Signal-regulatory protein alpha
From Wikipedia, the free encyclopedia
|
Signal-regulatory protein alpha
|
|||||||||||
| Identifiers | |||||||||||
| Symbol(s) | SIRPA; P84; BIT; CD172A; MFR; MYD-1; PTPNS1; SHPS-1; SHPS1; SIRP; SIRP-ALPHA-1; SIRPalpha; SIRPalpha2 | ||||||||||
| External IDs | OMIM: 602461 MGI: 108563 HomoloGene: 7246 | ||||||||||
|
|||||||||||
| RNA expression pattern | |||||||||||
|
|
|||||||||||
| Orthologs | |||||||||||
| Human | Mouse | ||||||||||
| Entrez | 140885 | 19261 | |||||||||
| Ensembl | ENSG00000198053 | ENSMUSG00000037902 | |||||||||
| Uniprot | P78324 | P97797 | |||||||||
| Refseq | NM_001040022 (mRNA) NP_001035111 (protein) |
NM_007547 (mRNA) NP_031573 (protein) |
|||||||||
| Location | Chr 20: 1.82 - 1.87 Mb | Chr 2: 129.28 - 129.32 Mb | |||||||||
| Pubmed search | [1] | [2] | |||||||||
Signal-regulatory protein alpha, also known as SIRPA, is a human gene.[1] SIRPA has also recently been designated CD172A (cluster of differentiation 172A).
The protein encoded by this gene is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. This protein can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and serve as substrates of PTPs. This protein was found to participate in signal transduction mediated by various growth factor receptors. CD47 has been demonstrated to be a ligand for this receptor protein. This gene and its product share very high similarity with several other members of the SIRP family. These related genes are located in close proximity to each other on chromosome 20p13. Multiple alternatively spliced transcript variants have been determined for this gene.[1]
[edit] References
[edit] Further reading
- Oldenborg PA (2004). "Role of CD47 in erythroid cells and in autoimmunity.". Leuk. Lymphoma 45 (7): 1319–27. doi:. PMID 15359629.
- Margolis RL, Breschel TS, Li SH, et al. (1996). "Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain.". Somat. Cell Mol. Genet. 21 (4): 279–84. PMID 8525433.
- Ohnishi H, Kubota M, Ohtake A, et al. (1996). "Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule.". J. Biol. Chem. 271 (41): 25569–74. PMID 8810330.
- Fujioka Y, Matozaki T, Noguchi T, et al. (1997). "A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion.". Mol. Cell. Biol. 16 (12): 6887–99. PMID 8943344.
- Kharitonenkov A, Chen Z, Sures I, et al. (1997). "A family of proteins that inhibit signalling through tyrosine kinase receptors.". Nature 386 (6621): 181–6. doi:. PMID 9062191.
- Yamao T, Matozaki T, Amano K, et al. (1997). "Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes.". Biochem. Biophys. Res. Commun. 231 (1): 61–7. doi:. PMID 9070220.
- Sano S, Ohnishi H, Omori A, et al. (1997). "BIT, an immune antigen receptor-like molecule in the brain.". FEBS Lett. 411 (2-3): 327–34. PMID 9271230.
- Brooke GP, Parsons KR, Howard CJ (1998). "Cloning of two members of the SIRP alpha family of protein tyrosine phosphatase binding proteins in cattle that are expressed on monocytes and a subpopulation of dendritic cells and which mediate binding to CD4 T cells.". Eur. J. Immunol. 28 (1): 1–11. PMID 9485180.
- Timms JF, Carlberg K, Gu H, et al. (1998). "Identification of major binding proteins and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophages.". Mol. Cell. Biol. 18 (7): 3838–50. PMID 9632768.
- Veillette A, Thibaudeau E, Latour S (1998). "High expression of inhibitory receptor SHPS-1 and its association with protein-tyrosine phosphatase SHP-1 in macrophages.". J. Biol. Chem. 273 (35): 22719–28. PMID 9712903.
- Jiang P, Lagenaur CF, Narayanan V (1999). "Integrin-associated protein is a ligand for the P84 neural adhesion molecule.". J. Biol. Chem. 274 (2): 559–62. PMID 9872987.
- Ohnishi H, Yamada M, Kubota M, et al. (1999). "Tyrosine phosphorylation and association of BIT with SHP-2 induced by neurotrophins.". J. Neurochem. 72 (4): 1402–8. PMID 10098842.
- Timms JF, Swanson KD, Marie-Cardine A, et al. (1999). "SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages.". Curr. Biol. 9 (16): 927–30. PMID 10469599.
- Seiffert M, Cant C, Chen Z, et al. (1999). "Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47.". Blood 94 (11): 3633–43. PMID 10572074.
- Sano S, Ohnishi H, Kubota M (2000). "Gene structure of mouse BIT/SHPS-1.". Biochem. J. 344 Pt 3: 667–75. PMID 10585853.
- Yang J, Cheng Z, Niu T, et al. (2000). "Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1.". J. Biol. Chem. 275 (6): 4066–71. PMID 10660565.
- Stofega MR, Argetsinger LS, Wang H, et al. (2000). "Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha.". J. Biol. Chem. 275 (36): 28222–9. doi:. PMID 10842184.
- Wu CJ, Chen Z, Ullrich A, et al. (2000). "Inhibition of EGFR-mediated phosphoinositide-3-OH kinase (PI3-K) signaling and glioblastoma phenotype by signal-regulatory proteins (SIRPs).". Oncogene 19 (35): 3999–4010. doi:. PMID 10962556.
- Latour S, Tanaka H, Demeure C, et al. (2001). "Bidirectional negative regulation of human T and dendritic cells by CD47 and its cognate receptor signal-regulator protein-alpha: down-regulation of IL-12 responsiveness and inhibition of dendritic cell activation.". J. Immunol. 167 (5): 2547–54. PMID 11509594.
- Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:. PMID 11780052.
 |
This membrane protein-related article is a stub. You can help Wikipedia by expanding it. |
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
