322919 |doi= 10.1007/s00439-004-1172-0 }}
*{{cite journal | author=Nielsen C, Laustrup H, Voss A, ''et al.'' |title=A putative regulatory polymorphism in PD-1 is associated with nephropathy in a population-based cohort of systemic lupus erythematosus patients. |journal=Lupus |volume=13 |issue= 7 |pages= 510-6 |year= 2005 |pmid= 15352422 |doi= }}
*{{cite journal | author=Johansson M, Arlestig L, Möller B, Rantapää-Dahlqvist S |title=Association of a PDCD1 polymorphism with renal manifestations in systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=52 |issue= 6 |pages= 1665-9 |year= 2005 |pmid= 15934088 |doi= 10.1002/art.21058 }}
*{{cite journal | author=Nielsen C, Ohm-Laursen L, Barington T, ''et al.'' |title=Alternative splice variants of the human PD-1 gene. |journal=Cell. Immunol. |volume=235 |issue= 2 |pages= 109-16 |year= 2005 |pmid= 16171790 |doi= 10.1016/j.cellimm.2005.07.007 }}
*{{cite journal | author=Parry RV, Chemnitz JM, Frauwirth KA, ''et al.'' |title=CTLA-4 and PD-1 receptors inhibit T-cell activation by distinct mechanisms. |journal=Mol. Cell. Biol. |volume=25 |issue= 21 |pages= 9543-53 |year= 2005 |pmid= 16227604 |doi= 10.1128/MCB.25.21.9543-9553.2005 }}
*{{cite journal | author=Kobayashi M, Kawano S, Hatachi S, ''et al.'' |title=Enhanced expression of programmed death-1 (PD-1)/PD-L1 in salivary glands of patients with Sjögren's syndrome. |journal=J. Rheumatol. |volume=32 |issue= 11 |pages= 2156-63 |year= 2005 |pmid= 16265694 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PHEX... {November 19, 2007 10:56:14 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:56:58 AM PST}
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| 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 = Phosphate regulating endopeptidase homolog, X-linked (hypophosphatemia, vitamin D resistant rickets)
| HGNCid = 8918
| Symbol = PHEX
| AltSymbols =; HPDR; HPDR1; HYP; HYP1; PEX; XLH
| OMIM = 300550
| ECnumber =
| Homologene = 37310
| MGIid = 107489
| GeneAtlas_image1 = PBB_GE_PHEX_210617_at_tn.png
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0004245 |text = neprilysin activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| 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:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5251
| Hs_Ensembl = ENSG00000102174
| Hs_RefseqProtein = NP_000435
| Hs_RefseqmRNA = NM_000444
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 21960480
| Hs_GenLoc_end = 22179348
| Hs_Uniprot = P78562
| Mm_EntrezGene = 18675
| Mm_Ensembl = ENSMUSG00000057457
| Mm_RefseqmRNA = NM_011077
| Mm_RefseqProtein = NP_035207
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 152502791
| Mm_GenLoc_end = 152759383
| Mm_Uniprot = Q3TYM9
}}
}}
'''Phosphate regulating endopeptidase homolog, X-linked (hypophosphatemia, vitamin D resistant rickets)''', also known as '''PHEX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PHEX phosphate regulating endopeptidase homolog, X-linked (hypophosphatemia, vitamin D resistant rickets)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5251| 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=Tenenhouse HS |title=X-linked hypophosphataemia: a homologous disorder in humans and mice. |journal=Nephrol. Dial. Transplant. |volume=14 |issue= 2 |pages= 333-41 |year= 1999 |pmid= 10069185 |doi= }}
*{{cite journal | author=Drezner MK |title=PHEX gene and hypophosphatemia. |journal=Kidney Int. |volume=57 |issue= 1 |pages= 9-18 |year= 2000 |pmid= 10620182 |doi= 10.1046/j.1523-1755.2000.00807.x }}
*{{cite journal | author=Quarles LD |title=FGF23, PHEX, and MEPE regulation of phosphate homeostasis and skeletal mineralization. |journal=Am. J. Physiol. Endocrinol. Metab. |volume=285 |issue= 1 |pages= E1-9 |year= 2003 |pmid= 12791601 |doi= 10.1152/ajpendo.00016.2003 }}
*{{cite journal | author=Baroncelli GI, Bertelloni S, Sodini F, ''et al.'' |title=Genetic advances, biochemical and clinical features and critical approach to treatment of patients with X-linked hypophosphatemic rickets. |journal=Pediatric endocrinology reviews : PER |volume=1 |issue= 4 |pages= 361-79 |year= 2006 |pmid= 16437029 |doi= }}
*{{cite journal | author=Econs MJ, Pericak-Vance MA, Betz H, ''et al.'' |title=The human glycine receptor: a new probe that is linked to the X-linked hypophosphatemic rickets gene. |journal=Genomics |volume=7 |issue= 3 |pages= 439-41 |year= 1990 |pmid= 2163973 |doi= }}
*{{cite journal | author= |title=A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets. The HYP Consortium. |journal=Nat. Genet. |volume=11 |issue= 2 |pages= 130-6 |year= 1995 |pmid= 7550339 |doi= 10.1038/ng1095-130 }}
*{{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=Grieff M, Mumm S, Waeltz P, ''et al.'' |title=Expression and cloning of the human X-linked hypophosphatemia gene cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 3 |pages= 635-9 |year= 1997 |pmid= 9070861 |doi= 10.1006/bbrc.1997.6153 }}
*{{cite journal | author=Beck L, Soumounou Y, Martel J, ''et al.'' |title=Pex/PEX tissue distribution and evidence for a deletion in the 3' region of the Pex gene in X-linked hypophosphatemic mice. |journal=J. Clin. Invest. |volume=99 |issue= 6 |pages= 1200-9 |year= 1997 |pmid= 9077527 |doi= }}
*{{cite journal | author=Rowe PS, Oudet CL, Francis F, ''et al.'' |title=Distribution of mutations in the PEX gene in families with X-linked hypophosphataemic rickets (HYP). |journal=Hum. Mol. Genet. |volume=6 |issue= 4 |pages= 539-49 |year= 1997 |pmid= 9097956 |doi= }}
*{{cite journal | author=Holm IA, Huang X, Kunkel LM |title=Mutational analysis of the PEX gene in patients with X-linked hypophosphatemic rickets. |journal=Am. J. Hum. Genet. |volume=60 |issue= 4 |pages= 790-7 |year= 1997 |pmid= 9106524 |doi= }}
*{{cite journal | author=Francis F, Strom TM, Hennig S, ''et al.'' |title=Genomic organization of the human PEX gene mutated in X-linked dominant hypophosphatemic rickets. |journal=Genome Res. |volume=7 |issue= 6 |pages= 573-85 |year= 1997 |pmid= 9199930 |doi= }}
*{{cite journal | author=Guo R, Quarles LD |title=Cloning and sequencing of human PEX from a bone cDNA library: evidence for its developmental stage-specific regulation in osteoblasts. |journal=J. Bone Miner. Res. |volume=12 |issue= 7 |pages= 1009-17 |year= 1997 |pmid= 9199999 |doi= }}
*{{cite journal | author=Lipman ML, Panda D, Bennett HP, ''et al.'' |title=Cloning of human PEX cDNA. Expression, subcellular localization, and endopeptidase activity. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13729-37 |year= 1998 |pmid= 9593714 |doi= }}
*{{cite journal | author=Econs MJ, Friedman NE, Rowe PS, ''et al.'' |title=A PHEX gene mutation is responsible for adult-onset vitamin D-resistant hypophosphatemic osteomalacia: evidence that the disorder is not a distinct entity from X-linked hypophosphatemic rickets. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 10 |pages= 3459-62 |year= 1998 |pmid= 9768646 |doi= }}
*{{cite journal | author=Dixon PH, Christie PT, Wooding C, ''et al.'' |title=Mutational analysis of PHEX gene in X-linked hypophosphatemia. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 10 |pages= 3615-23 |year= 1998 |pmid= 9768674 |doi= }}
*{{cite journal | author=Filisetti D, Ostermann G, von Bredow M, ''et al.'' |title=Non-random distribution of mutations in the PHEX gene, and under-detected missense mutations at non-conserved residues. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 5 |pages= 615-9 |year= 1999 |pmid= 10439971 |doi= 10.1038/sj.ejhg.5200341 }}
*{{cite journal | author=Blydt-Hansen TD, Tenenhouse HS, Goodyer P |title=PHEX expression in parathyroid gland and parathyroid hormone dysregulation in X-linked hypophosphatemia. |journal=Pediatr. Nephrol. |volume=13 |issue= 7 |pages= 607-11 |year= 1999 |pmid= 10460513 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP2CB... {November 19, 2007 10:56:58 AM PST}
- SEARCH REDIRECT: Control Box Found: PPP2CB {November 19, 2007 10:57:20 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:57:21 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:57:21 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:57:21 AM PST}
- UPDATED: Updated protein page: PPP2CB {November 19, 2007 10:57:28 AM PST}
- INFO: Beginning work on PPP2R5A... {November 19, 2007 10:57:28 AM PST}
- SEARCH REDIRECT: Control Box Found: PPP2R5A {November 19, 2007 10:57:59 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:58:02 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:58:02 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:58:02 AM PST}
- UPDATED: Updated protein page: PPP2R5A {November 19, 2007 10:58:08 AM PST}
- INFO: Beginning work on RAD23B... {November 19, 2007 10:58:08 AM PST}
- SEARCH REDIRECT: Control Box Found: RAD23B {November 19, 2007 10:58:42 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 10:58:44 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 10:58:44 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 10:58:44 AM PST}
- UPDATED: Updated protein page: RAD23B {November 19, 2007 10:58:52 AM PST}
- INFO: Beginning work on RNASE1... {November 19, 2007 10:58:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 10:59:23 AM 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_RNASE1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dza.
| PDB = {{PDB2|1dza}}, {{PDB2|1e21}}, {{PDB2|1h8x}}, {{PDB2|1z7x}}
| Name = Ribonuclease, RNase A family, 1 (pancreatic)
| HGNCid = 10044
| Symbol = RNASE1
| AltSymbols =; MGC12408; RIB1; RNS1
| OMIM = 180440
| ECnumber =
| Homologene = 7919
| MGIid = 97919
| GeneAtlas_image1 = PBB_GE_RNASE1_201785_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004522 |text = pancreatic ribonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6035
| Hs_Ensembl = ENSG00000129538
| Hs_RefseqProtein = NP_002924
| Hs_RefseqmRNA = NM_002933
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 20339356
| Hs_GenLoc_end = 20340876
| Hs_Uniprot = P07998
| Mm_EntrezGene = 19752
| Mm_Ensembl = ENSMUSG00000035896
| Mm_RefseqmRNA = NM_011271
| Mm_RefseqProtein = NP_035401
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 50066953
| Mm_GenLoc_end = 50068718
| Mm_Uniprot = Q8C6G3
}}
}}
'''Ribonuclease, RNase A family, 1 (pancreatic)''', also known as '''RNASE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RNASE1 ribonuclease, RNase A family, 1 (pancreatic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6035| 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 pancreatic-type of secretory ribonucleases, a subset of the ribonuclease A superfamily. The encoded endonuclease cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2',3'-cyclic nucleotides, with a pH optimum near 8.0. The encoded protein is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: RNASE1 ribonuclease, RNase A family, 1 (pancreatic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6035| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nogués MV, Vilanova M, Cuchillo CM |title=Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites. |journal=Biochim. Biophys. Acta |volume=1253 |issue= 1 |pages= 16-24 |year= 1996 |pmid= 7492594 |doi= }}
*{{cite journal | author=Schienman JE, Holt RA, Auerbach MR, Stewart CB |title=Duplication and divergence of 2 distinct pancreatic ribonuclease genes in leaf-eating African and Asian colobine monkeys. |journal=Mol. Biol. Evol. |volume=23 |issue= 8 |pages= 1465-79 |year= 2006 |pmid= 16751256 |doi= 10.1093/molbev/msl025 }}
*{{cite journal | author=Sakakibara R, Hashida K, Kitahara T, Ishiguro M |title=Characterization of a unique nonsecretory ribonuclease from urine of pregnant women. |journal=J. Biochem. |volume=111 |issue= 3 |pages= 325-30 |year= 1992 |pmid= 1587793 |doi= }}
*{{cite journal | author=Haugg M, Schein CH |title=The DNA sequences of the human and hamster secretory ribonucleases determined with the polymerase chain reaction (PCR). |journal=Nucleic Acids Res. |volume=20 |issue= 3 |pages= 612 |year= 1992 |pmid= 1741299 |doi= }}
*{{cite journal | author=Sakakibara R, Hashida K, Tominaga N, ''et al.'' |title=A putative mouse oocyte maturation inhibitory protein from urine of pregnant women: N-terminal sequence homology with human nonsecretory ribonuclease. |journal=Chem. Pharm. Bull. |volume=39 |issue= 1 |pages= 146-9 |year= 1991 |pmid= 2049798 |doi= }}
*{{cite journal | author=Mizuta K, Awazu S, Yasuda T, Kishi K |title=Purification and characterization of three ribonucleases from human kidney: comparison with urine ribonucleases. |journal=Arch. Biochem. Biophys. |volume=281 |issue= 1 |pages= 144-51 |year= 1990 |pmid= 2383019 |doi= }}
*{{cite journal | author=Beintema JJ, Blank A, Schieven GL, ''et al.'' |title=Differences in glycosylation pattern of human secretory ribonucleases. |journal=Biochem. J. |volume=255 |issue= 2 |pages= 501-5 |year= 1989 |pmid= 3202829 |doi= }}
*{{cite journal | author=Beintema JJ, Wietzes P, Weickmann JL, Glitz DG |title=The amino acid sequence of human pancreatic ribonuclease. |journal=Anal. Biochem. |volume=136 |issue= 1 |pages= 48-64 |year= 1984 |pmid= 6201087 |doi= }}
*{{cite journal | author=Russo N, de Nigris M, Ciardiello A, ''et al.'' |title=Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease. |journal=FEBS Lett. |volume=369 |issue= 2-3 |pages= 352 |year= 1995 |pmid= 7649283 |doi= }}
*{{cite journal | author=Seno M, Futami J, Kosaka M, ''et al.'' |title=Nucleotide sequence encoding human pancreatic ribonuclease. |journal=Biochim. Biophys. Acta |volume=1218 |issue= 3 |pages= 466-8 |year= 1994 |pmid= 8049276 |doi= }}
*{{cite journal | author=Yasuda T, Nadano D, Takeshita H, Kishi K |title=Two distinct secretory ribonucleases from human cerebrum: purification, characterization and relationships to other ribonucleases. |journal=Biochem. J. |volume=296 ( Pt 3) |issue= |pages= 617-25 |year= 1994 |pmid= 8280059 |doi= }}
*{{cite journal | author=Kochetov AV, Lukasheva VV, Filipenko ML, ''et al.'' |title=[Primary structure of the coding part of the gene for human pancreatic ribonuclease and its chromosomal location] |journal=Bioorg. Khim. |volume=21 |issue= 9 |pages= 691-4 |year= 1996 |pmid= 8588814 |doi= }}
*{{cite journal | author=Papageorgiou AC, Shapiro R, Acharya KR |title=Molecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution. |journal=EMBO J. |volume=16 |issue= 17 |pages= 5162-77 |year= 1997 |pmid= 9311977 |doi= 10.1093/emboj/16.17.5162 }}
*{{cite journal | author=Klink TA, Woycechowsky KJ, Taylor KM, Raines RT |title=Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A. |journal=Eur. J. Biochem. |volume=267 |issue= 2 |pages= 566-72 |year= 2000 |pmid= 10632727 |doi= }}
*{{cite journal | author=Pous J, Canals A, Terzyan SS, ''et al.'' |title=Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases. |journal=J. Mol. Biol. |volume=303 |issue= 1 |pages= 49-60 |year= 2000 |pmid= 11021969 |doi= 10.1006/jmbi.2000.4506 }}
*{{cite journal | author=Pous J, Mallorquí-Fernández G, Peracaula R, ''et al.'' |title=Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=57 |issue= Pt 4 |pages= 498-505 |year= 2001 |pmid= 11264578 |doi= }}
*{{cite journal | author=Gaur D, Swaminathan S, Batra JK |title=Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor. Generation of inhibitor-resistant cytotoxic variants. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 24978-84 |year= 2001 |pmid= 11342552 |doi= 10.1074/jbc.M102440200 }}
*{{cite journal | author=Futami J, Maeda T, Kitazoe M, ''et al.'' |title=Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups. |journal=Biochemistry |volume=40 |issue= 25 |pages= 7518-24 |year= 2001 |pmid= 11412105 |doi= }}
*{{cite journal | author=Canals A, Pous J, Guasch A, ''et al.'' |title=The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization. |journal=Structure |volume=9 |issue= 10 |pages= 967-76 |year= 2002 |pmid= 11591351 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SOX2... {November 19, 2007 11:00:05 AM PST}
- SEARCH REDIRECT: Control Box Found: SOX2 {November 19, 2007 11:00:56 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:00:58 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:00:58 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:00:58 AM PST}
- UPDATED: Updated protein page: SOX2 {November 19, 2007 11:01:04 AM PST}
- INFO: Beginning work on SPTBN1... {November 19, 2007 11:01:04 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:01:59 AM 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_SPTBN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aa2.
| PDB = {{PDB2|1aa2}}, {{PDB2|1bkr}}, {{PDB2|1btn}}, {{PDB2|1mph}}
| Name = Spectrin, beta, non-erythrocytic 1
| HGNCid = 11275
| Symbol = SPTBN1
| AltSymbols =; ELF; SPTB2; betaSpII
| OMIM = 182790
| ECnumber =
| Homologene = 2354
| MGIid = 98388
| GeneAtlas_image1 = PBB_GE_SPTBN1_215918_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SPTBN1_200671_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SPTBN1_200672_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0008091 |text = spectrin}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6711
| Hs_Ensembl = ENSG00000115306
| Hs_RefseqProtein = NP_003119
| Hs_RefseqmRNA = NM_003128
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 54537143
| Hs_GenLoc_end = 54749366
| Hs_Uniprot = Q01082
| Mm_EntrezGene = 20742
| Mm_Ensembl = ENSMUSG00000020315
| Mm_RefseqmRNA = NM_009260
| Mm_RefseqProtein = NP_033286
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 29999722
| Mm_GenLoc_end = 30168144
| Mm_Uniprot = Q3TEM7
}}
}}
'''Spectrin, beta, non-erythrocytic 1''', also known as '''SPTBN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6711| 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 = Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. This gene is one member of a family of beta-spectrin genes. The encoded protein contains an N-terminal actin-binding domain, and 17 spectrin repeats which are involved in dimer formation. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6711| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hu RJ, Watanabe M, Bennett V |title=Characterization of human brain cDNA encoding the general isoform of beta-spectrin. |journal=J. Biol. Chem. |volume=267 |issue= 26 |pages= 18715-22 |year= 1992 |pmid= 1527002 |doi= }}
*{{cite journal | author=Yoon SH, Skalka H, Prchal JT |title=Presence of erythroid and nonerythroid spectrin transcripts in human lens and cerebellum. |journal=Invest. Ophthalmol. Vis. Sci. |volume=30 |issue= 8 |pages= 1860-6 |year= 1989 |pmid= 2474519 |doi= }}
*{{cite journal | author=Chang JG, Scarpa A, Eddy RL, ''et al.'' |title=Cloning of a portion of the chromosomal gene and cDNA for human beta-fodrin, the nonerythroid form of beta-spectrin. |journal=Genomics |volume=17 |issue= 2 |pages= 287-93 |year= 1993 |pmid= 8406479 |doi= 10.1006/geno.1993.1323 }}
*{{cite journal | author=Shimizu T, Takakuwa Y, Koizumi H, ''et al.'' |title=Calcium-dependent peripheral localization of 4.1-like proteins and fodrin in cultured human keratinocytes. |journal=Biol. Cell |volume=86 |issue= 1 |pages= 19-26 |year= 1996 |pmid= 8688828 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Holleran EA, Tokito MK, Karki S, Holzbaur EL |title=Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. |journal=J. Cell Biol. |volume=135 |issue= 6 Pt 2 |pages= 1815-29 |year= 1997 |pmid= 8991093 |doi= }}
*{{cite journal | author=Djinovic Carugo K, Bañuelos S, Saraste M |title=Crystal structure of a calponin homology domain. |journal=Nat. Struct. Biol. |volume=4 |issue= 3 |pages= 175-9 |year= 1997 |pmid= 9164454 |doi= }}
*{{cite journal | author=Scoles DR, Huynh DP, Morcos PA, ''et al.'' |title=Neurofibromatosis 2 tumour suppressor schwannomin interacts with betaII-spectrin. |journal=Nat. Genet. |volume=18 |issue= 4 |pages= 354-9 |year= 1998 |pmid= 9537418 |doi= 10.1038/ng0498-354 }}
*{{cite journal | author=Sihag RK |title=Brain beta-spectrin phosphorylation: phosphate analysis and identification of threonine-347 as a heparin-sensitive protein kinase phosphorylation site. |journal=J. Neurochem. |volume=71 |issue= 5 |pages= 2220-8 |year= 1998 |pmid= 9798950 |doi= }}
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}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SRD5A1... {November 19, 2007 11:01:59 AM PST}
- SEARCH REDIRECT: Control Box Found: SRD5A1 {November 19, 2007 11:02:20 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:02:22 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:02:22 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:02:22 AM PST}
- UPDATED: Updated protein page: SRD5A1 {November 19, 2007 11:02:28 AM PST}
end log.
