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P78324 (SHPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type substrate 1

Short name=SHP substrate 1
Short name=SHPS-1
Alternative name(s):
Brain Ig-like molecule with tyrosine-based activation motifs
Short name=Bit
CD172 antigen-like family member A
Inhibitory receptor SHPS-1
Macrophage fusion receptor
MyD-1 antigen
Signal-regulatory protein alpha-1
Short name=Sirp-alpha-1
Signal-regulatory protein alpha-2
Short name=Sirp-alpha-2
Signal-regulatory protein alpha-3
Short name=Sirp-alpha-3
p84
CD_antigen=CD172a
Gene names
Name:SIRPA
Synonyms:BIT, MFR, MYD1, PTPNS1, SHPS1, SIRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.10

Subunit structure

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 FYB. Binds PTK2B.

Subcellular location

Membrane; Single-pass type I membrane protein.

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.

Post-translational modification

N-glycosylated. Ref.2

Phosphorylated on tyrosine residues in response to stimulation with EGF, growth hormone, insulin and PDGF. Dephosphorylated by PTPN11. Ref.2 Ref.9

Sequence similarities

Contains 2 Ig-like C1-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78324-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P78324-2)

The sequence of this isoform differs from the canonical sequence as follows:
     422-422: Q → QVQSL
Note: No experimental confirmation available.
Isoform 4 (identifier: P78324-4)

The sequence of this isoform differs from the canonical sequence as follows:
     130-130: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 504474Tyrosine-protein phosphatase non-receptor type substrate 1
PRO_0000014941

Regions

Topological domain31 – 373343Extracellular Potential
Transmembrane374 – 39421Helical; Potential
Topological domain395 – 504110Cytoplasmic Potential
Domain32 – 137106Ig-like V-type
Domain148 – 247100Ig-like C1-type 1
Domain254 – 34895Ig-like C1-type 2
Motif429 – 4324SH2-binding Potential
Motif439 – 4446SH3-binding Potential
Motif453 – 4564SH2-binding Potential
Motif470 – 4734SH2-binding Potential
Motif496 – 4994SH2-binding Potential

Amino acid modifications

Modified residue4291Phosphotyrosine; by Tyr-kinases Potential
Modified residue4531Phosphotyrosine; by Tyr-kinases Potential
Modified residue4701Phosphotyrosine; by Tyr-kinases By similarity
Modified residue4961Phosphotyrosine; by Tyr-kinases By similarity
Glycosylation2451N-linked (GlcNAc...) Ref.11
Glycosylation2701N-linked (GlcNAc...) Ref.12
Glycosylation2921N-linked (GlcNAc...) Ref.12
Glycosylation3191N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 121 Ref.13 Ref.14
Disulfide bond170 ↔ 228 Potential
Disulfide bond273 ↔ 331 Potential

Natural variations

Alternative sequence1301Missing in isoform 4.
VSP_040799
Alternative sequence4221Q → QVQSL in isoform 2.
VSP_007030
Natural variant6 – 72PA → RS.
VAR_015462
Natural variant201A → P.
VAR_015463
Natural variant401D → E.
VAR_015464
Natural variant441L → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs1135193 [ dbSNP | Ensembl ].
VAR_015465
Natural variant501T → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855609 [ dbSNP | Ensembl ].
VAR_015466
Natural variant521T → I. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855610 [ dbSNP | Ensembl ].
VAR_015468
Natural variant541R → H. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855611 [ dbSNP | Ensembl ].
VAR_015470
Natural variant571A → V. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855612 [ dbSNP | Ensembl ].
VAR_015471
Natural variant611I → N.
VAR_015472
Natural variant681W → R.
VAR_015473
Natural variant751G → A. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs1057114 [ dbSNP | Ensembl ].
VAR_015474
Natural variant771E → K.
VAR_015475
Natural variant811N → H.
VAR_015477
Natural variant951D → E. Ref.1 Ref.2 Ref.4 Ref.6
VAR_015478
Natural variant961L → S. Ref.1 Ref.2 Ref.4 Ref.6
VAR_015479
Natural variant1001N → E Requires 2 nucleotide substitutions. Ref.1 Ref.2 Ref.4 Ref.6
VAR_015480
Natural variant1071R → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855615 [ dbSNP | Ensembl ].
VAR_015483
Natural variant1091G → S. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs17855616 [ dbSNP | Ensembl ].
VAR_015484
Natural variant1251R → Q.
VAR_015485
Natural variant1321V → T Requires 2 nucleotide substitutions. Ref.1 Ref.2 Ref.4 Ref.6
VAR_015486
Natural variant1341F → L.
VAR_015487
Natural variant1631Q → D Requires 2 nucleotide substitutions.
VAR_015488
Natural variant1811T → S.
VAR_015489
Natural variant1901E → Q.
VAR_015490
Natural variant201 – 2022VG → AR.
VAR_015491
Natural variant2141K → N.
VAR_015492
Natural variant2201E → G.
VAR_015493
Natural variant2221V → I.
VAR_015494
Natural variant2361Q → R.
VAR_015495
Natural variant239 – 2402PL → SF.
VAR_015496
Natural variant2511R → Q.
VAR_015497
Natural variant2611Q → L.
VAR_015498
Natural variant2631V → M.
VAR_015499
Natural variant2711V → I.
VAR_015500
Natural variant2761R → T.
VAR_015501
Natural variant3021V → L.
Corresponds to variant rs2422666 [ dbSNP | Ensembl ].
VAR_015502
Natural variant3391P → S.
VAR_015503
Natural variant3531P → L.
VAR_015504
Natural variant3571G → S.
VAR_015505
Natural variant3671S → P.
VAR_015506
Natural variant3701R → Q.
VAR_015507
Natural variant3891A → E.
VAR_015508
Natural variant4431Q → R.
VAR_015509
Natural variant4601P → L.
VAR_015510
Natural variant4861A → L Requires 2 nucleotide substitutions.
VAR_015511
Natural variant4911P → L.
VAR_015512

Experimental info

Sequence conflict2591T → I in CAA71944. Ref.7
Sequence conflict5031R → K in CAA71944. Ref.7

Secondary structure

........................................................ 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 5, 2011. Version 2.
Checksum: 18D2FD04F6182AD0

FASTA50454,967
        10         20         30         40         50         60 
MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET ATLRCTATSL 

        70         80         90        100        110        120 
IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN NMDFSIRIGN ITPADAGTYY 

       130        140        150        160        170        180 
CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA PVVSGPAARA TPQHTVSFTC ESHGFSPRDI 

       190        200        210        220        230        240 
TLKWFKNGNE LSDFQTNVDP VGESVSYSIH STAKVVLTRE DVHSQVICEV AHVTLQGDPL 

       250        260        270        280        290        300 
RGTANLSETI RVPPTLEVTQ QPVRAENQVN VTCQVRKFYP QRLQLTWLEN GNVSRTETAS 

       310        320        330        340        350        360 
TVTENKDGTY NWMSWLLVNV SAHRDDVKLT CQVEHDGQPA VSKSHDLKVS AHPKEQGSNT 

       370        380        390        400        410        420 
AAENTGSNER NIYIVVGVVC TLLVALLMAA LYLVRIRQKK AQGSTSSTRL HEPEKNAREI 

       430        440        450        460        470        480 
TQDTNDITYA DLNLPKGKKP APQAAEPNNH TEYASIQTSP QPASEDTLTY ADLDMVHLNR 

       490        500 
TPKQPAPKPE PSFSEYASVQ VPRK 

« Hide

Isoform 2 [UniParc].

Checksum: 098D9B24276FA4E1
Show »

FASTA50855,394
Isoform 4 [UniParc].

Checksum: AB4F162B7FF8D97A
Show »

FASTA50354,852

References

« Hide 'large scale' references
[1]"Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes."
Yamao T., Matozaki T., Amano K., Matsuda Y., Takahashi N., Ochi F., Fujioka Y., Kasuga M.
Biochem. Biophys. Res. Commun. 231:61-67(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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.
[2]"A family of proteins that inhibit signalling through tyrosine kinase receptors."
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.
Nature 386:181-186(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, PHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH PTPN11; PTPN6 AND GRB2, 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.
[3]"Gene structure of mouse BIT/SHPS-1."
Sano S., Ohnishi H., Kubota M.
Biochem. J. 344:667-675(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), 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.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), 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.
[7]"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."
Brooke G.P., Parsons K.R., Howard C.J.
Eur. J. Immunol. 28:1-11(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-504.
Tissue: Monocyte.
[8]"SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages."
Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E., Schraven B., Neel B.G.
Curr. Biol. 9:927-930(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FYB; SCAP2 AND PTK2B.
[9]"Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha."
Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C.
J. Biol. Chem. 275:28222-28229(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY JAK2, INTERACTION WITH PTPN11 AND JAK2.
[10]"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."
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.
J. Immunol. 167:2547-2554(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CD47.
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-245.
Tissue: Plasma.
[12]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-270 AND ASN-292.
Tissue: Liver.
[13]"The structure of the macrophage signal regulatory protein alpha (SIRPalpha) inhibitory receptor reveals a binding face reminiscent of that used by T cell receptors."
Hatherley D., Harlos K., Dunlop D.C., Stuart D.I., Barclay A.N.
J. Biol. Chem. 282:14567-14575(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-149, DISULFIDE BOND.
[14]"Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47."
Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I., Barclay A.N.
Mol. Cell 31:266-277(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-149 IN COMPLEX WITH CD47, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86043 mRNA. Translation: BAA12974.1.
Y10375 mRNA. Translation: CAA71403.1.
AB023430 mRNA. Translation: BAA87929.1.
AK290776 mRNA. Translation: BAF83465.1.
AK312521 mRNA. Translation: BAG35420.1.
AL034562 Genomic DNA. Translation: CAB38874.2.
AL034562, AL117335 Genomic DNA. Translation: CAM28287.1.
AL117335 Genomic DNA. Translation: CAC12723.2.
AL117335, AL034562 Genomic DNA. Translation: CAM28335.1.
BC026692 mRNA. Translation: AAH26692.1.
BC033092 mRNA. Translation: AAH33092.1.
BC038510 mRNA. Translation: AAH38510.1.
BC075849 mRNA. Translation: AAH75849.1.
Y11047 mRNA. Translation: CAA71944.1.
PIRJC5287.
RefSeqNP_001035111.1. NM_001040022.1.
NP_001035112.1. NM_001040023.1.
NP_542970.1. NM_080792.2.
XP_005260726.1. XM_005260669.1.
XP_005260727.1. XM_005260670.1.
UniGeneHs.581021.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JJSX-ray1.85A/B31-149[»]
2JJTX-ray2.30A/B31-149[»]
2UV3X-ray1.80A/B31-149[»]
2WNGX-ray2.49A31-349[»]
4CMMX-ray1.92A31-149[»]
ProteinModelPortalP78324.
SMRP78324. Positions 31-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126752. 7 interactions.
IntActP78324. 5 interactions.
MINTMINT-5004422.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteP78324.

Polymorphism databases

DMDM327478534.

Proteomic databases

PaxDbP78324.
PRIDEP78324.

Protocols and materials databases

DNASU140885.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356025; ENSP00000348307; ENSG00000198053. [P78324-1]
ENST00000358771; ENSP00000351621; ENSG00000198053. [P78324-1]
ENST00000400068; ENSP00000382941; ENSG00000198053. [P78324-2]
GeneID140885.
KEGGhsa:140885.
UCSCuc002wfq.3. human. [P78324-1]
uc002wft.3. human. [P78324-2]

Organism-specific databases

CTD140885.
GeneCardsGC20P001822.
HGNCHGNC:9662. SIRPA.
HPACAB002776.
CAB015122.
MIM602461. gene.
neXtProtNX_P78324.
PharmGKBPA34006.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39917.
HOVERGENHBG056632.
KOK06551.
OMAHEPEKNT.
OrthoDBEOG7CG6ZQ.
PhylomeDBP78324.
TreeFamTF341862.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.
SignaLinkP78324.

Gene expression databases

ArrayExpressP78324.
BgeeP78324.
GenevestigatorP78324.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF07654. C1-set. 2 hits.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00407. IGc1. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIRPA. human.
EvolutionaryTraceP78324.
GeneWikiSignal-regulatory_protein_alpha.
GenomeRNAi140885.
NextBio84534.
PROP78324.
SOURCESearch...

Entry information

Entry nameSHPS1_HUMAN
AccessionPrimary (citable) accession number: P78324
Secondary accession number(s): A2A2E1 expand/collapse secondary AC list , A8K411, B2R6C3, O00683, O43799, Q8N517, Q8TAL8, Q9H0Z2, Q9UDX2, Q9UIJ6, Q9Y4U9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries