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IGBP1

From Wikipedia, the free encyclopedia
IGBP1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIGBP1, ALPHA-4, IBP1, immunoglobulin (CD79A) binding protein 1, immunoglobulin binding protein 1, alpha4, MRXS28
External IDsOMIM: 300139; MGI: 1346500; HomoloGene: 44067; GeneCards: IGBP1; OMA:IGBP1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001551
NM_001370192
NM_001370193
NM_001370194

NM_008784

RefSeq (protein)

NP_001542
NP_001357121
NP_001357122
NP_001357123

NP_032810

Location (UCSC)Chr X: 70.13 – 70.17 MbChr X: 99.54 – 99.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Immunoglobulin-binding protein 1 is a protein that in humans is encoded by the IGBP1 gene.[5][6]

Function

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The proliferation and differentiation of B cells is dependent upon a B-cell antigen receptor (BCR) complex. Binding of antigens to specific B-cell receptors results in a tyrosine phosphorylation reaction through the BCR complex and leads to multiple signal transduction pathways.[6]

Interactions

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IGBP1 has been shown to interact with PPP4C,[7][8][9] PPP6C[8][9] and PPP2CA.[8][9][10][11]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000089289Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031221Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Onda M, Inui S, Maeda K, Suzuki M, Takahashi E, Sakaguchi N (Dec 1997). "Expression and chromosomal localization of the human alpha 4/IGBP1 gene, the structure of which is closely related to the yeast TAP42 protein of the rapamycin-sensitive signal transduction pathway". Genomics. 46 (3): 373–8. doi:10.1006/geno.1997.5048. PMID 9441740.
  6. ^ a b "Entrez Gene: IGBP1 immunoglobulin (CD79A) binding protein 1".
  7. ^ Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (Oct 2008). "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. 283 (43): 29273–84. doi:10.1074/jbc.M803443200. PMC 2662017. PMID 18715871.
  8. ^ a b c Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (Nov 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics. 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932. S2CID 7531012.
  9. ^ a b c Chen J, Peterson RT, Schreiber SL (Jun 1998). "Alpha 4 associates with protein phosphatases 2A, 4, and 6". Biochemical and Biophysical Research Communications. 247 (3): 827–32. doi:10.1006/bbrc.1998.8792. PMID 9647778.
  10. ^ Goudreault M, D'Ambrosio LM, Kean MJ, Mullin MJ, Larsen BG, Sanchez A, Chaudhry S, Chen GI, Sicheri F, Nesvizhskii AI, Aebersold R, Raught B, Gingras AC (Jan 2009). "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein". Molecular & Cellular Proteomics. 8 (1): 157–71. doi:10.1074/mcp.M800266-MCP200. PMC 2621004. PMID 18782753.
  11. ^ Chung H, Nairn AC, Murata K, Brautigan DL (Aug 1999). "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2". Biochemistry. 38 (32): 10371–6. doi:10.1021/bi990902g. PMID 10441131.

Further reading

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