Signal-regulatory protein alpha

Signal-regulatory protein alpha

Signal-regulatory protein alpha, also known as SIRPA, is a human gene.cite web | title = Entrez Gene: SIRPA signal-regulatory protein alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=140885| accessdate = ] SIRPA has also recently been designated CD172A (cluster of differentiation 172A).

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: SIRPA signal-regulatory protein alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=140885| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Oldenborg PA |title=Role of CD47 in erythroid cells and in autoimmunity. |journal=Leuk. Lymphoma |volume=45 |issue= 7 |pages= 1319–27 |year= 2004 |pmid= 15359629 |doi= 10.1080/1042819042000201989
*cite journal | author=Margolis RL, Breschel TS, Li SH, "et al." |title=Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain. |journal=Somat. Cell Mol. Genet. |volume=21 |issue= 4 |pages= 279–84 |year= 1996 |pmid= 8525433 |doi=
*cite journal | author=Ohnishi H, Kubota M, Ohtake A, "et al." |title=Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25569–74 |year= 1996 |pmid= 8810330 |doi=
*cite journal | author=Fujioka Y, Matozaki T, Noguchi T, "et al." |title=A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion. |journal=Mol. Cell. Biol. |volume=16 |issue= 12 |pages= 6887–99 |year= 1997 |pmid= 8943344 |doi=
*cite journal | author=Kharitonenkov A, Chen Z, Sures I, "et al." |title=A family of proteins that inhibit signalling through tyrosine kinase receptors. |journal=Nature |volume=386 |issue= 6621 |pages= 181–6 |year= 1997 |pmid= 9062191 |doi= 10.1038/386181a0
*cite journal | author=Yamao T, Matozaki T, Amano K, "et al." |title=Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 1 |pages= 61–7 |year= 1997 |pmid= 9070220 |doi= 10.1006/bbrc.1996.6047
*cite journal | author=Sano S, Ohnishi H, Omori A, "et al." |title=BIT, an immune antigen receptor-like molecule in the brain. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 327–34 |year= 1997 |pmid= 9271230 |doi=
*cite journal | author=Brooke GP, Parsons KR, Howard CJ |title=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. |journal=Eur. J. Immunol. |volume=28 |issue= 1 |pages= 1–11 |year= 1998 |pmid= 9485180 |doi=
*cite journal | author=Timms JF, Carlberg K, Gu H, "et al." |title=Identification of major binding proteins and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophages. |journal=Mol. Cell. Biol. |volume=18 |issue= 7 |pages= 3838–50 |year= 1998 |pmid= 9632768 |doi=
*cite journal | author=Veillette A, Thibaudeau E, Latour S |title=High expression of inhibitory receptor SHPS-1 and its association with protein-tyrosine phosphatase SHP-1 in macrophages. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22719–28 |year= 1998 |pmid= 9712903 |doi=
*cite journal | author=Jiang P, Lagenaur CF, Narayanan V |title=Integrin-associated protein is a ligand for the P84 neural adhesion molecule. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 559–62 |year= 1999 |pmid= 9872987 |doi=
*cite journal | author=Ohnishi H, Yamada M, Kubota M, "et al." |title=Tyrosine phosphorylation and association of BIT with SHP-2 induced by neurotrophins. |journal=J. Neurochem. |volume=72 |issue= 4 |pages= 1402–8 |year= 1999 |pmid= 10098842 |doi=
*cite journal | author=Timms JF, Swanson KD, Marie-Cardine A, "et al." |title=SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages. |journal=Curr. Biol. |volume=9 |issue= 16 |pages= 927–30 |year= 1999 |pmid= 10469599 |doi=
*cite journal | author=Seiffert M, Cant C, Chen Z, "et al." |title=Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47. |journal=Blood |volume=94 |issue= 11 |pages= 3633–43 |year= 1999 |pmid= 10572074 |doi=
*cite journal | author=Sano S, Ohnishi H, Kubota M |title=Gene structure of mouse BIT/SHPS-1. |journal=Biochem. J. |volume=344 Pt 3 |issue= |pages= 667–75 |year= 2000 |pmid= 10585853 |doi=
*cite journal | author=Yang J, Cheng Z, Niu T, "et al." |title=Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4066–71 |year= 2000 |pmid= 10660565 |doi=
*cite journal | author=Stofega MR, Argetsinger LS, Wang H, "et al." |title=Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28222–9 |year= 2000 |pmid= 10842184 |doi= 10.1074/jbc.M004238200
*cite journal | author=Wu CJ, Chen Z, Ullrich A, "et al." |title=Inhibition of EGFR-mediated phosphoinositide-3-OH kinase (PI3-K) signaling and glioblastoma phenotype by signal-regulatory proteins (SIRPs). |journal=Oncogene |volume=19 |issue= 35 |pages= 3999–4010 |year= 2000 |pmid= 10962556 |doi= 10.1038/sj.onc.1203748
*cite journal | author=Latour S, Tanaka H, Demeure C, "et al." |title=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. |journal=J. Immunol. |volume=167 |issue= 5 |pages= 2547–54 |year= 2001 |pmid= 11509594 |doi=
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужно решить контрольную?

Look at other dictionaries:

  • Protein kinase A — In cell biology, Protein kinase A (PKA) refers to a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP dependent protein kinase (EC 2.7.11.11). Protein kinase A has several functions… …   Wikipedia

  • Protein kinase — A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). This class of protein may further be separated into subsets as in the case of protein kinase C PKC alpha, PKC beta,… …   Wikipedia

  • Protein tyrosine phosphatase — Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post translational modification that can create novel… …   Wikipedia

  • Protein domain — Pyruvate kinase, a protein from three domains (PDB 1pkn) A protein domain is a part of protein sequence and structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three… …   Wikipedia

  • Peripheral membrane protein — Peripheral membrane proteins are proteins that adhere only temporarily to the biological membrane with which they are associated. These molecules attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The… …   Wikipedia

  • Ras (protein) — Pfam box Symbol = Ras Name = width =250 caption = Triphosphate Structure of H Ras p21 GNBP in complex with GppNHp and Mg2+ (PDB Code 5p21). Important sequence elements are highlighted. Pfam= PF00071 InterPro= IPR013753 SMART= PROSITE = PDOC00859… …   Wikipedia

  • LDL-receptor-related protein associated protein — Low density lipoprotein receptor related protein associated protein 1, also known as LRPAP1, is a human gene.cite web | title = Entrez Gene: LRPAP1 low density lipoprotein receptor related protein associated protein 1| url =… …   Wikipedia

  • Estrogen receptor alpha — Estrogen receptor 1 PDB rendering based on 1a52 …   Wikipedia

  • Retinoid X receptor alpha — Retinoid X receptor, alpha PDB rendering based on 1by4 …   Wikipedia

  • Retinoic acid receptor alpha — Retinoic acid receptor, alpha PDB rendering based on 1dkf …   Wikipedia

Share the article and excerpts

Direct link
… Do a right-click on the link above
and select “Copy Link”