Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory protein alpha-2) (Sirp-alpha-2) (Signal-regulatory protein alpha-3) (Sirp-alpha-3) (p84) (CD antigen CD172a)

 SHPS1_HUMAN             Reviewed;         504 AA.
P78324; A2A2E1; A8K411; B2R6C3; O00683; O43799; Q8N517; Q8TAL8;
Q9H0Z2; Q9UDX2; Q9UIJ6; Q9Y4U9;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 2.
25-OCT-2017, entry version 183.
RecName: Full=Tyrosine-protein phosphatase non-receptor type substrate 1;
Short=SHP substrate 1;
Short=SHPS-1;
AltName: Full=Brain Ig-like molecule with tyrosine-based activation motifs;
Short=Bit;
AltName: Full=CD172 antigen-like family member A;
AltName: Full=Inhibitory receptor SHPS-1;
AltName: Full=Macrophage fusion receptor;
AltName: Full=MyD-1 antigen;
AltName: Full=Signal-regulatory protein alpha-1;
Short=Sirp-alpha-1;
AltName: Full=Signal-regulatory protein alpha-2;
Short=Sirp-alpha-2;
AltName: Full=Signal-regulatory protein alpha-3;
Short=Sirp-alpha-3;
AltName: Full=p84;
AltName: CD_antigen=CD172a;
Flags: Precursor;
Name=SIRPA; Synonyms=BIT, MFR, MYD1, PTPNS1, SHPS1, SIRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-44; SER-50;
ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96; GLU-100; SER-107;
SER-109 AND THR-132.
TISSUE=Brain;
PubMed=9070220; DOI=10.1006/bbrc.1996.6047;
Yamao T., Matozaki T., Amano K., Matsuda Y., Takahashi N., Ochi F.,
Fujioka Y., Kasuga M.;
"Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal
localization of genes.";
Biochem. Biophys. Res. Commun. 231:61-67(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, PHOSPHORYLATION,
GLYCOSYLATION, INTERACTION WITH PTPN11; PTPN6 AND GRB2, AND VARIANTS
SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96;
GLU-100; SER-107; SER-109 AND THR-132.
TISSUE=Placenta;
PubMed=9062191; DOI=10.1038/386181a0;
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J.,
Ullrich A.;
"A family of proteins that inhibit signalling through tyrosine kinase
receptors.";
Nature 386:181-186(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10585853; DOI=10.1042/bj3440667;
Sano S., Ohnishi H., Kubota M.;
"Gene structure of mouse BIT/SHPS-1.";
Biochem. J. 344:667-675(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95; SER-96;
GLU-100; SER-107; SER-109 AND THR-132.
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS SER-44; SER-50; ILE-52; HIS-54; VAL-57; ALA-75; GLU-95;
SER-96; GLU-100; SER-107; SER-109 AND THR-132.
TISSUE=Brain, Kidney, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-504.
TISSUE=Monocyte;
PubMed=9485180;
DOI=10.1002/(SICI)1521-4141(199801)28:01<1::AID-IMMU1>3.3.CO;2-M;
Brooke G.P., Parsons K.R., Howard C.J.;
"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. 28:1-11(1998).
[8]
FUNCTION, AND INTERACTION WITH FYB1; SCAP2 AND PTK2B.
PubMed=10469599; DOI=10.1016/S0960-9822(99)80401-1;
Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
Schraven B., Neel B.G.;
"SHPS-1 is a scaffold for assembling distinct adhesion-regulated
multi-protein complexes in macrophages.";
Curr. Biol. 9:927-930(1999).
[9]
PHOSPHORYLATION BY JAK2, AND INTERACTION WITH PTPN11 AND JAK2.
PubMed=10842184; DOI=10.1074/jbc.M004238200;
Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C.;
"Negative regulation of growth hormone receptor/JAK2 signaling by
signal regulatory protein alpha.";
J. Biol. Chem. 275:28222-28229(2000).
[10]
FUNCTION, AND INTERACTION WITH CD47.
PubMed=11509594; DOI=10.4049/jimmunol.167.5.2547;
Latour S., Tanaka H., Demeure C., Mateo V., Rubio M., Brown E.J.,
Maliszewski C., Lindberg F.P., Oldenborg A., Ullrich A.,
Delespesse G., Sarfati M.;
"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. 167:2547-2554(2001).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-245.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-292.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-496, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-149, AND DISULFIDE BOND.
PubMed=17369261; DOI=10.1074/jbc.M611511200;
Hatherley D., Harlos K., Dunlop D.C., Stuart D.I., Barclay A.N.;
"The structure of the macrophage signal regulatory protein alpha
(SIRPalpha) inhibitory receptor reveals a binding face reminiscent of
that used by T cell receptors.";
J. Biol. Chem. 282:14567-14575(2007).
[16]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-149 IN COMPLEX WITH CD47,
AND DISULFIDE BOND.
PubMed=18657508; DOI=10.1016/j.molcel.2008.05.026;
Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I.,
Barclay A.N.;
"Paired receptor specificity explained by structures of signal
regulatory proteins alone and complexed with CD47.";
Mol. Cell 31:266-277(2008).
-!- FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts
as docking protein and induces translocation of PTPN6, PTPN11 and
other binding partners from the cytosol to the plasma membrane.
Supports adhesion of cerebellar neurons, neurite outgrowth and
glial cell attachment. May play a key role in intracellular
signaling during synaptogenesis and in synaptic function (By
similarity). Involved in the negative regulation of receptor
tyrosine kinase-coupled cellular responses induced by cell
adhesion, growth factors or insulin. Mediates negative regulation
of phagocytosis, mast cell activation and dendritic cell
activation. CD47 binding prevents maturation of immature dendritic
cells and inhibits cytokine production by mature dendritic cells.
{ECO:0000250, ECO:0000269|PubMed:10469599,
ECO:0000269|PubMed:11509594}.
-!- SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in
macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro.
Binds FGR (By similarity). Binds JAK2 irrespective of its
phosphorylation status and forms a stable complex. Binds SCAP1
and/or SCAP2. The resulting complex recruits FYB1. Binds PTK2B.
{ECO:0000250, ECO:0000269|PubMed:18657508}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P78324-1; Sequence=Displayed;
Name=2;
IsoId=P78324-2; Sequence=VSP_007030;
Note=No experimental confirmation available.;
Name=4;
IsoId=P78324-4; Sequence=VSP_040799;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain.
Detected on myeloid cells, but not T-cells. Detected at lower
levels in heart, placenta, lung, testis, ovary, colon, liver,
small intestine, prostate, spleen, kidney, skeletal muscle and
pancreas.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9062191}.
-!- PTM: Phosphorylated on tyrosine residues in response to
stimulation with EGF, growth hormone, insulin and PDGF.
Dephosphorylated by PTPN11. {ECO:0000269|PubMed:10842184,
ECO:0000269|PubMed:9062191}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D86043; BAA12974.1; -; mRNA.
EMBL; Y10375; CAA71403.1; -; mRNA.
EMBL; AB023430; BAA87929.1; -; mRNA.
EMBL; AK290776; BAF83465.1; -; mRNA.
EMBL; AK312521; BAG35420.1; -; mRNA.
EMBL; AL034562; CAB38874.2; -; Genomic_DNA.
EMBL; AL034562; CAM28287.1; -; Genomic_DNA.
EMBL; AL117335; CAM28287.1; JOINED; Genomic_DNA.
EMBL; AL117335; CAC12723.2; -; Genomic_DNA.
EMBL; AL117335; CAM28335.1; -; Genomic_DNA.
EMBL; AL034562; CAM28335.1; JOINED; Genomic_DNA.
EMBL; BC026692; AAH26692.1; -; mRNA.
EMBL; BC033092; AAH33092.1; -; mRNA.
EMBL; BC038510; AAH38510.1; -; mRNA.
EMBL; BC075849; AAH75849.1; -; mRNA.
EMBL; Y11047; CAA71944.1; -; mRNA.
CCDS; CCDS13022.1; -. [P78324-1]
CCDS; CCDS82593.1; -. [P78324-2]
PIR; JC5287; JC5287.
RefSeq; NP_001035111.1; NM_001040022.1. [P78324-1]
RefSeq; NP_001035112.1; NM_001040023.1. [P78324-1]
RefSeq; NP_001317657.1; NM_001330728.1. [P78324-2]
RefSeq; NP_542970.1; NM_080792.2. [P78324-1]
RefSeq; XP_005260727.1; XM_005260670.3. [P78324-2]
UniGene; Hs.581021; -.
PDB; 2JJS; X-ray; 1.85 A; A/B=31-149.
PDB; 2JJT; X-ray; 2.30 A; A/B=31-149.
PDB; 2UV3; X-ray; 1.80 A; A/B=31-149.
PDB; 2WNG; X-ray; 2.49 A; A=31-350.
PDB; 4CMM; X-ray; 1.92 A; A=31-149.
PDBsum; 2JJS; -.
PDBsum; 2JJT; -.
PDBsum; 2UV3; -.
PDBsum; 2WNG; -.
PDBsum; 4CMM; -.
ProteinModelPortal; P78324; -.
SMR; P78324; -.
BioGrid; 126752; 16.
IntAct; P78324; 7.
MINT; MINT-5004422; -.
STRING; 9606.ENSP00000348307; -.
iPTMnet; P78324; -.
PhosphoSitePlus; P78324; -.
UniCarbKB; P78324; -.
BioMuta; SIRPA; -.
DMDM; 327478534; -.
EPD; P78324; -.
MaxQB; P78324; -.
PaxDb; P78324; -.
PeptideAtlas; P78324; -.
PRIDE; P78324; -.
DNASU; 140885; -.
Ensembl; ENST00000356025; ENSP00000348307; ENSG00000198053. [P78324-1]
Ensembl; ENST00000358771; ENSP00000351621; ENSG00000198053. [P78324-1]
Ensembl; ENST00000400068; ENSP00000382941; ENSG00000198053. [P78324-1]
Ensembl; ENST00000622179; ENSP00000478763; ENSG00000198053. [P78324-2]
GeneID; 140885; -.
KEGG; hsa:140885; -.
UCSC; uc002wfq.3; human. [P78324-1]
CTD; 140885; -.
DisGeNET; 140885; -.
EuPathDB; HostDB:ENSG00000198053.11; -.
GeneCards; SIRPA; -.
HGNC; HGNC:9662; SIRPA.
HPA; CAB002776; -.
HPA; CAB015122; -.
HPA; HPA054437; -.
HPA; HPA058511; -.
MIM; 602461; gene.
neXtProt; NX_P78324; -.
OpenTargets; ENSG00000198053; -.
PharmGKB; PA34006; -.
eggNOG; ENOG410IKYM; Eukaryota.
eggNOG; ENOG410YKK2; LUCA.
GeneTree; ENSGT00440000033339; -.
HOVERGEN; HBG056632; -.
InParanoid; P78324; -.
KO; K06551; -.
OMA; RAAEPNN; -.
OrthoDB; EOG091G05RP; -.
PhylomeDB; P78324; -.
TreeFam; TF341862; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-391160; Signal regulatory protein family interactions.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P78324; -.
SIGNOR; P78324; -.
ChiTaRS; SIRPA; human.
EvolutionaryTrace; P78324; -.
GeneWiki; Signal-regulatory_protein_alpha; -.
GenomeRNAi; 140885; -.
PRO; PR:P78324; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000198053; -.
Genevisible; P78324; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07654; C1-set; 2.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00407; IGc1; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; SH3-binding; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 504 Tyrosine-protein phosphatase non-receptor
type substrate 1.
/FTId=PRO_0000014941.
TOPO_DOM 31 373 Extracellular. {ECO:0000255}.
TRANSMEM 374 394 Helical. {ECO:0000255}.
TOPO_DOM 395 504 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 137 Ig-like V-type.
DOMAIN 148 247 Ig-like C1-type 1.
DOMAIN 254 348 Ig-like C1-type 2.
MOTIF 429 432 SH2-binding. {ECO:0000255}.
MOTIF 439 444 SH3-binding. {ECO:0000255}.
MOTIF 453 456 SH2-binding. {ECO:0000255}.
MOTIF 470 473 SH2-binding. {ECO:0000255}.
MOTIF 496 499 SH2-binding. {ECO:0000255}.
MOD_RES 429 429 Phosphotyrosine; by Tyr-kinases.
{ECO:0000255}.
MOD_RES 453 453 Phosphotyrosine; by Tyr-kinases.
{ECO:0000255}.
MOD_RES 470 470 Phosphotyrosine; by Tyr-kinases.
{ECO:0000250|UniProtKB:P97710}.
MOD_RES 496 496 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 121 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17369261,
ECO:0000269|PubMed:18657508}.
DISULFID 170 228 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 273 331 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 130 130 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_040799.
VAR_SEQ 422 422 Q -> QVQSL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007030.
VARIANT 6 7 PA -> RS.
/FTId=VAR_015462.
VARIANT 20 20 A -> P.
/FTId=VAR_015463.
VARIANT 40 40 D -> E.
/FTId=VAR_015464.
VARIANT 44 44 L -> S (in dbSNP:rs143735290).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015465.
VARIANT 50 50 T -> S (in dbSNP:rs17855609).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015466.
VARIANT 52 52 T -> I (in dbSNP:rs17855610).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015468.
VARIANT 54 54 R -> H (in dbSNP:rs17855611).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015470.
VARIANT 57 57 A -> V (in dbSNP:rs17855612).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015471.
VARIANT 61 61 I -> N.
/FTId=VAR_015472.
VARIANT 68 68 W -> R.
/FTId=VAR_015473.
VARIANT 75 75 G -> A (in dbSNP:rs1057114).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015474.
VARIANT 77 77 E -> K.
/FTId=VAR_015475.
VARIANT 81 81 N -> H.
/FTId=VAR_015477.
VARIANT 95 95 D -> E (in dbSNP:rs138283486).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015478.
VARIANT 96 96 L -> S. {ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015479.
VARIANT 100 100 N -> E (requires 2 nucleotide
substitutions; dbSNP:rs386811662).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015480.
VARIANT 107 107 R -> S (in dbSNP:rs17855615).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015483.
VARIANT 109 109 G -> S (in dbSNP:rs17855616).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015484.
VARIANT 125 125 R -> Q (in dbSNP:rs767136065).
/FTId=VAR_015485.
VARIANT 132 132 V -> T (requires 2 nucleotide
substitutions; dbSNP:rs386811663).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9062191,
ECO:0000269|PubMed:9070220}.
/FTId=VAR_015486.
VARIANT 134 134 F -> L.
/FTId=VAR_015487.
VARIANT 163 163 Q -> D (requires 2 nucleotide
substitutions).
/FTId=VAR_015488.
VARIANT 181 181 T -> S.
/FTId=VAR_015489.
VARIANT 190 190 E -> Q.
/FTId=VAR_015490.
VARIANT 201 202 VG -> AR.
/FTId=VAR_015491.
VARIANT 214 214 K -> N.
/FTId=VAR_015492.
VARIANT 220 220 E -> G.
/FTId=VAR_015493.
VARIANT 222 222 V -> I (in dbSNP:rs143385810).
/FTId=VAR_015494.
VARIANT 236 236 Q -> R.
/FTId=VAR_015495.
VARIANT 239 240 PL -> SF.
/FTId=VAR_015496.
VARIANT 251 251 R -> Q (in dbSNP:rs377448893).
/FTId=VAR_015497.
VARIANT 261 261 Q -> L.
/FTId=VAR_015498.
VARIANT 263 263 V -> M (in dbSNP:rs754806675).
/FTId=VAR_015499.
VARIANT 271 271 V -> I.
/FTId=VAR_015500.
VARIANT 276 276 R -> T.
/FTId=VAR_015501.
VARIANT 302 302 V -> L (in dbSNP:rs2422666).
/FTId=VAR_015502.
VARIANT 339 339 P -> S.
/FTId=VAR_015503.
VARIANT 353 353 P -> L (in dbSNP:rs138876160).
/FTId=VAR_015504.
VARIANT 357 357 G -> S.
/FTId=VAR_015505.
VARIANT 367 367 S -> P.
/FTId=VAR_015506.
VARIANT 370 370 R -> Q (in dbSNP:rs778218860).
/FTId=VAR_015507.
VARIANT 389 389 A -> E.
/FTId=VAR_015508.
VARIANT 443 443 Q -> R.
/FTId=VAR_015509.
VARIANT 460 460 P -> L.
/FTId=VAR_015510.
VARIANT 486 486 A -> L (requires 2 nucleotide
substitutions).
/FTId=VAR_015511.
VARIANT 491 491 P -> L (in dbSNP:rs367629199).
/FTId=VAR_015512.
CONFLICT 259 259 T -> I (in Ref. 7; CAA71944).
{ECO:0000305}.
CONFLICT 503 503 R -> K (in Ref. 7; CAA71944).
{ECO:0000305}.
STRAND 41 46 {ECO:0000244|PDB:2UV3}.
STRAND 51 53 {ECO:0000244|PDB:2UV3}.
STRAND 56 58 {ECO:0000244|PDB:2UV3}.
STRAND 66 70 {ECO:0000244|PDB:2UV3}.
STRAND 77 85 {ECO:0000244|PDB:2UV3}.
STRAND 90 94 {ECO:0000244|PDB:2UV3}.
STRAND 106 110 {ECO:0000244|PDB:2UV3}.
HELIX 113 115 {ECO:0000244|PDB:2UV3}.
STRAND 117 125 {ECO:0000244|PDB:2UV3}.
STRAND 127 129 {ECO:0000244|PDB:2UV3}.
STRAND 132 136 {ECO:0000244|PDB:2UV3}.
STRAND 140 145 {ECO:0000244|PDB:2UV3}.
STRAND 152 154 {ECO:0000244|PDB:2WNG}.
STRAND 165 178 {ECO:0000244|PDB:2WNG}.
STRAND 181 186 {ECO:0000244|PDB:2WNG}.
STRAND 194 199 {ECO:0000244|PDB:2WNG}.
STRAND 207 216 {ECO:0000244|PDB:2WNG}.
HELIX 221 223 {ECO:0000244|PDB:2WNG}.
STRAND 225 231 {ECO:0000244|PDB:2WNG}.
STRAND 240 245 {ECO:0000244|PDB:2WNG}.
HELIX 246 248 {ECO:0000244|PDB:2WNG}.
STRAND 255 261 {ECO:0000244|PDB:2WNG}.
STRAND 269 281 {ECO:0000244|PDB:2WNG}.
STRAND 283 289 {ECO:0000244|PDB:2WNG}.
STRAND 292 298 {ECO:0000244|PDB:2WNG}.
STRAND 310 318 {ECO:0000244|PDB:2WNG}.
STRAND 328 335 {ECO:0000244|PDB:2WNG}.
STRAND 341 346 {ECO:0000244|PDB:2WNG}.
SEQUENCE 504 AA; 54967 MW; 18D2FD04F6182AD0 CRC64;
MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET ATLRCTATSL
IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN NMDFSIRIGN ITPADAGTYY
CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA PVVSGPAARA TPQHTVSFTC ESHGFSPRDI
TLKWFKNGNE LSDFQTNVDP VGESVSYSIH STAKVVLTRE DVHSQVICEV AHVTLQGDPL
RGTANLSETI RVPPTLEVTQ QPVRAENQVN VTCQVRKFYP QRLQLTWLEN GNVSRTETAS
TVTENKDGTY NWMSWLLVNV SAHRDDVKLT CQVEHDGQPA VSKSHDLKVS AHPKEQGSNT
AAENTGSNER NIYIVVGVVC TLLVALLMAA LYLVRIRQKK AQGSTSSTRL HEPEKNAREI
TQDTNDITYA DLNLPKGKKP APQAAEPNNH TEYASIQTSP QPASEDTLTY ADLDMVHLNR
TPKQPAPKPE PSFSEYASVQ VPRK


Related products :

Catalog number Product name Quantity
EIAAB38325 Bos taurus,Bovine,CD172 antigen-like family member A,Inhibitory receptor SHPS-1,MYD1,MyD-1 antigen,PTPNS1,SHP substrate 1,SHPS1,SHPS-1,Signal-regulatory protein alpha-1,SIRP,SIRPA,Sirp-alpha-1,Tyrosin
18-661-15013 Tyrosine-protein phosphatase non-receptor type substrate 1 - SHP substrate 1; SHPS-1; Inhibitory receptor SHPS-1; Signal-regulatory protein alpha-1; Sirp-alpha-1; Sirp-alpha-2; Sirp-alpha-3; MyD-1 ant 0.1 mg
15-288-21487 Tyrosine-protein phosphatase non-receptor type substrate 1 - SHP substrate 1; SHPS-1; Inhibitory receptor SHPS-1; Signal-regulatory protein alpha-1; Sirp-alpha-1; Sirp-alpha-2; Sirp-alpha-3; MyD-1 ant 0.05 mg
15-288-21487 Tyrosine-protein phosphatase non-receptor type substrate 1 - SHP substrate 1; SHPS-1; Inhibitory receptor SHPS-1; Signal-regulatory protein alpha-1; Sirp-alpha-1; Sirp-alpha-2; Sirp-alpha-3; MyD-1 ant 0.1 mg
EIAAB38323 Bit,Bit,Brain Ig-like molecule with tyrosine-based activation motifs,CD172 antigen-like family member A,Inhibitory receptor SHPS-1,Macrophage fusion receptor,Macrophage membrane protein MFP150,Mfr,Ptp
EIAAB38503 CD172 antigen-like family member B,Homo sapiens,Human,Signal-regulatory protein beta-2,Signal-regulatory protein gamma,SIRPB2,SIRP-b2,SIRP-beta-2,SIRPG,SIRP-gamma
EIAAB38326 Bit,BIT,Brain Ig-like molecule with tyrosine-based activation motifs,CD172 antigen-like family member A,Homo sapiens,Human,Inhibitory receptor SHPS-1,Macrophage fusion receptor,MFR,MYD1,MyD-1 antigen,
EIAAB38324 Bit,Bit,Brain Ig-like molecule with tyrosine-based activation motifs,CD172 antigen-like family member A,Inhibitory receptor SHPS-1,Mouse,mSIRP-alpha1,Mus musculus,Myd1,MyD-1 antigen,p84,Ptpns1,SHP sub
EIAAB38502 Homo sapiens,Human,Protein tyrosine phosphatase non-receptor type substrate 1-like 2,PTPNS1L2,Signal-regulatory protein delta,SIRPD,SIRP-delta
EIAAB38499 CD172 antigen-like family member B,Homo sapiens,Human,Signal-regulatory protein beta-1,SIRPB1,SIRP-beta-1
EIAAB38500 Homo sapiens,Human,Protein tyrosine phosphatase non-receptor type substrate 1-like 3,Protein tyrosine phosphatase non-receptor type substrate protein,PTPN1L,PTPNS1L3,Signal-regulatory protein beta-2,S
T-3002.0250 CD172a _ Clone OX41 Signal Regulatory Protein; SIRP 250
T-3002.0250 CD172a _ Clone OX41 Signal Regulatory Protein; SIRP 250ìg
YSRTMCA274B CD172a, SIRP (Signal Regulatory Protein), Clone MRC OX_41, Mab anti_Rat, Biotin 0.1 mg.
YSRTMCA274PE Rat OX_41 Antigen, SIRP (Signal Regulatory Protein), Clone MRC OX_41, Mab anti_, RPE 100 tests
E0954h ELISA kit Homo sapiens,Human,Protein-tyrosine phosphatase alpha,PTPA,PTPRA,PTPRL2,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
E0954h ELISA Homo sapiens,Human,Protein-tyrosine phosphatase alpha,PTPA,PTPRA,PTPRL2,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
U0954h CLIA Homo sapiens,Human,Protein-tyrosine phosphatase alpha,PTPA,PTPRA,PTPRL2,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
YSRTMCA274F Rat OX_41 Antigen, SIRP (Signal Regulatory Protein), Clone MRC OX_41, Mab anti_, FITC 0.1 mg.
U0954m CLIA LCA-related phosphatase,Lrp,Mouse,Mus musculus,Protein-tyrosine phosphatase alpha,Ptpa,Ptpra,PTPTY-28,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
E0954m ELISA kit LCA-related phosphatase,Lrp,Mouse,Mus musculus,Protein-tyrosine phosphatase alpha,Ptpa,Ptpra,PTPTY-28,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
E0954m ELISA LCA-related phosphatase,Lrp,Mouse,Mus musculus,Protein-tyrosine phosphatase alpha,Ptpa,Ptpra,PTPTY-28,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
YSRTMCA274R Rat OX_41 Antigen, SIRP (Signal Regulatory Protein), Clone MRC OX_41, Mab anti_; frozen_paraffin, IH_flow_WB 0.25 mg.
YSRTMCA274G Rat OX_41 Antigen, SIRP (Signal Regulatory Protein), Clone MRC OX_41, Mab anti_; frozen_paraffin, IH_flow_WB 1 mg.
YSRTMCA274GA Rat OX_41 Antigen, SIRP (Signal Regulatory Protein), Clone MRC OX_41, Mab anti_; frozen_paraffin, IH_flow_WB 0.1 mg.


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur