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Q86WV1

- SKAP1_HUMAN

UniProt

Q86WV1 - SKAP1_HUMAN

Protein

Src kinase-associated phosphoprotein 1

Gene

SKAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway. Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase binding Source: UniProtKB
    3. protein phosphatase binding Source: UniProtKB
    4. SH2 domain binding Source: UniProtKB
    5. SH3/SH2 adaptor activity Source: UniProtKB
    6. SH3 domain binding Source: BHF-UCL

    GO - Biological processi

    1. positive regulation of signal transduction Source: GOC
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. T cell receptor signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    SignaLinkiQ86WV1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Src kinase-associated phosphoprotein 1
    Alternative name(s):
    Src family-associated phosphoprotein 1
    Src kinase-associated phosphoprotein of 55 kDa
    Short name:
    SKAP-55
    Short name:
    pp55
    Gene namesi
    Name:SKAP1
    Synonyms:SCAP1, SKAP55
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:15605. SKAP1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane
    Note: Upon T-cell stimulation, translocates to lipid rafts at the cell membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: HPA
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi219 – 2191Y → F: Impairs interaction with PTPRC. No effect on interaction with FYN or GRB2. 2 Publications
    Mutagenesisi232 – 2321Y → F: Abolishes interaction with PTPRC, translocation to cell membrane upon T-cell stimulation and activation of the MAP kinase pathway. No effect on interaction with FYN or GRB2. 2 Publications
    Mutagenesisi271 – 2711Y → F: No effect on interaction with PTPRC and translocation to cell membrane upon T-cell stimulation. Abolishes interaction with FYN and GRB2 and activation of the MAP kinase pathway. 2 Publications
    Mutagenesisi295 – 2951Y → F: Abolishes FYB-dependent activation of ITGAL clustering. 1 Publication
    Mutagenesisi298 – 2981Y → F: Impairs interaction with FYB. 1 Publication
    Mutagenesisi333 – 3331W → R: Abolishes homodimerization, interaction with FYB and activation of the MAP kinase pathway. 3 Publications

    Organism-specific databases

    PharmGKBiPA162403362.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Src kinase-associated phosphoprotein 1PRO_0000270173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei142 – 1421PhosphotyrosineBy similarity
    Modified residuei219 – 2191Phosphotyrosine1 Publication
    Modified residuei232 – 2321Phosphotyrosine1 Publication
    Modified residuei271 – 2711Phosphotyrosine; by FYN1 Publication
    Modified residuei295 – 2951Phosphotyrosine; by FYNCurated

    Post-translational modificationi

    Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-271 is required for GRB2 interaction. Phosphorylation by FYN on Tyr-295 abolishes interaction with FYB. Tyr-232 is dephosphorylated by PTPRC Probable.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86WV1.
    PaxDbiQ86WV1.
    PRIDEiQ86WV1.

    PTM databases

    PhosphoSiteiQ86WV1.

    Expressioni

    Tissue specificityi

    Highly expressed in thymocytes and peripheral blood lymphocytes. Also expressed in spleen cells and testis. Present in T-cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ86WV1.
    BgeeiQ86WV1.
    CleanExiHS_SKAP1.
    GenevestigatoriQ86WV1.

    Organism-specific databases

    HPAiCAB025882.
    HPA002969.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with FYN and PTPRC. Interacts with GRB2 when phosphorylated on Tyr-271. Interacts with FYB, which is required for SKAP2 protein stability. Part of a complex consisting of SKAP1, FYB and CLNK. Interacts with RASGRP1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FYBO151176EBI-2477305,EBI-1753267

    Protein-protein interaction databases

    BioGridi114184. 11 interactions.
    IntActiQ86WV1. 3 interactions.
    MINTiMINT-6939971.
    STRINGi9606.ENSP00000338171.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi108 – 11912
    Beta strandi121 – 1244
    Beta strandi126 – 13611
    Beta strandi139 – 1457
    Beta strandi152 – 1565
    Beta strandi161 – 1644
    Helixi166 – 1683
    Helixi172 – 1765
    Beta strandi177 – 1815
    Beta strandi183 – 1853
    Beta strandi188 – 1914
    Helixi195 – 21218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U5DX-ray1.70A/B/C/D108-213[»]
    ProteinModelPortaliQ86WV1.
    SMRiQ86WV1. Positions 7-213, 301-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86WV1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini107 – 210104PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini294 – 35562SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 2956Interaction with FYB

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi220 – 23011Poly-GluAdd
    BLAST

    Domaini

    The SH3 domain interacts with FYB.

    Sequence similaritiesi

    Belongs to the SKAP family.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG76786.
    HOGENOMiHOG000231109.
    HOVERGENiHBG052827.
    InParanoidiQ86WV1.
    KOiK17699.
    OMAiHLRRDSK.
    OrthoDBiEOG7K6PVB.
    PhylomeDBiQ86WV1.
    TreeFamiTF331055.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00233. PH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86WV1-1) [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

    MQAAALPEEI RWLLEDAEEF LAEGLRNENL SAVARDHRDH ILRGFQQIKA    50
    RYYWDFQPQG GDIGQDSSDD NHSGTLGLSL TSDAPFLSDY QDEGMEDIVK 100
    GAQELDNVIK QGYLEKKSKD HSFFGSEWQK RWCVVSRGLF YYYANEKSKQ 150
    PKGTFLIKGY GVRMAPHLRR DSKKESCFEL TSQDRRSYEF TATSPAEARD 200
    WVDQISFLLK DLSSLTIPYE EDEEEEEKEE TYDDIDGFDS PSCGSQCRPT 250
    ILPGSVGIKE PTEEKEEEDI YEVLPDEEHD LEEDESGTRR KGVDYASYYQ 300
    GLWDCHGDQP DELSFQRGDL IRILSKEYNM YGWWVGELNS LVGIVPKEYL 350
    TTAFEVEER 359
    Length:359
    Mass (Da):41,432
    Last modified:November 24, 2009 - v3
    Checksum:i630FE4C17295BD6D
    GO
    Isoform 2 (identifier: Q86WV1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         293-293: Missing.

    Show »
    Length:358
    Mass (Da):41,333
    Checksum:i158BBE1D48539DAC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti187 – 1871S → T in CAA72101. (PubMed:9195899)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti161 – 1611G → S.1 Publication
    Corresponds to variant rs2278868 [ dbSNP | Ensembl ].
    VAR_029811
    Natural varianti242 – 2421S → G.
    Corresponds to variant rs35288886 [ dbSNP | Ensembl ].
    VAR_035343

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei293 – 2931Missing in isoform 2. 1 PublicationVSP_022179

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11215 mRNA. Translation: CAA72101.1.
    AC006468 Genomic DNA. No translation available.
    AC027152 Genomic DNA. No translation available.
    AC036222 Genomic DNA. No translation available.
    AC090627 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94749.1.
    CH471109 Genomic DNA. Translation: EAW94750.1.
    BC047870 mRNA. Translation: AAH47870.1.
    CCDSiCCDS32674.1. [Q86WV1-1]
    RefSeqiNP_001068567.1. NM_001075099.1. [Q86WV1-2]
    NP_003717.3. NM_003726.3. [Q86WV1-1]
    UniGeneiHs.316931.

    Genome annotation databases

    EnsembliENST00000336915; ENSP00000338171; ENSG00000141293. [Q86WV1-1]
    ENST00000584924; ENSP00000464311; ENSG00000141293. [Q86WV1-1]
    GeneIDi8631.
    KEGGihsa:8631.
    UCSCiuc002ini.1. human. [Q86WV1-1]
    uc002inj.1. human. [Q86WV1-2]

    Polymorphism databases

    DMDMi269849660.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11215 mRNA. Translation: CAA72101.1 .
    AC006468 Genomic DNA. No translation available.
    AC027152 Genomic DNA. No translation available.
    AC036222 Genomic DNA. No translation available.
    AC090627 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94749.1 .
    CH471109 Genomic DNA. Translation: EAW94750.1 .
    BC047870 mRNA. Translation: AAH47870.1 .
    CCDSi CCDS32674.1. [Q86WV1-1 ]
    RefSeqi NP_001068567.1. NM_001075099.1. [Q86WV1-2 ]
    NP_003717.3. NM_003726.3. [Q86WV1-1 ]
    UniGenei Hs.316931.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U5D X-ray 1.70 A/B/C/D 108-213 [» ]
    ProteinModelPortali Q86WV1.
    SMRi Q86WV1. Positions 7-213, 301-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114184. 11 interactions.
    IntActi Q86WV1. 3 interactions.
    MINTi MINT-6939971.
    STRINGi 9606.ENSP00000338171.

    PTM databases

    PhosphoSitei Q86WV1.

    Polymorphism databases

    DMDMi 269849660.

    Proteomic databases

    MaxQBi Q86WV1.
    PaxDbi Q86WV1.
    PRIDEi Q86WV1.

    Protocols and materials databases

    DNASUi 8631.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336915 ; ENSP00000338171 ; ENSG00000141293 . [Q86WV1-1 ]
    ENST00000584924 ; ENSP00000464311 ; ENSG00000141293 . [Q86WV1-1 ]
    GeneIDi 8631.
    KEGGi hsa:8631.
    UCSCi uc002ini.1. human. [Q86WV1-1 ]
    uc002inj.1. human. [Q86WV1-2 ]

    Organism-specific databases

    CTDi 8631.
    GeneCardsi GC17M046210.
    HGNCi HGNC:15605. SKAP1.
    HPAi CAB025882.
    HPA002969.
    MIMi 604969. gene.
    neXtProti NX_Q86WV1.
    PharmGKBi PA162403362.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG76786.
    HOGENOMi HOG000231109.
    HOVERGENi HBG052827.
    InParanoidi Q86WV1.
    KOi K17699.
    OMAi HLRRDSK.
    OrthoDBi EOG7K6PVB.
    PhylomeDBi Q86WV1.
    TreeFami TF331055.

    Enzyme and pathway databases

    SignaLinki Q86WV1.

    Miscellaneous databases

    EvolutionaryTracei Q86WV1.
    GeneWikii SKAP1.
    GenomeRNAii 8631.
    NextBioi 32353.
    PROi Q86WV1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86WV1.
    Bgeei Q86WV1.
    CleanExi HS_SKAP1.
    Genevestigatori Q86WV1.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00233. PH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of SKAP55, a novel protein that associates with p59fyn in human T-lymphocytes."
      Marie-Cardine A., Bruyns E., Eckerskorn C., Kirchgessner H., Meuer S., Schraven B.
      J. Biol. Chem. 272:16077-16080(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 101-110; 120-130 AND 153-158, PHOSPHORYLATION, INTERACTION WITH FYN, TISSUE SPECIFICITY, VARIANT SER-161.
      Tissue: Blood.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 2).
      Tissue: Pancreas.
    5. "Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130."
      Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B., Koretzky G.A.
      J. Biol. Chem. 273:25789-25795(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYB, MUTAGENESIS OF TRP-333.
    6. "FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells."
      Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.
      Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYB, SUBCELLULAR LOCATION.
    7. "SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55."
      Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E.
      EMBO J. 19:2889-2899(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYB, MUTAGENESIS OF TYR-295 AND TYR-298, FUNCTION.
    8. "SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation."
      Wu L., Yu Z., Shen S.-H.
      J. Biol. Chem. 277:40420-40427(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, MUTAGENESIS OF TYR-219; TYR-232; TYR-271 AND TRP-333, PHOSPHORYLATION, INTERACTION WITH GRB2.
    9. "SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription."
      Wu L., Fu J., Shen S.-H.
      Mol. Cell. Biol. 22:2673-2686(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-219 AND TYR-232, DEPHOSPHORYLATION BY PTPRC, MUTAGENESIS OF TYR-219; TYR-232 AND TYR-271, SUBCELLULAR LOCATION, FUNCTION.
    10. "SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates."
      Wang H., Moon E.-Y., Azouz A., Wu X., Smith A., Schneider H., Hogg N., Rudd C.E.
      Nat. Immunol. 4:366-374(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells."
      Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K., Wange R.L.
      J. Biol. Chem. 280:23576-23583(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYB, MUTAGENESIS OF TRP-333.
    12. "An essential role for SKAP-55 in LFA-1 clustering on T cells that cannot be substituted by SKAP-55R."
      Jo E.-K., Wang H., Rudd C.E.
      J. Exp. Med. 201:1733-1739(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein."
      Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.
      J. Biol. Chem. 281:13743-13750(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH FYB.
    14. "The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1."
      Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X., Freund C., Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.
      Mol. Cell. Biol. 26:7130-7144(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "SKAP55 modulates T cell antigen receptor-induced activation of the Ras-Erk-AP1 pathway by binding RasGRP1."
      Kosco K.A., Cerignoli F., Williams S., Abraham R.T., Mustelin T.
      Mol. Immunol. 45:510-522(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASGRP1.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Structural basis for the dimerization and phosphoinositide specificity of the Src kinase-associated phosphoproteins SKAP55 and SKAP-HOM."
      Tang Y., Swanson K.D., Neel B.G., Eck M.J.
      Submitted (JUL-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 108-213.

    Entry informationi

    Entry nameiSKAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q86WV1
    Secondary accession number(s): D3DTV1, O15268
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 101 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3