Biology:IGBP1

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Immunoglobulin-binding protein 1 is a protein that in humans is encoded by the IGBP1 gene.[1][2]

Function

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.[2]

Interactions

IGBP1 has been shown to interact with PPP4C,[3][4][5] PPP6C[4][5] and PPP2CA.[4][5][6][7]

References

  1. "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. Dec 1997. doi:10.1006/geno.1997.5048. PMID 9441740. 
  2. 2.0 2.1 "Entrez Gene: IGBP1 immunoglobulin (CD79A) binding protein 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3476. 
  3. "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry 283 (43): 29273–84. Oct 2008. doi:10.1074/jbc.M803443200. PMID 18715871. 
  4. 4.0 4.1 4.2 "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics 4 (11): 1725–40. Nov 2005. doi:10.1074/mcp.M500231-MCP200. PMID 16085932. 
  5. 5.0 5.1 5.2 "Alpha 4 associates with protein phosphatases 2A, 4, and 6". Biochemical and Biophysical Research Communications 247 (3): 827–32. Jun 1998. doi:10.1006/bbrc.1998.8792. PMID 9647778. Bibcode1998BBRC..247..827C. 
  6. "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. Jan 2009. doi:10.1074/mcp.M800266-MCP200. PMID 18782753. 
  7. "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. Aug 1999. doi:10.1021/bi990902g. PMID 10441131. 

Further reading