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P78324

- SHPS1_HUMAN

UniProt

P78324 - SHPS1_HUMAN

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
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (05 Apr 2011)
      Previous versions | rss
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    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

    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

    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...)2 Publications
    Glycosylationi270 – 2701N-linked (GlcNAc...)2 Publications
    Disulfide bondi273 ↔ 331PROSITE-ProRule annotation
    Glycosylationi292 – 2921N-linked (GlcNAc...)2 Publications
    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

    ArrayExpressiP78324.
    BgeeiP78324.
    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. 7 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.
    HOVERGENiHBG056632.
    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

    MEPAGPAPGR LGPLLCLLLA ASCAWSGVAG EEELQVIQPD KSVLVAAGET    50
    ATLRCTATSL IPVGPIQWFR GAGPGRELIY NQKEGHFPRV TTVSDLTKRN 100
    NMDFSIRIGN ITPADAGTYY CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA 150
    PVVSGPAARA TPQHTVSFTC ESHGFSPRDI TLKWFKNGNE LSDFQTNVDP 200
    VGESVSYSIH STAKVVLTRE DVHSQVICEV AHVTLQGDPL RGTANLSETI 250
    RVPPTLEVTQ QPVRAENQVN VTCQVRKFYP QRLQLTWLEN GNVSRTETAS 300
    TVTENKDGTY NWMSWLLVNV SAHRDDVKLT CQVEHDGQPA VSKSHDLKVS 350
    AHPKEQGSNT AAENTGSNER NIYIVVGVVC TLLVALLMAA LYLVRIRQKK 400
    AQGSTSSTRL HEPEKNAREI TQDTNDITYA DLNLPKGKKP APQAAEPNNH 450
    TEYASIQTSP QPASEDTLTY ADLDMVHLNR TPKQPAPKPE PSFSEYASVQ 500
    VPRK 504
    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. [P78324-2]
    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. 7 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 . [P78324-2 ]
    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.
    HOVERGENi HBG056632.
    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

    ArrayExpressi P78324.
    Bgeei P78324.
    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

    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 1, 2014
    This is version 152 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