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P78324

- SHPS1_HUMAN

UniProt

P78324 - SHPS1_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type substrate 1

Gene

SIRPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell adhesion Source: ProtInc
  3. leukocyte migration Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinkiP78324.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SIRPA
Synonyms:BIT, MFR, MYD1, PTPNS1, SHPS1, SIRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9662. SIRPA.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: ProtInc
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34006.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 504474Tyrosine-protein phosphatase non-receptor type substrate 1PRO_0000014941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 1212 PublicationsPROSITE-ProRule annotation
Disulfide bondi170 ↔ 228PROSITE-ProRule annotation
Glycosylationi245 – 2451N-linked (GlcNAc...)1 Publication
Glycosylationi270 – 2701N-linked (GlcNAc...)1 Publication
Disulfide bondi273 ↔ 331PROSITE-ProRule annotation
Glycosylationi292 – 2921N-linked (GlcNAc...)1 Publication
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
Modified residuei429 – 4291Phosphotyrosine; by Tyr-kinasesSequence Analysis
Modified residuei453 – 4531Phosphotyrosine; by Tyr-kinasesSequence Analysis
Modified residuei470 – 4701Phosphotyrosine; by Tyr-kinasesBy similarity
Modified residuei496 – 4961Phosphotyrosine; by Tyr-kinasesBy similarity

Post-translational modificationi

N-glycosylated.3 Publications
Phosphorylated on tyrosine residues in response to stimulation with EGF, growth hormone, insulin and PDGF. Dephosphorylated by PTPN11.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP78324.
PaxDbiP78324.
PRIDEiP78324.

PTM databases

PhosphoSiteiP78324.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP78324.
ExpressionAtlasiP78324. baseline and differential.
GenevestigatoriP78324.

Organism-specific databases

HPAiCAB002776.
CAB015122.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi126752. 8 interactions.
IntActiP78324. 5 interactions.
MINTiMINT-5004422.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466
Beta strandi51 – 533
Beta strandi56 – 583
Beta strandi66 – 705
Beta strandi77 – 859
Beta strandi90 – 945
Beta strandi106 – 1105
Helixi113 – 1153
Beta strandi117 – 1259
Beta strandi127 – 1293
Beta strandi132 – 1365
Beta strandi140 – 1456
Beta strandi152 – 1543
Beta strandi165 – 17814
Beta strandi181 – 1866
Beta strandi194 – 1996
Beta strandi207 – 21610
Helixi221 – 2233
Beta strandi225 – 2317
Beta strandi240 – 2456
Helixi246 – 2483
Beta strandi255 – 2617
Beta strandi269 – 28113
Beta strandi283 – 2897
Beta strandi292 – 2987
Beta strandi310 – 3189
Beta strandi328 – 3358
Beta strandi341 – 3466

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JJSX-ray1.85A/B31-149[»]
2JJTX-ray2.30A/B31-149[»]
2UV3X-ray1.80A/B31-149[»]
2WNGX-ray2.49A31-350[»]
4CMMX-ray1.92A31-149[»]
ProteinModelPortaliP78324.
SMRiP78324. Positions 31-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78324.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 373343ExtracellularSequence AnalysisAdd
BLAST
Topological domaini395 – 504110CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei374 – 39421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 137106Ig-like V-typeAdd
BLAST
Domaini148 – 247100Ig-like C1-type 1Add
BLAST
Domaini254 – 34895Ig-like C1-type 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi429 – 4324SH2-bindingSequence Analysis
Motifi439 – 4446SH3-bindingSequence Analysis
Motifi453 – 4564SH2-bindingSequence Analysis
Motifi470 – 4734SH2-bindingSequence Analysis
Motifi496 – 4994SH2-bindingSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG39917.
GeneTreeiENSGT00440000033339.
HOVERGENiHBG056632.
InParanoidiP78324.
KOiK06551.
OMAiHEPEKNT.
OrthoDBiEOG7CG6ZQ.
PhylomeDBiP78324.
TreeFamiTF341862.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07654. C1-set. 2 hits.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00407. IGc1. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78324-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET
60 70 80 90 100
ATLRCTATSL IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN
110 120 130 140 150
NMDFSIRIGN ITPADAGTYY CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA
160 170 180 190 200
PVVSGPAARA TPQHTVSFTC ESHGFSPRDI TLKWFKNGNE LSDFQTNVDP
210 220 230 240 250
VGESVSYSIH STAKVVLTRE DVHSQVICEV AHVTLQGDPL RGTANLSETI
260 270 280 290 300
RVPPTLEVTQ QPVRAENQVN VTCQVRKFYP QRLQLTWLEN GNVSRTETAS
310 320 330 340 350
TVTENKDGTY NWMSWLLVNV SAHRDDVKLT CQVEHDGQPA VSKSHDLKVS
360 370 380 390 400
AHPKEQGSNT AAENTGSNER NIYIVVGVVC TLLVALLMAA LYLVRIRQKK
410 420 430 440 450
AQGSTSSTRL HEPEKNAREI TQDTNDITYA DLNLPKGKKP APQAAEPNNH
460 470 480 490 500
TEYASIQTSP QPASEDTLTY ADLDMVHLNR TPKQPAPKPE PSFSEYASVQ

VPRK
Length:504
Mass (Da):54,967
Last modified:April 5, 2011 - v2
Checksum:i18D2FD04F6182AD0
GO
Isoform 2 (identifier: P78324-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     422-422: Q → QVQSL

Note: No experimental confirmation available.

Show »
Length:508
Mass (Da):55,394
Checksum:i098D9B24276FA4E1
GO
Isoform 4 (identifier: P78324-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:503
Mass (Da):54,852
Checksum:iAB4F162B7FF8D97A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591T → I in CAA71944. (PubMed:9485180)Curated
Sequence conflicti503 – 5031R → K in CAA71944. (PubMed:9485180)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 72PA → RS.
VAR_015462
Natural varianti20 – 201A → P.
VAR_015463
Natural varianti40 – 401D → E.
VAR_015464
Natural varianti44 – 441L → S.4 Publications
Corresponds to variant rs1135193 [ dbSNP | Ensembl ].
VAR_015465
Natural varianti50 – 501T → S.4 Publications
Corresponds to variant rs17855609 [ dbSNP | Ensembl ].
VAR_015466
Natural varianti52 – 521T → I.4 Publications
Corresponds to variant rs17855610 [ dbSNP | Ensembl ].
VAR_015468
Natural varianti54 – 541R → H.4 Publications
Corresponds to variant rs17855611 [ dbSNP | Ensembl ].
VAR_015470
Natural varianti57 – 571A → V.4 Publications
Corresponds to variant rs17855612 [ dbSNP | Ensembl ].
VAR_015471
Natural varianti61 – 611I → N.
VAR_015472
Natural varianti68 – 681W → R.
VAR_015473
Natural varianti75 – 751G → A.4 Publications
Corresponds to variant rs1057114 [ dbSNP | Ensembl ].
VAR_015474
Natural varianti77 – 771E → K.
VAR_015475
Natural varianti81 – 811N → H.
VAR_015477
Natural varianti95 – 951D → E.4 Publications
VAR_015478
Natural varianti96 – 961L → S.4 Publications
VAR_015479
Natural varianti100 – 1001N → E Requires 2 nucleotide substitutions. 4 Publications
VAR_015480
Natural varianti107 – 1071R → S.4 Publications
Corresponds to variant rs17855615 [ dbSNP | Ensembl ].
VAR_015483
Natural varianti109 – 1091G → S.4 Publications
Corresponds to variant rs17855616 [ dbSNP | Ensembl ].
VAR_015484
Natural varianti125 – 1251R → Q.
VAR_015485
Natural varianti132 – 1321V → T Requires 2 nucleotide substitutions. 4 Publications
VAR_015486
Natural varianti134 – 1341F → L.
VAR_015487
Natural varianti163 – 1631Q → D Requires 2 nucleotide substitutions.
VAR_015488
Natural varianti181 – 1811T → S.
VAR_015489
Natural varianti190 – 1901E → Q.
VAR_015490
Natural varianti201 – 2022VG → AR.
VAR_015491
Natural varianti214 – 2141K → N.
VAR_015492
Natural varianti220 – 2201E → G.
VAR_015493
Natural varianti222 – 2221V → I.
VAR_015494
Natural varianti236 – 2361Q → R.
VAR_015495
Natural varianti239 – 2402PL → SF.
VAR_015496
Natural varianti251 – 2511R → Q.
VAR_015497
Natural varianti261 – 2611Q → L.
VAR_015498
Natural varianti263 – 2631V → M.
VAR_015499
Natural varianti271 – 2711V → I.
VAR_015500
Natural varianti276 – 2761R → T.
VAR_015501
Natural varianti302 – 3021V → L.
Corresponds to variant rs2422666 [ dbSNP | Ensembl ].
VAR_015502
Natural varianti339 – 3391P → S.
VAR_015503
Natural varianti353 – 3531P → L.
VAR_015504
Natural varianti357 – 3571G → S.
VAR_015505
Natural varianti367 – 3671S → P.
VAR_015506
Natural varianti370 – 3701R → Q.
VAR_015507
Natural varianti389 – 3891A → E.
VAR_015508
Natural varianti443 – 4431Q → R.
VAR_015509
Natural varianti460 – 4601P → L.
VAR_015510
Natural varianti486 – 4861A → L Requires 2 nucleotide substitutions.
VAR_015511
Natural varianti491 – 4911P → L.
VAR_015512

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 1301Missing in isoform 4. CuratedVSP_040799
Alternative sequencei422 – 4221Q → QVQSL in isoform 2. 1 PublicationVSP_007030

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13022.1. [P78324-1]
PIRiJC5287.
RefSeqiNP_001035111.1. NM_001040022.1. [P78324-1]
NP_001035112.1. NM_001040023.1. [P78324-1]
NP_542970.1. NM_080792.2. [P78324-1]
XP_005260726.1. XM_005260669.1. [P78324-2]
XP_005260727.1. XM_005260670.1. [P78324-2]
UniGeneiHs.581021.

Genome annotation databases

EnsembliENST00000356025; ENSP00000348307; ENSG00000198053. [P78324-1]
ENST00000358771; ENSP00000351621; ENSG00000198053. [P78324-1]
ENST00000400068; ENSP00000382941; ENSG00000198053. [P78324-1]
ENST00000622179; ENSP00000478763; ENSG00000198053. [P78324-2]
GeneIDi140885.
KEGGihsa:140885.
UCSCiuc002wfq.3. human. [P78324-1]
uc002wft.3. human. [P78324-2]

Polymorphism databases

DMDMi327478534.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13022.1. [P78324-1 ]
PIRi JC5287.
RefSeqi NP_001035111.1. NM_001040022.1. [P78324-1 ]
NP_001035112.1. NM_001040023.1. [P78324-1 ]
NP_542970.1. NM_080792.2. [P78324-1 ]
XP_005260726.1. XM_005260669.1. [P78324-2 ]
XP_005260727.1. XM_005260670.1. [P78324-2 ]
UniGenei Hs.581021.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JJS X-ray 1.85 A/B 31-149 [» ]
2JJT X-ray 2.30 A/B 31-149 [» ]
2UV3 X-ray 1.80 A/B 31-149 [» ]
2WNG X-ray 2.49 A 31-350 [» ]
4CMM X-ray 1.92 A 31-149 [» ]
ProteinModelPortali P78324.
SMRi P78324. Positions 31-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126752. 8 interactions.
IntActi P78324. 5 interactions.
MINTi MINT-5004422.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei P78324.

Polymorphism databases

DMDMi 327478534.

Proteomic databases

MaxQBi P78324.
PaxDbi P78324.
PRIDEi P78324.

Protocols and materials databases

DNASUi 140885.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356025 ; ENSP00000348307 ; ENSG00000198053 . [P78324-1 ]
ENST00000358771 ; ENSP00000351621 ; ENSG00000198053 . [P78324-1 ]
ENST00000400068 ; ENSP00000382941 ; ENSG00000198053 . [P78324-1 ]
ENST00000622179 ; ENSP00000478763 ; ENSG00000198053 . [P78324-2 ]
GeneIDi 140885.
KEGGi hsa:140885.
UCSCi uc002wfq.3. human. [P78324-1 ]
uc002wft.3. human. [P78324-2 ]

Organism-specific databases

CTDi 140885.
GeneCardsi GC20P001822.
HGNCi HGNC:9662. SIRPA.
HPAi CAB002776.
CAB015122.
MIMi 602461. gene.
neXtProti NX_P78324.
PharmGKBi PA34006.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39917.
GeneTreei ENSGT00440000033339.
HOVERGENi HBG056632.
InParanoidi P78324.
KOi K06551.
OMAi HEPEKNT.
OrthoDBi EOG7CG6ZQ.
PhylomeDBi P78324.
TreeFami TF341862.

Enzyme and pathway databases

Reactomei REACT_12051. Cell surface interactions at the vascular wall.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
SignaLinki P78324.

Miscellaneous databases

ChiTaRSi SIRPA. human.
EvolutionaryTracei P78324.
GeneWikii Signal-regulatory_protein_alpha.
GenomeRNAii 140885.
NextBioi 84534.
PROi P78324.
SOURCEi Search...

Gene expression databases

Bgeei P78324.
ExpressionAtlasi P78324. baseline and differential.
Genevestigatori P78324.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003597. Ig_C1-set.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view ]
Pfami PF07654. C1-set. 2 hits.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
SM00407. IGc1. 2 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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.

Entry informationi

Entry nameiSHPS1_HUMAN
AccessioniPrimary (citable) accession number: P78324
Secondary accession number(s): A2A2E1
, A8K411, B2R6C3, O00683, O43799, Q8N517, Q8TAL8, Q9H0Z2, Q9UDX2, Q9UIJ6, Q9Y4U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: April 5, 2011
Last modified: October 29, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3