Log page index:
User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 21:10, 17 November 2007 (UTC)
Proteins without matches (10)
Proteins with a High Potential Match (6)
Redirected Proteins (9)
Manual Inspection (Page not found) (16)
Updated (9)
Protein Status Grid - Date: 21:10, 17 November 2007 (UTC)
Vebose Log - Date: 21:10, 17 November 2007 (UTC)
- INFO: Beginning work on ACAN... {November 17, 2007 12:45:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:46:29 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 = PBB_Protein_ACAN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1tdq.
| PDB = {{PDB2|1tdq}}
| Name = Aggrecan
| HGNCid = 319
| Symbol = ACAN
| AltSymbols =; AGC1; AGCAN; CSPG1; CSPGCP; MSK16; SEDK
| OMIM = 155760
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_ACAN_207692_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACAN_205679_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ACAN_217161_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0005540 |text = hyaluronic acid binding}} {{GNF_GO|id=GO:0030021 |text = extracellular matrix structural constituent conferring compression resistance}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005604 |text = basement membrane}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001502 |text = cartilage condensation}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030166 |text = proteoglycan biosynthetic process}} {{GNF_GO|id=GO:0030199 |text = collagen fibril organization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 176
| Hs_Ensembl = ENSG00000157766
| Hs_RefseqProtein = XP_001131727
| Hs_RefseqmRNA = XM_001131727
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 87147709
| Hs_GenLoc_end = 87218716
| Hs_Uniprot = P16112
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Aggrecan''', also known as '''ACAN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACAN aggrecan| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=176| 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 aggrecan/versican proteoglycan family. The encoded protein is an integral part of the extracellular matrix in cartilagenous tissue and it withstands compression in cartilage. Mutations in this gene may be involved in skeletal dysplasia and spinal degeneration. Multiple alternatively spliced transcript variants that encode different protein isoforms have been observed in this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ACAN aggrecan| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=176| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Watanabe H, Yamada Y, Kimata K |title=Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage structure and function. |journal=J. Biochem. |volume=124 |issue= 4 |pages= 687-93 |year= 1999 |pmid= 9756610 |doi= }}
*{{cite journal | author=Roughley P, Martens D, Rantakokko J, ''et al.'' |title=The involvement of aggrecan polymorphism in degeneration of human intervertebral disc and articular cartilage. |journal=European cells & materials |volume=11 |issue= |pages= 1-7; discussion 7 |year= 2006 |pmid= 16425147 |doi= }}
*{{cite journal | author=Fosang AJ, Neame PJ, Last K, ''et al.'' |title=The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. |journal=J. Biol. Chem. |volume=267 |issue= 27 |pages= 19470-4 |year= 1992 |pmid= 1326552 |doi= }}
*{{cite journal | author=Sandy JD, Flannery CR, Neame PJ, Lohmander LS |title=The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. |journal=J. Clin. Invest. |volume=89 |issue= 5 |pages= 1512-6 |year= 1992 |pmid= 1569188 |doi= }}
*{{cite journal | author=Doege KJ, Sasaki M, Kimura T, Yamada Y |title=Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms. |journal=J. Biol. Chem. |volume=266 |issue= 2 |pages= 894-902 |year= 1991 |pmid= 1985970 |doi= }}
*{{cite journal | author=Baldwin CT, Reginato AM, Prockop DJ |title=A new epidermal growth factor-like domain in the human core protein for the large cartilage-specific proteoglycan. Evidence for alternative splicing of the domain. |journal=J. Biol. Chem. |volume=264 |issue= 27 |pages= 15747-50 |year= 1989 |pmid= 2789216 |doi= }}
*{{cite journal | author=Kimata K, Barrach HJ, Brown KS, Pennypacker JP |title=Absence of proteoglycan core protein in cartilage from the cmd/cmd (cartilage matrix deficiency) mouse. |journal=J. Biol. Chem. |volume=256 |issue= 13 |pages= 6961-8 |year= 1981 |pmid= 7240256 |doi= }}
*{{cite journal | author=Glumoff V, Savontaus M, Vehanen J, Vuorio E |title=Analysis of aggrecan and tenascin gene expression in mouse skeletal tissues by northern and in situ hybridization using species specific cDNA probes. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 3 |pages= 613-22 |year= 1994 |pmid= 7524681 |doi= }}
*{{cite journal | author=Ilic MZ, Mok MT, Williamson OD, ''et al.'' |title=Catabolism of aggrecan by explant cultures of human articular cartilage in the presence of retinoic acid. |journal=Arch. Biochem. Biophys. |volume=322 |issue= 1 |pages= 22-30 |year= 1995 |pmid= 7574678 |doi= 10.1006/abbi.1995.1431 }}
*{{cite journal | author=Valhmu WB, Palmer GD, Rivers PA, ''et al.'' |title=Structure of the human aggrecan gene: exon-intron organization and association with the protein domains. |journal=Biochem. J. |volume=309 ( Pt 2) |issue= |pages= 535-42 |year= 1995 |pmid= 7626017 |doi= }}
*{{cite journal | author=Barry FP, Neame PJ, Sasse J, Pearson D |title=Length variation in the keratan sulfate domain of mammalian aggrecan. |journal=Matrix Biol. |volume=14 |issue= 4 |pages= 323-8 |year= 1995 |pmid= 7827755 |doi= }}
*{{cite journal | author=Fosang AJ, Last K, Neame PJ, ''et al.'' |title=Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan. |journal=Biochem. J. |volume=304 ( Pt 2) |issue= |pages= 347-51 |year= 1995 |pmid= 7998967 |doi= }}
*{{cite journal | author=Fosang AJ, Last K, Knäuper V, ''et al.'' |title=Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain. |journal=Biochem. J. |volume=295 ( Pt 1) |issue= |pages= 273-6 |year= 1993 |pmid= 8216228 |doi= }}
*{{cite journal | author=Korenberg JR, Chen XN, Doege K, ''et al.'' |title=Assignment of the human aggrecan gene (AGC1) to 15q26 using fluorescence in situ hybridization analysis. |journal=Genomics |volume=16 |issue= 2 |pages= 546-8 |year= 1993 |pmid= 8314595 |doi= 10.1006/geno.1993.1228 }}
*{{cite journal | author=Dudhia J, Davidson CM, Wells TM, ''et al.'' |title=Age-related changes in the content of the C-terminal region of aggrecan in human articular cartilage. |journal=Biochem. J. |volume=313 ( Pt 3) |issue= |pages= 933-40 |year= 1996 |pmid= 8611178 |doi= }}
*{{cite journal | author=Fülöp C, Cs-Szabó G, Glant TT |title=Species-specific alternative splicing of the epidermal growth factor-like domain 1 of cartilage aggrecan. |journal=Biochem. J. |volume=319 ( Pt 3) |issue= |pages= 935-40 |year= 1996 |pmid= 8921002 |doi= }}
*{{cite journal | author=Kirschfink M, Blase L, Engelmann S, Schwartz-Albiez R |title=Secreted chondroitin sulfate proteoglycan of human B cell lines binds to the complement protein C1q and inhibits complex formation of C1. |journal=J. Immunol. |volume=158 |issue= 3 |pages= 1324-31 |year= 1997 |pmid= 9013976 |doi= }}
*{{cite journal | author=Parkar AA, Kahmann JD, Howat SL, ''et al.'' |title=TSG-6 interacts with hyaluronan and aggrecan in a pH-dependent manner via a common functional element: implications for its regulation in inflamed cartilage. |journal=FEBS Lett. |volume=428 |issue= 3 |pages= 171-6 |year= 1998 |pmid= 9654129 |doi= }}
*{{cite journal | author=Fosang AJ, Last K, Fujii Y, ''et al.'' |title=Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain. |journal=FEBS Lett. |volume=430 |issue= 3 |pages= 186-90 |year= 1998 |pmid= 9688535 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AIRE... {November 17, 2007 12:46:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:47:31 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_AIRE_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xwh.
| PDB = {{PDB2|1xwh}}
| Name = Autoimmune regulator (autoimmune polyendocrinopathy candidiasis ectodermal dystrophy)
| HGNCid = 360
| Symbol = AIRE
| AltSymbols =; AIRE1; APECED; APS1; APSI; PGA1
| OMIM = 607358
| ECnumber =
| Homologene = 327
| MGIid = 1338803
| GeneAtlas_image1 = PBB_GE_AIRE_208090_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0045182 |text = translation regulator activity}} {{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:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 326
| Hs_Ensembl = ENSG00000160224
| Hs_RefseqProtein = NP_000374
| Hs_RefseqmRNA = NM_000383
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 44530191
| Hs_GenLoc_end = 44542486
| Hs_Uniprot = O43918
| Mm_EntrezGene = 11634
| Mm_Ensembl = ENSMUSG00000000731
| Mm_RefseqmRNA = NM_009646
| Mm_RefseqProtein = NP_033776
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 77433160
| Mm_GenLoc_end = 77446709
| Mm_Uniprot = Q3ZB65
}}
}}
'''Autoimmune regulator (autoimmune polyendocrinopathy candidiasis ectodermal dystrophy)''', also known as '''AIRE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AIRE autoimmune regulator (autoimmune polyendocrinopathy candidiasis ectodermal dystrophy)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=326| 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 transcriptional regulator that forms nuclear bodies and interacts with the transcriptional coactivator CBP. At least three splice variant mRNAs products have been described including one which results in a premature stop codon and a transcript predicted to be a candidate for nuclear-mediated decay (NMD). Defects in this gene cause the rare autosomal-recessive systemic autoimmune disease termed autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED).<ref name="entrez">{{cite web | title = Entrez Gene: AIRE autoimmune regulator (autoimmune polyendocrinopathy candidiasis ectodermal dystrophy)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=326| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Björses P, Aaltonen J, Horelli-Kuitunen N, ''et al.'' |title=Gene defect behind APECED: a new clue to autoimmunity. |journal=Hum. Mol. Genet. |volume=7 |issue= 10 |pages= 1547-53 |year= 1998 |pmid= 9735375 |doi= }}
*{{cite journal | author=Heino M, Peterson P, Kudoh J, ''et al.'' |title=APECED mutations in the autoimmune regulator (AIRE) gene. |journal=Hum. Mutat. |volume=18 |issue= 3 |pages= 205-11 |year= 2001 |pmid= 11524731 |doi= 10.1002/humu.1176 }}
*{{cite journal | author=Sato K, Nakajima K, Imamura H, ''et al.'' |title=A novel missense mutation of AIRE gene in a patient with autoimmune polyendocrinopathy, candidiasis and ectodermal dystrophy (APECED), accompanied with progressive muscular atrophy: case report and review of the literature in Japan. |journal=Endocr. J. |volume=49 |issue= 6 |pages= 625-33 |year= 2003 |pmid= 12625412 |doi= }}
*{{cite journal | author=Ruan QG, She JX |title=Autoimmune polyglandular syndrome type 1 and the autoimmune regulator. |journal=Clin. Lab. Med. |volume=24 |issue= 1 |pages= 305-17 |year= 2004 |pmid= 15157567 |doi= 10.1016/j.cll.2004.01.008 }}
*{{cite journal | author=Holmdahl R |title=Aire-ing self antigen variability and tolerance. |journal=Eur. J. Immunol. |volume=37 |issue= 3 |pages= 598-601 |year= 2007 |pmid= 17323409 |doi= 10.1002/eji.200737152 }}
*{{cite journal | author=Aaltonen J, Björses P, Sandkuijl L, ''et al.'' |title=An autosomal locus causing autoimmune disease: autoimmune polyglandular disease type I assigned to chromosome 21. |journal=Nat. Genet. |volume=8 |issue= 1 |pages= 83-7 |year= 1995 |pmid= 7987397 |doi= 10.1038/ng0994-83 }}
*{{cite journal | author=Aaltonen J, Horelli-Kuitunen N, Fan JB, ''et al.'' |title=High-resolution physical and transcriptional mapping of the autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy locus on chromosome 21q22.3 by FISH. |journal=Genome Res. |volume=7 |issue= 8 |pages= 820-9 |year= 1997 |pmid= 9267805 |doi= }}
*{{cite journal | author=Nagamine K, Peterson P, Scott HS, ''et al.'' |title=Positional cloning of the APECED gene. |journal=Nat. Genet. |volume=17 |issue= 4 |pages= 393-8 |year= 1997 |pmid= 9398839 |doi= 10.1038/ng1297-393 }}
*{{cite journal | author= |title=An autoimmune disease, APECED, caused by mutations in a novel gene featuring two PHD-type zinc-finger domains. |journal=Nat. Genet. |volume=17 |issue= 4 |pages= 399-403 |year= 1997 |pmid= 9398840 |doi= 10.1038/ng1297-399 }}
*{{cite journal | author=Scott HS, Heino M, Peterson P, ''et al.'' |title=Common mutations in autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy patients of different origins. |journal=Mol. Endocrinol. |volume=12 |issue= 8 |pages= 1112-9 |year= 1998 |pmid= 9717837 |doi= }}
*{{cite journal | author=Heino M, Scott HS, Chen Q, ''et al.'' |title=Mutation analyses of North American APS-1 patients. |journal=Hum. Mutat. |volume=13 |issue= 1 |pages= 69-74 |year= 1999 |pmid= 9888391 |doi= 10.1002/(SICI)1098-1004(1999)13:1<69::AID-HUMU8>3.0.CO;2-6 }}
*{{cite journal | author=Björses P, Pelto-Huikko M, Kaukonen J, ''et al.'' |title=Localization of the APECED protein in distinct nuclear structures. |journal=Hum. Mol. Genet. |volume=8 |issue= 2 |pages= 259-66 |year= 1999 |pmid= 9931333 |doi= }}
*{{cite journal | author=Rinderle C, Christensen HM, Schweiger S, ''et al.'' |title=AIRE encodes a nuclear protein co-localizing with cytoskeletal filaments: altered sub-cellular distribution of mutants lacking the PHD zinc fingers. |journal=Hum. Mol. Genet. |volume=8 |issue= 2 |pages= 277-90 |year= 1999 |pmid= 9931335 |doi= }}
*{{cite journal | author=Björses P, Halonen M, Palvimo JJ, ''et al.'' |title=Mutations in the AIRE gene: effects on subcellular location and transactivation function of the autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy protein. |journal=Am. J. Hum. Genet. |volume=66 |issue= 2 |pages= 378-92 |year= 2000 |pmid= 10677297 |doi= }}
*{{cite journal | author=Pitkänen J, Doucas V, Sternsdorf T, ''et al.'' |title=The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16802-9 |year= 2000 |pmid= 10748110 |doi= 10.1074/jbc.M908944199 }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Pitkänen J, Vähämurto P, Krohn K, Peterson P |title=Subcellular localization of the autoimmune regulator protein. characterization of nuclear targeting and transcriptional activation domain. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19597-602 |year= 2001 |pmid= 11274163 |doi= 10.1074/jbc.M008322200 }}
*{{cite journal | author=Saugier-Veber P, Drouot N, Wolf LM, ''et al.'' |title=Identification of a novel mutation in the autoimmune regulator (AIRE-1) gene in a French family with autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy. |journal=Eur. J. Endocrinol. |volume=144 |issue= 4 |pages= 347-51 |year= 2001 |pmid= 11275943 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APBB1... {November 17, 2007 12:46:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:46:57 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_APBB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2e45.
| PDB = {{PDB2|2e45}}
| Name = Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)
| HGNCid = 581
| Symbol = APBB1
| AltSymbols =; FE65; MGC:9072; RIR
| OMIM = 602709
| ECnumber =
| Homologene = 898
| MGIid = 107765
| GeneAtlas_image1 = PBB_GE_APBB1_202652_at_tn.png
| Function = {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0035035 |text = histone acetyltransferase binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}} {{GNF_GO|id=GO:0030426 |text = growth cone}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007409 |text = axonogenesis}} {{GNF_GO|id=GO:0030048 |text = actin filament-based movement}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0045749 |text = negative regulation of S phase of mitotic cell cycle}} {{GNF_GO|id=GO:0050760 |text = negative regulation of thymidylate synthase biosynthetic process}} {{GNF_GO|id=GO:0050821 |text = protein stabilization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 322
| Hs_Ensembl = ENSG00000166313
| Hs_RefseqProtein = NP_001155
| Hs_RefseqmRNA = NM_001164
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 6372964
| Hs_GenLoc_end = 6389153
| Hs_Uniprot = O00213
| Mm_EntrezGene = 11785
| Mm_Ensembl = ENSMUSG00000037032
| Mm_RefseqmRNA = NM_009685
| Mm_RefseqProtein = NP_033815
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 105432305
| Mm_GenLoc_end = 105442536
| Mm_Uniprot = Q80Y77
}}
}}
'''Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)''', also known as '''APBB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=322| 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 Fe65 protein family. It is an adaptor protein localized in the nucleus. It interacts with the Alzheimer's disease amyloid precursor protein (APP), transcription factor CP2/LSF/LBP1 and the low-density lipoprotein receptor-related protein. APP functions as a cytosolic anchoring site that can prevent the gene product's nuclear translocation. This encoded protein could play an important role in the pathogenesis of Alzheimer's disease. It is thought to regulate transcription. Also it is observed to block cell cycle progression by downregulating thymidylate synthase expression. Multiple alternatively spliced transcript variants have been described for this gene but some of their full length sequence is not known.<ref name="entrez">{{cite web | title = Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=322| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Russo T, Faraonio R, Minopoli G, ''et al.'' |title=Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein. |journal=FEBS Lett. |volume=434 |issue= 1-2 |pages= 1-7 |year= 1998 |pmid= 9738440 |doi= }}
*{{cite journal | author=Askanas V, Engel WK |title=Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging. |journal=Current opinion in rheumatology |volume=15 |issue= 6 |pages= 737-44 |year= 2004 |pmid= 14569203 |doi= }}
*{{cite journal | author=Borg JP, Ooi J, Levy E, Margolis B |title=The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6229-41 |year= 1996 |pmid= 8887653 |doi= }}
*{{cite journal | author=Bressler SL, Gray MD, Sopher BL, ''et al.'' |title=cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1589-98 |year= 1997 |pmid= 8894693 |doi= }}
*{{cite journal | author=McLoughlin DM, Miller CC |title=The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system. |journal=FEBS Lett. |volume=397 |issue= 2-3 |pages= 197-200 |year= 1997 |pmid= 8955346 |doi= }}
*{{cite journal | author=Zambrano N, Buxbaum JD, Minopoli G, ''et al.'' |title=Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6399-405 |year= 1997 |pmid= 9045663 |doi= }}
*{{cite journal | author=Ermekova KS, Zambrano N, Linn H, ''et al.'' |title=The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 32869-77 |year= 1998 |pmid= 9407065 |doi= }}
*{{cite journal | author=Duilio A, Faraonio R, Minopoli G, ''et al.'' |title=Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. |journal=Biochem. J. |volume=330 ( Pt 1) |issue= |pages= 513-9 |year= 1998 |pmid= 9461550 |doi= }}
*{{cite journal | author=Blanco G, Irving NG, Brown SD, ''et al.'' |title=Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein. |journal=Mamm. Genome |volume=9 |issue= 6 |pages= 473-5 |year= 1998 |pmid= 9585438 |doi= }}
*{{cite journal | author=Zambrano N, Minopoli G, de Candia P, Russo T |title=The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1. |journal=J. Biol. Chem. |volume=273 |issue= 32 |pages= 20128-33 |year= 1998 |pmid= 9685356 |doi= }}
*{{cite journal | author=Hu Q, Kukull WA, Bressler SL, ''et al.'' |title=The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type. |journal=Hum. Genet. |volume=103 |issue= 3 |pages= 295-303 |year= 1998 |pmid= 9799084 |doi= }}
*{{cite journal | author=Trommsdorff M, Borg JP, Margolis B, Herz J |title=Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33556-60 |year= 1999 |pmid= 9837937 |doi= }}
*{{cite journal | author=Sabo SL, Lanier LM, Ikin AF, ''et al.'' |title=Regulation of beta-amyloid secretion by FE65, an amyloid protein precursor-binding protein. |journal=J. Biol. Chem. |volume=274 |issue= 12 |pages= 7952-7 |year= 1999 |pmid= 10075692 |doi= }}
*{{cite journal | author=Hu Q, Hearn MG, Jin LW, ''et al.'' |title=Alternatively spliced isoforms of FE65 serve as neuron-specific and non-neuronal markers. |journal=J. Neurosci. Res. |volume=58 |issue= 5 |pages= 632-40 |year= 2000 |pmid= 10561691 |doi= }}
*{{cite journal | author=Lambrechts A, Kwiatkowski AV, Lanier LM, ''et al.'' |title=cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36143-51 |year= 2000 |pmid= 10945997 |doi= 10.1074/jbc.M006274200 }}
*{{cite journal | author=Minopoli G, de Candia P, Bonetti A, ''et al.'' |title=The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6545-50 |year= 2001 |pmid= 11085987 |doi= 10.1074/jbc.M007340200 }}
*{{cite journal | author=Lau KF, McLoughlin DM, Standen CL, ''et al.'' |title=Fe65 and X11beta co-localize with and compete for binding to the amyloid precursor protein. |journal=Neuroreport |volume=11 |issue= 16 |pages= 3607-10 |year= 2001 |pmid= 11095528 |doi= }}
*{{cite journal | author=McLoughlin DM, Standen CL, Lau KF, ''et al.'' |title=The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9303-7 |year= 2001 |pmid= 11115513 |doi= 10.1074/jbc.M010023200 }}
*{{cite journal | author=Zambrano N, Bruni P, Minopoli G, ''et al.'' |title=The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene. |journal=J. Biol. Chem. |volume=276 |issue= 23 |pages= 19787-92 |year= 2001 |pmid= 11279131 |doi= 10.1074/jbc.M100792200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EFNB1... {November 17, 2007 12:47:31 PM PST}
- SEARCH REDIRECT: Control Box Found: EFNB1 {November 17, 2007 12:48:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:48:20 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:48:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:48:20 PM PST}
- UPDATED: Updated protein page:
EFNB1 {November 17, 2007 12:48:26 PM PST}
- INFO: Beginning work on EIF5A... {November 17, 2007 12:48:26 PM PST}
- SEARCH REDIRECT: Control Box Found: EIF5A {November 17, 2007 12:49:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:49:10 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:49:10 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:49:10 PM PST}
- UPDATED: Updated protein page:
EIF5A {November 17, 2007 12:49:19 PM PST}
- INFO: Beginning work on ERCC1... {November 17, 2007 12:49:19 PM PST}
- SEARCH REDIRECT: Control Box Found: ERCC1 {November 17, 2007 12:49:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:49:55 PM PST}
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- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:49:55 PM PST}
- UPDATED: Updated protein page:
ERCC1 {November 17, 2007 12:50:02 PM PST}
- INFO: Beginning work on FLI1... {November 17, 2007 12:50:02 PM PST}
- SEARCH REDIRECT: Control Box Found: FLI1 {November 17, 2007 12:50:31 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:50:32 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:50:32 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:50:32 PM PST}
- UPDATED: Updated protein page:
FLI1 {November 17, 2007 12:50:39 PM PST}
- INFO: Beginning work on FOLH1... {November 17, 2007 12:50:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:51:32 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_FOLH1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z8l.
| PDB = {{PDB2|1z8l}}, {{PDB2|2c6c}}, {{PDB2|2c6g}}, {{PDB2|2c6p}}, {{PDB2|2cij}}, {{PDB2|2jbj}}, {{PDB2|2jbk}}, {{PDB2|2oot}}, {{PDB2|2pvv}}, {{PDB2|2pvw}}
| Name = Folate hydrolase (prostate-specific membrane antigen) 1
| HGNCid = 3788
| Symbol = FOLH1
| AltSymbols =; PSM; FGCP; FOLH; GCP2; GCPII; NAALAD1; NAALAdase; PSMA; mGCP
| OMIM = 600934
| ECnumber =
| Homologene = 71658
| MGIid =
| GeneAtlas_image1 = PBB_GE_FOLH1_205860_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_FOLH1_211303_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_FOLH1_215363_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004180 |text = carboxypeptidase activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016805 |text = dipeptidase activity}} {{GNF_GO|id=GO:0043275 |text = glutamate carboxypeptidase II activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2346
| Hs_Ensembl = ENSG00000086205
| Hs_RefseqProtein = NP_001014986
| Hs_RefseqmRNA = NM_001014986
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 49124766
| Hs_GenLoc_end = 49186798
| Hs_Uniprot = Q04609
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Folate hydrolase (prostate-specific membrane antigen) 1''', also known as '''FOLH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FOLH1 folate hydrolase (prostate-specific membrane antigen) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2346| 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 type II transmembrane glycoprotein belonging to the M28 peptidase family. The protein acts as a glutamate carboxypeptidase on different alternative substrates, including the nutrient folate and the neuropeptide N-acetyl-l-aspartyl-l-glutamate and is expressed in a number of tissues such as prostate, central and peripheral nervous system and kidney. A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. In the prostate the protein is up-regulated in cancerous cells and is used as an effective diagnostic and prognostic indicator of prostate cancer. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: FOLH1 folate hydrolase (prostate-specific membrane antigen) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2346| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bander NH, Nanus DM, Milowsky MI, ''et al.'' |title=Targeted systemic therapy of prostate cancer with a monoclonal antibody to prostate-specific membrane antigen. |journal=Semin. Oncol. |volume=30 |issue= 5 |pages= 667-76 |year= 2003 |pmid= 14571414 |doi= }}
*{{cite journal | author=Rajasekaran AK, Anilkumar G, Christiansen JJ |title=Is prostate-specific membrane antigen a multifunctional protein? |journal=Am. J. Physiol., Cell Physiol. |volume=288 |issue= 5 |pages= C975-81 |year= 2005 |pmid= 15840561 |doi= 10.1152/ajpcell.00506.2004 }}
*{{cite journal | author=Israeli RS, Powell CT, Corr JG, ''et al.'' |title=Expression of the prostate-specific membrane antigen. |journal=Cancer Res. |volume=54 |issue= 7 |pages= 1807-11 |year= 1994 |pmid= 7511053 |doi= }}
*{{cite journal | author=Troyer JK, Beckett ML, Wright GL |title=Detection and characterization of the prostate-specific membrane antigen (PSMA) in tissue extracts and body fluids. |journal=Int. J. Cancer |volume=62 |issue= 5 |pages= 552-8 |year= 1995 |pmid= 7665226 |doi= }}
*{{cite journal | author=Su SL, Huang IP, Fair WR, ''et al.'' |title=Alternatively spliced variants of prostate-specific membrane antigen RNA: ratio of expression as a potential measurement of progression. |journal=Cancer Res. |volume=55 |issue= 7 |pages= 1441-3 |year= 1995 |pmid= 7882349 |doi= }}
*{{cite journal | author=Israeli RS, Powell CT, Fair WR, Heston WD |title=Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen. |journal=Cancer Res. |volume=53 |issue= 2 |pages= 227-30 |year= 1993 |pmid= 8417812 |doi= }}
*{{cite journal | author=Carter RE, Feldman AR, Coyle JT |title=Prostate-specific membrane antigen is a hydrolase with substrate and pharmacologic characteristics of a neuropeptidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 2 |pages= 749-53 |year= 1996 |pmid= 8570628 |doi= }}
*{{cite journal | author=Rinker-Schaeffer CW, Hawkins AL, Su SL, ''et al.'' |title=Localization and physical mapping of the prostate-specific membrane antigen (PSM) gene to human chromosome 11. |journal=Genomics |volume=30 |issue= 1 |pages= 105-8 |year= 1996 |pmid= 8595888 |doi= 10.1006/geno.1995.0019 }}
*{{cite journal | author=Rawlings ND, Barrett AJ |title=Structure of membrane glutamate carboxypeptidase. |journal=Biochim. Biophys. Acta |volume=1339 |issue= 2 |pages= 247-52 |year= 1997 |pmid= 9187245 |doi= }}
*{{cite journal | author=Bzdega T, Turi T, Wroblewska B, ''et al.'' |title=Molecular cloning of a peptidase against N-acetylaspartylglutamate from a rat hippocampal cDNA library. |journal=J. Neurochem. |volume=69 |issue= 6 |pages= 2270-7 |year= 1997 |pmid= 9375657 |doi= }}
*{{cite journal | author=Luthi-Carter R, Barczak AK, Speno H, Coyle JT |title=Hydrolysis of the neuropeptide N-acetylaspartylglutamate (NAAG) by cloned human glutamate carboxypeptidase II. |journal=Brain Res. |volume=795 |issue= 1-2 |pages= 341-8 |year= 1998 |pmid= 9622670 |doi= }}
*{{cite journal | author=Maraj BH, Leek JP, Karayi M, ''et al.'' |title=Detailed genetic mapping around a putative prostate-specific membrane antigen locus on human chromosome 11p11.2. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 1 |pages= 3-9 |year= 1998 |pmid= 9691167 |doi= }}
*{{cite journal | author=Luthi-Carter R, Barczak AK, Speno H, Coyle JT |title=Molecular characterization of human brain N-acetylated alpha-linked acidic dipeptidase (NAALADase). |journal=J. Pharmacol. Exp. Ther. |volume=286 |issue= 2 |pages= 1020-5 |year= 1998 |pmid= 9694964 |doi= }}
*{{cite journal | author=Grauer LS, Lawler KD, Marignac JL, ''et al.'' |title=Identification, purification, and subcellular localization of prostate-specific membrane antigen PSM' protein in the LNCaP prostatic carcinoma cell line. |journal=Cancer Res. |volume=58 |issue= 21 |pages= 4787-9 |year= 1998 |pmid= 9809977 |doi= }}
*{{cite journal | author=Pinto JT, Suffoletto BP, Berzin TM, ''et al.'' |title=Prostate-specific membrane antigen: a novel folate hydrolase in human prostatic carcinoma cells. |journal=Clin. Cancer Res. |volume=2 |issue= 9 |pages= 1445-51 |year= 1999 |pmid= 9816319 |doi= }}
*{{cite journal | author=O'Keefe DS, Su SL, Bacich DJ, ''et al.'' |title=Mapping, genomic organization and promoter analysis of the human prostate-specific membrane antigen gene. |journal=Biochim. Biophys. Acta |volume=1443 |issue= 1-2 |pages= 113-27 |year= 1999 |pmid= 9838072 |doi= }}
*{{cite journal | author=Speno HS, Luthi-Carter R, Macias WL, ''et al.'' |title=Site-directed mutagenesis of predicted active site residues in glutamate carboxypeptidase II. |journal=Mol. Pharmacol. |volume=55 |issue= 1 |pages= 179-85 |year= 1999 |pmid= 9882712 |doi= }}
*{{cite journal | author=Pangalos MN, Neefs JM, Somers M, ''et al.'' |title=Isolation and expression of novel human glutamate carboxypeptidases with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV activity. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8470-83 |year= 1999 |pmid= 10085079 |doi= }}
*{{cite journal | author=Devlin AM, Ling EH, Peerson JM, ''et al.'' |title=Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. |journal=Hum. Mol. Genet. |volume=9 |issue= 19 |pages= 2837-44 |year= 2001 |pmid= 11092759 |doi= }}
*{{cite journal | author=Lapidus RG, Tiffany CW, Isaacs JT, Slusher BS |title=Prostate-specific membrane antigen (PSMA) enzyme activity is elevated in prostate cancer cells. |journal=Prostate |volume=45 |issue= 4 |pages= 350-4 |year= 2000 |pmid= 11102961 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GPI... {November 17, 2007 12:51:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:52:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GPI_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dqr.
| PDB = {{PDB2|1dqr}}, {{PDB2|1g98}}, {{PDB2|1gzd}}, {{PDB2|1gzv}}, {{PDB2|1hm5}}, {{PDB2|1hox}}, {{PDB2|1iat}}, {{PDB2|1iri}}, {{PDB2|1jiq}}, {{PDB2|1jlh}}, {{PDB2|1koj}}, {{PDB2|1n8t}}, {{PDB2|1nuh}}, {{PDB2|1xtb}}
| Name = Glucose phosphate isomerase
| HGNCid = 4458
| Symbol = GPI
| AltSymbols =; PGI; AMF; GNPI; NLK; PHI; SA-36
| OMIM = 172400
| ECnumber =
| Homologene = 145
| MGIid = 95797
| GeneAtlas_image1 = PBB_GE_GPI_208308_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004347 |text = glucose-6-phosphate isomerase activity}} {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006094 |text = gluconeogenesis}} {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007599 |text = hemostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2821
| Hs_Ensembl = ENSG00000105220
| Hs_RefseqProtein = NP_000166
| Hs_RefseqmRNA = NM_000175
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 39547727
| Hs_GenLoc_end = 39583072
| Hs_Uniprot = P06744
| Mm_EntrezGene = 14751
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001004276
| Mm_RefseqProtein = XP_001004276
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Glucose phosphate isomerase''', also known as '''GPI''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GPI glucose phosphate isomerase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2821| 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 belongs to the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. The protein encoded by this gene is a dimeric enzyme that catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. The protein functions in different capacities inside and outside the cell. In the cytoplasm, the gene product is involved in glycolysis and gluconeogenesis, while outside the cell it functions as a neurotrophic factor for spinal and sensory neurons. Defects in this gene are the cause of nonspherocytic hemolytic anemia and a severe enzyme deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.<ref name="entrez">{{cite web | title = Entrez Gene: GPI glucose phosphate isomerase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2821| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kugler W, Lakomek M |title=Glucose-6-phosphate isomerase deficiency. |journal=Baillieres Best Pract. Res. Clin. Haematol. |volume=13 |issue= 1 |pages= 89-101 |year= 2000 |pmid= 10916680 |doi= }}
*{{cite journal | author=Walker JI, Faik P, Morgan MJ |title=Characterization of the 5' end of the gene for human glucose phosphate isomerase (GPI). |journal=Genomics |volume=7 |issue= 4 |pages= 638-43 |year= 1990 |pmid= 2387591 |doi= }}
*{{cite journal | author=Brownstein BH, Silverman GA, Little RD, ''et al.'' |title=Isolation of single-copy human genes from a library of yeast artificial chromosome clones. |journal=Science |volume=244 |issue= 4910 |pages= 1348-51 |year= 1989 |pmid= 2544027 |doi= }}
*{{cite journal | author=Mizrachi Y |title=Neurotrophic activity of monomeric glucophosphoisomerase was blocked by human immunodeficiency virus (HIV-1) and peptides from HIV-1 envelope glycoprotein. |journal=J. Neurosci. Res. |volume=23 |issue= 2 |pages= 217-24 |year= 1989 |pmid= 2547084 |doi= 10.1002/jnr.490230212 }}
*{{cite journal | author=Gurney ME, Apatoff BR, Spear GT, ''et al.'' |title=Neuroleukin: a lymphokine product of lectin-stimulated T cells. |journal=Science |volume=234 |issue= 4776 |pages= 574-81 |year= 1986 |pmid= 3020690 |doi= }}
*{{cite journal | author=Faik P, Walker JI, Redmill AA, Morgan MJ |title=Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3' sequences. |journal=Nature |volume=332 |issue= 6163 |pages= 455-7 |year= 1988 |pmid= 3352745 |doi= 10.1038/332455a0 }}
*{{cite journal | author=Zanella A, Izzo C, Rebulla P, ''et al.'' |title=The first stable variant of erythrocyte glucose-phosphate isomerase associated with severe hemolytic anemia. |journal=Am. J. Hematol. |volume=9 |issue= 1 |pages= 1-11 |year= 1981 |pmid= 7435496 |doi= }}
*{{cite journal | author=Faik P, Walker JI, Morgan MJ |title=Identification of a novel tandemly repeated sequence present in an intron of the glucose phosphate isomerase (GPI) gene in mouse and man. |journal=Genomics |volume=21 |issue= 1 |pages= 122-7 |year= 1994 |pmid= 7545951 |doi= 10.1006/geno.1994.1233 }}
*{{cite journal | author=Xu W, Beutler E |title=The characterization of gene mutations for human glucose phosphate isomerase deficiency associated with chronic hemolytic anemia. |journal=J. Clin. Invest. |volume=94 |issue= 6 |pages= 2326-9 |year= 1995 |pmid= 7989588 |doi= }}
*{{cite journal | author=Walker JI, Layton DM, Bellingham AJ, ''et al.'' |title=DNA sequence abnormalities in human glucose 6-phosphate isomerase deficiency. |journal=Hum. Mol. Genet. |volume=2 |issue= 3 |pages= 327-9 |year= 1993 |pmid= 8499925 |doi= }}
*{{cite journal | author=Xu W, Lee P, Beutler E |title=Human glucose phosphate isomerase: exon mapping and gene structure. |journal=Genomics |volume=29 |issue= 3 |pages= 732-9 |year= 1996 |pmid= 8575767 |doi= 10.1006/geno.1995.9944 }}
*{{cite journal | author=Baronciani L, Zanella A, Bianchi P, ''et al.'' |title=Study of the molecular defects in glucose phosphate isomerase-deficient patients affected by chronic hemolytic anemia. |journal=Blood |volume=88 |issue= 6 |pages= 2306-10 |year= 1996 |pmid= 8822952 |doi= }}
*{{cite journal | author=Kanno H, Fujii H, Hirono A, ''et al.'' |title=Molecular analysis of glucose phosphate isomerase deficiency associated with hereditary hemolytic anemia. |journal=Blood |volume=88 |issue= 6 |pages= 2321-5 |year= 1996 |pmid= 8822954 |doi= }}
*{{cite journal | author=Beutler E, West C, Britton HA, ''et al.'' |title=Glucosephosphate isomerase (GPI) deficiency mutations associated with hereditary nonspherocytic hemolytic anemia (HNSHA). |journal=Blood Cells Mol. Dis. |volume=23 |issue= 3 |pages= 402-9 |year= 1998 |pmid= 9446754 |doi= 10.1006/bcmd.1997.0157 }}
*{{cite journal | author=Kanno H, Fujii H, Miwa S |title=Expression and enzymatic characterization of human glucose phosphate isomerase (GPI) variants accounting for GPI deficiency. |journal=Blood Cells Mol. Dis. |volume=24 |issue= 1 |pages= 54-61 |year= 1998 |pmid= 9616041 |doi= 10.1006/bcmd.1998.0170 }}
*{{cite journal | author=Kugler W, Breme K, Laspe P, ''et al.'' |title=Molecular basis of neurological dysfunction coupled with haemolytic anaemia in human glucose-6-phosphate isomerase (GPI) deficiency. |journal=Hum. Genet. |volume=103 |issue= 4 |pages= 450-4 |year= 1998 |pmid= 9856489 |doi= }}
*{{cite journal | author=Belyaeva OV, Balanovsky OP, Ashworth LK, ''et al.'' |title=Fine mapping of a polymorphic CA repeat marker on human chromosome 19 and its use in population studies. |journal=Gene |volume=230 |issue= 2 |pages= 259-66 |year= 1999 |pmid= 10216265 |doi= }}
*{{cite journal | author=Yakirevich E, Naot Y |title=Cloning of a glucose phosphate isomerase/neuroleukin-like sperm antigen involved in sperm agglutination. |journal=Biol. Reprod. |volume=62 |issue= 4 |pages= 1016-23 |year= 2000 |pmid= 10727272 |doi= }}
*{{cite journal | author=Haga A, Niinaka Y, Raz A |title=Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein. |journal=Biochim. Biophys. Acta |volume=1480 |issue= 1-2 |pages= 235-44 |year= 2000 |pmid= 11004567 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRIA1... {November 17, 2007 12:52:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:52:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| 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 = Glutamate receptor, ionotropic, AMPA 1
| HGNCid = 4571
| Symbol = GRIA1
| AltSymbols =; GLUH1; GLUR1; GLURA; HBGR1; MGC133252
| OMIM = 138248
| ECnumber =
| Homologene = 20226
| MGIid = 95808
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004971 |text = alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005234 |text = extracellular-glutamate-gated ion channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015277 |text = kainate selective glutamate receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0014069 |text = postsynaptic density}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007616 |text = long-term memory}} {{GNF_GO|id=GO:0031623 |text = receptor internalization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2890
| Hs_Ensembl = ENSG00000155511
| Hs_RefseqProtein = NP_000818
| Hs_RefseqmRNA = NM_000827
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 152850499
| Hs_GenLoc_end = 153171354
| Hs_Uniprot = P42261
| Mm_EntrezGene = 14799
| Mm_Ensembl = ENSMUSG00000020524
| Mm_RefseqmRNA = NM_008165
| Mm_RefseqProtein = NP_032191
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 57017321
| Mm_GenLoc_end = 57143990
| Mm_Uniprot = Q5NBY0
}}
}}
'''Glutamate receptor, ionotropic, AMPA 1''', also known as '''GRIA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRIA1 glutamate receptor, ionotropic, AMPA 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2890| 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 = Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. The GRIA1 belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Each of the members (GRIA1-4) include flip and flop isoforms generated by alternative RNA splicing. The receptor subunits encoded by each isoform vary in their signal transduction properties. The isoform presented here is the flop isoform. In situ hybridization experiments showed that human GRIA1 mRNA is present in granule and pyramidal cells in the hippocampal formation.<ref name="entrez">{{cite web | title = Entrez Gene: GRIA1 glutamate receptor, ionotropic, AMPA 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2890| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sun W, Ferrer-Montiel AV, Schinder AF, ''et al.'' |title=Molecular cloning, chromosomal mapping, and functional expression of human brain glutamate receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 4 |pages= 1443-7 |year= 1992 |pmid= 1311100 |doi= }}
*{{cite journal | author=McNamara JO, Eubanks JH, McPherson JD, ''et al.'' |title=Chromosomal localization of human glutamate receptor genes. |journal=J. Neurosci. |volume=12 |issue= 7 |pages= 2555-62 |year= 1992 |pmid= 1319477 |doi= }}
*{{cite journal | author=Potier MC, Spillantini MG, Carter NP |title=The human glutamate receptor cDNA GluR1: cloning, sequencing, expression and localization to chromosome 5. |journal=DNA Seq. |volume=2 |issue= 4 |pages= 211-8 |year= 1992 |pmid= 1320959 |doi= }}
*{{cite journal | author=Puckett C, Gomez CM, Korenberg JR, ''et al.'' |title=Molecular cloning and chromosomal localization of one of the human glutamate receptor genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7557-61 |year= 1991 |pmid= 1652753 |doi= }}
*{{cite journal | author=Yakel JL, Vissavajjhala P, Derkach VA, ''et al.'' |title=Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 5 |pages= 1376-80 |year= 1995 |pmid= 7877986 |doi= }}
*{{cite journal | author=Eastwood SL, Burnet PW, Beckwith J, ''et al.'' |title=AMPA glutamate receptors and their flip and flop mRNAs in human hippocampus. |journal=Neuroreport |volume=5 |issue= 11 |pages= 1325-8 |year= 1994 |pmid= 7919190 |doi= }}
*{{cite journal | author=Roche KW, Raymond LA, Blackstone C, Huganir RL |title=Transmembrane topology of the glutamate receptor subunit GluR6. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11679-82 |year= 1994 |pmid= 8163463 |doi= }}
*{{cite journal | author=McLaughlin DP, Cheetham ME, Kerwin RW |title=Expression of alternatively-spliced glutamate receptors in human hippocampus. |journal=Eur. J. Pharmacol. |volume=244 |issue= 1 |pages= 89-92 |year= 1993 |pmid= 8420792 |doi= }}
*{{cite journal | author=Roche KW, O'Brien RJ, Mammen AL, ''et al.'' |title=Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. |journal=Neuron |volume=16 |issue= 6 |pages= 1179-88 |year= 1996 |pmid= 8663994 |doi= }}
*{{cite journal | author=Brakeman PR, Lanahan AA, O'Brien R, ''et al.'' |title=Homer: a protein that selectively binds metabotropic glutamate receptors. |journal=Nature |volume=386 |issue= 6622 |pages= 284-8 |year= 1997 |pmid= 9069287 |doi= 10.1038/386284a0 }}
*{{cite journal | author=Barria A, Derkach V, Soderling T |title=Identification of the Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 32727-30 |year= 1998 |pmid= 9407043 |doi= }}
*{{cite journal | author=Ripellino JA, Neve RL, Howe JR |title=Expression and heteromeric interactions of non-N-methyl-D-aspartate glutamate receptor subunits in the developing and adult cerebellum. |journal=Neuroscience |volume=82 |issue= 2 |pages= 485-97 |year= 1998 |pmid= 9466455 |doi= }}
*{{cite journal | author=Leonard AS, Davare MA, Horne MC, ''et al.'' |title=SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. |journal=J. Biol. Chem. |volume=273 |issue= 31 |pages= 19518-24 |year= 1998 |pmid= 9677374 |doi= }}
*{{cite journal | author=Xiao B, Tu JC, Petralia RS, ''et al.'' |title=Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins. |journal=Neuron |volume=21 |issue= 4 |pages= 707-16 |year= 1998 |pmid= 9808458 |doi= }}
*{{cite journal | author=Montague AA, Greer CA |title=Differential distribution of ionotropic glutamate receptor subunits in the rat olfactory bulb. |journal=J. Comp. Neurol. |volume=405 |issue= 2 |pages= 233-46 |year= 1999 |pmid= 10023812 |doi= }}
*{{cite journal | author=Leuschner WD, Hoch W |title=Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16907-16 |year= 1999 |pmid= 10358037 |doi= }}
*{{cite journal | author=Shi SH, Hayashi Y, Petralia RS, ''et al.'' |title=Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation. |journal=Science |volume=284 |issue= 5421 |pages= 1811-6 |year= 1999 |pmid= 10364548 |doi= }}
*{{cite journal | author=Rubio ME, Wenthold RJ |title=Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors. |journal=J. Neurochem. |volume=73 |issue= 3 |pages= 942-8 |year= 1999 |pmid= 10461883 |doi= }}
*{{cite journal | author=Mahlknecht U, Bucala R, Hoelzer D, Verdin E |title=High resolution physical mapping of human HDAC3, a potential tumor suppressor gene in the 5q31 region. |journal=Cytogenet. Cell Genet. |volume=86 |issue= 3-4 |pages= 237-9 |year= 2000 |pmid= 10575214 |doi= }}
*{{cite journal | author=Stinehelfer S, Vruwink M, Burette A |title=Immunolocalization of mGluR1alpha in specific populations of local circuit neurons in the cerebral cortex. |journal=Brain Res. |volume=861 |issue= 1 |pages= 37-44 |year= 2000 |pmid= 10751563 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GTF2I... {November 17, 2007 12:52:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:53:20 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_GTF2I_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1q60.
| PDB = {{PDB2|1q60}}, {{PDB2|2d9b}}, {{PDB2|2dn4}}
| Name = General transcription factor II, i
| HGNCid = 4659
| Symbol = GTF2I
| AltSymbols =; WBS; BAP-135; BAP135; BTKAP1; DIWS; IB291; SPIN; TFII-I; WBSCR6
| OMIM = 601679
| ECnumber =
| Homologene = 7748
| MGIid = 1202722
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2969
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001130609
| Hs_RefseqmRNA = XM_001130609
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 14886
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_903569
| Mm_RefseqProtein = XP_908662
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''General transcription factor II, i''', also known as '''GTF2I''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2I general transcription factor II, i| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2969| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a multifunctional phosphoprotein with roles in transcription and signal transduction. It is deleted in Williams-Beuren syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at chromosome 7q11.23. The exon(s) encoding 5' UTR has not been fully defined, but this gene is known to contain at least 34 exons, and its alternative splicing generates 4 transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: GTF2I general transcription factor II, i| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2969| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Roy AL, Meisterernst M, Pognonec P, Roeder RG |title=Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF. |journal=Nature |volume=354 |issue= 6350 |pages= 245-8 |year= 1992 |pmid= 1961251 |doi= 10.1038/354245a0 }}
*{{cite journal | author=Roy AL, Carruthers C, Gutjahr T, Roeder RG |title=Direct role for Myc in transcription initiation mediated by interactions with TFII-I. |journal=Nature |volume=365 |issue= 6444 |pages= 359-61 |year= 1993 |pmid= 8377829 |doi= 10.1038/365359a0 }}
*{{cite journal | author=Yang W, Desiderio S |title=BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 2 |pages= 604-9 |year= 1997 |pmid= 9012831 |doi= }}
*{{cite journal | author=Grueneberg DA, Henry RW, Brauer A, ''et al.'' |title=A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I. |journal=Genes Dev. |volume=11 |issue= 19 |pages= 2482-93 |year= 1997 |pmid= 9334314 |doi= }}
*{{cite journal | author=Roy AL, Du H, Gregor PD, ''et al.'' |title=Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1. |journal=EMBO J. |volume=16 |issue= 23 |pages= 7091-104 |year= 1998 |pmid= 9384587 |doi= 10.1093/emboj/16.23.7091 }}
*{{cite journal | author=Pérez Jurado LA, Wang YK, Peoples R, ''et al.'' |title=A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK. |journal=Hum. Mol. Genet. |volume=7 |issue= 3 |pages= 325-34 |year= 1998 |pmid= 9466987 |doi= }}
*{{cite journal | author=Kim DW, Cheriyath V, Roy AL, Cochran BH |title=TFII-I enhances activation of the c-fos promoter through interactions with upstream elements. |journal=Mol. Cell. Biol. |volume=18 |issue= 6 |pages= 3310-20 |year= 1998 |pmid= 9584171 |doi= }}
*{{cite journal | author=Cheriyath V, Novina CD, Roy AL |title=TFII-I regulates Vbeta promoter activity through an initiator element. |journal=Mol. Cell. Biol. |volume=18 |issue= 8 |pages= 4444-54 |year= 1998 |pmid= 9671454 |doi= }}
*{{cite journal | author=Novina CD, Cheriyath V, Roy AL |title=Regulation of TFII-I activity by phosphorylation. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33443-8 |year= 1999 |pmid= 9837922 |doi= }}
*{{cite journal | author=Novina CD, Kumar S, Bajpai U, ''et al.'' |title=Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase. |journal=Mol. Cell. Biol. |volume=19 |issue= 7 |pages= 5014-24 |year= 1999 |pmid= 10373551 |doi= }}
*{{cite journal | author=Kim DW, Cochran BH |title=Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter. |journal=Mol. Cell. Biol. |volume=20 |issue= 4 |pages= 1140-8 |year= 2000 |pmid= 10648599 |doi= }}
*{{cite journal | author=Cheriyath V, Roy AL |title=Alternatively spliced isoforms of TFII-I. Complex formation, nuclear translocation, and differential gene regulation. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26300-8 |year= 2000 |pmid= 10854432 |doi= 10.1074/jbc.M002980200 }}
*{{cite journal | author=Parker R, Phan T, Baumeister P, ''et al.'' |title=Identification of TFII-I as the endoplasmic reticulum stress response element binding factor ERSF: its autoregulation by stress and interaction with ATF6. |journal=Mol. Cell. Biol. |volume=21 |issue= 9 |pages= 3220-33 |year= 2001 |pmid= 11287625 |doi= 10.1128/MCB.21.9.3220-3233.2001 }}
*{{cite journal | author=Kim DW, Cochran BH |title=JAK2 activates TFII-I and regulates its interaction with extracellular signal-regulated kinase. |journal=Mol. Cell. Biol. |volume=21 |issue= 10 |pages= 3387-97 |year= 2001 |pmid= 11313464 |doi= 10.1128/MCB.21.10.3387-3397.2000 }}
*{{cite journal | author=Egloff AM, Desiderio S |title=Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 27806-15 |year= 2001 |pmid= 11373296 |doi= 10.1074/jbc.M103692200 }}
*{{cite journal | author=Cheriyath V, Desgranges ZP, Roy AL |title=c-Src-dependent transcriptional activation of TFII-I. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22798-805 |year= 2002 |pmid= 11934902 |doi= 10.1074/jbc.M202956200 }}
*{{cite journal | author=Casteel DE, Zhuang S, Gudi T, ''et al.'' |title=cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 32003-14 |year= 2002 |pmid= 12082086 |doi= 10.1074/jbc.M112332200 }}
*{{cite journal | author=Tussie-Luna MI, Michel B, Hakre S, Roy AL |title=The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta /Siz2 is a transcriptional cofactor for TFII-I. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 43185-93 |year= 2003 |pmid= 12193603 |doi= 10.1074/jbc.M207635200 }}
*{{cite journal | author=Tussié-Luna MI, Bayarsaihan D, Seto E, ''et al.'' |title=Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 20 |pages= 12807-12 |year= 2002 |pmid= 12239342 |doi= 10.1073/pnas.192464499 }}
*{{cite journal | author=Wen YD, Cress WD, Roy AL, Seto E |title=Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I. |journal=J. Biol. Chem. |volume=278 |issue= 3 |pages= 1841-7 |year= 2003 |pmid= 12393887 |doi= 10.1074/jbc.M206528200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GYPA... {November 17, 2007 12:53:20 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:54:17 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_GYPA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1afo.
| PDB = {{PDB2|1afo}}
| Name = Glycophorin A (MNS blood group)
| HGNCid = 4702
| Symbol = GYPA
| AltSymbols =; MN; MNS; CD235a; GPA; GPErik; GPSAT; GpMiIII; HGpMiIII; HGpMiV; HGpMiX; HGpMiXI; HGpSta(C)
| OMIM = 111300
| ECnumber =
| Homologene = 48076
| MGIid =
| GeneAtlas_image1 = PBB_GE_GYPA_205837_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GYPA_205838_at_tn.png
| GeneAtlas_image3 = PBB_GE_GYPA_211820_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2993
| Hs_Ensembl = ENSG00000170180
| Hs_RefseqProtein = NP_002090
| Hs_RefseqmRNA = NM_002099
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 145249906
| Hs_GenLoc_end = 145281294
| Hs_Uniprot = P02724
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Glycophorin A (MNS blood group)''', also known as '''GYPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GYPA glycophorin A (MNS blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2993| 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 = Glycophorins A (GYPA) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. GYPA gene consists of 7 exons and has 97% sequence homology with GYPB from the 5' UTR to the coding sequence encoding the first 45 amino acids. In addition to the M or N and S or s antigens, that commonly occur in all populations, about 40 related variant phenotypes have been identified. These variants include all the variants of the Miltenberger complex and several isoforms of Sta; also, Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. Most of the variants are the result of gene recombinations between GYPA and GYPB.<ref name="entrez">{{cite web | title = Entrez Gene: GYPA glycophorin A (MNS blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2993| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Blumenfeld OO, Huang CH |title=Molecular genetics of the glycophorin gene family, the antigens for MNSs blood groups: multiple gene rearrangements and modulation of splice site usage result in extensive diversification. |journal=Hum. Mutat. |volume=6 |issue= 3 |pages= 199-209 |year= 1996 |pmid= 8535438 |doi= 10.1002/humu.1380060302 }}
*{{cite journal | author=Blumenfeld OO, Huang CH |title=Molecular genetics of glycophorin MNS variants. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=4 |issue= 4 |pages= 357-65 |year= 1997 |pmid= 9269716 |doi= }}
*{{cite journal | author=Johnson ST, McFarland JG, Kelly KJ, ''et al.'' |title=Transfusion support with RBCs from an Mk homozygote in a case of autoimmune hemolytic anemia following diphtheria-pertussis-tetanus vaccination. |journal=Transfusion |volume=42 |issue= 5 |pages= 567-71 |year= 2002 |pmid= 12084164 |doi= }}
*{{cite journal | author=Tomita M, Marchesi VT |title=Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=72 |issue= 8 |pages= 2964-8 |year= 1976 |pmid= 1059087 |doi= }}
*{{cite journal | author=Lemmon MA, Flanagan JM, Hunt JF, ''et al.'' |title=Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7683-9 |year= 1992 |pmid= 1560003 |doi= }}
*{{cite journal | author=Huang CH, Spruell P, Moulds JJ, Blumenfeld OO |title=Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype. |journal=Blood |volume=80 |issue= 1 |pages= 257-63 |year= 1992 |pmid= 1611092 |doi= }}
*{{cite journal | author=Huang CH, Kikuchi M, McCreary J, Blumenfeld OO |title=Gene conversion confined to a direct repeat of the acceptor splice site generates allelic diversity at human glycophorin (GYP) locus. |journal=J. Biol. Chem. |volume=267 |issue= 5 |pages= 3336-42 |year= 1992 |pmid= 1737789 |doi= }}
*{{cite journal | author=Barton P, Collins A, Hoogenraad N |title=A variant of glycophorin A resulting from the deletion of exon 4. |journal=Biochim. Biophys. Acta |volume=1090 |issue= 2 |pages= 265-6 |year= 1991 |pmid= 1932122 |doi= }}
*{{cite journal | author=Huang CH, Blumenfeld OO |title=Identification of recombination events resulting in three hybrid genes encoding human MiV, MiV(J.L.), and Sta glycophorins. |journal=Blood |volume=77 |issue= 8 |pages= 1813-20 |year= 1991 |pmid= 2015404 |doi= }}
*{{cite journal | author=Huang CH, Blumenfeld OO |title=Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use of a pseudoexon in construction of two delta-alpha-delta hybrid genes resulting in antigenic diversification. |journal=J. Biol. Chem. |volume=266 |issue= 11 |pages= 7248-55 |year= 1991 |pmid= 2016325 |doi= }}
*{{cite journal | author=Hamid J, Burness AT |title=The mechanism of production of multiple mRNAs for human glycophorin A. |journal=Nucleic Acids Res. |volume=18 |issue= 19 |pages= 5829-36 |year= 1990 |pmid= 2216775 |doi= }}
*{{cite journal | author=Dill K, Hu SH, Berman E, ''et al.'' |title=One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla. |journal=J. Protein Chem. |volume=9 |issue= 2 |pages= 129-36 |year= 1990 |pmid= 2386609 |doi= }}
*{{cite journal | author=Kudo S, Fukuda M |title=Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 12 |pages= 4619-23 |year= 1989 |pmid= 2734312 |doi= }}
*{{cite journal | author=Matsui Y, Natori S, Obinata M |title=Isolation of the cDNA clone for mouse glycophorin, erythroid-specific membrane protein. |journal=Gene |volume=77 |issue= 2 |pages= 325-32 |year= 1989 |pmid= 2753361 |doi= }}
*{{cite journal | author=Vignal A, Rahuel C, el Maliki B, ''et al.'' |title=Molecular analysis of glycophorin A and B gene structure and expression in homozygous Miltenberger class V (Mi. V) human erythrocytes. |journal=Eur. J. Biochem. |volume=184 |issue= 2 |pages= 337-44 |year= 1989 |pmid= 2792104 |doi= }}
*{{cite journal | author=Tate CG, Tanner MJ |title=Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta. |journal=Biochem. J. |volume=254 |issue= 3 |pages= 743-50 |year= 1988 |pmid= 3196288 |doi= }}
*{{cite journal | author=Huang CH, Puglia KV, Bigbee WL, ''et al.'' |title=A family study of multiple mutations of alpha and delta glycophorins (glycophorins A and B). |journal=Hum. Genet. |volume=81 |issue= 1 |pages= 26-30 |year= 1989 |pmid= 3198123 |doi= }}
*{{cite journal | author=Rahuel C, London J, d'Auriol L, ''et al.'' |title=Characterization of cDNA clones for human glycophorin A. Use for gene localization and for analysis of normal of glycophorin-A-deficient (Finnish type) genomic DNA. |journal=Eur. J. Biochem. |volume=172 |issue= 1 |pages= 147-53 |year= 1988 |pmid= 3345758 |doi= }}
*{{cite journal | author=Siebert PD, Fukuda M |title=Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 6 |pages= 1665-9 |year= 1986 |pmid= 3456608 |doi= }}
*{{cite journal | author=Siebert PD, Fukuda M |title=Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and genomic relationship to glycophorin A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 19 |pages= 6735-9 |year= 1987 |pmid= 3477806 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL17A... {November 17, 2007 12:54:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:55:01 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Interleukin 17A
| HGNCid = 5981
| Symbol = IL17A
| AltSymbols =; CTLA8; IL-17; IL-17A; IL17
| OMIM = 603149
| ECnumber =
| Homologene = 1651
| MGIid = 107364
| GeneAtlas_image1 = PBB_GE_IL17A_208402_at_tn.png
| GeneAtlas_image2 = PBB_GE_IL17A_216876_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008219 |text = cell death}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3605
| Hs_Ensembl = ENSG00000112115
| Hs_RefseqProtein = NP_002181
| Hs_RefseqmRNA = NM_002190
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 52159144
| Hs_GenLoc_end = 52163395
| Hs_Uniprot = Q16552
| Mm_EntrezGene = 16171
| Mm_Ensembl = ENSMUSG00000025929
| Mm_RefseqmRNA = NM_010552
| Mm_RefseqProtein = NP_034682
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 20716056
| Mm_GenLoc_end = 20719647
| Mm_Uniprot = Q544E6
}}
}}
'''Interleukin 17A''', also known as '''IL17A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL17A interleukin 17A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3605| 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 proinflammatory cytokine produced by activated T cells. This cytokine regulates the activities of NF-kappaB and mitogen-activated protein kinases. This cytokine can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of this cytokine are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.<ref name="entrez">{{cite web | title = Entrez Gene: IL17A interleukin 17A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3605| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gaffen SL |title=Biology of recently discovered cytokines: interleukin-17--a unique inflammatory cytokine with roles in bone biology and arthritis. |journal=Arthritis Res. Ther. |volume=6 |issue= 6 |pages= 240-7 |year= 2005 |pmid= 15535837 |doi= 10.1186/ar1444 }}
*{{cite journal | author=Lubberts E, Koenders MI, van den Berg WB |title=The role of T-cell interleukin-17 in conducting destructive arthritis: lessons from animal models. |journal=Arthritis Res. Ther. |volume=7 |issue= 1 |pages= 29-37 |year= 2006 |pmid= 15642151 |doi= 10.1186/ar1478 }}
*{{cite journal | author=Yao Z, Painter SL, Fanslow WC, ''et al.'' |title=Human IL-17: a novel cytokine derived from T cells. |journal=J. Immunol. |volume=155 |issue= 12 |pages= 5483-6 |year= 1996 |pmid= 7499828 |doi= }}
*{{cite journal | author=Rouvier E, Luciani MF, Mattéi MG, ''et al.'' |title=CTLA-8, cloned from an activated T cell, bearing AU-rich messenger RNA instability sequences, and homologous to a herpesvirus saimiri gene. |journal=J. Immunol. |volume=150 |issue= 12 |pages= 5445-56 |year= 1993 |pmid= 8390535 |doi= }}
*{{cite journal | author=Fossiez F, Djossou O, Chomarat P, ''et al.'' |title=T cell interleukin-17 induces stromal cells to produce proinflammatory and hematopoietic cytokines. |journal=J. Exp. Med. |volume=183 |issue= 6 |pages= 2593-603 |year= 1996 |pmid= 8676080 |doi= }}
*{{cite journal | author=Yao Z, Spriggs MK, Derry JM, ''et al.'' |title=Molecular characterization of the human interleukin (IL)-17 receptor. |journal=Cytokine |volume=9 |issue= 11 |pages= 794-800 |year= 1998 |pmid= 9367539 |doi= }}
*{{cite journal | author=Murphy KP, Gagne P, Pazmany C, Moody MD |title=Expression of human interleukin-17 in Pichia pastoris: purification and characterization. |journal=Protein Expr. Purif. |volume=12 |issue= 2 |pages= 208-14 |year= 1998 |pmid= 9518462 |doi= 10.1006/prep.1997.0832 }}
*{{cite journal | author=Teunissen MB, Koomen CW, de Waal Malefyt R, ''et al.'' |title=Interleukin-17 and interferon-gamma synergize in the enhancement of proinflammatory cytokine production by human keratinocytes. |journal=J. Invest. Dermatol. |volume=111 |issue= 4 |pages= 645-9 |year= 1998 |pmid= 9764847 |doi= 10.1046/j.1523-1747.1998.00347.x }}
*{{cite journal | author=Shalom-Barak T, Quach J, Lotz M |title=Interleukin-17-induced gene expression in articular chondrocytes is associated with activation of mitogen-activated protein kinases and NF-kappaB. |journal=J. Biol. Chem. |volume=273 |issue= 42 |pages= 27467-73 |year= 1998 |pmid= 9765276 |doi= }}
*{{cite journal | author=Shin HC, Benbernou N, Fekkar H, ''et al.'' |title=Regulation of IL-17, IFN-gamma and IL-10 in human CD8(+) T cells by cyclic AMP-dependent signal transduction pathway. |journal=Cytokine |volume=10 |issue= 11 |pages= 841-50 |year= 1999 |pmid= 9878122 |doi= 10.1006/cyto.1998.0375 }}
*{{cite journal | author=Laan M, Cui ZH, Hoshino H, ''et al.'' |title=Neutrophil recruitment by human IL-17 via C-X-C chemokine release in the airways. |journal=J. Immunol. |volume=162 |issue= 4 |pages= 2347-52 |year= 1999 |pmid= 9973514 |doi= }}
*{{cite journal | author=Kotake S, Udagawa N, Takahashi N, ''et al.'' |title=IL-17 in synovial fluids from patients with rheumatoid arthritis is a potent stimulator of osteoclastogenesis. |journal=J. Clin. Invest. |volume=103 |issue= 9 |pages= 1345-52 |year= 1999 |pmid= 10225978 |doi= }}
*{{cite journal | author=Shin HC, Benbernou N, Esnault S, Guenounou M |title=Expression of IL-17 in human memory CD45RO+ T lymphocytes and its regulation by protein kinase A pathway. |journal=Cytokine |volume=11 |issue= 4 |pages= 257-66 |year= 1999 |pmid= 10328864 |doi= 10.1006/cyto.1998.0433 }}
*{{cite journal | author=Andoh A, Takaya H, Makino J, ''et al.'' |title=Cooperation of interleukin-17 and interferon-gamma on chemokine secretion in human fetal intestinal epithelial cells. |journal=Clin. Exp. Immunol. |volume=125 |issue= 1 |pages= 56-63 |year= 2001 |pmid= 11472426 |doi= }}
*{{cite journal | author=Laan M, Palmberg L, Larsson K, Lindén A |title=Free, soluble interleukin-17 protein during severe inflammation in human airways. |journal=Eur. Respir. J. |volume=19 |issue= 3 |pages= 534-7 |year= 2002 |pmid= 11936535 |doi= }}
*{{cite journal | author=Andoh A, Fujino S, Bamba S, ''et al.'' |title=IL-17 selectively down-regulates TNF-alpha-induced RANTES gene expression in human colonic subepithelial myofibroblasts. |journal=J. Immunol. |volume=169 |issue= 4 |pages= 1683-7 |year= 2002 |pmid= 12165487 |doi= }}
*{{cite journal | author=Andoh A, Shimada M, Bamba S, ''et al.'' |title=Extracellular signal-regulated kinases 1 and 2 participate in interleukin-17 plus tumor necrosis factor-alpha-induced stabilization of interleukin-6 mRNA in human pancreatic myofibroblasts. |journal=Biochim. Biophys. Acta |volume=1591 |issue= 1-3 |pages= 69-74 |year= 2002 |pmid= 12183057 |doi= }}
*{{cite journal | author=Hsieh HG, Loong CC, Lin CY |title=Interleukin-17 induces src/MAPK cascades activation in human renal epithelial cells. |journal=Cytokine |volume=19 |issue= 4 |pages= 159-74 |year= 2003 |pmid= 12297109 |doi= }}
*{{cite journal | author=Aggarwal S, Ghilardi N, Xie MH, ''et al.'' |title=Interleukin-23 promotes a distinct CD4 T cell activation state characterized by the production of interleukin-17. |journal=J. Biol. Chem. |volume=278 |issue= 3 |pages= 1910-4 |year= 2003 |pmid= 12417590 |doi= 10.1074/jbc.M207577200 }}
*{{cite journal | author=Maertzdorf J, Osterhaus AD, Verjans GM |title=IL-17 expression in human herpetic stromal keratitis: modulatory effects on chemokine production by corneal fibroblasts. |journal=J. Immunol. |volume=169 |issue= 10 |pages= 5897-903 |year= 2003 |pmid= 12421973 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ING1... {November 17, 2007 12:55:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:55:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Inhibitor of growth family, member 1
| HGNCid = 6062
| Symbol = ING1
| AltSymbols =; p24ING1c; p33; p33ING1; p33ING1b; p47; p47ING1a
| OMIM = 601566
| ECnumber =
| Homologene = 40119
| MGIid = 1349481
| GeneAtlas_image1 = PBB_GE_ING1_209808_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_ING1_208415_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ING1_210350_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3621
| Hs_Ensembl = ENSG00000153487
| Hs_RefseqProtein = NP_005528
| Hs_RefseqmRNA = NM_005537
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 110163084
| Hs_GenLoc_end = 110171422
| Hs_Uniprot = Q9UK53
| Mm_EntrezGene = 26356
| Mm_Ensembl = ENSMUSG00000045969
| Mm_RefseqmRNA = XM_976418
| Mm_RefseqProtein = XP_981512
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 11556038
| Mm_GenLoc_end = 11563222
| Mm_Uniprot = Q3ULE3
}}
}}
'''Inhibitor of growth family, member 1''', also known as '''ING1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ING1 inhibitor of growth family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3621| 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 tumor suppressor protein that can induce cell growth arrest and apoptosis. The encoded protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. Reduced expression and rearrangement of this gene have been detected in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: ING1 inhibitor of growth family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3621| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Campos EI, Chin MY, Kuo WH, Li G |title=Biological functions of the ING family tumor suppressors. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 19-20 |pages= 2597-613 |year= 2004 |pmid= 15526165 |doi= 10.1007/s00018-004-4199-4 }}
*{{cite journal | author=Garkavtsev I, Kazarov A, Gudkov A, Riabowol K |title=Suppression of the novel growth inhibitor p33ING1 promotes neoplastic transformation. |journal=Nat. Genet. |volume=14 |issue= 4 |pages= 415-20 |year= 1997 |pmid= 8944021 |doi= 10.1038/ng1296-415 }}
*{{cite journal | author=Helbing CC, Veillette C, Riabowol K, ''et al.'' |title=A novel candidate tumor suppressor, ING1, is involved in the regulation of apoptosis. |journal=Cancer Res. |volume=57 |issue= 7 |pages= 1255-8 |year= 1997 |pmid= 9102209 |doi= }}
*{{cite journal | author=Garkavtsev I, Riabowol K |title=Extension of the replicative life span of human diploid fibroblasts by inhibition of the p33ING1 candidate tumor suppressor. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 2014-9 |year= 1997 |pmid= 9121449 |doi= }}
*{{cite journal | author=Garkavtsev I, Demetrick D, Riabowol K |title=Cellular localization and chromosome mapping of a novel candidate tumor suppressor gene (ING1). |journal=Cytogenet. Cell Genet. |volume=76 |issue= 3-4 |pages= 176-8 |year= 1997 |pmid= 9186514 |doi= }}
*{{cite journal | author=Zeremski M, Horrigan SK, Grigorian IA, ''et al.'' |title=Localization of the candidate tumor suppressor gene ING1 to human chromosome 13q34. |journal=Somat. Cell Mol. Genet. |volume=23 |issue= 3 |pages= 233-6 |year= 1997 |pmid= 9330636 |doi= }}
*{{cite journal | author=Garkavtsev I, Grigorian IA, Ossovskaya VS, ''et al.'' |title=The candidate tumour suppressor p33ING1 cooperates with p53 in cell growth control. |journal=Nature |volume=391 |issue= 6664 |pages= 295-8 |year= 1998 |pmid= 9440695 |doi= 10.1038/34675 }}
*{{cite journal | author=Shinoura N, Muramatsu Y, Nishimura M, ''et al.'' |title=Adenovirus-mediated transfer of p33ING1 with p53 drastically augments apoptosis in gliomas. |journal=Cancer Res. |volume=59 |issue= 21 |pages= 5521-8 |year= 1999 |pmid= 10554029 |doi= }}
*{{cite journal | author=Jäger D, Stockert E, Scanlan MJ, ''et al.'' |title=Cancer-testis antigens and ING1 tumor suppressor gene product are breast cancer antigens: characterization of tissue-specific ING1 transcripts and a homologue gene. |journal=Cancer Res. |volume=59 |issue= 24 |pages= 6197-204 |year= 2000 |pmid= 10626813 |doi= }}
*{{cite journal | author=Sanchez-Cespedes M, Okami K, Cairns P, Sidransky D |title=Molecular analysis of the candidate tumor suppressor gene ING1 in human head and neck tumors with 13q deletions. |journal=Genes Chromosomes Cancer |volume=27 |issue= 3 |pages= 319-22 |year= 2000 |pmid= 10679922 |doi= }}
*{{cite journal | author=Tokunaga E, Maehara Y, Oki E, ''et al.'' |title=Diminished expression of ING1 mRNA and the correlation with p53 expression in breast cancers. |journal=Cancer Lett. |volume=152 |issue= 1 |pages= 15-22 |year= 2000 |pmid= 10754201 |doi= }}
*{{cite journal | author=Baranova AV, Ivanov DV, Makeeva NV, ''et al.'' |title=[Genomic organization of the suppressor gene for tumor growth ING1] |journal=Mol. Biol. (Mosk.) |volume=34 |issue= 2 |pages= 263-9 |year= 2000 |pmid= 10779953 |doi= }}
*{{cite journal | author=Saito A, Furukawa T, Fukushige S, ''et al.'' |title=p24/ING1-ALT1 and p47/ING1-ALT2, distinct alternative transcripts of p33/ING1. |journal=J. Hum. Genet. |volume=45 |issue= 3 |pages= 177-81 |year= 2000 |pmid= 10807544 |doi= }}
*{{cite journal | author=Gunduz M, Ouchida M, Fukushima K, ''et al.'' |title=Genomic structure of the human ING1 gene and tumor-specific mutations detected in head and neck squamous cell carcinomas. |journal=Cancer Res. |volume=60 |issue= 12 |pages= 3143-6 |year= 2000 |pmid= 10866301 |doi= }}
*{{cite journal | author=Skowyra D, Zeremski M, Neznanov N, ''et al.'' |title=Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 8734-9 |year= 2001 |pmid= 11118440 |doi= 10.1074/jbc.M007664200 }}
*{{cite journal | author=Nagashima M, Shiseki M, Miura K, ''et al.'' |title=DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 17 |pages= 9671-6 |year= 2001 |pmid= 11481424 |doi= 10.1073/pnas.161151798 }}
*{{cite journal | author=Scott M, Bonnefin P, Vieyra D, ''et al.'' |title=UV-induced binding of ING1 to PCNA regulates the induction of apoptosis. |journal=J. Cell. Sci. |volume=114 |issue= Pt 19 |pages= 3455-62 |year= 2001 |pmid= 11682605 |doi= }}
*{{cite journal | author=Kuzmichev A, Zhang Y, Erdjument-Bromage H, ''et al.'' |title=Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1). |journal=Mol. Cell. Biol. |volume=22 |issue= 3 |pages= 835-48 |year= 2002 |pmid= 11784859 |doi= }}
*{{cite journal | author=Nouman GS, Angus B, Lunec J, ''et al.'' |title=Comparative assessment expression of the inhibitor of growth 1 gene (ING1) in normal and neoplastic tissues. |journal=Hybrid. Hybridomics |volume=21 |issue= 1 |pages= 1-10 |year= 2002 |pmid= 11991811 |doi= 10.1089/15368590252917584 }}
*{{cite journal | author=Bromidge T, Lynas C |title=Relative levels of alternative transcripts of the ING1 gene and lack of mutations of p33/ING1 in haematological malignancies. |journal=Leuk. Res. |volume=26 |issue= 7 |pages= 631-5 |year= 2002 |pmid= 12008079 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KPNA5... {November 17, 2007 12:55:40 PM PST}
- SEARCH REDIRECT: Control Box Found: KPNA5 {November 17, 2007 12:56:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:56:18 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:56:18 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:56:18 PM PST}
- UPDATED: Updated protein page:
KPNA5 {November 17, 2007 12:56:24 PM PST}
- INFO: Beginning work on MAP2K6... {November 17, 2007 1:00:03 PM PST}
- SEARCH REDIRECT: Control Box Found: MAP2K6 {November 17, 2007 1:00:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:00:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:00:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:00:44 PM PST}
- UPDATED: Updated protein page:
MAP2K6 {November 17, 2007 1:00:50 PM PST}
- INFO: Beginning work on MAX... {November 17, 2007 12:56:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:57:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MAX_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1an2.
| PDB = {{PDB2|1an2}}, {{PDB2|1hlo}}, {{PDB2|1nkp}}, {{PDB2|1nlw}}, {{PDB2|1r05}}
| Name = MYC associated factor X
| HGNCid = 6913
| Symbol = MAX
| AltSymbols =; MGC10775; MGC11225; MGC18164; MGC34679; MGC36767; orf1
| OMIM = 154950
| ECnumber =
| Homologene = 1786
| MGIid = 96921
| GeneAtlas_image1 = PBB_GE_MAX_214108_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAX_208403_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_MAX_209331_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{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:0045449 |text = regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4149
| Hs_Ensembl = ENSG00000125952
| Hs_RefseqProtein = NP_002373
| Hs_RefseqmRNA = NM_002382
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 64542645
| Hs_GenLoc_end = 64638980
| Hs_Uniprot = P61244
| Mm_EntrezGene = 17187
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001002021
| Mm_RefseqProtein = XP_001002021
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''MYC associated factor X''', also known as '''MAX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAX MYC associated factor X| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4149| 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 basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown.<ref name="entrez">{{cite web | title = Entrez Gene: MAX MYC associated factor X| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4149| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Grandori C, Cowley SM, James LP, Eisenman RN |title=The Myc/Max/Mad network and the transcriptional control of cell behavior. |journal=Annu. Rev. Cell Dev. Biol. |volume=16 |issue= |pages= 653-99 |year= 2001 |pmid= 11031250 |doi= 10.1146/annurev.cellbio.16.1.653 }}
*{{cite journal | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1-14 |year= 2001 |pmid= 11602341 |doi= }}
*{{cite journal | author=Wechsler DS, Dang CV |title=Opposite orientations of DNA bending by c-Myc and Max. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 16 |pages= 7635-9 |year= 1992 |pmid= 1323849 |doi= }}
*{{cite journal | author=Wagner AJ, Le Beau MM, Diaz MO, Hay N |title=Expression, regulation, and chromosomal localization of the Max gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 7 |pages= 3111-5 |year= 1992 |pmid= 1557420 |doi= }}
*{{cite journal | author=Mäkelä TP, Koskinen PJ, Västrik I, Alitalo K |title=Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation. |journal=Science |volume=256 |issue= 5055 |pages= 373-7 |year= 1992 |pmid= 1566084 |doi= }}
*{{cite journal | author=Gilladoga AD, Edelhoff S, Blackwood EM, ''et al.'' |title=Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in situ hybridization. |journal=Oncogene |volume=7 |issue= 6 |pages= 1249-51 |year= 1992 |pmid= 1594250 |doi= }}
*{{cite journal | author=Blackwood EM, Eisenman RN |title=Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. |journal=Science |volume=251 |issue= 4998 |pages= 1211-7 |year= 1991 |pmid= 2006410 |doi= }}
*{{cite journal | author=Zervos AS, Faccio L, Gatto JP, ''et al.'' |title=Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 23 |pages= 10531-4 |year= 1995 |pmid= 7479834 |doi= }}
*{{cite journal | author=Bousset K, Henriksson M, Lüscher-Firzlaff JM, ''et al.'' |title=Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers. |journal=Oncogene |volume=8 |issue= 12 |pages= 3211-20 |year= 1993 |pmid= 8247525 |doi= }}
*{{cite journal | author=Ayer DE, Kretzner L, Eisenman RN |title=Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. |journal=Cell |volume=72 |issue= 2 |pages= 211-22 |year= 1993 |pmid= 8425218 |doi= }}
*{{cite journal | author=Västrik I, Koskinen PJ, Alitalo R, Mäkelä TP |title=Alternative mRNA forms and open reading frames of the max gene. |journal=Oncogene |volume=8 |issue= 2 |pages= 503-7 |year= 1993 |pmid= 8426752 |doi= }}
*{{cite journal | author=Ferré-D'Amaré AR, Prendergast GC, Ziff EB, Burley SK |title=Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. |journal=Nature |volume=363 |issue= 6424 |pages= 38-45 |year= 1993 |pmid= 8479534 |doi= 10.1038/363038a0 }}
*{{cite journal | author=Hurlin PJ, Quéva C, Koskinen PJ, ''et al.'' |title=Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5646-59 |year= 1996 |pmid= 8521822 |doi= }}
*{{cite journal | author=Grandori C, Mac J, Siëbelt F, ''et al.'' |title=Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo. |journal=EMBO J. |volume=15 |issue= 16 |pages= 4344-57 |year= 1996 |pmid= 8861962 |doi= }}
*{{cite journal | author=Brownlie P, Ceska T, Lamers M, ''et al.'' |title=The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control. |journal=Structure |volume=5 |issue= 4 |pages= 509-20 |year= 1997 |pmid= 9115440 |doi= }}
*{{cite journal | author=Meroni G, Reymond A, Alcalay M, ''et al.'' |title=Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor. |journal=EMBO J. |volume=16 |issue= 10 |pages= 2892-906 |year= 1997 |pmid= 9184233 |doi= 10.1093/emboj/16.10.2892 }}
*{{cite journal | author=Gupta MP, Amin CS, Gupta M, ''et al.'' |title=Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression. |journal=Mol. Cell. Biol. |volume=17 |issue= 7 |pages= 3924-36 |year= 1997 |pmid= 9199327 |doi= }}
*{{cite journal | author=Gupta K, Anand G, Yin X, ''et al.'' |title=Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc. |journal=Oncogene |volume=16 |issue= 9 |pages= 1149-59 |year= 1998 |pmid= 9528857 |doi= 10.1038/sj.onc.1201634 }}
*{{cite journal | author=Lavigne P, Crump MP, Gagné SM, ''et al.'' |title=Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. |journal=J. Mol. Biol. |volume=281 |issue= 1 |pages= 165-81 |year= 1998 |pmid= 9680483 |doi= 10.1006/jmbi.1998.1914 }}
*{{cite journal | author=FitzGerald MJ, Arsura M, Bellas RE, ''et al.'' |title=Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc. |journal=Oncogene |volume=18 |issue= 15 |pages= 2489-98 |year= 1999 |pmid= 10229200 |doi= 10.1038/sj.onc.1202611 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NEUROD1... {November 17, 2007 12:57:12 PM PST}
- SEARCH REDIRECT: Control Box Found: NEUROD1 {November 17, 2007 12:57:43 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:57:47 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:57:47 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:57:47 PM PST}
- UPDATED: Updated protein page:
NEUROD1 {November 17, 2007 12:57:52 PM PST}
- INFO: Beginning work on NPC1... {November 17, 2007 12:57:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:58:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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 = Niemann-Pick disease, type C1
| HGNCid = 7897
| Symbol = NPC1
| AltSymbols =; NPC
| OMIM = 607623
| ECnumber =
| Homologene = 228
| MGIid = 1097712
| GeneAtlas_image1 = PBB_GE_NPC1_202679_at_tn.png
| Function = {{GNF_GO|id=GO:0005478 |text = transporter activity}} {{GNF_GO|id=GO:0008158 |text = hedgehog receptor activity}} {{GNF_GO|id=GO:0015248 |text = sterol transporter activity}}
| Component = {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007041 |text = lysosomal transport}} {{GNF_GO|id=GO:0008206 |text = bile acid metabolic process}} {{GNF_GO|id=GO:0030301 |text = cholesterol transport}} {{GNF_GO|id=GO:0042632 |text = cholesterol homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4864
| Hs_Ensembl = ENSG00000141458
| Hs_RefseqProtein = NP_000262
| Hs_RefseqmRNA = NM_000271
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 19365463
| Hs_GenLoc_end = 19420426
| Hs_Uniprot = O15118
| Mm_EntrezGene = 18145
| Mm_Ensembl = ENSMUSG00000024413
| Mm_RefseqmRNA = NM_008720
| Mm_RefseqProtein = NP_032746
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 12333387
| Mm_GenLoc_end = 12379894
| Mm_Uniprot = Q3U2B2
}}
}}
'''Niemann-Pick disease, type C1''', also known as '''NPC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NPC1 Niemann-Pick disease, type C1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4864| 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 = NPC1 was identified as the gene that when mutated, results in Niemann-Pick C disease. NPC1 encodes a putative integral membrane protein containing motifs consistent with a role in intracellular transport of cholesterol to post-lysosomal destinations.<ref name="entrez">{{cite web | title = Entrez Gene: NPC1 Niemann-Pick disease, type C1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4864| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vanier MT, Suzuki K |title=Recent advances in elucidating Niemann-Pick C disease. |journal=Brain Pathol. |volume=8 |issue= 1 |pages= 163-74 |year= 1998 |pmid= 9458174 |doi= }}
*{{cite journal | author=Liscum L, Klansek JJ |title=Niemann-Pick disease type C. |journal=Curr. Opin. Lipidol. |volume=9 |issue= 2 |pages= 131-5 |year= 1998 |pmid= 9559270 |doi= }}
*{{cite journal | author=Morris JA, Carstea ED |title=Niemann-Pick C disease: cholesterol handling gone awry. |journal=Molecular medicine today |volume=4 |issue= 12 |pages= 525-31 |year= 1999 |pmid= 9866822 |doi= }}
*{{cite journal | author=Garver WS, Heidenreich RA |title=The Niemann-Pick C proteins and trafficking of cholesterol through the late endosomal/lysosomal system. |journal=Curr. Mol. Med. |volume=2 |issue= 5 |pages= 485-505 |year= 2003 |pmid= 12125814 |doi= }}
*{{cite journal | author=Carstea ED, Polymeropoulos MH, Parker CC, ''et al.'' |title=Linkage of Niemann-Pick disease type C to human chromosome 18. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 5 |pages= 2002-4 |year= 1993 |pmid= 8446622 |doi= }}
*{{cite journal | author=Carstea ED, Morris JA, Coleman KG, ''et al.'' |title=Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. |journal=Science |volume=277 |issue= 5323 |pages= 228-31 |year= 1997 |pmid= 9211849 |doi= }}
*{{cite journal | author=Greer WL, Riddell DC, Byers DM, ''et al.'' |title=Linkage of Niemann-Pick disease type D to the same region of human chromosome 18 as Niemann-Pick disease type C. |journal=Am. J. Hum. Genet. |volume=61 |issue= 1 |pages= 139-42 |year= 1997 |pmid= 9245994 |doi= }}
*{{cite journal | author=Greer WL, Riddell DC, Gillan TL, ''et al.'' |title=The Nova Scotia (type D) form of Niemann-Pick disease is caused by a G3097-->T transversion in NPC1. |journal=Am. J. Hum. Genet. |volume=63 |issue= 1 |pages= 52-4 |year= 1998 |pmid= 9634529 |doi= }}
*{{cite journal | author=Watari H, Blanchette-Mackie EJ, Dwyer NK, ''et al.'' |title=Niemann-Pick C1 protein: obligatory roles for N-terminal domains and lysosomal targeting in cholesterol mobilization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 805-10 |year= 1999 |pmid= 9927649 |doi= }}
*{{cite journal | author=Patel SC, Suresh S, Kumar U, ''et al.'' |title=Localization of Niemann-Pick C1 protein in astrocytes: implications for neuronal degeneration in Niemann- Pick type C disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 4 |pages= 1657-62 |year= 1999 |pmid= 9990080 |doi= }}
*{{cite journal | author=Morris JA, Zhang D, Coleman KG, ''et al.'' |title=The genomic organization and polymorphism analysis of the human Niemann-Pick C1 gene. |journal=Biochem. Biophys. Res. Commun. |volume=261 |issue= 2 |pages= 493-8 |year= 1999 |pmid= 10425213 |doi= 10.1006/bbrc.1999.1070 }}
*{{cite journal | author=Yamamoto T, Nanba E, Ninomiya H, ''et al.'' |title=NPC1 gene mutations in Japanese patients with Niemann-Pick disease type C. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 10-6 |year= 1999 |pmid= 10480349 |doi= }}
*{{cite journal | author=Greer WL, Dobson MJ, Girouard GS, ''et al.'' |title=Mutations in NPC1 highlight a conserved NPC1-specific cysteine-rich domain. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1252-60 |year= 1999 |pmid= 10521290 |doi= }}
*{{cite journal | author=Millat G, Marçais C, Rafi MA, ''et al.'' |title=Niemann-Pick C1 disease: the I1061T substitution is a frequent mutant allele in patients of Western European descent and correlates with a classic juvenile phenotype. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1321-9 |year= 1999 |pmid= 10521297 |doi= }}
*{{cite journal | author=Davies JP, Ioannou YA |title=Topological analysis of Niemann-Pick C1 protein reveals that the membrane orientation of the putative sterol-sensing domain is identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and sterol regulatory element binding protein cleavage-activating protein. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24367-74 |year= 2000 |pmid= 10821832 |doi= 10.1074/jbc.M002184200 }}
*{{cite journal | author=Millat G, Marçais C, Tomasetto C, ''et al.'' |title=Niemann-Pick C1 disease: correlations between NPC1 mutations, levels of NPC1 protein, and phenotypes emphasize the functional significance of the putative sterol-sensing domain and of the cysteine-rich luminal loop. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1373-85 |year= 2001 |pmid= 11333381 |doi= }}
*{{cite journal | author=Sun X, Marks DL, Park WD, ''et al.'' |title=Niemann-Pick C variant detection by altered sphingolipid trafficking and correlation with mutations within a specific domain of NPC1. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1361-72 |year= 2001 |pmid= 11349231 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PABPC1... {November 17, 2007 1:01:39 PM PST}
- SEARCH REDIRECT: Control Box Found: PABPC1 {November 17, 2007 1:02:05 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:02:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:02:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:02:06 PM PST}
- UPDATED: Updated protein page:
PABPC1 {November 17, 2007 1:02:12 PM PST}
- INFO: Beginning work on PRG2... {November 17, 2007 12:59:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:59:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_PRG2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h8u.
| PDB = {{PDB2|1h8u}}, {{PDB2|2brs}}
| Name = Proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)
| HGNCid = 9362
| Symbol = PRG2
| AltSymbols =; MBP; BMPG; MGC14537
| OMIM = 605601
| ECnumber =
| Homologene = 2044
| MGIid = 103294
| GeneAtlas_image1 = PBB_GE_PRG2_211743_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5553
| Hs_Ensembl = ENSG00000186652
| Hs_RefseqProtein = NP_002719
| Hs_RefseqmRNA = NM_002728
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 56910832
| Hs_GenLoc_end = 56914684
| Hs_Uniprot = P13727
| Mm_EntrezGene = 19074
| Mm_Ensembl = ENSMUSG00000027073
| Mm_RefseqmRNA = NM_008920
| Mm_RefseqProtein = NP_032946
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 84781300
| Mm_GenLoc_end = 84784471
| Mm_Uniprot = Q545D8
}}
}}
'''Proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)''', also known as '''PRG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRG2 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5553| 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 the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in placenta and pregnancy serum, where it exists as a complex with several other proteins including pregnancy-associated plasma protein A (PAPPA), angiotensinogen (AGT), and C3dg. This protein may be involved in antiparasitic defense mechanisms as a cytotoxin and helminthotoxin, and in immune hypersensitivity reactions. It is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases.<ref name="entrez">{{cite web | title = Entrez Gene: PRG2 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5553| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vanhaesebroeck B, Alessi DR |title=The PI3K-PDK1 connection: more than just a road to PKB. |journal=Biochem. J. |volume=346 Pt 3 |issue= |pages= 561-76 |year= 2000 |pmid= 10698680 |doi= }}
*{{cite journal | author=Yoshimatsu K, Ohya Y, Shikata Y, ''et al.'' |title=Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins. |journal=Mol. Immunol. |volume=29 |issue= 4 |pages= 537-46 |year= 1992 |pmid= 1565101 |doi= }}
*{{cite journal | author=Barker RL, Loegering DA, Arakawa KC, ''et al.'' |title=Cloning and sequence analysis of the human gene encoding eosinophil major basic protein. |journal=Gene |volume=86 |issue= 2 |pages= 285-9 |year= 1990 |pmid= 2323577 |doi= }}
*{{cite journal | author=Gabay JE, Scott RW, Campanelli D, ''et al.'' |title=Antibiotic proteins of human polymorphonuclear leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5610-4 |year= 1989 |pmid= 2501794 |doi= }}
*{{cite journal | author=Wasmoen TL, McKean DJ, Benirschke K, ''et al.'' |title=Evidence of eosinophil granule major basic protein in human placenta. |journal=J. Exp. Med. |volume=170 |issue= 6 |pages= 2051-63 |year= 1990 |pmid= 2584934 |doi= }}
*{{cite journal | author=Barker RL, Gleich GJ, Pease LR |title=Acidic precursor revealed in human eosinophil granule major basic protein cDNA. |journal=J. Exp. Med. |volume=168 |issue= 4 |pages= 1493-8 |year= 1988 |pmid= 3171483 |doi= }}
*{{cite journal | author=McGrogan M, Simonsen C, Scott R, ''et al.'' |title=Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein. |journal=J. Exp. Med. |volume=168 |issue= 6 |pages= 2295-308 |year= 1989 |pmid= 3199069 |doi= }}
*{{cite journal | author=Wasmoen TL, Bell MP, Loegering DA, ''et al.'' |title=Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. |journal=J. Biol. Chem. |volume=263 |issue= 25 |pages= 12559-63 |year= 1988 |pmid= 3410852 |doi= }}
*{{cite journal | author=Weller PF, Ackerman SJ, Smith JA |title=Eosinophil granule cationic proteins: major basic protein is distinct from the smaller subunit of eosinophil peroxidase. |journal=J. Leukoc. Biol. |volume=43 |issue= 1 |pages= 1-4 |year= 1988 |pmid= 3422083 |doi= }}
*{{cite journal | author=Kristensen T, Oxvig C, Sand O, ''et al.'' |title=Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA. |journal=Biochemistry |volume=33 |issue= 6 |pages= 1592-8 |year= 1994 |pmid= 7508748 |doi= }}
*{{cite journal | author=Oxvig C, Haaning J, Højrup P, Sottrup-Jensen L |title=Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum. |journal=Biochem. Mol. Biol. Int. |volume=33 |issue= 2 |pages= 329-36 |year= 1994 |pmid= 7524900 |doi= }}
*{{cite journal | author=Bonno M, Oxvig C, Kephart GM, ''et al.'' |title=Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta. |journal=Lab. Invest. |volume=71 |issue= 4 |pages= 560-6 |year= 1994 |pmid= 7526035 |doi= }}
*{{cite journal | author=Li MS, Sun L, Satoh T, ''et al.'' |title=Human eosinophil major basic protein, a mediator of allergic inflammation, is expressed by alternative splicing from two promoters. |journal=Biochem. J. |volume=305 ( Pt 3) |issue= |pages= 921-7 |year= 1995 |pmid= 7531438 |doi= }}
*{{cite journal | author=Oxvig C, Haaning J, Kristensen L, ''et al.'' |title=Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma. |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 13645-51 |year= 1995 |pmid= 7539791 |doi= }}
*{{cite journal | author=Oxvig C, Sand O, Kristensen T, ''et al.'' |title=Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein. |journal=J. Biol. Chem. |volume=268 |issue= 17 |pages= 12243-6 |year= 1993 |pmid= 7685339 |doi= }}
*{{cite journal | author=Levi-Schaffer F, Lacy P, Severs NJ, ''et al.'' |title=Association of granulocyte-macrophage colony-stimulating factor with the crystalloid granules of human eosinophils. |journal=Blood |volume=85 |issue= 9 |pages= 2579-86 |year= 1995 |pmid= 7727786 |doi= }}
*{{cite journal | author=Oxvig C, Gleich GJ, Sottrup-Jensen L |title=Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein. |journal=FEBS Lett. |volume=341 |issue= 2-3 |pages= 213-7 |year= 1994 |pmid= 8137941 |doi= }}
*{{cite journal | author=Shikata Y, Hayashi Y, Yoshimatsu K, ''et al.'' |title=Pro-major basic protein has three types of sugar chains at the pro-portion. |journal=Biochim. Biophys. Acta |volume=1163 |issue= 3 |pages= 243-9 |year= 1993 |pmid= 8507662 |doi= }}
*{{cite journal | author=Nittoh T, Watanabe M, Okayama H, ''et al.'' |title=Cloning of cDNA for rat eosinophil major basic protein. |journal=Biochim. Biophys. Acta |volume=1264 |issue= 3 |pages= 261-4 |year= 1996 |pmid= 8547309 |doi= }}
*{{cite journal | author=Delcommenne M, Tan C, Gray V, ''et al.'' |title=Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11211-6 |year= 1998 |pmid= 9736715 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKCH... {November 17, 2007 12:59:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:00:03 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_PRKCH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2fk9.
| PDB = {{PDB2|2fk9}}
| Name = Protein kinase C, eta
| HGNCid = 9403
| Symbol = PRKCH
| AltSymbols =; MGC26269; MGC5363; PKC-L; PKCL; PRKCL; nPKC-eta
| OMIM = 605437
| ECnumber =
| Homologene = 84384
| MGIid = 97600
| GeneAtlas_image1 = PBB_GE_PRKCH_206099_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKCH_218764_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004697 |text = protein kinase C activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5583
| Hs_Ensembl = ENSG00000027075
| Hs_RefseqProtein = NP_006246
| Hs_RefseqmRNA = NM_006255
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 60858186
| Hs_GenLoc_end = 61087443
| Hs_Uniprot = P24723
| Mm_EntrezGene = 18755
| Mm_Ensembl = ENSMUSG00000021108
| Mm_RefseqmRNA = NM_008856
| Mm_RefseqProtein = NP_032882
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 74503879
| Mm_GenLoc_end = 74697023
| Mm_Uniprot = Q3U1I0
}}
}}
'''Protein kinase C, eta''', also known as '''PRKCH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKCH protein kinase C, eta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5583| 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 = Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipids-dependent protein kinase. It is predominantly expressed in epithelial tissues and has been shown to reside specifically in the cell nucleus. This protein kinase can regulate keratinocyte differentiation by activating the MAP kinase MAPK13 (p38delta)-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha (CEBPA). It is also found to mediate the transcription activation of the transglutaminase 1 (TGM1) gene.<ref name="entrez">{{cite web | title = Entrez Gene: PRKCH protein kinase C, eta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5583| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Greif H, Ben-Chaim J, Shimon T, ''et al.'' |title=The protein kinase C-related PKC-L(eta) gene product is localized in the cell nucleus. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 1304-11 |year= 1992 |pmid= 1545811 |doi= }}
*{{cite journal | author=Bacher N, Zisman Y, Berent E, Livneh E |title=Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 1404 |year= 1992 |pmid= 1545821 |doi= }}
*{{cite journal | author=Liyanage M, Frith D, Livneh E, Stabel S |title=Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo. |journal=Biochem. J. |volume=283 ( Pt 3) |issue= |pages= 781-7 |year= 1992 |pmid= 1590767 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi= }}
*{{cite journal | author=Chowdhury IH, Koyanagi Y, Kobayashi S, ''et al.'' |title=The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway. |journal=Virology |volume=176 |issue= 1 |pages= 126-32 |year= 1990 |pmid= 1970444 |doi= }}
*{{cite journal | author=Bacher N, Zisman Y, Berent E, Livneh E |title=Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. |journal=Mol. Cell. Biol. |volume=11 |issue= 1 |pages= 126-33 |year= 1991 |pmid= 1986216 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41. |journal=J. Immunol. |volume=144 |issue= 10 |pages= 3928-35 |year= 1990 |pmid= 2139676 |doi= }}
*{{cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi= }}
*{{cite journal | author=Fields AP, Bednarik DP, Hess A, May WS |title=Human immunodeficiency virus induces phosphorylation of its cell surface receptor. |journal=Nature |volume=333 |issue= 6170 |pages= 278-80 |year= 1988 |pmid= 3259291 |doi= 10.1038/333278a0 }}
*{{cite journal | author=Chirmule N, Goonewardena H, Pahwa S, ''et al.'' |title=HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19364-9 |year= 1995 |pmid= 7642615 |doi= }}
*{{cite journal | author=Ward NE, Gravitt KR, O'Brian CA |title=Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein. |journal=Cancer Lett. |volume=88 |issue= 1 |pages= 37-40 |year= 1995 |pmid= 7850771 |doi= }}
*{{cite journal | author=Palmer RH, Ridden J, Parker PJ |title=Identification of multiple, novel, protein kinase C-related gene products. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 5-8 |year= 1995 |pmid= 7988719 |doi= }}
*{{cite journal | author=Gupta S, Aggarwal S, Kim C, Gollapudi S |title=Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report. |journal=Int. J. Immunopharmacol. |volume=16 |issue= 3 |pages= 197-204 |year= 1994 |pmid= 8206685 |doi= }}
*{{cite journal | author=Parada NA, Cruikshank WW, Danis HL, ''et al.'' |title=IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 100-6 |year= 1996 |pmid= 8599832 |doi= 10.1006/cimm.1996.0054 }}
*{{cite journal | author=Denning MF, Dlugosz AA, Threadgill DW, ''et al.'' |title=Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5325-31 |year= 1996 |pmid= 8621384 |doi= }}
*{{cite journal | author=Ueda E, Ohno S, Kuroki T, ''et al.'' |title=The eta isoform of protein kinase C mediates transcriptional activation of the human transglutaminase 1 gene. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9790-4 |year= 1996 |pmid= 8621660 |doi= }}
*{{cite journal | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi= }}
*{{cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi= }}
*{{cite journal | author=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMA1... {November 17, 2007 1:00:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:01:39 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_PSMA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, alpha type, 1
| HGNCid = 9530
| Symbol = PSMA1
| AltSymbols =; HC2; MGC14542; MGC14575; MGC14751; MGC1667; MGC21459; MGC22853; MGC23915; NU; PROS30
| OMIM = 602854
| ECnumber =
| Homologene = 2080
| MGIid = 1347005
| GeneAtlas_image1 = PBB_GE_PSMA1_210759_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMA1_201676_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PSMA1_211746_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005844 |text = polysome}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5682
| Hs_Ensembl = ENSG00000129084
| Hs_RefseqProtein = NP_002777
| Hs_RefseqmRNA = NM_002786
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 14482999
| Hs_GenLoc_end = 14621739
| Hs_Uniprot = P25786
| Mm_EntrezGene = 26440
| Mm_Ensembl = ENSMUSG00000030751
| Mm_RefseqmRNA = NM_011965
| Mm_RefseqProtein = NP_036095
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 114056081
| Mm_GenLoc_end = 114065641
| Mm_Uniprot = Q3TS44
}}
}}
'''Proteasome (prosome, macropain) subunit, alpha type, 1''', also known as '''PSMA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMA1 proteasome (prosome, macropain) subunit, alpha type, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5682| 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. Two alternative transcripts encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: PSMA1 proteasome (prosome, macropain) subunit, alpha type, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5682| 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=Silva Pereira I, Bey F, Coux O, Scherrer K |title=Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes. |journal=Gene |volume=120 |issue= 2 |pages= 235-42 |year= 1992 |pmid= 1398136 |doi= }}
*{{cite journal | author=Shimbara N, Orino E, Sone S, ''et al.'' |title=Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 18100-9 |year= 1992 |pmid= 1517242 |doi= }}
*{{cite journal | author=Kanayama H, Tanaka K, Aki M, ''et al.'' |title=Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells. |journal=Cancer Res. |volume=51 |issue= 24 |pages= 6677-85 |year= 1992 |pmid= 1660345 |doi= }}
*{{cite journal | author=DeMartino GN, Orth K, McCullough ML, ''et al.'' |title=The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. |journal=Biochim. Biophys. Acta |volume=1079 |issue= 1 |pages= 29-38 |year= 1991 |pmid= 1888762 |doi= }}
*{{cite journal | author=Tamura T, Lee DH, Osaka F, ''et al.'' |title=Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes). |journal=Biochim. Biophys. Acta |volume=1089 |issue= 1 |pages= 95-102 |year= 1991 |pmid= 2025653 |doi= }}
*{{cite journal | author=Bey F, Silva Pereira I, Coux O, ''et al.'' |title=The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family. |journal=Mol. Gen. Genet. |volume=237 |issue= 1-2 |pages= 193-205 |year= 1993 |pmid= 7681138 |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=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=Gerards WL, de Jong WW, Bloemendal H, Boelens W |title=The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits. |journal=J. Mol. Biol. |volume=275 |issue= 1 |pages= 113-21 |year= 1998 |pmid= 9451443 |doi= 10.1006/jmbi.1997.1429 }}
*{{cite journal | author=Tipler CP, Hutchon SP, Hendil K, ''et al.'' |title=Purification and characterization of 26S proteasomes from human and mouse spermatozoa. |journal=Mol. Hum. Reprod. |volume=3 |issue= 12 |pages= 1053-60 |year= 1998 |pmid= 9464850 |doi= }}
*{{cite journal | author=Henry L, Baz A, Château MT, ''et al.'' |title=Proteasome (prosome) subunit variations during the differentiation of myeloid U937 cells. |journal=Analytical cellular pathology : the journal of the European Society for Analytical Cellular Pathology |volume=15 |issue= 3 |pages= 131-44 |year= 1998 |pmid= 9497851 |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=Dahlmann B, Kopp F, Kristensen P, Hendil KB |title=Identical subunit topographies of human and yeast 20S proteasomes. |journal=Arch. Biochem. Biophys. |volume=363 |issue= 2 |pages= 296-300 |year= 1999 |pmid= 10068451 |doi= 10.1006/abbi.1999.1104 }}
*{{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=Tanahashi N, Murakami Y, Minami Y, ''et al.'' |title=Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14336-45 |year= 2000 |pmid= 10799514 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RACGAP1... {November 17, 2007 1:02:12 PM PST}
- SEARCH REDIRECT: Control Box Found: RACGAP1 {November 17, 2007 1:02:40 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:02:41 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:02:41 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:02:41 PM PST}
- UPDATED: Updated protein page:
RACGAP1 {November 17, 2007 1:02:47 PM PST}
- INFO: Beginning work on SERPINB2... {November 17, 2007 12:58:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:59:02 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_SERPINB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1by7.
| PDB = {{PDB2|1by7}}, {{PDB2|1jrr}}, {{PDB2|2arq}}, {{PDB2|2arr}}
| Name = Serpin peptidase inhibitor, clade B (ovalbumin), member 2
| HGNCid = 8584
| Symbol = SERPINB2
| AltSymbols =; PAI; HsT1201; PAI-2; PAI2; PLANH2
| OMIM = 173390
| ECnumber =
| Homologene = 20571
| MGIid = 97609
| GeneAtlas_image1 = PBB_GE_SERPINB2_204614_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0008243 |text = plasminogen activator activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5055
| Hs_Ensembl = ENSG00000197632
| Hs_RefseqProtein = NP_002566
| Hs_RefseqmRNA = NM_002575
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 59705922
| Hs_GenLoc_end = 59722100
| Hs_Uniprot = P05120
| Mm_EntrezGene = 18788
| Mm_Ensembl = ENSMUSG00000062345
| Mm_RefseqmRNA = NM_011111
| Mm_RefseqProtein = NP_035241
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 109338970
| Mm_GenLoc_end = 109353139
| Mm_Uniprot = Q542A3
}}
}}
'''Serpin peptidase inhibitor, clade B (ovalbumin), member 2''', also known as '''SERPINB2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPINB2 serpin peptidase inhibitor, clade B (ovalbumin), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5055| accessdate = }}</ref>
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{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Ellis V, Wun TC, Behrendt N, ''et al.'' |title=Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 9904-8 |year= 1990 |pmid= 2161846 |doi= }}
*{{cite journal | author=Estreicher A, Mühlhauser J, Carpentier JL, ''et al.'' |title=The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes. |journal=J. Cell Biol. |volume=111 |issue= 2 |pages= 783-92 |year= 1990 |pmid= 2166055 |doi= }}
*{{cite journal | author=Samia JA, Alexander SJ, Horton KW, ''et al.'' |title=Chromosomal organization and localization of the human urokinase inhibitor gene: perfect structural conservation with ovalbumin. |journal=Genomics |volume=6 |issue= 1 |pages= 159-67 |year= 1990 |pmid= 2303256 |doi= }}
*{{cite journal | author=Schwartz BS, Monroe MC, Bradshaw JD |title=Endotoxin-induced production of plasminogen activator inhibitor by human monocytes is autonomous and can be inhibited by lipid X. |journal=Blood |volume=73 |issue= 8 |pages= 2188-95 |year= 1989 |pmid= 2471561 |doi= }}
*{{cite journal | author=Ye RD, Ahern SM, Le Beau MM, ''et al.'' |title=Structure of the gene for human plasminogen activator inhibitor-2. The nearest mammalian homologue of chicken ovalbumin. |journal=J. Biol. Chem. |volume=264 |issue= 10 |pages= 5495-502 |year= 1989 |pmid= 2494165 |doi= }}
*{{cite journal | author=Laug WE, Aebersold R, Jong A, ''et al.'' |title=Isolation of multiple types of plasminogen activator inhibitors from vascular smooth muscle cells. |journal=Thromb. Haemost. |volume=61 |issue= 3 |pages= 517-21 |year= 1989 |pmid= 2799763 |doi= }}
*{{cite journal | author=Kruithof EK, Cousin E |title=Plasminogen activator inhibitor 2. Isolation and characterization of the promoter region of the gene. |journal=Biochem. Biophys. Res. Commun. |volume=156 |issue= 1 |pages= 383-8 |year= 1988 |pmid= 2845977 |doi= }}
*{{cite journal | author=Ye RD, Wun TC, Sadler JE |title=cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta. |journal=J. Biol. Chem. |volume=262 |issue= 8 |pages= 3718-25 |year= 1987 |pmid= 3029122 |doi= }}
*{{cite journal | author=Antalis TM, Clark MA, Barnes T, ''et al.'' |title=Cloning and expression of a cDNA coding for a human monocyte-derived plasminogen activator inhibitor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 4 |pages= 985-9 |year= 1988 |pmid= 3257578 |doi= }}
*{{cite journal | author=Schleuning WD, Medcalf RL, Hession C, ''et al.'' |title=Plasminogen activator inhibitor 2: regulation of gene transcription during phorbol ester-mediated differentiation of U-937 human histiocytic lymphoma cells. |journal=Mol. Cell. Biol. |volume=7 |issue= 12 |pages= 4564-7 |year= 1988 |pmid= 3325828 |doi= }}
*{{cite journal | author=Webb AC, Collins KL, Snyder SE, ''et al.'' |title=Human monocyte Arg-Serpin cDNA. Sequence, chromosomal assignment, and homology to plasminogen activator-inhibitor. |journal=J. Exp. Med. |volume=166 |issue= 1 |pages= 77-94 |year= 1987 |pmid= 3496414 |doi= }}
*{{cite journal | author=Dickinson JL, Bates EJ, Ferrante A, Antalis TM |title=Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor alpha-induced apoptosis. Evidence for an alternate biological function. |journal=J. Biol. Chem. |volume=270 |issue= 46 |pages= 27894-904 |year= 1996 |pmid= 7499264 |doi= }}
*{{cite journal | author=Mikus P, Urano T, Liljeström P, Ny T |title=Plasminogen-activator inhibitor type 2 (PAI-2) is a spontaneously polymerising SERPIN. Biochemical characterisation of the recombinant intracellular and extracellular forms. |journal=Eur. J. Biochem. |volume=218 |issue= 3 |pages= 1071-82 |year= 1994 |pmid= 7506655 |doi= }}
*{{cite journal | author=Jensen PJ, Wu Q, Janowitz P, ''et al.'' |title=Plasminogen activator inhibitor type 2: an intracellular keratinocyte differentiation product that is incorporated into the cornified envelope. |journal=Exp. Cell Res. |volume=217 |issue= 1 |pages= 65-71 |year= 1995 |pmid= 7867722 |doi= 10.1006/excr.1995.1064 }}
*{{cite journal | author=Akiyama H, Ikeda K, Kondo H, ''et al.'' |title=Microglia express the type 2 plasminogen activator inhibitor in the brain of control subjects and patients with Alzheimer's disease. |journal=Neurosci. Lett. |volume=164 |issue= 1-2 |pages= 233-5 |year= 1994 |pmid= 8152607 |doi= }}
*{{cite journal | author=Ragno P, Montuori N, Vassalli JD, Rossi G |title=Processing of complex between urokinase and its type-2 inhibitor on the cell surface. A possible regulatory mechanism of urokinase activity. |journal=FEBS Lett. |volume=323 |issue= 3 |pages= 279-84 |year= 1993 |pmid= 8388810 |doi= }}
*{{cite journal | author=Bartuski AJ, Kamachi Y, Schick C, ''et al.'' |title=Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3. |journal=Genomics |volume=43 |issue= 3 |pages= 321-8 |year= 1997 |pmid= 9268635 |doi= 10.1006/geno.1997.4827 }}
*{{cite journal | author=Mahony D, Stringer BW, Dickinson JL, Antalis TM |title=DNase I hypersensitive sites in the 5' flanking region of the human plasminogen activator inhibitor type 2 (PAI-2) gene are associated with basal and tumor necrosis factor-alpha-induced transcription in monocytes. |journal=Eur. J. Biochem. |volume=256 |issue= 3 |pages= 550-9 |year= 1998 |pmid= 9780231 |doi= }}
*{{cite journal | author=Nishida Y, Hayashi Y, Imai Y, Itoh H |title=Expression and localization of the urokinase-type plasminogen activator receptor (uPAR) in the human placenta. |journal=The Kobe journal of medical sciences |volume=44 |issue= 1 |pages= 31-43 |year= 1999 |pmid= 9846056 |doi= }}
}}
{{refend}}
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end log.