Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 21:38, 17 November 2007 (UTC)
[edit]Proteins without matches (14)
[edit]Proteins with a High Potential Match (7)
[edit]Redirected Proteins (4)
[edit]Manual Inspection (Page not found) (21)
[edit]
Protein Status Grid - Date: 21:38, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 21:38, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on AMH... {November 17, 2007 1:06:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:06:41 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Anti-Mullerian hormone
| HGNCid = 464
| Symbol = AMH
| AltSymbols =; MIF; MIS
| OMIM = 600957
| ECnumber =
| Homologene = 68060
| MGIid = 88006
| GeneAtlas_image1 = PBB_GE_AMH_206516_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001880 |text = Mullerian duct regression}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007506 |text = gonadal mesoderm development}} {{GNF_GO|id=GO:0007530 |text = sex determination}} {{GNF_GO|id=GO:0007548 |text = sex differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 268
| Hs_Ensembl = ENSG00000104899
| Hs_RefseqProtein = NP_000470
| Hs_RefseqmRNA = NM_000479
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 2200122
| Hs_GenLoc_end = 2203071
| Hs_Uniprot = P03971
| Mm_EntrezGene = 11705
| Mm_Ensembl = ENSMUSG00000035262
| Mm_RefseqmRNA = NM_007445
| Mm_RefseqProtein = NP_031471
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 80208377
| Mm_GenLoc_end = 80210777
| Mm_Uniprot = Q5EC55
}}
}}
'''Anti-Mullerian hormone''', also known as '''AMH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMH anti-Mullerian hormone| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=268| 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 = Anti-Mullerian hormone is a member of the transforming growth factor-beta gene family which mediates male sexual differentiation. Anti-Mullerian hormone causes the regression of Mullerian ducts which would otherwise differentiate into the uterus and fallopian tubes. Some mutations in the anti-Mullerian hormone result in persistent Mullerian duct syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: AMH anti-Mullerian hormone| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=268| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Teixeira J, Donahoe PK |title=Molecular biology of MIS and its receptors. |journal=J. Androl. |volume=17 |issue= 4 |pages= 336-41 |year= 1996 |pmid= 8889695 |doi= }}
*{{cite journal | author=Lane AH, Donahoe PK |title=New insights into mullerian inhibiting substance and its mechanism of action. |journal=J. Endocrinol. |volume=158 |issue= 1 |pages= 1-6 |year= 1998 |pmid= 9713320 |doi= }}
*{{cite journal | author=Josso N, di Clemente N, Gouédard L |title=Anti-Müllerian hormone and its receptors. |journal=Mol. Cell. Endocrinol. |volume=179 |issue= 1-2 |pages= 25-32 |year= 2001 |pmid= 11420127 |doi= }}
*{{cite journal | author=Picard JY, Belville C |title=[Genetics and molecular pathology of anti-Mullerian hormone and its receptor] |journal=J. Soc. Biol. |volume=196 |issue= 3 |pages= 217-21 |year= 2003 |pmid= 12462075 |doi= }}
*{{cite journal | author=Sinisi AA, Pasquali D, Notaro A, Bellastella A |title=Sexual differentiation. |journal=J. Endocrinol. Invest. |volume=26 |issue= 3 Suppl |pages= 23-8 |year= 2004 |pmid= 12834017 |doi= }}
*{{cite journal | author=Josso N, Picard JY, Rey R, di Clemente N |title=Testicular anti-Müllerian hormone: history, genetics, regulation and clinical applications. |journal=Pediatric endocrinology reviews : PER |volume=3 |issue= 4 |pages= 347-58 |year= 2006 |pmid= 16816803 |doi= }}
*{{cite journal | author=Seifer DB, Maclaughlin DT |title=Mullerian Inhibiting Substance is an ovarian growth factor of emerging clinical significance. |journal=Fertil. Steril. |volume=88 |issue= 3 |pages= 539-46 |year= 2007 |pmid= 17559842 |doi= 10.1016/j.fertnstert.2007.02.014 }}
*{{cite journal | author=Carré-Eusèbe D, Imbeaud S, Harbison M, ''et al.'' |title=Variants of the anti-Müllerian hormone gene in a compound heterozygote with the persistent Müllerian duct syndrome and his family. |journal=Hum. Genet. |volume=90 |issue= 4 |pages= 389-94 |year= 1993 |pmid= 1483695 |doi= }}
*{{cite journal | author=Whitman GF, Pantazis CG |title=Cellular localization of müllerian inhibiting substance messenger ribonucleic acid during human ovarian follicular development. |journal=Am. J. Obstet. Gynecol. |volume=165 |issue= 6 Pt 1 |pages= 1881-6 |year= 1992 |pmid= 1750488 |doi= }}
*{{cite journal | author=Knebelmann B, Boussin L, Guerrier D, ''et al.'' |title=Anti-Müllerian hormone Bruxelles: a nonsense mutation associated with the persistent Müllerian duct syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3767-71 |year= 1991 |pmid= 2023927 |doi= }}
*{{cite journal | author=Legeai L, Lefèvre G, Vigier B, ''et al.'' |title=A monoclonal antibody against human testicular anti-müllerian hormone. |journal=American journal of reproductive immunology and microbiology : AJRIM |volume=18 |issue= 2 |pages= 39-43 |year= 1989 |pmid= 2467567 |doi= }}
*{{cite journal | author=Cohen-Haguenauer O, Picard JY, Mattéi MG, ''et al.'' |title=Mapping of the gene for anti-müllerian hormone to the short arm of human chromosome 19. |journal=Cytogenet. Cell Genet. |volume=44 |issue= 1 |pages= 2-6 |year= 1987 |pmid= 3028714 |doi= }}
*{{cite journal | author=Cate RL, Mattaliano RJ, Hession C, ''et al.'' |title=Isolation of the bovine and human genes for Müllerian inhibiting substance and expression of the human gene in animal cells. |journal=Cell |volume=45 |issue= 5 |pages= 685-98 |year= 1986 |pmid= 3754790 |doi= }}
*{{cite journal | author=Imbeaud S, Carré-Eusèbe D, Rey R, ''et al.'' |title=Molecular genetics of the persistent müllerian duct syndrome: a study of 19 families. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 125-31 |year= 1994 |pmid= 8162013 |doi= }}
*{{cite journal | author=Maggard MA, Catlin EA, Hudson PL, ''et al.'' |title=Reduction of epidermal growth factor receptor phosphorylation by activated Mullerian inhibiting substance is vanadate-sensitive. |journal=Metab. Clin. Exp. |volume=45 |issue= 2 |pages= 190-5 |year= 1996 |pmid= 8596488 |doi= }}
*{{cite journal | author=Nachtigal MW, Ingraham HA |title=Bioactivation of Müllerian inhibiting substance during gonadal development by a kex2/subtilisin-like endoprotease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 15 |pages= 7711-6 |year= 1996 |pmid= 8755541 |doi= }}
*{{cite journal | author=Mishina Y, Rey R, Finegold MJ, ''et al.'' |title=Genetic analysis of the Müllerian-inhibiting substance signal transduction pathway in mammalian sexual differentiation. |journal=Genes Dev. |volume=10 |issue= 20 |pages= 2577-87 |year= 1997 |pmid= 8895659 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BMPR1A... {November 17, 2007 1:06:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:07:14 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BMPR1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1es7.
| PDB = {{PDB2|1es7}}, {{PDB2|1rew}}, {{PDB2|2goo}}, {{PDB2|2h62}}, {{PDB2|2h64}}
| Name = Bone morphogenetic protein receptor, type IA
| HGNCid = 1076
| Symbol = BMPR1A
| AltSymbols =; ACVRLK3; ALK3; CD292
| OMIM = 601299
| ECnumber =
| Homologene = 20911
| MGIid = 1338938
| GeneAtlas_image1 = PBB_GE_BMPR1A_213578_at_tn.png
| GeneAtlas_image2 = PBB_GE_BMPR1A_204832_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005024 |text = transforming growth factor beta receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046332 |text = SMAD binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 657
| Hs_Ensembl = ENSG00000107779
| Hs_RefseqProtein = NP_004320
| Hs_RefseqmRNA = NM_004329
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 88506387
| Hs_GenLoc_end = 88674925
| Hs_Uniprot = P36894
| Mm_EntrezGene = 12166
| Mm_Ensembl = ENSMUSG00000021796
| Mm_RefseqmRNA = NM_009758
| Mm_RefseqProtein = NP_033888
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 33240158
| Mm_GenLoc_end = 33331638
| Mm_Uniprot = Q3UP52
}}
}}
'''Bone morphogenetic protein receptor, type IA''', also known as '''BMPR1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BMPR1A bone morphogenetic protein receptor, type IA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=657| 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 bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.<ref name="entrez">{{cite web | title = Entrez Gene: BMPR1A bone morphogenetic protein receptor, type IA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=657| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nickel J, Dreyer MK, Kirsch T, Sebald W |title=The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists. |journal=The Journal of bone and joint surgery. American volume |volume=83-A Suppl 1 |issue= Pt 1 |pages= S7-14 |year= 2001 |pmid= 11263668 |doi= }}
*{{cite journal | author=Liu F, Ventura F, Doody J, Massagué J |title=Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. |journal=Mol. Cell. Biol. |volume=15 |issue= 7 |pages= 3479-86 |year= 1995 |pmid= 7791754 |doi= }}
*{{cite journal | author=ten Dijke P, Ichijo H, Franzén P, ''et al.'' |title=Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity. |journal=Oncogene |volume=8 |issue= 10 |pages= 2879-87 |year= 1993 |pmid= 8397373 |doi= }}
*{{cite journal | author=Ishidou Y, Kitajima I, Obama H, ''et al.'' |title=Enhanced expression of type I receptors for bone morphogenetic proteins during bone formation. |journal=J. Bone Miner. Res. |volume=10 |issue= 11 |pages= 1651-9 |year= 1996 |pmid= 8592941 |doi= }}
*{{cite journal | author=Yamada N, Kato M, ten Dijke P, ''et al.'' |title=Bone morphogenetic protein type IB receptor is progressively expressed in malignant glioma tumours. |journal=Br. J. Cancer |volume=73 |issue= 5 |pages= 624-9 |year= 1996 |pmid= 8605097 |doi= }}
*{{cite journal | author=Nishitoh H, Ichijo H, Kimura M, ''et al.'' |title=Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21345-52 |year= 1996 |pmid= 8702914 |doi= }}
*{{cite journal | author=Wu X, Robinson CE, Fong HW, Gimble JM |title=Analysis of the native murine bone morphogenetic protein serine threonine kinase type I receptor (ALK-3). |journal=J. Cell. Physiol. |volume=168 |issue= 2 |pages= 453-61 |year= 1996 |pmid= 8707881 |doi= 10.1002/(SICI)1097-4652(199608)168:2<453::AID-JCP24>3.0.CO;2-2 }}
*{{cite journal | author=Erlacher L, McCartney J, Piek E, ''et al.'' |title=Cartilage-derived morphogenetic proteins and osteogenic protein-1 differentially regulate osteogenesis. |journal=J. Bone Miner. Res. |volume=13 |issue= 3 |pages= 383-92 |year= 1998 |pmid= 9525338 |doi= }}
*{{cite journal | author=Zhang D, Mehler MF, Song Q, Kessler JA |title=Development of bone morphogenetic protein receptors in the nervous system and possible roles in regulating trkC expression. |journal=J. Neurosci. |volume=18 |issue= 9 |pages= 3314-26 |year= 1998 |pmid= 9547239 |doi= }}
*{{cite journal | author=Kurozumi K, Nishita M, Yamaguchi K, ''et al.'' |title=BRAM1, a BMP receptor-associated molecule involved in BMP signalling. |journal=Genes Cells |volume=3 |issue= 4 |pages= 257-64 |year= 1998 |pmid= 9663660 |doi= }}
*{{cite journal | author=Ide H, Saito-Ohara F, Ohnami S, ''et al.'' |title=Assignment of the BMPR1A and BMPR1B genes to human chromosome 10q22.3 and 4q23-->q24 byin situ hybridization and radiation hybrid map ping. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 285-6 |year= 1998 |pmid= 9730621 |doi= }}
*{{cite journal | author=Souchelnytskyi S, Nakayama T, Nakao A, ''et al.'' |title=Physical and functional interaction of murine and Xenopus Smad7 with bone morphogenetic protein receptors and transforming growth factor-beta receptors. |journal=J. Biol. Chem. |volume=273 |issue= 39 |pages= 25364-70 |year= 1998 |pmid= 9738003 |doi= }}
*{{cite journal | author=You L, Kruse FE, Pohl J, Völcker HE |title=Bone morphogenetic proteins and growth and differentiation factors in the human cornea. |journal=Invest. Ophthalmol. Vis. Sci. |volume=40 |issue= 2 |pages= 296-311 |year= 1999 |pmid= 9950587 |doi= }}
*{{cite journal | author=Aström AK, Jin D, Imamura T, ''et al.'' |title=Chromosomal localization of three human genes encoding bone morphogenetic protein receptors. |journal=Mamm. Genome |volume=10 |issue= 3 |pages= 299-302 |year= 1999 |pmid= 10051328 |doi= }}
*{{cite journal | author=Ebisawa T, Tada K, Kitajima I, ''et al.'' |title=Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue= |pages= 3519-27 |year= 2000 |pmid= 10504300 |doi= }}
*{{cite journal | author=Kirsch T, Nickel J, Sebald W |title=Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2. |journal=FEBS Lett. |volume=468 |issue= 2-3 |pages= 215-9 |year= 2000 |pmid= 10692589 |doi= }}
*{{cite journal | author=Gilboa L, Nohe A, Geissendörfer T, ''et al.'' |title=Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. |journal=Mol. Biol. Cell |volume=11 |issue= 3 |pages= 1023-35 |year= 2000 |pmid= 10712517 |doi= }}
*{{cite journal | author=Kim IY, Lee DH, Ahn HJ, ''et al.'' |title=Expression of bone morphogenetic protein receptors type-IA, -IB and -II correlates with tumor grade in human prostate cancer tissues. |journal=Cancer Res. |volume=60 |issue= 11 |pages= 2840-4 |year= 2000 |pmid= 10850425 |doi= }}
*{{cite journal | author=Kirsch T, Sebald W, Dreyer MK |title=Crystal structure of the BMP-2-BRIA ectodomain complex. |journal=Nat. Struct. Biol. |volume=7 |issue= 6 |pages= 492-6 |year= 2000 |pmid= 10881198 |doi= 10.1038/75903 }}
*{{cite journal | author=Wan M, Shi X, Feng X, Cao X |title=Transcriptional mechanisms of bone morphogenetic protein-induced osteoprotegrin gene expression. |journal=J. Biol. Chem. |volume=276 |issue= 13 |pages= 10119-25 |year= 2001 |pmid= 11139569 |doi= 10.1074/jbc.M006918200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAV2... {November 17, 2007 1:07:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:07:43 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Caveolin 2
| HGNCid = 1528
| Symbol = CAV2
| AltSymbols =; CAV; MGC12294
| OMIM = 601048
| ECnumber =
| Homologene = 942
| MGIid = 107571
| GeneAtlas_image1 = PBB_GE_CAV2_203323_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAV2_203324_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016599 |text = caveolar membrane}} {{GNF_GO|id=GO:0030133 |text = transport vesicle}} {{GNF_GO|id=GO:0045121 |text = lipid raft}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0001937 |text = negative regulation of endothelial cell proliferation}} {{GNF_GO|id=GO:0051259 |text = protein oligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 858
| Hs_Ensembl = ENSG00000105971
| Hs_RefseqProtein = NP_001224
| Hs_RefseqmRNA = NM_001233
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 115926680
| Hs_GenLoc_end = 115935830
| Hs_Uniprot = P51636
| Mm_EntrezGene = 12390
| Mm_Ensembl = ENSMUSG00000000058
| Mm_RefseqmRNA = NM_016900
| Mm_RefseqProtein = NP_058596
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 17231310
| Mm_GenLoc_end = 17239004
| Mm_Uniprot = Q924U3
}}
}}
'''Caveolin 2''', also known as '''CAV2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CAV2 caveolin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=858| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. Two transcript variants encoding distinct isoforms have been identified for this gene. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by one transcript.<ref name="entrez">{{cite web | title = Entrez Gene: CAV2 caveolin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=858| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Engelman JA, Zhang X, Galbiati F, ''et al.'' |title=Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy. |journal=Am. J. Hum. Genet. |volume=63 |issue= 6 |pages= 1578-87 |year= 1999 |pmid= 9837809 |doi= }}
*{{cite journal | author=Glenney JR |title=The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles. |journal=FEBS Lett. |volume=314 |issue= 1 |pages= 45-8 |year= 1992 |pmid= 1360410 |doi= }}
*{{cite journal | author=Murata M, Peränen J, Schreiner R, ''et al.'' |title=VIP21/caveolin is a cholesterol-binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 22 |pages= 10339-43 |year= 1995 |pmid= 7479780 |doi= }}
*{{cite journal | author=Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, ''et al.'' |title=Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening. |journal=Genomics |volume=23 |issue= 1 |pages= 42-50 |year= 1995 |pmid= 7829101 |doi= 10.1006/geno.1994.1457 }}
*{{cite journal | author=Scherer PE, Okamoto T, Chun M, ''et al.'' |title=Identification, sequence, and expression of caveolin-2 defines a caveolin gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 131-5 |year= 1996 |pmid= 8552590 |doi= }}
*{{cite journal | author=Scherer PE, Lewis RY, Volonte D, ''et al.'' |title=Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29337-46 |year= 1997 |pmid= 9361015 |doi= }}
*{{cite journal | author=Galbiati F, Volonte D, Gil O, ''et al.'' |title=Expression of caveolin-1 and -2 in differentiating PC12 cells and dorsal root ganglion neurons: caveolin-2 is up-regulated in response to cell injury. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 17 |pages= 10257-62 |year= 1998 |pmid= 9707634 |doi= }}
*{{cite journal | author=Engelman JA, Zhang XL, Lisanti MP |title=Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers. |journal=FEBS Lett. |volume=436 |issue= 3 |pages= 403-10 |year= 1998 |pmid= 9801158 |doi= }}
*{{cite journal | author=Fra AM, Mastroianni N, Mancini M, ''et al.'' |title=Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors. |journal=Genomics |volume=56 |issue= 3 |pages= 355-6 |year= 1999 |pmid= 10087206 |doi= 10.1006/geno.1998.5723 }}
*{{cite journal | author=Volonte D, Galbiati F, Li S, ''et al.'' |title=Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12702-9 |year= 1999 |pmid= 10212252 |doi= }}
*{{cite journal | author=Engelman JA, Zhang XL, Lisanti MP |title=Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines. |journal=FEBS Lett. |volume=448 |issue= 2-3 |pages= 221-30 |year= 1999 |pmid= 10218480 |doi= }}
*{{cite journal | author=Mora R, Bonilha VL, Marmorstein A, ''et al.'' |title=Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25708-17 |year= 1999 |pmid= 10464308 |doi= }}
*{{cite journal | author=Fra AM, Pasqualetto E, Mancini M, Sitia R |title=Genomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2. |journal=Gene |volume=243 |issue= 1-2 |pages= 75-83 |year= 2000 |pmid= 10675615 |doi= }}
*{{cite journal | author=Schwab W, Kasper M, Gavlik JM, ''et al.'' |title=Characterization of caveolins from human knee joint catilage: expression of caveolin-1, -2, and -3 in chondrocytes and association with integrin beta1. |journal=Histochem. Cell Biol. |volume=113 |issue= 3 |pages= 221-5 |year= 2000 |pmid= 10817676 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=de Marco MC, Kremer L, Albar JP, ''et al.'' |title=BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 23009-17 |year= 2001 |pmid= 11294831 |doi= 10.1074/jbc.M009739200 }}
*{{cite journal | author=Andoh A, Saotome T, Sato H, ''et al.'' |title=Epithelial expression of caveolin-2, but not caveolin-1, is enhanced in the inflamed mucosa of patients with ulcerative colitis. |journal=Inflamm. Bowel Dis. |volume=7 |issue= 3 |pages= 210-4 |year= 2002 |pmid= 11515846 |doi= }}
*{{cite journal | author=Xu XR, Huang J, Xu ZG, ''et al.'' |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089-94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTNNA1... {November 17, 2007 1:09:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:10:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTNNA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dov.
| PDB = {{PDB2|1dov}}, {{PDB2|1dow}}, {{PDB2|1h6g}}, {{PDB2|1l7c}}
| Name = Catenin (cadherin-associated protein), alpha 1, 102kDa
| HGNCid = 2509
| Symbol = CTNNA1
| AltSymbols =; CAP102; FLJ36832
| OMIM = 116805
| ECnumber =
| Homologene = 1433
| MGIid = 88274
| GeneAtlas_image1 = PBB_GE_CTNNA1_200764_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CTNNA1_200765_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CTNNA1_210844_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017166 |text = vinculin binding}} {{GNF_GO|id=GO:0045296 |text = cadherin binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0043297 |text = apical junction assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1495
| Hs_Ensembl = ENSG00000044115
| Hs_RefseqProtein = NP_001894
| Hs_RefseqmRNA = NM_001903
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 138117006
| Hs_GenLoc_end = 138298619
| Hs_Uniprot = P35221
| Mm_EntrezGene = 12385
| Mm_Ensembl = ENSMUSG00000037815
| Mm_RefseqmRNA = NM_009818
| Mm_RefseqProtein = NP_033948
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 35244863
| Mm_GenLoc_end = 35380747
| Mm_Uniprot = Q3TGQ3
}}
}}
'''Catenin (cadherin-associated protein), alpha 1, 102kDa''', also known as '''CTNNA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTNNA1 catenin (cadherin-associated protein), alpha 1, 102kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1495| 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=Nagafuchi A, Takeichi M, Tsukita S |title=The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression. |journal=Cell |volume=65 |issue= 5 |pages= 849-57 |year= 1991 |pmid= 1904011 |doi= }}
*{{cite journal | author=Herrenknecht K, Ozawa M, Eckerskorn C, ''et al.'' |title=The uvomorulin-anchorage protein alpha catenin is a vinculin homologue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 20 |pages= 9156-60 |year= 1991 |pmid= 1924379 |doi= }}
*{{cite journal | author=Kinch MS, Clark GJ, Der CJ, Burridge K |title=Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. |journal=J. Cell Biol. |volume=130 |issue= 2 |pages= 461-71 |year= 1995 |pmid= 7542250 |doi= }}
*{{cite journal | author=Sacco PA, McGranahan TM, Wheelock MJ, Johnson KR |title=Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20201-6 |year= 1995 |pmid= 7650039 |doi= }}
*{{cite journal | author=Daniel JM, Reynolds AB |title=The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 4819-24 |year= 1995 |pmid= 7651399 |doi= }}
*{{cite journal | author=Aberle H, Butz S, Stappert J, ''et al.'' |title=Assembly of the cadherin-catenin complex in vitro with recombinant proteins. |journal=J. Cell. Sci. |volume=107 ( Pt 12) |issue= |pages= 3655-63 |year= 1995 |pmid= 7706414 |doi= }}
*{{cite journal | author=Knudsen KA, Soler AP, Johnson KR, Wheelock MJ |title=Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin. |journal=J. Cell Biol. |volume=130 |issue= 1 |pages= 67-77 |year= 1995 |pmid= 7790378 |doi= }}
*{{cite journal | author=Rimm DL, Kebriaei P, Morrow JS |title=Molecular cloning reveals alternative splice forms of human alpha(E)-catenin. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 3 |pages= 1691-9 |year= 1994 |pmid= 7945318 |doi= 10.1006/bbrc.1994.2381 }}
*{{cite journal | author=Oyama T, Kanai Y, Ochiai A, ''et al.'' |title=A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines. |journal=Cancer Res. |volume=54 |issue= 23 |pages= 6282-7 |year= 1994 |pmid= 7954478 |doi= }}
*{{cite journal | author=McPherson JD, Morton RA, Ewing CM, ''et al.'' |title=Assignment of the human alpha-catenin gene (CTNNA1) to chromosome 5q21-q22. |journal=Genomics |volume=19 |issue= 1 |pages= 188-90 |year= 1994 |pmid= 8188230 |doi= 10.1006/geno.1994.1042 }}
*{{cite journal | author=Su LK, Vogelstein B, Kinzler KW |title=Association of the APC tumor suppressor protein with catenins. |journal=Science |volume=262 |issue= 5140 |pages= 1734-7 |year= 1994 |pmid= 8259519 |doi= }}
*{{cite journal | author=Oda T, Kanai Y, Shimoyama Y, ''et al.'' |title=Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human cancer cell line. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 3 |pages= 897-904 |year= 1993 |pmid= 8323564 |doi= 10.1006/bbrc.1993.1710 }}
*{{cite journal | author=Furukawa Y, Nakatsuru S, Nagafuchi A, ''et al.'' |title=Structure, expression and chromosome assignment of the human catenin (cadherin-associated protein) alpha 1 gene (CTNNA1). |journal=Cytogenet. Cell Genet. |volume=65 |issue= 1-2 |pages= 74-8 |year= 1993 |pmid= 8404069 |doi= }}
*{{cite journal | author=Obama H, Ozawa M |title=Identification of the domain of alpha-catenin involved in its association with beta-catenin and plakoglobin (gamma-catenin). |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11017-20 |year= 1997 |pmid= 9110993 |doi= }}
*{{cite journal | author=Linkels M, Bussemakers MJ, Nollet F, ''et al.'' |title=Molecular cloning of an alternative human alphaE-catenin cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=237 |issue= 1 |pages= 177-81 |year= 1997 |pmid= 9266853 |doi= 10.1006/bbrc.1997.7058 }}
*{{cite journal | author=Lewalle JM, Bajou K, Desreux J, ''et al.'' |title=Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro. |journal=Exp. Cell Res. |volume=237 |issue= 2 |pages= 347-56 |year= 1998 |pmid= 9434630 |doi= 10.1006/excr.1997.3799 }}
*{{cite journal | author=Reuver SM, Garner CC |title=E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton. |journal=J. Cell. Sci. |volume=111 ( Pt 8) |issue= |pages= 1071-80 |year= 1998 |pmid= 9512503 |doi= }}
*{{cite journal | author=Watabe-Uchida M, Uchida N, Imamura Y, ''et al.'' |title=alpha-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells. |journal=J. Cell Biol. |volume=142 |issue= 3 |pages= 847-57 |year= 1998 |pmid= 9700171 |doi= }}
*{{cite journal | author=Roe S, Koslov ER, Rimm DL |title=A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity. |journal=Cell Adhes. Commun. |volume=5 |issue= 4 |pages= 283-96 |year= 1998 |pmid= 9762469 |doi= }}
*{{cite journal | author=Itoh M, Morita K, Tsukita S |title=Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5981-6 |year= 1999 |pmid= 10026224 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP2B6... {November 17, 2007 1:10:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:10:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome P450, family 2, subfamily B, polypeptide 6
| HGNCid = 2615
| Symbol = CYP2B6
| AltSymbols =; CYP2B; CPB6; CYPIIB6; IIB1; P450
| OMIM = 123930
| ECnumber =
| Homologene = 73894
| MGIid = 88598
| GeneAtlas_image1 = PBB_GE_CYP2B6_206754_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYP2B6_206755_at_tn.png
| GeneAtlas_image3 = PBB_GE_CYP2B6_217133_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1555
| Hs_Ensembl = ENSG00000197408
| Hs_RefseqProtein = NP_000758
| Hs_RefseqmRNA = NM_000767
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 46189044
| Hs_GenLoc_end = 46216141
| Hs_Uniprot = P20813
| Mm_EntrezGene = 13088
| Mm_Ensembl = ENSMUSG00000030483
| Mm_RefseqmRNA = NM_009998
| Mm_RefseqProtein = NP_034128
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 25606418
| Mm_GenLoc_end = 25635383
| Mm_Uniprot = Q61461
}}
}}
'''Cytochrome P450, family 2, subfamily B, polypeptide 6''', also known as '''CYP2B6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP2B6 cytochrome P450, family 2, subfamily B, polypeptide 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1555| 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, CYP2B6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by phenobarbital. The enzyme is known to metabolize some xenobiotics, such as the anti-cancer drugs cyclophosphamide and ifosphamide. Transcript variants for this gene have been described; however, it has not been resolved whether these transcripts are in fact produced by this gene or by a closely related pseudogene, CYP2B7. Both the gene and the pseudogene are located in the middle of a CYP2A pseudogene found in a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q.<ref name="entrez">{{cite web | title = Entrez Gene: CYP2B6 cytochrome P450, family 2, subfamily B, polypeptide 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1555| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Nelson DR, Zeldin DC, Hoffman SM, ''et al.'' |title=Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. |journal=Pharmacogenetics |volume=14 |issue= 1 |pages= 1-18 |year= 2004 |pmid= 15128046 |doi= }}
*{{cite journal | author=Miles JS, McLaren AW, Gonzalez FJ, Wolf CR |title=Alternative splicing in the human cytochrome P450IIB6 gene: use of a cryptic exon within intron 3 and splice acceptor site within exon 4. |journal=Nucleic Acids Res. |volume=18 |issue= 1 |pages= 189 |year= 1990 |pmid= 2308828 |doi= }}
*{{cite journal | author=Yamano S, Nhamburo PT, Aoyama T, ''et al.'' |title=cDNA cloning and sequence and cDNA-directed expression of human P450 IIB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver. |journal=Biochemistry |volume=28 |issue= 18 |pages= 7340-8 |year= 1990 |pmid= 2573390 |doi= }}
*{{cite journal | author=Miles JS, McLaren AW, Wolf CR |title=Alternative splicing in the human cytochrome P450IIB6 gene generates a high level of aberrant messages. |journal=Nucleic Acids Res. |volume=17 |issue= 20 |pages= 8241-55 |year= 1989 |pmid= 2813061 |doi= }}
*{{cite journal | author=Miles JS, Spurr NK, Gough AC, ''et al.'' |title=A novel human cytochrome P450 gene (P450IIB): chromosomal localization and evidence for alternative splicing. |journal=Nucleic Acids Res. |volume=16 |issue= 13 |pages= 5783-95 |year= 1988 |pmid= 2899870 |doi= }}
*{{cite journal | author=Fernandez-Salguero P, Hoffman SM, Cholerton S, ''et al.'' |title=A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. |journal=Am. J. Hum. Genet. |volume=57 |issue= 3 |pages= 651-60 |year= 1995 |pmid= 7668294 |doi= }}
*{{cite journal | author=Trask B, Fertitta A, Christensen M, ''et al.'' |title=Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers. |journal=Genomics |volume=15 |issue= 1 |pages= 133-45 |year= 1993 |pmid= 8432525 |doi= }}
*{{cite journal | author=Hoffman SM, Fernandez-Salguero P, Gonzalez FJ, Mohrenweiser HW |title=Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19. |journal=J. Mol. Evol. |volume=41 |issue= 6 |pages= 894-900 |year= 1996 |pmid= 8587134 |doi= }}
*{{cite journal | author=Lewis DF, Lake BG |title=Molecular modelling of mammalian CYP2B isoforms and their interaction with substrates, inhibitors and redox partners. |journal=Xenobiotica |volume=27 |issue= 5 |pages= 443-78 |year= 1997 |pmid= 9179987 |doi= }}
*{{cite journal | author=Sueyoshi T, Kawamoto T, Zelko I, ''et al.'' |title=The repressed nuclear receptor CAR responds to phenobarbital in activating the human CYP2B6 gene. |journal=J. Biol. Chem. |volume=274 |issue= 10 |pages= 6043-6 |year= 1999 |pmid= 10037683 |doi= }}
*{{cite journal | author=Gervot L, Rochat B, Gautier JC, ''et al.'' |title=Human CYP2B6: expression, inducibility and catalytic activities. |journal=Pharmacogenetics |volume=9 |issue= 3 |pages= 295-306 |year= 1999 |pmid= 10471061 |doi= }}
*{{cite journal | author=Thum T, Borlak J |title=Gene expression in distinct regions of the heart. |journal=Lancet |volume=355 |issue= 9208 |pages= 979-83 |year= 2000 |pmid= 10768437 |doi= }}
*{{cite journal | author=Ariyoshi N, Miyazaki M, Toide K, ''et al.'' |title=A single nucleotide polymorphism of CYP2b6 found in Japanese enhances catalytic activity by autoactivation. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 5 |pages= 1256-60 |year= 2001 |pmid= 11243870 |doi= 10.1006/bbrc.2001.4524 }}
*{{cite journal | author=Oda Y, Hamaoka N, Hiroi T, ''et al.'' |title=Involvement of human liver cytochrome P4502B6 in the metabolism of propofol. |journal=British journal of clinical pharmacology |volume=51 |issue= 3 |pages= 281-5 |year= 2001 |pmid= 11298076 |doi= }}
*{{cite journal | author=Yanagihara Y, Kariya S, Ohtani M, ''et al.'' |title=Involvement of CYP2B6 in n-demethylation of ketamine in human liver microsomes. |journal=Drug Metab. Dispos. |volume=29 |issue= 6 |pages= 887-90 |year= 2001 |pmid= 11353758 |doi= }}
*{{cite journal | author=Lang T, Klein K, Fischer J, ''et al.'' |title=Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver. |journal=Pharmacogenetics |volume=11 |issue= 5 |pages= 399-415 |year= 2001 |pmid= 11470993 |doi= }}
*{{cite journal | author=Hidestrand M, Oscarson M, Salonen JS, ''et al.'' |title=CYP2B6 and CYP2C19 as the major enzymes responsible for the metabolism of selegiline, a drug used in the treatment of Parkinson's disease, as revealed from experiments with recombinant enzymes. |journal=Drug Metab. Dispos. |volume=29 |issue= 11 |pages= 1480-4 |year= 2002 |pmid= 11602525 |doi= }}
*{{cite journal | author=Drocourt L, Ourlin JC, Pascussi JM, ''et al.'' |title=Expression of CYP3A4, CYP2B6, and CYP2C9 is regulated by the vitamin D receptor pathway in primary human hepatocytes. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25125-32 |year= 2002 |pmid= 11991950 |doi= 10.1074/jbc.M201323200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ERCC6... {November 17, 2007 1:10:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:11:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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 = Excision repair cross-complementing rodent repair deficiency, complementation group 6
| HGNCid = 3438
| Symbol = ERCC6
| AltSymbols =; CSB; ARMD5; CKN2; COFS; RAD26
| OMIM = 609413
| ECnumber =
| Homologene = 6279
| MGIid = 1100494
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003678 |text = DNA helicase activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0004386 |text = helicase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2074
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000115
| Hs_RefseqmRNA = NM_000124
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 319955
| Mm_Ensembl = ENSMUSG00000054051
| Mm_RefseqmRNA = XM_484360
| Mm_RefseqProtein = XP_484360
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 31399142
| Mm_GenLoc_end = 31409248
| Mm_Uniprot =
}}
}}
'''Excision repair cross-complementing rodent repair deficiency, complementation group 6''', also known as '''ERCC6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ERCC6 excision repair cross-complementing rodent repair deficiency, complementation group 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2074| 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 ERCC6 protein is a DNA-binding protein important in transcription-coupled excision repair. The protein has ATP-stimulated ATPase activity; there are contradictory publications reporting presence or absence of helicase activity. The protein appears to interact with several transcription and excision repair proteins, and may promote complex formation at repair sites.<ref name="entrez">{{cite web | title = Entrez Gene: ERCC6 excision repair cross-complementing rodent repair deficiency, complementation group 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2074| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cleaver JE, Thompson LH, Richardson AS, States JC |title=A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. |journal=Hum. Mutat. |volume=14 |issue= 1 |pages= 9-22 |year= 1999 |pmid= 10447254 |doi= 10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6 }}
*{{cite journal | author=Troelstra C, van Gool A, de Wit J, ''et al.'' |title=ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. |journal=Cell |volume=71 |issue= 6 |pages= 939-53 |year= 1993 |pmid= 1339317 |doi= }}
*{{cite journal | author=Troelstra C, Landsvater RM, Wiegant J, ''et al.'' |title=Localization of the nucleotide excision repair gene ERCC6 to human chromosome 10q11-q21. |journal=Genomics |volume=12 |issue= 4 |pages= 745-9 |year= 1992 |pmid= 1349298 |doi= }}
*{{cite journal | author=Fryns JP, Bulcke J, Verdu P, ''et al.'' |title=Apparent late-onset Cockayne syndrome and interstitial deletion of the long arm of chromosome 10 (del(10)(q11.23q21.2)). |journal=Am. J. Med. Genet. |volume=40 |issue= 3 |pages= 343-4 |year= 1991 |pmid= 1951442 |doi= 10.1002/ajmg.1320400320 }}
*{{cite journal | author=Troelstra C, Odijk H, de Wit J, ''et al.'' |title=Molecular cloning of the human DNA excision repair gene ERCC-6. |journal=Mol. Cell. Biol. |volume=10 |issue= 11 |pages= 5806-13 |year= 1990 |pmid= 2172786 |doi= }}
*{{cite journal | author=Wang XW, Yeh H, Schaeffer L, ''et al.'' |title=p53 modulation of TFIIH-associated nucleotide excision repair activity. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 188-95 |year= 1995 |pmid= 7663514 |doi= 10.1038/ng0695-188 }}
*{{cite journal | author=Henning KA, Li L, Iyer N, ''et al.'' |title=The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. |journal=Cell |volume=82 |issue= 4 |pages= 555-64 |year= 1995 |pmid= 7664335 |doi= }}
*{{cite journal | author=Troelstra C, Hesen W, Bootsma D, Hoeijmakers JH |title=Structure and expression of the excision repair gene ERCC6, involved in the human disorder Cockayne's syndrome group B. |journal=Nucleic Acids Res. |volume=21 |issue= 3 |pages= 419-26 |year= 1993 |pmid= 8382798 |doi= }}
*{{cite journal | author=Iyer N, Reagan MS, Wu KJ, ''et al.'' |title=Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. |journal=Biochemistry |volume=35 |issue= 7 |pages= 2157-67 |year= 1996 |pmid= 8652557 |doi= 10.1021/bi9524124 }}
*{{cite journal | author=Selby CP, Sancar A |title=Human transcription-repair coupling factor CSB/ERCC6 is a DNA-stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1885-90 |year= 1997 |pmid= 8999876 |doi= }}
*{{cite journal | author=Boulikas T |title=Nuclear import of DNA repair proteins. |journal=Anticancer Res. |volume=17 |issue= 2A |pages= 843-63 |year= 1997 |pmid= 9137418 |doi= }}
*{{cite journal | author=Selby CP, Sancar A |title=Cockayne syndrome group B protein enhances elongation by RNA polymerase II. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 21 |pages= 11205-9 |year= 1997 |pmid= 9326587 |doi= }}
*{{cite journal | author=Tantin D, Kansal A, Carey M |title=Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 6803-14 |year= 1997 |pmid= 9372911 |doi= }}
*{{cite journal | author=Mallery DL, Tanganelli B, Colella S, ''et al.'' |title=Molecular analysis of mutations in the CSB (ERCC6) gene in patients with Cockayne syndrome. |journal=Am. J. Hum. Genet. |volume=62 |issue= 1 |pages= 77-85 |year= 1998 |pmid= 9443879 |doi= }}
*{{cite journal | author=Lindsay HD, Griffiths DJ, Edwards RJ, ''et al.'' |title=S-phase-specific activation of Cds1 kinase defines a subpathway of the checkpoint response in Schizosaccharomyces pombe. |journal=Genes Dev. |volume=12 |issue= 3 |pages= 382-95 |year= 1998 |pmid= 9450932 |doi= }}
*{{cite journal | author=Tantin D |title=RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 27794-9 |year= 1998 |pmid= 9774388 |doi= }}
*{{cite journal | author=Dianov G, Bischoff C, Sunesen M, Bohr VA |title=Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome group B cells. |journal=Nucleic Acids Res. |volume=27 |issue= 5 |pages= 1365-8 |year= 1999 |pmid= 9973627 |doi= }}
*{{cite journal | author=Colella S, Nardo T, Mallery D, ''et al.'' |title=Alterations in the CSB gene in three Italian patients with the severe form of Cockayne syndrome (CS) but without clinical photosensitivity. |journal=Hum. Mol. Genet. |volume=8 |issue= 5 |pages= 935-41 |year= 1999 |pmid= 10196384 |doi= }}
*{{cite journal | author=Cheng L, Guan Y, Li L, ''et al.'' |title=Expression in normal human tissues of five nucleotide excision repair genes measured simultaneously by multiplex reverse transcription-polymerase chain reaction. |journal=Cancer Epidemiol. Biomarkers Prev. |volume=8 |issue= 9 |pages= 801-7 |year= 1999 |pmid= 10498399 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FANCD2... {November 17, 2007 1:11:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:21:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_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 = Fanconi anemia, complementation group D2
| HGNCid = 3585
| Symbol = FANCD2
| AltSymbols =; FACD; FAD; FANCD; DKFZp762A223; FA-D2; FA4; FAD2; FLJ23826
| OMIM = 227646
| ECnumber =
| Homologene = 13212
| MGIid = 2448480
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000793 |text = condensed chromosome}} {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2177
| Hs_Ensembl = ENSG00000144554
| Hs_RefseqProtein = NP_001018125
| Hs_RefseqmRNA = NM_001018115
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 10043113
| Hs_GenLoc_end = 10118614
| Hs_Uniprot = Q9BXW9
| Mm_EntrezGene = 211651
| Mm_Ensembl = ENSMUSG00000034023
| Mm_RefseqmRNA = NM_001033244
| Mm_RefseqProtein = NP_001028416
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 113497462
| Mm_GenLoc_end = 113562794
| Mm_Uniprot = Q3TLN3
}}
}}
'''Fanconi anemia, complementation group D2''', also known as '''FANCD2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FANCD2 Fanconi anemia, complementation group D2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2177| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group D2. This protein is monoubiquinated in response to DNA damage, resulting in its localization to nuclear foci with other proteins (BRCA1 AND BRCA2) involved in homology-directed DNA repair. Alternative splicing results in two transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: FANCD2 Fanconi anemia, complementation group D2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2177| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Whitney M, Thayer M, Reifsteck C, ''et al.'' |title=Microcell mediated chromosome transfer maps the Fanconi anaemia group D gene to chromosome 3p. |journal=Nat. Genet. |volume=11 |issue= 3 |pages= 341-3 |year= 1995 |pmid= 7581463 |doi= 10.1038/ng1195-341 }}
*{{cite journal | author=Hejna JA, Timmers CD, Reifsteck C, ''et al.'' |title=Localization of the Fanconi anemia complementation group D gene to a 200-kb region on chromosome 3p25.3. |journal=Am. J. Hum. Genet. |volume=66 |issue= 5 |pages= 1540-51 |year= 2000 |pmid= 10762542 |doi= }}
*{{cite journal | author=Timmers C, Taniguchi T, Hejna J, ''et al.'' |title=Positional cloning of a novel Fanconi anemia gene, FANCD2. |journal=Mol. Cell |volume=7 |issue= 2 |pages= 241-8 |year= 2001 |pmid= 11239453 |doi= }}
*{{cite journal | author=Garcia-Higuera I, Taniguchi T, Ganesan S, ''et al.'' |title=Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway. |journal=Mol. Cell |volume=7 |issue= 2 |pages= 249-62 |year= 2001 |pmid= 11239454 |doi= }}
*{{cite journal | author=Futaki M, Liu JM |title=Chromosomal breakage syndromes and the BRCA1 genome surveillance complex. |journal=Trends in molecular medicine |volume=7 |issue= 12 |pages= 560-5 |year= 2002 |pmid= 11733219 |doi= }}
*{{cite journal | author=Wilson JB, Johnson MA, Stuckert AP, ''et al.'' |title=The Chinese hamster FANCG/XRCC9 mutant NM3 fails to express the monoubiquitinated form of the FANCD2 protein, is hypersensitive to a range of DNA damaging agents and exhibits a normal level of spontaneous sister chromatid exchange. |journal=Carcinogenesis |volume=22 |issue= 12 |pages= 1939-46 |year= 2002 |pmid= 11751423 |doi= }}
*{{cite journal | author=Grompe M |title=FANCD2: a branch-point in DNA damage response? |journal=Nat. Med. |volume=8 |issue= 6 |pages= 555-6 |year= 2002 |pmid= 12042798 |doi= 10.1038/nm0602-555 }}
*{{cite journal | author=Taniguchi T, Garcia-Higuera I, Xu B, ''et al.'' |title=Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways. |journal=Cell |volume=109 |issue= 4 |pages= 459-72 |year= 2002 |pmid= 12086603 |doi= }}
*{{cite journal | author=Pace P, Johnson M, Tan WM, ''et al.'' |title=FANCE: the link between Fanconi anaemia complex assembly and activity. |journal=EMBO J. |volume=21 |issue= 13 |pages= 3414-23 |year= 2002 |pmid= 12093742 |doi= 10.1093/emboj/cdf355 }}
*{{cite journal | author=Taniguchi T, Garcia-Higuera I, Andreassen PR, ''et al.'' |title=S-phase-specific interaction of the Fanconi anemia protein, FANCD2, with BRCA1 and RAD51. |journal=Blood |volume=100 |issue= 7 |pages= 2414-20 |year= 2002 |pmid= 12239151 |doi= 10.1182/blood-2002-01-0278 }}
*{{cite journal | author=Tamary H, Bar-Yam R, Zemach M, ''et al.'' |title=The molecular biology of Fanconi anemia. |journal=Isr. Med. Assoc. J. |volume=4 |issue= 10 |pages= 819-23 |year= 2002 |pmid= 12389351 |doi= }}
*{{cite journal | author=Nakanishi K, Taniguchi T, Ranganathan V, ''et al.'' |title=Interaction of FANCD2 and NBS1 in the DNA damage response. |journal=Nat. Cell Biol. |volume=4 |issue= 12 |pages= 913-20 |year= 2003 |pmid= 12447395 |doi= 10.1038/ncb879 }}
*{{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=Goldberg M, Stucki M, Falck J, ''et al.'' |title=MDC1 is required for the intra-S-phase DNA damage checkpoint. |journal=Nature |volume=421 |issue= 6926 |pages= 952-6 |year= 2003 |pmid= 12607003 |doi= 10.1038/nature01445 }}
*{{cite journal | author=Stewart GS, Wang B, Bignell CR, ''et al.'' |title=MDC1 is a mediator of the mammalian DNA damage checkpoint. |journal=Nature |volume=421 |issue= 6926 |pages= 961-6 |year= 2003 |pmid= 12607005 |doi= 10.1038/nature01446 }}
*{{cite journal | author=Gordon SM, Buchwald M |title=Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems. |journal=Blood |volume=102 |issue= 1 |pages= 136-41 |year= 2003 |pmid= 12649160 |doi= 10.1182/blood-2002-11-3517 }}
*{{cite journal | author=Jin S, Mao H, Schnepp RW, ''et al.'' |title=Menin associates with FANCD2, a protein involved in repair of DNA damage. |journal=Cancer Res. |volume=63 |issue= 14 |pages= 4204-10 |year= 2003 |pmid= 12874027 |doi= }}
*{{cite journal | author=Vandenberg CJ, Gergely F, Ong CY, ''et al.'' |title=BRCA1-independent ubiquitination of FANCD2. |journal=Mol. Cell |volume=12 |issue= 1 |pages= 247-54 |year= 2003 |pmid= 12887909 |doi= }}
*{{cite journal | author=Meetei AR, de Winter JP, Medhurst AL, ''et al.'' |title=A novel ubiquitin ligase is deficient in Fanconi anemia. |journal=Nat. Genet. |volume=35 |issue= 2 |pages= 165-70 |year= 2003 |pmid= 12973351 |doi= 10.1038/ng1241 }}
*{{cite journal | author=Reuter TY, Medhurst AL, Waisfisz Q, ''et al.'' |title=Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport. |journal=Exp. Cell Res. |volume=289 |issue= 2 |pages= 211-21 |year= 2003 |pmid= 14499622 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FCAR... {November 17, 2007 1:21:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:21:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FCAR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ovz.
| PDB = {{PDB2|1ovz}}, {{PDB2|1ow0}}, {{PDB2|1uct}}
| Name = Fc fragment of IgA, receptor for
| HGNCid = 3608
| Symbol = FCAR
| AltSymbols =; CD89
| OMIM = 147045
| ECnumber =
| Homologene = 48064
| MGIid =
| GeneAtlas_image1 = PBB_GE_FCAR_211307_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FCAR_211816_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0019862 |text = IgA 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:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2204
| Hs_Ensembl = ENSG00000186431
| Hs_RefseqProtein = NP_001991
| Hs_RefseqmRNA = NM_002000
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 60077534
| Hs_GenLoc_end = 60095055
| Hs_Uniprot = P24071
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Fc fragment of IgA, receptor for''', also known as '''FCAR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCAR Fc fragment of IgA, receptor for| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2204| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the immunoglobulin gene superfamily and encodes a receptor for the Fc region of IgA. The receptor is a transmembrane glycoprotein present on the surface of myeloid lineage cells such as neutrophils, monocytes, macrophages, and eosinophils, where it mediates immunologic responses to pathogens. It interacts with IgA-opsonized targets and triggers several immunologic defense processes, including phagocytosis, antibody-dependent cell-mediated cytotoxicity, and stimulation of the release of inflammatory mediators. Ten transcript variants encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: FCAR Fc fragment of IgA, receptor for| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2204| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Morton HC, van Egmond M, van de Winkel JG |title=Structure and function of human IgA Fc receptors (Fc alpha R). |journal=Crit. Rev. Immunol. |volume=16 |issue= 4 |pages= 423-40 |year= 1997 |pmid= 8954257 |doi= }}
*{{cite journal | author=Morton HC, Brandtzaeg P |title=CD89: the human myeloid IgA Fc receptor. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=49 |issue= 3 |pages= 217-29 |year= 2001 |pmid= 11478396 |doi= }}
*{{cite journal | author=Martin AM, Kulski JK, Witt C, ''et al.'' |title=Leukocyte Ig-like receptor complex (LRC) in mice and men. |journal=Trends Immunol. |volume=23 |issue= 2 |pages= 81-8 |year= 2002 |pmid= 11929131 |doi= }}
*{{cite journal | author=Monteiro RC, Van De Winkel JG |title=IgA Fc receptors. |journal=Annu. Rev. Immunol. |volume=21 |issue= |pages= 177-204 |year= 2003 |pmid= 12524384 |doi= 10.1146/annurev.immunol.21.120601.141011 }}
*{{cite journal | author=Kremer EJ, Kalatzis V, Baker E, ''et al.'' |title=The gene for the human IgA Fc receptor maps to 19q13.4. |journal=Hum. Genet. |volume=89 |issue= 1 |pages= 107-8 |year= 1992 |pmid= 1577457 |doi= }}
*{{cite journal | author=Maliszewski CR, March CJ, Schoenborn MA, ''et al.'' |title=Expression cloning of a human Fc receptor for IgA. |journal=J. Exp. Med. |volume=172 |issue= 6 |pages= 1665-72 |year= 1991 |pmid= 2258698 |doi= }}
*{{cite journal | author=Pfefferkorn LC, Yeaman GR |title=Association of IgA-Fc receptors (Fc alpha R) with Fc epsilon RI gamma 2 subunits in U937 cells. Aggregation induces the tyrosine phosphorylation of gamma 2. |journal=J. Immunol. |volume=153 |issue= 7 |pages= 3228-36 |year= 1994 |pmid= 7522255 |doi= }}
*{{cite journal | author=de Wit TP, Morton HC, Capel PJ, van de Winkel JG |title=Structure of the gene for the human myeloid IgA Fc receptor (CD89). |journal=J. Immunol. |volume=155 |issue= 3 |pages= 1203-9 |year= 1995 |pmid= 7636188 |doi= }}
*{{cite journal | author=Dürrbaum-Landmann I, Kaltenhäuser E, Flad HD, Ernst M |title=HIV-1 envelope protein gp120 affects phenotype and function of monocytes in vitro. |journal=J. Leukoc. Biol. |volume=55 |issue= 4 |pages= 545-51 |year= 1994 |pmid= 8145026 |doi= }}
*{{cite journal | author=Monteiro RC, Hostoffer RW, Cooper MD, ''et al.'' |title=Definition of immunoglobulin A receptors on eosinophils and their enhanced expression in allergic individuals. |journal=J. Clin. Invest. |volume=92 |issue= 4 |pages= 1681-5 |year= 1993 |pmid= 8408621 |doi= }}
*{{cite journal | author=Morton HC, van den Herik-Oudijk IE, Vossebeld P, ''et al.'' |title=Functional association between the human myeloid immunoglobulin A Fc receptor (CD89) and FcR gamma chain. Molecular basis for CD89/FcR gamma chain association. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29781-7 |year= 1996 |pmid= 8530370 |doi= }}
*{{cite journal | author=Morton HC, Schiel AE, Janssen SW, van de Winkel JG |title=Alternatively spliced forms of the human myeloid Fc alpha receptor (CD89) in neutrophils. |journal=Immunogenetics |volume=43 |issue= 4 |pages= 246-7 |year= 1996 |pmid= 8575829 |doi= }}
*{{cite journal | author=Patry C, Sibille Y, Lehuen A, Monteiro RC |title=Identification of Fc alpha receptor (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages. |journal=J. Immunol. |volume=156 |issue= 11 |pages= 4442-8 |year= 1996 |pmid= 8666819 |doi= }}
*{{cite journal | author=Carayannopoulos L, Hexham JM, Capra JD |title=Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Calpha2 and Calpha3 in human IgA1. |journal=J. Exp. Med. |volume=183 |issue= 4 |pages= 1579-86 |year= 1996 |pmid= 8666916 |doi= }}
*{{cite journal | author=Pleass RJ, Andrews PD, Kerr MA, Woof JM |title=Alternative splicing of the human IgA Fc receptor CD89 in neutrophils and eosinophils. |journal=Biochem. J. |volume=318 ( Pt 3) |issue= |pages= 771-7 |year= 1996 |pmid= 8836118 |doi= }}
*{{cite journal | author=Reterink TJ, Verweij CL, van Es LA, Daha MR |title=Alternative splicing of IgA Fc receptor (CD89) transcripts. |journal=Gene |volume=175 |issue= 1-2 |pages= 279-80 |year= 1996 |pmid= 8917112 |doi= }}
*{{cite journal | author=van Dijk TB, Bracke M, Caldenhoven E, ''et al.'' |title=Cloning and characterization of Fc alpha Rb, a novel Fc alpha receptor (CD89) isoform expressed in eosinophils and neutrophils. |journal=Blood |volume=88 |issue= 11 |pages= 4229-38 |year= 1996 |pmid= 8943858 |doi= }}
*{{cite journal | author=Toyabe S, Kuwano Y, Takeda K, ''et al.'' |title=IgA nephropathy-specific expression of the IgA Fc receptors (CD89) on blood phagocytic cells. |journal=Clin. Exp. Immunol. |volume=110 |issue= 2 |pages= 226-32 |year= 1997 |pmid= 9367406 |doi= }}
*{{cite journal | author=Gulle H, Samstag A, Eibl MM, Wolf HM |title=Physical and functional association of Fc alpha R with protein tyrosine kinase Lyn. |journal=Blood |volume=91 |issue= 2 |pages= 383-91 |year= 1998 |pmid= 9427690 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGF23... {November 17, 2007 1:28:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:29:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FGF23_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2p39.
| PDB = {{PDB2|2p39}}
| Name = Fibroblast growth factor 23
| HGNCid = 3680
| Symbol = FGF23
| AltSymbols =; ADHR; HYPF; HPDR2; PHPTC
| OMIM = 605380
| ECnumber =
| Homologene = 10771
| MGIid = 1891427
| GeneAtlas_image1 = PBB_GE_FGF23_221166_at_tn.png
| Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030500 |text = regulation of bone mineralization}} {{GNF_GO|id=GO:0030643 |text = cellular phosphate ion homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8074
| Hs_Ensembl = ENSG00000118972
| Hs_RefseqProtein = NP_065689
| Hs_RefseqmRNA = NM_020638
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 4347654
| Hs_GenLoc_end = 4359155
| Hs_Uniprot = Q9GZV9
| Mm_EntrezGene = 64654
| Mm_Ensembl = ENSMUSG00000000182
| Mm_RefseqmRNA = XM_001003443
| Mm_RefseqProtein = XP_001003443
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 127038593
| Mm_GenLoc_end = 127046844
| Mm_Uniprot = Q0VBJ8
}}
}}
'''Fibroblast growth factor 23''', also known as '''FGF23''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FGF23 fibroblast growth factor 23| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8074| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The product of this gene inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of this gene was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations in this gene have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.<ref name="entrez">{{cite web | title = Entrez Gene: FGF23 fibroblast growth factor 23| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8074| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Silve C, Beck L |title=Is FGF23 the long sought after phosphaturic factor phosphatonin? |journal=Nephrol. Dial. Transplant. |volume=17 |issue= 6 |pages= 958-61 |year= 2003 |pmid= 12032180 |doi= }}
*{{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=Fukagawa M, Nii-Kono T, Kazama JJ |title=Role of fibroblast growth factor 23 in health and in chronic kidney disease. |journal=Curr. Opin. Nephrol. Hypertens. |volume=14 |issue= 4 |pages= 325-9 |year= 2005 |pmid= 15930999 |doi= }}
*{{cite journal | author=Imel EA, Econs MJ |title=Fibroblast growth factor 23: roles in health and disease. |journal=J. Am. Soc. Nephrol. |volume=16 |issue= 9 |pages= 2565-75 |year= 2006 |pmid= 16033853 |doi= 10.1681/ASN.2005050573 }}
*{{cite journal | author=Yamashita T, Yoshioka M, Itoh N |title=Identification of a novel fibroblast growth factor, FGF-23, preferentially expressed in the ventrolateral thalamic nucleus of the brain. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 2 |pages= 494-8 |year= 2000 |pmid= 11032749 |doi= 10.1006/bbrc.2000.3696 }}
*{{cite journal | author= |title=Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23. |journal=Nat. Genet. |volume=26 |issue= 3 |pages= 345-8 |year= 2000 |pmid= 11062477 |doi= 10.1038/81664 }}
*{{cite journal | author=White KE, Jonsson KB, Carn G, ''et al.'' |title=The autosomal dominant hypophosphatemic rickets (ADHR) gene is a secreted polypeptide overexpressed by tumors that cause phosphate wasting. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 2 |pages= 497-500 |year= 2001 |pmid= 11157998 |doi= }}
*{{cite journal | author=Shimada T, Mizutani S, Muto T, ''et al.'' |title=Cloning and characterization of FGF23 as a causative factor of tumor-induced osteomalacia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 11 |pages= 6500-5 |year= 2001 |pmid= 11344269 |doi= 10.1073/pnas.101545198 }}
*{{cite journal | author=Bowe AE, Finnegan R, Jan de Beur SM, ''et al.'' |title=FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate. |journal=Biochem. Biophys. Res. Commun. |volume=284 |issue= 4 |pages= 977-81 |year= 2001 |pmid= 11409890 |doi= 10.1006/bbrc.2001.5084 }}
*{{cite journal | author=White KE, Carn G, Lorenz-Depiereux B, ''et al.'' |title=Autosomal-dominant hypophosphatemic rickets (ADHR) mutations stabilize FGF-23. |journal=Kidney Int. |volume=60 |issue= 6 |pages= 2079-86 |year= 2002 |pmid= 11737582 |doi= 10.1046/j.1523-1755.2001.00064.x }}
*{{cite journal | author=Kruse K, Woelfel D, Strom TM, Storm TM |title=Loss of renal phosphate wasting in a child with autosomal dominant hypophosphatemic rickets caused by a FGF23 mutation. |journal=Horm. Res. |volume=55 |issue= 6 |pages= 305-8 |year= 2002 |pmid= 11805436 |doi= }}
*{{cite journal | author=Yamashita T, Konishi M, Miyake A, ''et al.'' |title=Fibroblast growth factor (FGF)-23 inhibits renal phosphate reabsorption by activation of the mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 28265-70 |year= 2002 |pmid= 12032146 |doi= 10.1074/jbc.M202527200 }}
*{{cite journal | author=Saito H, Kusano K, Kinosaki M, ''et al.'' |title=Human fibroblast growth factor-23 mutants suppress Na+-dependent phosphate co-transport activity and 1alpha,25-dihydroxyvitamin D3 production. |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2206-11 |year= 2003 |pmid= 12419819 |doi= 10.1074/jbc.M207872200 }}
*{{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=Bai XY, Miao D, Goltzman D, Karaplis AC |title=The autosomal dominant hypophosphatemic rickets R176Q mutation in fibroblast growth factor 23 resists proteolytic cleavage and enhances in vivo biological potency. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9843-9 |year= 2003 |pmid= 12519781 |doi= 10.1074/jbc.M210490200 }}
*{{cite journal | author=Larsson T, Zahradnik R, Lavigne J, ''et al.'' |title=Immunohistochemical detection of FGF-23 protein in tumors that cause oncogenic osteomalacia. |journal=Eur. J. Endocrinol. |volume=148 |issue= 2 |pages= 269-76 |year= 2003 |pmid= 12590648 |doi= }}
*{{cite journal | author=Campos M, Couture C, Hirata IY, ''et al.'' |title=Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein. |journal=Biochem. J. |volume=373 |issue= Pt 1 |pages= 271-9 |year= 2003 |pmid= 12678920 |doi= 10.1042/BJ20030287 }}
*{{cite journal | author=Segawa H, Kawakami E, Kaneko I, ''et al.'' |title=Effect of hydrolysis-resistant FGF23-R179Q on dietary phosphate regulation of the renal type-II Na/Pi transporter. |journal=Pflugers Arch. |volume=446 |issue= 5 |pages= 585-92 |year= 2004 |pmid= 12851820 |doi= 10.1007/s00424-003-1084-1 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on G6PC... {November 17, 2007 1:21:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:22:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Glucose-6-phosphatase, catalytic subunit
| HGNCid = 4056
| Symbol = G6PC
| AltSymbols =; G6PT; GSD1a; MGC163350
| OMIM = 232200
| ECnumber =
| Homologene = 20079
| MGIid = 95607
| GeneAtlas_image1 = PBB_GE_G6PC_206952_at_tn.png
| Function = {{GNF_GO|id=GO:0004346 |text = glucose-6-phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005978 |text = glycogen biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2538
| Hs_Ensembl = ENSG00000131482
| Hs_RefseqProtein = NP_000142
| Hs_RefseqmRNA = NM_000151
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 38306341
| Hs_GenLoc_end = 38318912
| Hs_Uniprot = P35575
| Mm_EntrezGene = 14377
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008061
| Mm_RefseqProtein = NP_032087
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Glucose-6-phosphatase, catalytic subunit''', also known as '''G6PC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: G6PC glucose-6-phosphatase, catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2538| 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 = Glucose-6-phosphatase is an integral membrane protein of the endoplasmic reticulum that catalyzes the hydrolysis of D-glucose 6-phosphate to D-glucose and orthophosphate. It is a key enzyme in glucose homeostasis, functioning in gluconeogenesis and glycogenolysis. Defects in the enzyme cause glycogen storage disease type I (von Gierke disease).<ref name="entrez">{{cite web | title = Entrez Gene: G6PC glucose-6-phosphatase, catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2538| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Barham SS, Berlin JD, Brackeen RB |title=The fine structural localization of testicular phosphatases in man: the control testis. |journal=Cell Tissue Res. |volume=166 |issue= 4 |pages= 497-510 |year= 1976 |pmid= 175958 |doi= }}
*{{cite journal | author=Narisawa K, Igarashi Y, Otomo H, Tada K |title=A new variant of glycogen storage disease type I probably due to a defect in the glucose-6-phosphate transport system. |journal=Biochem. Biophys. Res. Commun. |volume=83 |issue= 4 |pages= 1360-4 |year= 1978 |pmid= 212064 |doi= }}
*{{cite journal | author=Burchell A, Waddell ID |title=Diagnosis of a novel glycogen storage disease: type 1aSP. |journal=J. Inherit. Metab. Dis. |volume=13 |issue= 3 |pages= 247-9 |year= 1990 |pmid= 2172641 |doi= }}
*{{cite journal | author=Hill A, Waddell ID, Hopwood D, Burchell A |title=The microsomal glucose-6-phosphatase enzyme of human gall-bladder. |journal=J. Pathol. |volume=158 |issue= 1 |pages= 53-6 |year= 1989 |pmid= 2547044 |doi= 10.1002/path.1711580111 }}
*{{cite journal | author=Sacks W, Cowburn D, Bigler RE, ''et al.'' |title=Evidence for the cerebral uptake in vivo from two pools of glucose and the role of glucose-6-phosphatase in removing excess substrate from brain. |journal=Neurochem. Res. |volume=10 |issue= 2 |pages= 201-27 |year= 1985 |pmid= 2986020 |doi= }}
*{{cite journal | author=Lei KJ, Chen YT, Chen H, ''et al.'' |title=Genetic basis of glycogen storage disease type 1a: prevalent mutations at the glucose-6-phosphatase locus. |journal=Am. J. Hum. Genet. |volume=57 |issue= 4 |pages= 766-71 |year= 1995 |pmid= 7573034 |doi= }}
*{{cite journal | author=Parvari R, Moses S, Hershkovitz E, ''et al.'' |title=Characterization of the mutations in the glucose-6-phosphatase gene in Israeli patients with glycogen storage disease type 1a: R83C in six Jews and a novel V166G mutation in a Muslim Arab. |journal=J. Inherit. Metab. Dis. |volume=18 |issue= 1 |pages= 21-7 |year= 1995 |pmid= 7623438 |doi= }}
*{{cite journal | author=Hwu WL, Chuang SC, Tsai LP, ''et al.'' |title=Glucose-6-phosphatase gene G327A mutation is common in Chinese patients with glycogen storage disease type Ia. |journal=Hum. Mol. Genet. |volume=4 |issue= 6 |pages= 1095-6 |year= 1995 |pmid= 7655466 |doi= }}
*{{cite journal | author=Kajihara S, Matsuhashi S, Yamamoto K, ''et al.'' |title=Exon redefinition by a point mutation within exon 5 of the glucose-6-phosphatase gene is the major cause of glycogen storage disease type 1a in Japan. |journal=Am. J. Hum. Genet. |volume=57 |issue= 3 |pages= 549-55 |year= 1995 |pmid= 7668282 |doi= }}
*{{cite journal | author=Brody LC, Abel KJ, Castilla LH, ''et al.'' |title=Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17. |journal=Genomics |volume=25 |issue= 1 |pages= 238-47 |year= 1995 |pmid= 7774924 |doi= }}
*{{cite journal | author=Lei KJ, Pan CJ, Shelly LL, ''et al.'' |title=Identification of mutations in the gene for glucose-6-phosphatase, the enzyme deficient in glycogen storage disease type 1a. |journal=J. Clin. Invest. |volume=93 |issue= 5 |pages= 1994-9 |year= 1994 |pmid= 8182131 |doi= }}
*{{cite journal | author=Lei KJ, Shelly LL, Pan CJ, ''et al.'' |title=Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a. |journal=Science |volume=262 |issue= 5133 |pages= 580-3 |year= 1993 |pmid= 8211187 |doi= }}
*{{cite journal | author=Schmoll D, Allan BB, Burchell A |title=Cloning and sequencing of the 5' region of the human glucose-6-phosphatase gene: transcriptional regulation by cAMP, insulin and glucocorticoids in H4IIE hepatoma cells. |journal=FEBS Lett. |volume=383 |issue= 1-2 |pages= 63-6 |year= 1996 |pmid= 8612793 |doi= }}
*{{cite journal | author=Lei KJ, Chen H, Pan CJ, ''et al.'' |title=Glucose-6-phosphatase dependent substrate transport in the glycogen storage disease type-1a mouse. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 203-9 |year= 1996 |pmid= 8640227 |doi= 10.1038/ng0696-203 }}
*{{cite journal | author=Chevalier-Porst F, Bozon D, Bonardot AM, ''et al.'' |title=Mutation analysis in 24 French patients with glycogen storage disease type 1a. |journal=J. Med. Genet. |volume=33 |issue= 5 |pages= 358-60 |year= 1996 |pmid= 8733042 |doi= }}
*{{cite journal | author=Lee WJ, Lee HM, Chi CS, ''et al.'' |title=Genetic analysis of the glucose-6-phosphatase mutation of type 1a glycogen storage disease in a Chinese family. |journal=Clin. Genet. |volume=50 |issue= 4 |pages= 206-11 |year= 1997 |pmid= 9001800 |doi= }}
*{{cite journal | author=Parvari R, Lei KJ, Bashan N, ''et al.'' |title=Glycogen storage disease type 1a in Israel: biochemical, clinical, and mutational studies. |journal=Am. J. Med. Genet. |volume=72 |issue= 3 |pages= 286-90 |year= 1997 |pmid= 9332655 |doi= }}
*{{cite journal | author=Gerin I, Veiga-da-Cunha M, Achouri Y, ''et al.'' |title=Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type Ib. |journal=FEBS Lett. |volume=419 |issue= 2-3 |pages= 235-8 |year= 1998 |pmid= 9428641 |doi= }}
*{{cite journal | author=Kure S, Suzuki Y, Matsubara Y, ''et al.'' |title=Molecular analysis of glycogen storage disease type Ib: identification of a prevalent mutation among Japanese patients and assignment of a putative glucose-6-phosphate translocase gene to chromosome 11. |journal=Biochem. Biophys. Res. Commun. |volume=248 |issue= 2 |pages= 426-31 |year= 1998 |pmid= 9675154 |doi= 10.1006/bbrc.1998.8985 }}
*{{cite journal | author=Pan CJ, Lei KJ, Chou JY |title=Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 21658-62 |year= 1998 |pmid= 9705299 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNE... {November 17, 2007 1:29:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:30:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase
| HGNCid = 23657
| Symbol = GNE
| AltSymbols =; NM; DMRV; GLCNE; IBM2; Uae1
| OMIM = 603824
| ECnumber =
| Homologene = 3996
| MGIid = 1354951
| GeneAtlas_image1 = PBB_GE_GNE_205042_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004396 |text = hexokinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008761 |text = UDP-N-acetylglucosamine 2-epimerase activity}} {{GNF_GO|id=GO:0009384 |text = N-acylmannosamine kinase activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006047 |text = UDP-N-acetylglucosamine metabolic process}} {{GNF_GO|id=GO:0006054 |text = N-acetylneuraminate metabolic process}} {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0009103 |text = lipopolysaccharide biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10020
| Hs_Ensembl = ENSG00000159921
| Hs_RefseqProtein = NP_005467
| Hs_RefseqmRNA = NM_005476
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 36204430
| Hs_GenLoc_end = 36248450
| Hs_Uniprot = Q9Y223
| Mm_EntrezGene = 50798
| Mm_Ensembl = ENSMUSG00000028479
| Mm_RefseqmRNA = NM_015828
| Mm_RefseqProtein = NP_056643
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 44055175
| Mm_GenLoc_end = 44105277
| Mm_Uniprot = Q3TCI8
}}
}}
'''Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase''', also known as '''GNE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNE glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10020| 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 bifunctional enzyme, UDP-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase/N-acetylmannosamine kinase) regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. UDP-GlcNAc 2-epimerase activity is rate-limiting for the biosynthesis of sialic acid and is required for sialylation in hematopoietic cells. The activity of the enzyme can be controlled at the transcriptional level and can affect the sialylation and function of specific cell surface molecules expressed on B cells and myeloid cells. Modification of cell surface molecules with sialic acid is crucial for their function in many biologic processes, including cell adhesion and signal transduction. Differential sialylation of cell surface molecules is also implicated in the tumorigenicity and metastatic behavior of malignant cells. Sialuria is a rare inborn error of metabolism characterized by cytoplasmic accumulation and increased urinary excretion of free NeuAc.<ref name="entrez">{{cite web | title = Entrez Gene: GNE glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10020| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wilcken B, Don N, Greenaway R, ''et al.'' |title=Sialuria: a second case. |journal=J. Inherit. Metab. Dis. |volume=10 |issue= 2 |pages= 97-102 |year= 1987 |pmid= 2443758 |doi= }}
*{{cite journal | author=Weiss P, Tietze F, Gahl WA, ''et al.'' |title=Identification of the metabolic defect in sialuria. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 17635-6 |year= 1989 |pmid= 2808337 |doi= }}
*{{cite journal | author=Krasnewich DM, Tietze F, Krause W, ''et al.'' |title=Clinical and biochemical studies in an American child with sialuria. |journal=Biochem. Med. Metab. Biol. |volume=49 |issue= 1 |pages= 90-6 |year= 1993 |pmid= 8439453 |doi= }}
*{{cite journal | author=Mitrani-Rosenbaum S, Argov Z, Blumenfeld A, ''et al.'' |title=Hereditary inclusion body myopathy maps to chromosome 9p1-q1. |journal=Hum. Mol. Genet. |volume=5 |issue= 1 |pages= 159-163 |year= 1996 |pmid= 8789455 |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=Hinderlich S, Stäsche R, Zeitler R, Reutter W |title=A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24313-8 |year= 1997 |pmid= 9305887 |doi= }}
*{{cite journal | author=Stäsche R, Hinderlich S, Weise C, ''et al.'' |title=A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24319-24 |year= 1997 |pmid= 9305888 |doi= }}
*{{cite journal | author=Seppala R, Lehto VP, Gahl WA |title=Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. |journal=Am. J. Hum. Genet. |volume=64 |issue= 6 |pages= 1563-9 |year= 1999 |pmid= 10330343 |doi= }}
*{{cite journal | author=Keppler OT, Hinderlich S, Langner J, ''et al.'' |title=UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation. |journal=Science |volume=284 |issue= 5418 |pages= 1372-6 |year= 1999 |pmid= 10334995 |doi= }}
*{{cite journal | author=Ferreira H, Seppala R, Pinto R, ''et al.'' |title=Sialuria in a Portuguese girl: clinical, biochemical, and molecular characteristics. |journal=Mol. Genet. Metab. |volume=67 |issue= 2 |pages= 131-7 |year= 1999 |pmid= 10356312 |doi= 10.1006/mgme.1999.2852 }}
*{{cite journal | author=Lucka L, Krause M, Danker K, ''et al.'' |title=Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis. |journal=FEBS Lett. |volume=454 |issue= 3 |pages= 341-4 |year= 1999 |pmid= 10431835 |doi= }}
*{{cite journal | author=Leroy JG, Seppala R, Huizing M, ''et al.'' |title=Dominant inheritance of sialuria, an inborn error of feedback inhibition. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1419-27 |year= 2001 |pmid= 11326336 |doi= }}
*{{cite journal | author=Eisenberg I, Avidan N, Potikha T, ''et al.'' |title=The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. |journal=Nat. Genet. |volume=29 |issue= 1 |pages= 83-7 |year= 2001 |pmid= 11528398 |doi= 10.1038/ng718 }}
*{{cite journal | author=Kovach MJ, Waggoner B, Leal SM, ''et al.'' |title=Clinical delineation and localization to chromosome 9p13.3-p12 of a unique dominant disorder in four families: hereditary inclusion body myopathy, Paget disease of bone, and frontotemporal dementia. |journal=Mol. Genet. Metab. |volume=74 |issue= 4 |pages= 458-75 |year= 2002 |pmid= 11749051 |doi= 10.1006/mgme.2001.3256 }}
*{{cite journal | author=Kayashima T, Matsuo H, Satoh A, ''et al.'' |title=Nonaka myopathy is caused by mutations in the UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase gene (GNE). |journal=J. Hum. Genet. |volume=47 |issue= 2 |pages= 77-9 |year= 2002 |pmid= 11916006 |doi= }}
*{{cite journal | author=Tomimitsu H, Ishikawa K, Shimizu J, ''et al.'' |title=Distal myopathy with rimmed vacuoles: novel mutations in the GNE gene. |journal=Neurology |volume=59 |issue= 3 |pages= 451-4 |year= 2002 |pmid= 12177386 |doi= }}
*{{cite journal | author=Arai A, Tanaka K, Ikeuchi T, ''et al.'' |title=A novel mutation in the GNE gene and a linkage disequilibrium in Japanese pedigrees. |journal=Ann. Neurol. |volume=52 |issue= 4 |pages= 516-9 |year= 2002 |pmid= 12325084 |doi= 10.1002/ana.10341 }}
*{{cite journal | author=Darvish D, Vahedifar P, Huo Y |title=Four novel mutations associated with autosomal recessive inclusion body myopathy (MIM: 600737). |journal=Mol. Genet. Metab. |volume=77 |issue= 3 |pages= 252-6 |year= 2003 |pmid= 12409274 |doi= }}
*{{cite journal | author=Nishino I, Noguchi S, Murayama K, ''et al.'' |title=Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy. |journal=Neurology |volume=59 |issue= 11 |pages= 1689-93 |year= 2003 |pmid= 12473753 |doi= }}
*{{cite journal | author=Vasconcelos OM, Raju R, Dalakas MC |title=GNE mutations in an American family with quadriceps-sparing IBM and lack of mutations in s-IBM. |journal=Neurology |volume=59 |issue= 11 |pages= 1776-9 |year= 2003 |pmid= 12473769 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KLF6... {November 17, 2007 1:08:21 PM PST}
- SEARCH REDIRECT: Control Box Found: KLF6 {November 17, 2007 1:09:20 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:09:23 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:09:23 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:09:23 PM PST}
- UPDATED: Updated protein page: KLF6 {November 17, 2007 1:09:29 PM PST}
- INFO: Beginning work on MS4A1... {November 17, 2007 1:07:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:08:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Membrane-spanning 4-domains, subfamily A, member 1
| HGNCid = 7315
| Symbol = MS4A1
| AltSymbols =; B1; Bp35; CD20; LEU-16; MGC3969; MS4A2; S7
| OMIM = 112210
| ECnumber =
| Homologene = 7259
| MGIid = 88321
| GeneAtlas_image1 = PBB_GE_MS4A1_210356_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_MS4A1_217418_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0042113 |text = B cell activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 931
| Hs_Ensembl = ENSG00000156738
| Hs_RefseqProtein = NP_068769
| Hs_RefseqmRNA = NM_021950
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 59979858
| Hs_GenLoc_end = 59994801
| Hs_Uniprot = P11836
| Mm_EntrezGene = 12482
| Mm_Ensembl = ENSMUSG00000024673
| Mm_RefseqmRNA = NM_007641
| Mm_RefseqProtein = NP_031667
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 11316865
| Mm_GenLoc_end = 11333194
| Mm_Uniprot = Q542S5
}}
}}
'''Membrane-spanning 4-domains, subfamily A, member 1''', also known as '''MS4A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MS4A1 membrane-spanning 4-domains, subfamily A, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=931| 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 membrane-spanning 4A gene family. Members of this nascent protein family are characterized by common structural features and similar intron/exon splice boundaries and display unique expression patterns among hematopoietic cells and nonlymphoid tissues. This gene encodes a B-lymphocyte surface molecule which plays a role in the development and differentiation of B-cells into plasma cells. This family member is localized to 11q12, among a cluster of family members. Alternative splicing of this gene results in two transcript variants which encode the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: MS4A1 membrane-spanning 4-domains, subfamily A, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=931| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Macardle PJ, Nicholson IC |title=CD20. |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 2 |pages= 136-8 |year= 2003 |pmid= 12144126 |doi= }}
*{{cite journal | author=Tamayose K, Sato N, Ando J, ''et al.'' |title=CD3-negative, CD20-positive T-cell prolymphocytic leukemia: case report and review of the literature. |journal=Am. J. Hematol. |volume=71 |issue= 4 |pages= 331-5 |year= 2002 |pmid= 12447967 |doi= 10.1002/ajh.10224 }}
*{{cite journal | author=Küster H, Zhang L, Brini AT, ''et al.'' |title=The gene and cDNA for the human high affinity immunoglobulin E receptor beta chain and expression of the complete human receptor. |journal=J. Biol. Chem. |volume=267 |issue= 18 |pages= 12782-7 |year= 1992 |pmid= 1535625 |doi= }}
*{{cite journal | author=Tedder TF, Streuli M, Schlossman SF, Saito H |title=Isolation and structure of a cDNA encoding the B1 (CD20) cell-surface antigen of human B lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 1 |pages= 208-12 |year= 1988 |pmid= 2448768 |doi= }}
*{{cite journal | author=Einfeld DA, Brown JP, Valentine MA, ''et al.'' |title=Molecular cloning of the human B cell CD20 receptor predicts a hydrophobic protein with multiple transmembrane domains. |journal=EMBO J. |volume=7 |issue= 3 |pages= 711-7 |year= 1988 |pmid= 2456210 |doi= }}
*{{cite journal | author=Tedder TF, Disteche CM, Louie E, ''et al.'' |title=The gene that encodes the human CD20 (B1) differentiation antigen is located on chromosome 11 near the t(11;14)(q13;q32) translocation site. |journal=J. Immunol. |volume=142 |issue= 7 |pages= 2555-9 |year= 1989 |pmid= 2466898 |doi= }}
*{{cite journal | author=Tedder TF, Klejman G, Schlossman SF, Saito H |title=Structure of the gene encoding the human B lymphocyte differentiation antigen CD20 (B1). |journal=J. Immunol. |volume=142 |issue= 7 |pages= 2560-8 |year= 1989 |pmid= 2466899 |doi= }}
*{{cite journal | author=Loken MR, Shah VO, Dattilio KL, Civin CI |title=Flow cytometric analysis of human bone marrow. II. Normal B lymphocyte development. |journal=Blood |volume=70 |issue= 5 |pages= 1316-24 |year= 1987 |pmid= 3117132 |doi= }}
*{{cite journal | author=Stamenkovic I, Seed B |title=Analysis of two cDNA clones encoding the B lymphocyte antigen CD20 (B1, Bp35), a type III integral membrane protein. |journal=J. Exp. Med. |volume=167 |issue= 6 |pages= 1975-80 |year= 1988 |pmid= 3260267 |doi= }}
*{{cite journal | author=Bofill M, Janossy G, Janossa M, ''et al.'' |title=Human B cell development. II. Subpopulations in the human fetus. |journal=J. Immunol. |volume=134 |issue= 3 |pages= 1531-8 |year= 1985 |pmid= 3871452 |doi= }}
*{{cite journal | author=Deans JP, Kalt L, Ledbetter JA, ''et al.'' |title=Association of 75/80-kDa phosphoproteins and the tyrosine kinases Lyn, Fyn, and Lck with the B cell molecule CD20. Evidence against involvement of the cytoplasmic regions of CD20. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22632-8 |year= 1995 |pmid= 7545683 |doi= }}
*{{cite journal | author=Valentine MA, Licciardi KA, Clark EA, ''et al.'' |title=Insulin regulates serine/threonine phosphorylation in activated human B lymphocytes. |journal=J. Immunol. |volume=150 |issue= 1 |pages= 96-105 |year= 1993 |pmid= 7678037 |doi= }}
*{{cite journal | author=Bubien JK, Zhou LJ, Bell PD, ''et al.'' |title=Transfection of the CD20 cell surface molecule into ectopic cell types generates a Ca2+ conductance found constitutively in B lymphocytes. |journal=J. Cell Biol. |volume=121 |issue= 5 |pages= 1121-32 |year= 1993 |pmid= 7684739 |doi= }}
*{{cite journal | author=Shirakawa T, Li A, Dubowitz M, ''et al.'' |title=Association between atopy and variants of the beta subunit of the high-affinity immunoglobulin E receptor. |journal=Nat. Genet. |volume=7 |issue= 2 |pages= 125-9 |year= 1994 |pmid= 7920628 |doi= 10.1038/ng0694-125 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Szepetowski P, Perucca-Lostanlen D, Gaudray P |title=Mapping genes according to their amplification status in tumor cells: contribution to the map of 11q13. |journal=Genomics |volume=16 |issue= 3 |pages= 745-50 |year= 1993 |pmid= 8325649 |doi= }}
*{{cite journal | author=Algino KM, Thomason RW, King DE, ''et al.'' |title=CD20 (pan-B cell antigen) expression on bone marrow-derived T cells. |journal=Am. J. Clin. Pathol. |volume=106 |issue= 1 |pages= 78-81 |year= 1996 |pmid= 8701937 |doi= }}
*{{cite journal | author=Szöllósi J, Horejsí V, Bene L, ''et al.'' |title=Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. |journal=J. Immunol. |volume=157 |issue= 7 |pages= 2939-46 |year= 1996 |pmid= 8816400 |doi= }}
*{{cite journal | author=Kanzaki M, Lindorfer MA, Garrison JC, Kojima I |title=Activation of the calcium-permeable cation channel CD20 by alpha subunits of the Gi protein. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14733-9 |year= 1997 |pmid= 9169438 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NOD1... {November 17, 2007 1:30:11 PM PST}
- SEARCH REDIRECT: Control Box Found: NOD1 {November 17, 2007 1:30:40 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:30:41 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:30:41 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:30:41 PM PST}
- UPDATED: Updated protein page: NOD1 {November 17, 2007 1:30:48 PM PST}
- INFO: Beginning work on PAX8... {November 17, 2007 1:28:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:28:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PAX8_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k78.
| PDB = {{PDB2|1k78}}, {{PDB2|1mdm}}
| Name = Paired box gene 8
| HGNCid = 8622
| Symbol = PAX8
| AltSymbols =;
| OMIM = 167415
| ECnumber =
| Homologene = 2589
| MGIid = 97492
| GeneAtlas_image1 = PBB_GE_PAX8_121_at_tn.png
| GeneAtlas_image2 = PBB_GE_PAX8_207921_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PAX8_207923_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004550 |text = nucleoside diphosphate kinase activity}} {{GNF_GO|id=GO:0004996 |text = thyroid-stimulating hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}}
| Process = {{GNF_GO|id=GO:0006183 |text = GTP biosynthetic process}} {{GNF_GO|id=GO:0006228 |text = UTP biosynthetic process}} {{GNF_GO|id=GO:0006241 |text = CTP biosynthetic process}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7849
| Hs_Ensembl = ENSG00000125618
| Hs_RefseqProtein = NP_003457
| Hs_RefseqmRNA = NM_003466
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 113690046
| Hs_GenLoc_end = 113720991
| Hs_Uniprot = Q06710
| Mm_EntrezGene = 18510
| Mm_Ensembl = ENSMUSG00000026976
| Mm_RefseqmRNA = NM_011040
| Mm_RefseqProtein = NP_035170
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 24242560
| Mm_GenLoc_end = 24297608
| Mm_Uniprot = Q6GU20
}}
}}
'''Paired box gene 8''', also known as '''PAX8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAX8 paired box gene 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7849| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the paired box (PAX) family of transcription factors. Members of this gene family typically encode proteins which contain a paired box domain, an octapeptide, and a paired-type homeodomain. This nuclear protein is involved in thyroid follicular cell development and expression of thyroid-specific genes. Mutations in this gene have been associated with thyroid dysgenesis, thyroid follicular carcinomas and atypical follicular thyroid adenomas. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: PAX8 paired box gene 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7849| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Poleev A, Fickenscher H, Mundlos S, ''et al.'' |title=PAX8, a human paired box gene: isolation and expression in developing thyroid, kidney and Wilms' tumors. |journal=Development |volume=116 |issue= 3 |pages= 611-23 |year= 1993 |pmid= 1337742 |doi= }}
*{{cite journal | author=Poleev A, Wendler F, Fickenscher H, ''et al.'' |title=Distinct functional properties of three human paired-box-protein, PAX8, isoforms generated by alternative splicing in thyroid, kidney and Wilms' tumors. |journal=Eur. J. Biochem. |volume=228 |issue= 3 |pages= 899-911 |year= 1995 |pmid= 7737192 |doi= }}
*{{cite journal | author=Stapleton P, Weith A, Urbánek P, ''et al.'' |title=Chromosomal localization of seven PAX genes and cloning of a novel family member, PAX-9. |journal=Nat. Genet. |volume=3 |issue= 4 |pages= 292-8 |year= 1995 |pmid= 7981748 |doi= 10.1038/ng0493-292 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Kozmik Z, Kurzbauer R, Dörfler P, Busslinger M |title=Alternative splicing of Pax-8 gene transcripts is developmentally regulated and generates isoforms with different transactivation properties. |journal=Mol. Cell. Biol. |volume=13 |issue= 10 |pages= 6024-35 |year= 1993 |pmid= 8413205 |doi= }}
*{{cite journal | author=Pilz AJ, Povey S, Gruss P, Abbott CM |title=Mapping of the human homologs of the murine paired-box-containing genes. |journal=Mamm. Genome |volume=4 |issue= 2 |pages= 78-82 |year= 1993 |pmid= 8431641 |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=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Fraizer GC, Shimamura R, Zhang X, Saunders GF |title=PAX 8 regulates human WT1 transcription through a novel DNA binding site. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30678-87 |year= 1998 |pmid= 9388203 |doi= }}
*{{cite journal | author=Macchia PE, Lapi P, Krude H, ''et al.'' |title=PAX8 mutations associated with congenital hypothyroidism caused by thyroid dysgenesis. |journal=Nat. Genet. |volume=19 |issue= 1 |pages= 83-6 |year= 1998 |pmid= 9590296 |doi= 10.1038/ng0598-83 }}
*{{cite journal | author=Mansouri A, Chowdhury K, Gruss P |title=Follicular cells of the thyroid gland require Pax8 gene function. |journal=Nat. Genet. |volume=19 |issue= 1 |pages= 87-90 |year= 1998 |pmid= 9590297 |doi= 10.1038/ng0598-87 }}
*{{cite journal | author=Tell G, Pellizzari L, Esposito G, ''et al.'' |title=Structural defects of a Pax8 mutant that give rise to congenital hypothyroidism. |journal=Biochem. J. |volume=341 ( Pt 1) |issue= |pages= 89-93 |year= 1999 |pmid= 10377248 |doi= }}
*{{cite journal | author=De Leo R, Miccadei S, Zammarchi E, Civitareale D |title=Role for p300 in Pax 8 induction of thyroperoxidase gene expression. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34100-5 |year= 2000 |pmid= 10924503 |doi= 10.1074/jbc.M003043200 }}
*{{cite journal | author=Roberts EC, Deed RW, Inoue T, ''et al.'' |title=Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding. |journal=Mol. Cell. Biol. |volume=21 |issue= 2 |pages= 524-33 |year= 2001 |pmid= 11134340 |doi= 10.1128/MCB.21.2.524-533.2001 }}
*{{cite journal | author=Vilain C, Rydlewski C, Duprez L, ''et al.'' |title=Autosomal dominant transmission of congenital thyroid hypoplasia due to loss-of-function mutation of PAX8. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 1 |pages= 234-8 |year= 2001 |pmid= 11232006 |doi= }}
*{{cite journal | author=Congdon T, Nguyen LQ, Nogueira CR, ''et al.'' |title=A novel mutation (Q40P) in PAX8 associated with congenital hypothyroidism and thyroid hypoplasia: evidence for phenotypic variability in mother and child. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 8 |pages= 3962-7 |year= 2001 |pmid= 11502839 |doi= }}
*{{cite journal | author=Miccadei S, De Leo R, Zammarchi E, ''et al.'' |title=The synergistic activity of thyroid transcription factor 1 and Pax 8 relies on the promoter/enhancer interplay. |journal=Mol. Endocrinol. |volume=16 |issue= 4 |pages= 837-46 |year= 2002 |pmid= 11923479 |doi= }}
*{{cite journal | author=Marques AR, Espadinha C, Catarino AL, ''et al.'' |title=Expression of PAX8-PPAR gamma 1 rearrangements in both follicular thyroid carcinomas and adenomas. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 8 |pages= 3947-52 |year= 2002 |pmid= 12161538 |doi= }}
*{{cite journal | author=Di Palma T, Nitsch R, Mascia A, ''et al.'' |title=The paired domain-containing factor Pax8 and the homeodomain-containing factor TTF-1 directly interact and synergistically activate transcription. |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 3395-402 |year= 2003 |pmid= 12441357 |doi= 10.1074/jbc.M205977200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMA7... {November 17, 2007 1:22:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:23:02 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSMA7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, alpha type, 7
| HGNCid = 9536
| Symbol = PSMA7
| AltSymbols =; C6; HSPC; MGC3755; RC6-1; XAPC7
| OMIM = 606607
| ECnumber =
| Homologene = 2086
| MGIid = 1347070
| GeneAtlas_image1 = PBB_GE_PSMA7_216088_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMA7_201114_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5688
| Hs_Ensembl = ENSG00000101182
| Hs_RefseqProtein = NP_002783
| Hs_RefseqmRNA = NM_002792
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 60145186
| Hs_GenLoc_end = 60151881
| Hs_Uniprot = O14818
| Mm_EntrezGene = 26444
| Mm_Ensembl = ENSMUSG00000027566
| Mm_RefseqmRNA = NM_011969
| Mm_RefseqProtein = NP_036099
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 179965784
| Mm_GenLoc_end = 179971816
| Mm_Uniprot = Q3THL2
}}
}}
'''Proteasome (prosome, macropain) subunit, alpha type, 7''', also known as '''PSMA7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5688| 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.<ref name="entrez">{{cite web | title = Entrez Gene: PSMA7 proteasome (prosome, macropain) subunit, alpha type, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5688| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
*{{cite journal | author=Akioka H, Forsberg NE, Ishida N, ''et al.'' |title=Isolation and characterization of the HC8 subunit gene of the human proteasome. |journal=Biochem. Biophys. Res. Commun. |volume=207 |issue= 1 |pages= 318-23 |year= 1995 |pmid= 7857283 |doi= 10.1006/bbrc.1995.1190 }}
*{{cite journal | author=Huang J, Kwong J, Sun EC, Liang TJ |title=Proteasome complex as a potential cellular target of hepatitis B virus X protein. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5582-91 |year= 1996 |pmid= 8764072 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |doi= }}
*{{cite journal | author=Zhang Z, Torii N, Furusaka A, ''et al.'' |title=Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15157-65 |year= 2000 |pmid= 10748218 |doi= 10.1074/jbc.M910378199 }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
*{{cite journal | author=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29-37 |year= 2001 |pmid= 11205743 |doi= }}
*{{cite journal | author=Golubnitschaja-Labudova O, Liu R, Decker C, ''et al.'' |title=Altered gene expression in lymphocytes of patients with normal-tension glaucoma. |journal=Curr. Eye Res. |volume=21 |issue= 5 |pages= 867-76 |year= 2001 |pmid= 11262608 |doi= }}
*{{cite journal | author=Hartmann-Petersen R, Tanaka K, Hendil KB |title=Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 89-94 |year= 2001 |pmid= 11361004 |doi= 10.1006/abbi.2000.2178 }}
*{{cite journal | author=Cho S, Choi YJ, Kim JM, ''et al.'' |title=Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7. |journal=FEBS Lett. |volume=498 |issue= 1 |pages= 62-6 |year= 2001 |pmid= 11389899 |doi= }}
*{{cite journal | author=Krüger M, Beger C, Welch PJ, ''et al.'' |title=Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus internal ribosome entry site-mediated translation. |journal=Mol. Cell. Biol. |volume=21 |issue= 24 |pages= 8357-64 |year= 2001 |pmid= 11713272 |doi= 10.1128/MCB.21.24.8357-8364.2001 }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMB5... {November 17, 2007 1:23:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:23:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSMB5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, beta type, 5
| HGNCid = 9542
| Symbol = PSMB5
| AltSymbols =; X; LMPX; MB1; MGC104214
| OMIM = 600306
| ECnumber =
| Homologene = 55690
| MGIid = 1194513
| GeneAtlas_image1 = PBB_GE_PSMB5_208799_at_tn.png
| Function = {{GNF_GO|id=GO:0004263 |text = chymotrypsin activity}} {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0043161 |text = proteasomal ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5693
| Hs_Ensembl = ENSG00000100804
| Hs_RefseqProtein = NP_002788
| Hs_RefseqmRNA = NM_002797
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 22564900
| Hs_GenLoc_end = 22573949
| Hs_Uniprot = P28074
| Mm_EntrezGene = 19173
| Mm_Ensembl = ENSMUSG00000022193
| Mm_RefseqmRNA = NM_011186
| Mm_RefseqProtein = NP_035316
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 53568325
| Mm_GenLoc_end = 53572219
| Mm_Uniprot = Q3UZI1
}}
}}
'''Proteasome (prosome, macropain) subunit, beta type, 5''', also known as '''PSMB5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMB5 proteasome (prosome, macropain) subunit, beta type, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5693| 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is replaced by catalytic subunit 3i (proteasome beta 8 subunit).<ref name="entrez">{{cite web | title = Entrez Gene: PSMB5 proteasome (prosome, macropain) subunit, beta type, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5693| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Lee LW, Moomaw CR, Orth K, ''et al.'' |title=Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome). |journal=Biochim. Biophys. Acta |volume=1037 |issue= 2 |pages= 178-85 |year= 1990 |pmid= 2306472 |doi= }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
*{{cite journal | author=Belich MP, Glynne RJ, Senger G, ''et al.'' |title=Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins. |journal=Curr. Biol. |volume=4 |issue= 9 |pages= 769-76 |year= 1995 |pmid= 7820546 |doi= }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=207 |issue= 3 |pages= 1059 |year= 1995 |pmid= 7864893 |doi= }}
*{{cite journal | author=Akiyama K, Yokota K, Kagawa S, ''et al.'' |title=cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y. |journal=Science |volume=265 |issue= 5176 |pages= 1231-4 |year= 1994 |pmid= 8066462 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Abdulla S, Beck S, Belich M, ''et al.'' |title=Divergent intron arrangement in the MB1/LMP7 proteasome gene pair. |journal=Immunogenetics |volume=44 |issue= 4 |pages= 254-8 |year= 1996 |pmid= 8753855 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Kohda K, Matsuda Y, Ishibashi T, ''et al.'' |title=Structural analysis and chromosomal localization of the mouse Psmb5 gene coding for the constitutively expressed beta-type proteasome subunit. |journal=Immunogenetics |volume=47 |issue= 1 |pages= 77-87 |year= 1998 |pmid= 9382924 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |doi= }}
*{{cite journal | author=Rodriguez-Vilariño S, Arribas J, Arizti P, Castaño JG |title=Proteolytic processing and assembly of the C5 subunit into the proteasome complex. |journal=J. Biol. Chem. |volume=275 |issue= 9 |pages= 6592-9 |year= 2000 |pmid= 10692467 |doi= }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29-37 |year= 2001 |pmid= 11205743 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMC1... {November 17, 2007 1:23:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:24:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) 26S subunit, ATPase, 1
| HGNCid = 9547
| Symbol = PSMC1
| AltSymbols =; MGC24583; MGC8541; P26S4; S4; p56
| OMIM = 602706
| ECnumber =
| Homologene = 2095
| MGIid = 106054
| GeneAtlas_image1 = PBB_GE_PSMC1_204219_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0030163 |text = protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5700
| Hs_Ensembl = ENSG00000100764
| Hs_RefseqProtein = NP_002793
| Hs_RefseqmRNA = NM_002802
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 89792639
| Hs_GenLoc_end = 89808719
| Hs_Uniprot = P62191
| Mm_EntrezGene = 19179
| Mm_Ensembl = ENSMUSG00000021178
| Mm_RefseqmRNA = NM_008947
| Mm_RefseqProtein = NP_032973
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 100513381
| Mm_GenLoc_end = 100524242
| Mm_Uniprot = Q542I9
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, ATPase, 1''', also known as '''PSMC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMC1 proteasome (prosome, macropain) 26S subunit, ATPase, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5700| 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 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. This subunit and a 20S core alpha subunit interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. This subunit also interacts with the adenovirus E1A protein and this interaction alters the activity of the proteasome. Finally, this subunit interacts with ataxin-7, suggesting a role for the proteasome in the development of spinocerebellar ataxia type 7, a progressive neurodegenerative disorder.<ref name="entrez">{{cite web | title = Entrez Gene: PSMC1 proteasome (prosome, macropain) 26S subunit, ATPase, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5700| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Dubiel W, Ferrell K, Pratt G, Rechsteiner M |title=Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family. |journal=J. Biol. Chem. |volume=267 |issue= 32 |pages= 22699-702 |year= 1992 |pmid= 1429620 |doi= }}
*{{cite journal | author=Winkelmann DA, Kahan L |title=Immunochemical accessibility of ribosomal protein S4 in the 30 S ribosome. The interaction of S4 with S5 and S12. |journal=J. Mol. Biol. |volume=165 |issue= 2 |pages= 357-74 |year= 1983 |pmid= 6188845 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Dai RM, Chen E, Longo DL, ''et al.'' |title=Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3562-73 |year= 1998 |pmid= 9452483 |doi= }}
*{{cite journal | author=Tanahashi N, Suzuki M, Fujiwara T, ''et al.'' |title=Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 229-32 |year= 1998 |pmid= 9473509 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Gorbea C, Taillandier D, Rechsteiner M |title=Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7. |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 875-82 |year= 2000 |pmid= 10625621 |doi= }}
*{{cite journal | author=Zhang Z, Torii N, Furusaka A, ''et al.'' |title=Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15157-65 |year= 2000 |pmid= 10748218 |doi= 10.1074/jbc.M910378199 }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Turnell AS, Grand RJ, Gorbea C, ''et al.'' |title=Regulation of the 26S proteasome by adenovirus E1A. |journal=EMBO J. |volume=19 |issue= 17 |pages= 4759-73 |year= 2000 |pmid= 10970867 |doi= 10.1093/emboj/19.17.4759 }}
*{{cite journal | author=Hartmann-Petersen R, Tanaka K, Hendil KB |title=Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 89-94 |year= 2001 |pmid= 11361004 |doi= 10.1006/abbi.2000.2178 }}
*{{cite journal | author=Matilla A, Gorbea C, Einum DD, ''et al.'' |title=Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex. |journal=Hum. Mol. Genet. |volume=10 |issue= 24 |pages= 2821-31 |year= 2002 |pmid= 11734547 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on S100A1... {November 17, 2007 1:24:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:24:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_S100A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k2h.
| PDB = {{PDB2|1k2h}}, {{PDB2|1zfs}}
| Name = S100 calcium binding protein A1
| HGNCid = 10486
| Symbol = S100A1
| AltSymbols =; S100; S100-alpha; S100A
| OMIM = 176940
| ECnumber =
| Homologene = 4566
| MGIid = 1338917
| GeneAtlas_image1 = PBB_GE_S100A1_205334_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0048154 |text = S100 beta binding}} {{GNF_GO|id=GO:0048155 |text = S100 alpha binding}} {{GNF_GO|id=GO:0051117 |text = ATPase binding}}
| Component = {{GNF_GO|id=GO:0016529 |text = sarcoplasmic reticulum}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6271
| Hs_Ensembl = ENSG00000160678
| Hs_RefseqProtein = NP_006262
| Hs_RefseqmRNA = NM_006271
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 151867026
| Hs_GenLoc_end = 151871137
| Hs_Uniprot = P23297
| Mm_EntrezGene = 20193
| Mm_Ensembl = ENSMUSG00000044080
| Mm_RefseqmRNA = NM_011309
| Mm_RefseqProtein = NP_035439
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 90596964
| Mm_GenLoc_end = 90600319
| Mm_Uniprot = Q91V77
}}
}}
'''S100 calcium binding protein A1''', also known as '''S100A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: S100A1 S100 calcium binding protein A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6271| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of this protein has been implicated in cardiomyopathies.<ref name="entrez">{{cite web | title = Entrez Gene: S100A1 S100 calcium binding protein A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6271| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zimmer DB, Cornwall EH, Landar A, Song W |title=The S100 protein family: history, function, and expression. |journal=Brain Res. Bull. |volume=37 |issue= 4 |pages= 417-29 |year= 1995 |pmid= 7620916 |doi= }}
*{{cite journal | author=Schäfer BW, Heizmann CW |title=The S100 family of EF-hand calcium-binding proteins: functions and pathology. |journal=Trends Biochem. Sci. |volume=21 |issue= 4 |pages= 134-40 |year= 1996 |pmid= 8701470 |doi= }}
*{{cite journal | author=Garbuglia M, Verzini M, Sorci G, ''et al.'' |title=The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments. |journal=Braz. J. Med. Biol. Res. |volume=32 |issue= 10 |pages= 1177-85 |year= 2000 |pmid= 10510252 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Erne P, Heizmann CW |title=S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart. |journal=Biochemistry |volume=31 |issue= 42 |pages= 10258-64 |year= 1992 |pmid= 1384693 |doi= }}
*{{cite journal | author=Morii K, Tanaka R, Takahashi Y, ''et al.'' |title=Structure and chromosome assignment of human S100 alpha and beta subunit genes. |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 1 |pages= 185-91 |year= 1991 |pmid= 1998503 |doi= }}
*{{cite journal | author=Baudier J, Glasser N, Gerard D |title=Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein. |journal=J. Biol. Chem. |volume=261 |issue= 18 |pages= 8192-203 |year= 1986 |pmid= 3722149 |doi= }}
*{{cite journal | author=Kato K, Kimura S |title=S100ao (alpha alpha) protein is mainly located in the heart and striated muscles. |journal=Biochim. Biophys. Acta |volume=842 |issue= 2-3 |pages= 146-50 |year= 1985 |pmid= 4052452 |doi= }}
*{{cite journal | author=Schäfer BW, Wicki R, Engelkamp D, ''et al.'' |title=Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family. |journal=Genomics |volume=25 |issue= 3 |pages= 638-43 |year= 1995 |pmid= 7759097 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Mattei MG, ''et al.'' |title=Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6547-51 |year= 1993 |pmid= 8341667 |doi= }}
*{{cite journal | author=Garbuglia M, Verzini M, Giambanco I, ''et al.'' |title=Effects of calcium-binding proteins (S-100a(o), S-100a, S-100b) on desmin assembly in vitro. |journal=FASEB J. |volume=10 |issue= 2 |pages= 317-24 |year= 1996 |pmid= 8641565 |doi= }}
*{{cite journal | author=Landar A, Caddell G, Chessher J, Zimmer DB |title=Identification of an S100A1/S100B target protein: phosphoglucomutase. |journal=Cell Calcium |volume=20 |issue= 3 |pages= 279-85 |year= 1997 |pmid= 8894274 |doi= }}
*{{cite journal | author=Remppis A, Greten T, Schäfer BW, ''et al.'' |title=Altered expression of the Ca(2+)-binding protein S100A1 in human cardiomyopathy. |journal=Biochim. Biophys. Acta |volume=1313 |issue= 3 |pages= 253-7 |year= 1996 |pmid= 8898862 |doi= }}
*{{cite journal | author=Treves S, Scutari E, Robert M, ''et al.'' |title=Interaction of S100A1 with the Ca2+ release channel (ryanodine receptor) of skeletal muscle. |journal=Biochemistry |volume=36 |issue= 38 |pages= 11496-503 |year= 1997 |pmid= 9298970 |doi= 10.1021/bi970160w }}
*{{cite journal | author=Groves P, Finn BE, Kuźnicki J, Forsén S |title=A model for target protein binding to calcium-activated S100 dimers. |journal=FEBS Lett. |volume=421 |issue= 3 |pages= 175-9 |year= 1998 |pmid= 9468301 |doi= }}
*{{cite journal | author=Mandinova A, Atar D, Schäfer BW, ''et al.'' |title=Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium. |journal=J. Cell. Sci. |volume=111 ( Pt 14) |issue= |pages= 2043-54 |year= 1998 |pmid= 9645951 |doi= }}
*{{cite journal | author=Osterloh D, Ivanenkov VV, Gerke V |title=Hydrophobic residues in the C-terminal region of S100A1 are essential for target protein binding but not for dimerization. |journal=Cell Calcium |volume=24 |issue= 2 |pages= 137-51 |year= 1999 |pmid= 9803314 |doi= }}
*{{cite journal | author=Garbuglia M, Verzini M, Donato R |title=Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments. |journal=Cell Calcium |volume=24 |issue= 3 |pages= 177-91 |year= 1999 |pmid= 9883272 |doi= }}
*{{cite journal | author=Ridinger K, Ilg EC, Niggli FK, ''et al.'' |title=Clustered organization of S100 genes in human and mouse. |journal=Biochim. Biophys. Acta |volume=1448 |issue= 2 |pages= 254-63 |year= 1999 |pmid= 9920416 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SCGB1A1... {November 17, 2007 1:26:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:26:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Secretoglobin, family 1A, member 1 (uteroglobin)
| HGNCid = 12523
| Symbol = SCGB1A1
| AltSymbols =; CC10; CC16; CCSP; UGB
| OMIM = 192020
| ECnumber =
| Homologene = 2518
| MGIid = 98919
| GeneAtlas_image1 = PBB_GE_SCGB1A1_205725_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0019834 |text = phospholipase A2 inhibitor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007566 |text = embryo implantation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7356
| Hs_Ensembl = ENSG00000149021
| Hs_RefseqProtein = NP_003348
| Hs_RefseqmRNA = NM_003357
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 61943099
| Hs_GenLoc_end = 61947242
| Hs_Uniprot = P11684
| Mm_EntrezGene = 22287
| Mm_Ensembl = ENSMUSG00000024653
| Mm_RefseqmRNA = NM_011681
| Mm_RefseqProtein = NP_035811
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 9150685
| Mm_GenLoc_end = 9154981
| Mm_Uniprot = Q3UKV9
}}
}}
'''Secretoglobin, family 1A, member 1 (uteroglobin)''', also known as '''SCGB1A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCGB1A1 secretoglobin, family 1A, member 1 (uteroglobin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7356| 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=Wolf M, Klug J, Hackenberg R, ''et al.'' |title=Human CC10, the homologue of rabbit uteroglobin: genomic cloning, chromosomal localization and expression in endometrial cell lines. |journal=Hum. Mol. Genet. |volume=1 |issue= 6 |pages= 371-8 |year= 1993 |pmid= 1284526 |doi= }}
*{{cite journal | author=Bernard A, Roels H, Lauwerys R, ''et al.'' |title=Human urinary protein 1: evidence for identity with the Clara cell protein and occurrence in respiratory tract and urogenital secretions. |journal=Clin. Chim. Acta |volume=207 |issue= 3 |pages= 239-49 |year= 1992 |pmid= 1395029 |doi= }}
*{{cite journal | author=Singh G, Katyal SL, Brown WE, ''et al.'' |title=Amino-acid and cDNA nucleotide sequences of human Clara cell 10 kDa protein. |journal=Biochim. Biophys. Acta |volume=950 |issue= 3 |pages= 329-37 |year= 1988 |pmid= 3167058 |doi= }}
*{{cite journal | author=Singh G, Singh J, Katyal SL, ''et al.'' |title=Identification, cellular localization, isolation, and characterization of human Clara cell-specific 10 KD protein. |journal=J. Histochem. Cytochem. |volume=36 |issue= 1 |pages= 73-80 |year= 1988 |pmid= 3275712 |doi= }}
*{{cite journal | author=Jensen SM, Jones JE, Pass H, ''et al.'' |title=Clara cell 10 kDa protein mRNA in normal and atypical regions of human respiratory epithelium. |journal=Int. J. Cancer |volume=58 |issue= 5 |pages= 629-37 |year= 1994 |pmid= 7521325 |doi= }}
*{{cite journal | author=Umland TC, Swaminathan S, Singh G, ''et al.'' |title=Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution. |journal=Nat. Struct. Biol. |volume=1 |issue= 8 |pages= 538-45 |year= 1995 |pmid= 7664082 |doi= }}
*{{cite journal | author=Hay JG, Danel C, Chu CS, Crystal RG |title=Human CC10 gene expression in airway epithelium and subchromosomal locus suggest linkage to airway disease. |journal=Am. J. Physiol. |volume=268 |issue= 4 Pt 1 |pages= L565-75 |year= 1995 |pmid= 7733299 |doi= }}
*{{cite journal | author=Zhang Z, Zimonjic DB, Popescu NC, ''et al.'' |title=Human uteroglobin gene: structure, subchromosomal localization, and polymorphism. |journal=DNA Cell Biol. |volume=16 |issue= 1 |pages= 73-83 |year= 1997 |pmid= 9022046 |doi= }}
*{{cite journal | author=Laing IA, Goldblatt J, Eber E, ''et al.'' |title=A polymorphism of the CC16 gene is associated with an increased risk of asthma. |journal=J. Med. Genet. |volume=35 |issue= 6 |pages= 463-7 |year= 1998 |pmid= 9643286 |doi= }}
*{{cite journal | author=Zheng F, Kundu GC, Zhang Z, ''et al.'' |title=Uteroglobin is essential in preventing immunoglobulin A nephropathy in mice. |journal=Nat. Med. |volume=5 |issue= 9 |pages= 1018-25 |year= 1999 |pmid= 10470078 |doi= 10.1038/12458 }}
*{{cite journal | author=Müller-Schöttle F, Classen-Linke I, Alfer J, ''et al.'' |title=Expression of uteroglobin in the human endometrium. |journal=Mol. Hum. Reprod. |volume=5 |issue= 12 |pages= 1155-61 |year= 2000 |pmid= 10587371 |doi= }}
*{{cite journal | author=Kundu GC, Zhang Z, Mantile-Selvaggi G, ''et al.'' |title=Uteroglobin binding proteins: regulation of cellular motility and invasion in normal and cancer cells. |journal=Ann. N. Y. Acad. Sci. |volume=923 |issue= |pages= 234-48 |year= 2001 |pmid= 11193760 |doi= }}
*{{cite journal | author=Burmeister R, Boe IM, Nykjaer A, ''et al.'' |title=A two-receptor pathway for catabolism of Clara cell secretory protein in the kidney. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13295-301 |year= 2001 |pmid= 11278724 |doi= 10.1074/jbc.M010679200 }}
*{{cite journal | author=Matsunaga A, Numakura C, Kawakami T, ''et al.'' |title=Association of the uteroglobin gene polymorphism with IgA nephropathy. |journal=Am. J. Kidney Dis. |volume=39 |issue= 1 |pages= 36-41 |year= 2002 |pmid= 11774099 |doi= }}
*{{cite journal | author=Ghafouri B, Ståhlbom B, Tagesson C, Lindahl M |title=Newly identified proteins in human nasal lavage fluid from non-smokers and smokers using two-dimensional gel electrophoresis and peptide mass fingerprinting. |journal=Proteomics |volume=2 |issue= 1 |pages= 112-20 |year= 2002 |pmid= 11788998 |doi= }}
*{{cite journal | author=Narita I, Saito N, Goto S, ''et al.'' |title=Role of uteroglobin G38A polymorphism in the progression of IgA nephropathy in Japanese patients. |journal=Kidney Int. |volume=61 |issue= 5 |pages= 1853-8 |year= 2002 |pmid= 11967037 |doi= 10.1046/j.1523-1755.2002.00336.x }}
*{{cite journal | author=Shijubo N, Itoh Y, Abe S |title=[Anti-inflammatory molecule, Clara cell 10 kilodalton protein and respiratory diseases] |journal=Rinsho Byori |volume=50 |issue= 4 |pages= 370-3 |year= 2002 |pmid= 12014016 |doi= }}
*{{cite journal | author=Chowdhury B, Mantile-Selvaggi G, Miele L, ''et al.'' |title=Lys 43 and Asp 46 in alpha-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity. |journal=Biochem. Biophys. Res. Commun. |volume=295 |issue= 4 |pages= 877-83 |year= 2002 |pmid= 12127976 |doi= }}
*{{cite journal | author=Coppo R, Chiesa M, Cirina P, ''et al.'' |title=In human IgA nephropathy uteroglobin does not play the role inferred from transgenic mice. |journal=Am. J. Kidney Dis. |volume=40 |issue= 3 |pages= 495-503 |year= 2002 |pmid= 12200800 |doi= }}
*{{cite journal | author=Navab R, Wang Y, Chow YH, ''et al.'' |title=Regulation of human Clara cell 10 kD protein expression by chicken ovalbumin upstream promoter transcription factors (COUP-TFs). |journal=Am. J. Respir. Cell Mol. Biol. |volume=27 |issue= 3 |pages= 273-85 |year= 2002 |pmid= 12204889 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on STAR... {November 17, 2007 1:24:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:24:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Steroidogenic acute regulator
| HGNCid = 11359
| Symbol = STAR
| AltSymbols =; STARD1
| OMIM = 600617
| ECnumber =
| Homologene = 297
| MGIid = 102760
| GeneAtlas_image1 = PBB_GE_STAR_204548_at_tn.png
| Function = {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0015485 |text = cholesterol binding}} {{GNF_GO|id=GO:0017127 |text = cholesterol transporter activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006694 |text = steroid biosynthetic process}} {{GNF_GO|id=GO:0006700 |text = C21-steroid hormone biosynthetic process}} {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0008211 |text = glucocorticoid metabolic process}} {{GNF_GO|id=GO:0044255 |text = cellular lipid metabolic process}} {{GNF_GO|id=GO:0050810 |text = regulation of steroid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6770
| Hs_Ensembl = ENSG00000147465
| Hs_RefseqProtein = NP_000340
| Hs_RefseqmRNA = NM_000349
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 38119383
| Hs_GenLoc_end = 38127757
| Hs_Uniprot = P49675
| Mm_EntrezGene = 20845
| Mm_Ensembl = ENSMUSG00000031574
| Mm_RefseqmRNA = NM_011485
| Mm_RefseqProtein = NP_035615
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 27274058
| Mm_GenLoc_end = 27281527
| Mm_Uniprot = P51557
}}
}}
'''Steroidogenic acute regulator''', also known as '''STAR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: STAR steroidogenic acute regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6770| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene plays a key role in the acute regulation of steroid hormone synthesis by enhancing the conversion of cholesterol into pregnenolone. This protein permits the cleavage of cholesterol into pregnenolone by mediating the transport of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane. Mutations in this gene are a cause of congenital lipoid adrenal hyperplasia (CLAH), also called lipoid CAH. A pseudogene of this gene is located on chromosome 13. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: STAR steroidogenic acute regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6770| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Strauss JF, Kallen CB, Christenson LK, ''et al.'' |title=The steroidogenic acute regulatory protein (StAR): a window into the complexities of intracellular cholesterol trafficking. |journal=Recent Prog. Horm. Res. |volume=54 |issue= |pages= 369-94; discussion 394-5 |year= 1999 |pmid= 10548884 |doi= }}
*{{cite journal | author=Stocco DM |title=Clinical disorders associated with abnormal cholesterol transport: mutations in the steroidogenic acute regulatory protein. |journal=Mol. Cell. Endocrinol. |volume=191 |issue= 1 |pages= 19-25 |year= 2003 |pmid= 12044915 |doi= }}
*{{cite journal | author=Manna PR, Stocco DM |title=Regulation of the steroidogenic acute regulatory protein expression: functional and physiological consequences. |journal=Curr. Drug Targets Immune Endocr. Metabol. Disord. |volume=5 |issue= 1 |pages= 93-108 |year= 2005 |pmid= 15777208 |doi= }}
*{{cite journal | author=Miller WL |title=Steroidogenic acute regulatory protein (StAR), a novel mitochondrial cholesterol transporter. |journal=Biochim. Biophys. Acta |volume=1771 |issue= 6 |pages= 663-76 |year= 2007 |pmid= 17433772 |doi= 10.1016/j.bbalip.2007.02.012 }}
*{{cite journal | author=Sugawara T, Lin D, Holt JA, ''et al.'' |title=Structure of the human steroidogenic acute regulatory protein (StAR) gene: StAR stimulates mitochondrial cholesterol 27-hydroxylase activity. |journal=Biochemistry |volume=34 |issue= 39 |pages= 12506-12 |year= 1995 |pmid= 7547998 |doi= }}
*{{cite journal | author=Gradi A, Tang-Wai R, McBride HM, ''et al.'' |title=The human steroidogenic acute regulatory (StAR) gene is expressed in the urogenital system and encodes a mitochondrial polypeptide. |journal=Biochim. Biophys. Acta |volume=1258 |issue= 3 |pages= 228-33 |year= 1995 |pmid= 7548191 |doi= }}
*{{cite journal | author=Sugawara T, Holt JA, Driscoll D, ''et al.'' |title=Human steroidogenic acute regulatory protein: functional activity in COS-1 cells, tissue-specific expression, and mapping of the structural gene to 8p11.2 and a pseudogene to chromosome 13. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 11 |pages= 4778-82 |year= 1995 |pmid= 7761400 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Tee MK, Lin D, Sugawara T, ''et al.'' |title=T-->A transversion 11 bp from a splice acceptor site in the human gene for steroidogenic acute regulatory protein causes congenital lipoid adrenal hyperplasia. |journal=Hum. Mol. Genet. |volume=4 |issue= 12 |pages= 2299-305 |year= 1996 |pmid= 8634702 |doi= }}
*{{cite journal | author=Arakane F, Sugawara T, Nishino H, ''et al.'' |title=Steroidogenic acute regulatory protein (StAR) retains activity in the absence of its mitochondrial import sequence: implications for the mechanism of StAR action. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 24 |pages= 13731-6 |year= 1997 |pmid= 8943003 |doi= }}
*{{cite journal | author=Bose HS, Sugawara T, Strauss JF, Miller WL |title=The pathophysiology and genetics of congenital lipoid adrenal hyperplasia. International Congenital Lipoid Adrenal Hyperplasia Consortium. |journal=N. Engl. J. Med. |volume=335 |issue= 25 |pages= 1870-8 |year= 1996 |pmid= 8948562 |doi= }}
*{{cite journal | author=Nakae J, Tajima T, Sugawara T, ''et al.'' |title=Analysis of the steroidogenic acute regulatory protein (StAR) gene in Japanese patients with congenital lipoid adrenal hyperplasia. |journal=Hum. Mol. Genet. |volume=6 |issue= 4 |pages= 571-6 |year= 1997 |pmid= 9097960 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Sugawara T, Kiriakidou M, McAllister JM, ''et al.'' |title=Multiple steroidogenic factor 1 binding elements in the human steroidogenic acute regulatory protein gene 5'-flanking region are required for maximal promoter activity and cyclic AMP responsiveness. |journal=Biochemistry |volume=36 |issue= 23 |pages= 7249-55 |year= 1997 |pmid= 9188726 |doi= 10.1021/bi9628984 }}
*{{cite journal | author=Pollack SE, Furth EE, Kallen CB, ''et al.'' |title=Localization of the steroidogenic acute regulatory protein in human tissues. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 12 |pages= 4243-51 |year= 1998 |pmid= 9398748 |doi= }}
*{{cite journal | author=Christenson LK, McAllister JM, Martin KO, ''et al.'' |title=Oxysterol regulation of steroidogenic acute regulatory protein gene expression. Structural specificity and transcriptional and posttranscriptional actions. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30729-35 |year= 1998 |pmid= 9804848 |doi= }}
*{{cite journal | author=Korsch E, Peter M, Hiort O, ''et al.'' |title=Gonadal histology with testicular carcinoma in situ in a 15-year-old 46,XY female patient with a premature termination in the steroidogenic acute regulatory protein causing congenital lipoid adrenal hyperplasia. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 5 |pages= 1628-32 |year= 1999 |pmid= 10323391 |doi= }}
*{{cite journal | author=Katsumata N, Kawada Y, Yamamoto Y, ''et al.'' |title=A novel compound heterozygous mutation in the steroidogenic acute regulatory protein gene in a patient with congenital lipoid adrenal hyperplasia. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 11 |pages= 3983-7 |year= 1999 |pmid= 10566637 |doi= }}
*{{cite journal | author=Tsujishita Y, Hurley JH |title=Structure and lipid transport mechanism of a StAR-related domain. |journal=Nat. Struct. Biol. |volume=7 |issue= 5 |pages= 408-14 |year= 2000 |pmid= 10802740 |doi= 10.1038/75192 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGFB1I1... {November 17, 2007 1:24:58 PM PST}
- SEARCH REDIRECT: Control Box Found: TGFB1I1 {November 17, 2007 1:25:31 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:25:34 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:25:34 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:25:34 PM PST}
- UPDATED: Updated protein page: TGFB1I1 {November 17, 2007 1:25:44 PM PST}
- INFO: Beginning work on TNFAIP3... {November 17, 2007 1:25:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:26:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tumor necrosis factor, alpha-induced protein 3
| HGNCid = 11896
| Symbol = TNFAIP3
| AltSymbols =; A20; MGC104522; MGC138687; MGC138688; OTUD7C; TNFA1P2
| OMIM = 191163
| ECnumber =
| Homologene = 4582
| MGIid = 1196377
| GeneAtlas_image1 = PBB_GE_TNFAIP3_202644_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TNFAIP3_202643_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0043124 |text = negative regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7128
| Hs_Ensembl = ENSG00000118503
| Hs_RefseqProtein = NP_006281
| Hs_RefseqmRNA = NM_006290
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 138230151
| Hs_GenLoc_end = 138246135
| Hs_Uniprot = P21580
| Mm_EntrezGene = 21929
| Mm_Ensembl = ENSMUSG00000019850
| Mm_RefseqmRNA = NM_009397
| Mm_RefseqProtein = NP_033423
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 18690335
| Mm_GenLoc_end = 18704826
| Mm_Uniprot = Q3T9G9
}}
}}
'''Tumor necrosis factor, alpha-induced protein 3''', also known as '''TNFAIP3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNFAIP3 tumor necrosis factor, alpha-induced protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7128| 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 was identified as a gene whose expression is rapidly induced by the tumor necrosis factor (TNF). The protein encoded by this gene is a zinc finger protein, and has been shown to inhibit NF-kappa B activation as well as TNF-mediated apoptosis. Knockout studies of a similar gene in mice suggested that this gene is critical for limiting inflammation by terminating TNF-induced NF-kappa B responses.<ref name="entrez">{{cite web | title = Entrez Gene: TNFAIP3 tumor necrosis factor, alpha-induced protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7128| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Opipari AW, Boguski MS, Dixit VM |title=The A20 cDNA induced by tumor necrosis factor alpha encodes a novel type of zinc finger protein. |journal=J. Biol. Chem. |volume=265 |issue= 25 |pages= 14705-8 |year= 1990 |pmid= 2118515 |doi= }}
*{{cite journal | author=Dixit VM, Green S, Sarma V, ''et al.'' |title=Tumor necrosis factor-alpha induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2973-8 |year= 1990 |pmid= 2406243 |doi= }}
*{{cite journal | author=Cooper JT, Stroka DM, Brostjan C, ''et al.'' |title=A20 blocks endothelial cell activation through a NF-kappaB-dependent mechanism. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18068-73 |year= 1996 |pmid= 8663499 |doi= }}
*{{cite journal | author=Song HY, Rothe M, Goeddel DV |title=The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6721-5 |year= 1996 |pmid= 8692885 |doi= }}
*{{cite journal | author=Vincenz C, Dixit VM |title=14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 20029-34 |year= 1996 |pmid= 8702721 |doi= }}
*{{cite journal | author=De Valck D, Heyninck K, Van Criekinge W, ''et al.'' |title=A20, an inhibitor of cell death, self-associates by its zinc finger domain. |journal=FEBS Lett. |volume=384 |issue= 1 |pages= 61-4 |year= 1996 |pmid= 8797804 |doi= }}
*{{cite journal | author=De Valck D, Heyninck K, Van Criekinge W, ''et al.'' |title=A20 inhibits NF-kappaB activation independently of binding to 14-3-3 proteins. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 2 |pages= 590-4 |year= 1997 |pmid= 9299557 |doi= 10.1006/bbrc.1997.7343 }}
*{{cite journal | author=Eliopoulos AG, Blake SM, Floettmann JE, ''et al.'' |title=Epstein-Barr virus-encoded latent membrane protein 1 activates the JNK pathway through its extreme C terminus via a mechanism involving TRADD and TRAF2. |journal=J. Virol. |volume=73 |issue= 2 |pages= 1023-35 |year= 1999 |pmid= 9882303 |doi= }}
*{{cite journal | author=Heyninck K, Beyaert R |title=The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6. |journal=FEBS Lett. |volume=442 |issue= 2-3 |pages= 147-50 |year= 1999 |pmid= 9928991 |doi= }}
*{{cite journal | author=Heyninck K, De Valck D, Vanden Berghe W, ''et al.'' |title=The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN. |journal=J. Cell Biol. |volume=145 |issue= 7 |pages= 1471-82 |year= 1999 |pmid= 10385526 |doi= }}
*{{cite journal | author=De Valck D, Jin DY, Heyninck K, ''et al.'' |title=The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases. |journal=Oncogene |volume=18 |issue= 29 |pages= 4182-90 |year= 1999 |pmid= 10435631 |doi= 10.1038/sj.onc.1202787 }}
*{{cite journal | author=Zhang SQ, Kovalenko A, Cantarella G, Wallach D |title=Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. |journal=Immunity |volume=12 |issue= 3 |pages= 301-11 |year= 2000 |pmid= 10755617 |doi= }}
*{{cite journal | author=Lee EG, Boone DL, Chai S, ''et al.'' |title=Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. |journal=Science |volume=289 |issue= 5488 |pages= 2350-4 |year= 2000 |pmid= 11009421 |doi= }}
*{{cite journal | author=Klinkenberg M, Van Huffel S, Heyninck K, Beyaert R |title=Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions. |journal=FEBS Lett. |volume=498 |issue= 1 |pages= 93-7 |year= 2001 |pmid= 11389905 |doi= }}
*{{cite journal | author=Van Huffel S, Delaei F, Heyninck K, ''et al.'' |title=Identification of a novel A20-binding inhibitor of nuclear factor-kappa B activation termed ABIN-2. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 30216-23 |year= 2001 |pmid= 11390377 |doi= 10.1074/jbc.M100048200 }}
*{{cite journal | author=Evans PC, Taylor ER, Coadwell J, ''et al.'' |title=Isolation and characterization of two novel A20-like proteins. |journal=Biochem. J. |volume=357 |issue= Pt 3 |pages= 617-23 |year= 2001 |pmid= 11463333 |doi= }}
*{{cite journal | author=Baltathakis I, Alcantara O, Boldt DH |title=Expression of different NF-kappaB pathway genes in dendritic cells (DCs) or macrophages assessed by gene expression profiling. |journal=J. Cell. Biochem. |volume=83 |issue= 2 |pages= 281-90 |year= 2001 |pmid= 11573245 |doi= }}
*{{cite journal | author=Zetoune FS, Murthy AR, Shao Z, ''et al.'' |title=A20 inhibits NF-kappa B activation downstream of multiple Map3 kinases and interacts with the I kappa B signalosome. |journal=Cytokine |volume=15 |issue= 6 |pages= 282-98 |year= 2002 |pmid= 11594795 |doi= 10.1006/cyto.2001.0921 }}
*{{cite journal | author=Wu WS, Xu ZX, Chang KS |title=The promyelocytic leukemia protein represses A20-mediated transcription. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31734-9 |year= 2002 |pmid= 12080044 |doi= 10.1074/jbc.M201648200 }}
*{{cite journal | author=He KL, Ting AT |title=A20 inhibits tumor necrosis factor (TNF) alpha-induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells. |journal=Mol. Cell. Biol. |volume=22 |issue= 17 |pages= 6034-45 |year= 2002 |pmid= 12167698 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on WFS1... {November 17, 2007 1:26:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:27:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Wolfram syndrome 1 (wolframin)
| HGNCid = 12762
| Symbol = WFS1
| AltSymbols =; DFNA14; DFNA38; DFNA6; DIDMOAD; WFRS; WFS; WOLFRAMIN
| OMIM = 606201
| ECnumber =
| Homologene = 4380
| MGIid = 1328355
| GeneAtlas_image1 = PBB_GE_WFS1_202908_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7466
| Hs_Ensembl = ENSG00000109501
| Hs_RefseqProtein = NP_005996
| Hs_RefseqmRNA = NM_006005
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 6322478
| Hs_GenLoc_end = 6355893
| Hs_Uniprot = O76024
| Mm_EntrezGene = 22393
| Mm_Ensembl = ENSMUSG00000039474
| Mm_RefseqmRNA = NM_011716
| Mm_RefseqProtein = NP_035846
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 37254356
| Mm_GenLoc_end = 37277167
| Mm_Uniprot = Q3TDI2
}}
}}
'''Wolfram syndrome 1 (wolframin)''', also known as '''WFS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: WFS1 Wolfram syndrome 1 (wolframin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7466| 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 transmembrane protein. Mutations in this gene are associated with an autosomal recessive syndrome characterized by insulin-dependent diabetes mellitus and bilateral progressive optic atrophy, usually presenting in childhood or early adult life. Diverse neurologic symptoms, including a predisposition to psychiatric illness, may also be associated with this disorder. A large number and variety of mutations in this gene, particularly in exon 8, can be associated with this syndrome. Mutations in this gene can also cause autosomal dominant deafness 6 (DFNA6), also known as DFNA14 or DFNA38.<ref name="entrez">{{cite web | title = Entrez Gene: WFS1 Wolfram syndrome 1 (wolframin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7466| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Khanim F, Kirk J, Latif F, Barrett TG |title=WFS1/wolframin mutations, Wolfram syndrome, and associated diseases. |journal=Hum. Mutat. |volume=17 |issue= 5 |pages= 357-67 |year= 2001 |pmid= 11317350 |doi= 10.1002/humu.1110 }}
*{{cite journal | author=Cryns K, Sivakumaran TA, Van den Ouweland JM, ''et al.'' |title=Mutational spectrum of the WFS1 gene in Wolfram syndrome, nonsyndromic hearing impairment, diabetes mellitus, and psychiatric disease. |journal=Hum. Mutat. |volume=22 |issue= 4 |pages= 275-87 |year= 2004 |pmid= 12955714 |doi= 10.1002/humu.10258 }}
*{{cite journal | author=McHugh RK, Friedman RA |title=Genetics of hearing loss: Allelism and modifier genes produce a phenotypic continuum. |journal=The anatomical record. Part A, Discoveries in molecular, cellular, and evolutionary biology |volume=288 |issue= 4 |pages= 370-81 |year= 2006 |pmid= 16550584 |doi= 10.1002/ar.a.20297 }}
*{{cite journal | author=Polymeropoulos MH, Swift RG, Swift M |title=Linkage of the gene for Wolfram syndrome to markers on the short arm of chromosome 4. |journal=Nat. Genet. |volume=8 |issue= 1 |pages= 95-7 |year= 1995 |pmid= 7987399 |doi= 10.1038/ng0994-95 }}
*{{cite journal | author=Lesperance MM, Hall JW, Bess FH, ''et al.'' |title=A gene for autosomal dominant nonsyndromic hereditary hearing impairment maps to 4p16.3. |journal=Hum. Mol. Genet. |volume=4 |issue= 10 |pages= 1967-72 |year= 1996 |pmid= 8595423 |doi= }}
*{{cite journal | author=Inoue H, Tanizawa Y, Wasson J, ''et al.'' |title=A gene encoding a transmembrane protein is mutated in patients with diabetes mellitus and optic atrophy (Wolfram syndrome). |journal=Nat. Genet. |volume=20 |issue= 2 |pages= 143-8 |year= 1998 |pmid= 9771706 |doi= 10.1038/2441 }}
*{{cite journal | author=Strom TM, Hörtnagel K, Hofmann S, ''et al.'' |title=Diabetes insipidus, diabetes mellitus, optic atrophy and deafness (DIDMOAD) caused by mutations in a novel gene (wolframin) coding for a predicted transmembrane protein. |journal=Hum. Mol. Genet. |volume=7 |issue= 13 |pages= 2021-8 |year= 1999 |pmid= 9817917 |doi= }}
*{{cite journal | author=Van Camp G, Kunst H, Flothmann K, ''et al.'' |title=A gene for autosomal dominant hearing impairment (DFNA14) maps to a region on chromosome 4p16.3 that does not overlap the DFNA6 locus. |journal=J. Med. Genet. |volume=36 |issue= 7 |pages= 532-6 |year= 1999 |pmid= 10424813 |doi= }}
*{{cite journal | author=Hardy C, Khanim F, Torres R, ''et al.'' |title=Clinical and molecular genetic analysis of 19 Wolfram syndrome kindreds demonstrating a wide spectrum of mutations in WFS1. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1279-90 |year= 1999 |pmid= 10521293 |doi= }}
*{{cite journal | author=Furlong RA, Ho LW, Rubinsztein JS, ''et al.'' |title=A rare coding variant within the wolframin gene in bipolar and unipolar affective disorder cases. |journal=Neurosci. Lett. |volume=277 |issue= 2 |pages= 123-6 |year= 2000 |pmid= 10624825 |doi= }}
*{{cite journal | author=Awata T, Inoue K, Kurihara S, ''et al.'' |title=Missense variations of the gene responsible for Wolfram syndrome (WFS1/wolframin) in Japanese: possible contribution of the Arg456His mutation to type 1 diabetes as a nonautoimmune genetic basis. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 612-6 |year= 2000 |pmid= 10679252 |doi= 10.1006/bbrc.2000.2169 }}
*{{cite journal | author=Ohtsuki T, Ishiguro H, Yoshikawa T, Arinami T |title=WFS1 gene mutation search in depressive patients: detection of five missense polymorphisms but no association with depression or bipolar affective disorder. |journal=Journal of affective disorders |volume=58 |issue= 1 |pages= 11-7 |year= 2000 |pmid= 10760554 |doi= }}
*{{cite journal | author=Gómez-Zaera M, Strom TM, Rodríguez B, ''et al.'' |title=Presence of a major WFS1 mutation in Spanish Wolfram syndrome pedigrees. |journal=Mol. Genet. Metab. |volume=72 |issue= 1 |pages= 72-81 |year= 2001 |pmid= 11161832 |doi= 10.1006/mgme.2000.3107 }}
*{{cite journal | author=Kaytor EN, Zhu JL, Pao CI, Phillips LS |title=Physiological concentrations of insulin promote binding of nuclear proteins to the insulin-like growth factor I gene. |journal=Endocrinology |volume=142 |issue= 3 |pages= 1041-9 |year= 2001 |pmid= 11181517 |doi= }}
*{{cite journal | author=Takeda K, Inoue H, Tanizawa Y, ''et al.'' |title=WFS1 (Wolfram syndrome 1) gene product: predominant subcellular localization to endoplasmic reticulum in cultured cells and neuronal expression in rat brain. |journal=Hum. Mol. Genet. |volume=10 |issue= 5 |pages= 477-84 |year= 2001 |pmid= 11181571 |doi= }}
*{{cite journal | author=Tessa A, Carbone I, Matteoli MC, ''et al.'' |title=Identification of novel WFS1 mutations in Italian children with Wolfram syndrome. |journal=Hum. Mutat. |volume=17 |issue= 4 |pages= 348-9 |year= 2001 |pmid= 11295831 |doi= 10.1002/humu.32 }}
*{{cite journal | author=Bespalova IN, Van Camp G, Bom SJ, ''et al.'' |title=Mutations in the Wolfram syndrome 1 gene (WFS1) are a common cause of low frequency sensorineural hearing loss. |journal=Hum. Mol. Genet. |volume=10 |issue= 22 |pages= 2501-8 |year= 2002 |pmid= 11709537 |doi= }}
*{{cite journal | author=Young TL, Ives E, Lynch E, ''et al.'' |title=Non-syndromic progressive hearing loss DFNA38 is caused by heterozygous missense mutation in the Wolfram syndrome gene WFS1. |journal=Hum. Mol. Genet. |volume=10 |issue= 22 |pages= 2509-14 |year= 2002 |pmid= 11709538 |doi= }}
*{{cite journal | author=Crawford J, Zielinski MA, Fisher LJ, ''et al.'' |title=Is there a relationship between Wolfram syndrome carrier status and suicide? |journal=Am. J. Med. Genet. |volume=114 |issue= 3 |pages= 343-6 |year= 2002 |pmid= 11920861 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on WNT1... {November 17, 2007 1:27:57 PM PST}
- SEARCH REDIRECT: Control Box Found: WNT1 {November 17, 2007 1:28:20 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:28:22 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:28:22 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:28:22 PM PST}
- UPDATED: Updated protein page: WNT1 {November 17, 2007 1:28:28 PM PST}
end log.
