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O75563

- SKAP2_HUMAN

UniProt

O75563 - SKAP2_HUMAN

Protein

Src kinase-associated phosphoprotein 2

Gene

SKAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.2 Publications

    GO - Molecular functioni

    1. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. B cell activation Source: UniProtKB-KW
    2. negative regulation of cell proliferation Source: Ensembl
    3. positive regulation of signal transduction Source: GOC
    4. protein complex assembly Source: ProtInc
    5. signal transduction Source: ProtInc

    Keywords - Biological processi

    B-cell activation

    Enzyme and pathway databases

    ReactomeiREACT_23916. Signal regulatory protein (SIRP) family interactions.
    SignaLinkiO75563.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Src kinase-associated phosphoprotein 2
    Alternative name(s):
    Pyk2/RAFTK-associated protein
    Retinoic acid-induced protein 70
    SKAP55 homolog
    Short name:
    SKAP-55HOM
    Short name:
    SKAP-HOM
    Src family-associated phosphoprotein 2
    Src kinase-associated phosphoprotein 55-related protein
    Src-associated adapter protein with PH and SH3 domains
    Gene namesi
    Name:SKAP2
    Synonyms:PRAP, RA70, SAPS, SCAP2, SKAP55R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:15687. SKAP2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleus Source: HPA
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162403393.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Src kinase-associated phosphoprotein 2PRO_0000270179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphotyrosine1 Publication
    Modified residuei151 – 1511PhosphotyrosineBy similarity
    Modified residuei261 – 2611PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-261 upon T-cell activation Probable. Dephosphorylated on Tyr-75 by PTPN22.5 PublicationsCurated

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO75563.
    PRIDEiO75563.

    2D gel databases

    OGPiO75563.

    PTM databases

    PhosphoSiteiO75563.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Present in platelets (at protein level).3 Publications

    Inductioni

    By retinoic acid.2 Publications

    Gene expression databases

    ArrayExpressiO75563.
    BgeeiO75563.
    CleanExiHS_SKAP2.
    GenevestigatoriO75563.

    Organism-specific databases

    HPAiHPA005560.
    HPA024045.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with PTPNS1. Part of a complex consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting of SKAP2, FYB and LILRB3. May interact with actin By similarity. Interacts with FYB, which is required for SKAP2 protein stability. Interacts with LAT, GRB2, PTK2B and PRAM1. May interact with FYN, HCK and LYN. Interacts with FASLG.By similarity7 Publications

    Protein-protein interaction databases

    BioGridi114448. 11 interactions.
    IntActiO75563. 3 interactions.
    STRINGi9606.ENSP00000005587.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OMHX-ray2.90E/F/G/H71-79[»]
    ProteinModelPortaliO75563.
    SMRiO75563. Positions 14-221, 304-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini116 – 219104PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini297 – 35862SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 6451HomodimerizationBy similarityAdd
    BLAST

    Domaini

    The SH3 domain interacts with FYB and PTK2B.

    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

    eggNOGiNOG46742.
    HOGENOMiHOG000231109.
    HOVERGENiHBG052827.
    InParanoidiO75563.
    OMAiWDCTGAL.
    OrthoDBiEOG7K6PVB.
    PhylomeDBiO75563.
    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]

    Sequencei

    Sequence statusi: Complete.

    O75563-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNPSSTSSP YPLPEEIRNL LADVETFVAD ILKGENLSKK AKEKRESLIK    50
    KIKDVKSIYL QEFQDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAP 100
    SDGAQFPPIA AQDLPFVLKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY 150
    YYGSDKDKQQ KGEFAIDGYS VRMNNTLRKD GKKDCCFEIS APDKRIYQFT 200
    AASPKDAEEW VQQLKFVLQD MESDIIPEDY DERGELYDDV DHPLPISNPL 250
    TSSQPIDDEI YEELPEEEED SAPVKVEEQR KMSQDSVHHT SGDKSTDYAN 300
    FYQGLWDCTG AFSDELSFKR GDVIYILSKE YNRYGWWVGE MKGAIGLVPK 350
    AYIMEMYDI 359
    Length:359
    Mass (Da):41,217
    Last modified:November 1, 1998 - v1
    Checksum:i65F266535A89281E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61S → C in BAA36194. (PubMed:9837776)Curated
    Sequence conflicti352 – 3521Y → H in BAD96605. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti202 – 2021A → S.3 Publications
    Corresponds to variant rs1129771 [ dbSNP | Ensembl ].
    VAR_029812
    Natural varianti253 – 2531S → T.
    Corresponds to variant rs17154402 [ dbSNP | Ensembl ].
    VAR_029813

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014486 mRNA. Translation: BAA36194.1.
    AJ004886 mRNA. Translation: CAA06193.1.
    AF072166 mRNA. Translation: AAC39924.1.
    AF051323 mRNA. Translation: AAC99296.1.
    AK313209 mRNA. Translation: BAG36025.1.
    AK222885 mRNA. Translation: BAD96605.1.
    AC003999 Genomic DNA. Translation: AAS02033.1.
    AC011299 Genomic DNA. Translation: AAS07536.1.
    CH236948 Genomic DNA. Translation: EAL24231.1.
    CH471073 Genomic DNA. Translation: EAW93859.1.
    BC002893 mRNA. Translation: AAH02893.1.
    BC036044 mRNA. Translation: AAH36044.1.
    CCDSiCCDS5400.1.
    RefSeqiNP_003921.2. NM_003930.3.
    XP_005249958.1. XM_005249901.1.
    UniGeneiHs.200770.
    Hs.610137.

    Genome annotation databases

    EnsembliENST00000345317; ENSP00000005587; ENSG00000005020.
    GeneIDi8935.
    KEGGihsa:8935.
    UCSCiuc003syc.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014486 mRNA. Translation: BAA36194.1 .
    AJ004886 mRNA. Translation: CAA06193.1 .
    AF072166 mRNA. Translation: AAC39924.1 .
    AF051323 mRNA. Translation: AAC99296.1 .
    AK313209 mRNA. Translation: BAG36025.1 .
    AK222885 mRNA. Translation: BAD96605.1 .
    AC003999 Genomic DNA. Translation: AAS02033.1 .
    AC011299 Genomic DNA. Translation: AAS07536.1 .
    CH236948 Genomic DNA. Translation: EAL24231.1 .
    CH471073 Genomic DNA. Translation: EAW93859.1 .
    BC002893 mRNA. Translation: AAH02893.1 .
    BC036044 mRNA. Translation: AAH36044.1 .
    CCDSi CCDS5400.1.
    RefSeqi NP_003921.2. NM_003930.3.
    XP_005249958.1. XM_005249901.1.
    UniGenei Hs.200770.
    Hs.610137.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OMH X-ray 2.90 E/F/G/H 71-79 [» ]
    ProteinModelPortali O75563.
    SMRi O75563. Positions 14-221, 304-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114448. 11 interactions.
    IntActi O75563. 3 interactions.
    STRINGi 9606.ENSP00000005587.

    PTM databases

    PhosphoSitei O75563.

    2D gel databases

    OGPi O75563.

    Proteomic databases

    PaxDbi O75563.
    PRIDEi O75563.

    Protocols and materials databases

    DNASUi 8935.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345317 ; ENSP00000005587 ; ENSG00000005020 .
    GeneIDi 8935.
    KEGGi hsa:8935.
    UCSCi uc003syc.3. human.

    Organism-specific databases

    CTDi 8935.
    GeneCardsi GC07M026706.
    H-InvDB HIX0025350.
    HGNCi HGNC:15687. SKAP2.
    HPAi HPA005560.
    HPA024045.
    MIMi 605215. gene.
    neXtProti NX_O75563.
    PharmGKBi PA162403393.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46742.
    HOGENOMi HOG000231109.
    HOVERGENi HBG052827.
    InParanoidi O75563.
    OMAi WDCTGAL.
    OrthoDBi EOG7K6PVB.
    PhylomeDBi O75563.
    TreeFami TF331055.

    Enzyme and pathway databases

    Reactomei REACT_23916. Signal regulatory protein (SIRP) family interactions.
    SignaLinki O75563.

    Miscellaneous databases

    ChiTaRSi SKAP2. human.
    GeneWikii SKAP2.
    GenomeRNAii 8935.
    NextBioi 33596.
    PROi O75563.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75563.
    Bgeei O75563.
    CleanExi HS_SKAP2.
    Genevestigatori O75563.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN, FUNCTION, VARIANT SER-202.
      Tissue: Testis.
    2. "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55."
      Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.
      FEBS Lett. 435:55-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH FYB, VARIANT SER-202.
      Tissue: Leukocyte.
    3. "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: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FYB, PHOSPHORYLATION.
      Tissue: Lymphocyte.
    4. "Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation."
      Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H., Avraham S., Yasuda M., Matsumoto M.
      J. Biol. Chem. 278:42225-42233(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PTK2B, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION.
      Tissue: Hippocampus.
    5. "Src-associated adaptor protein with PH and SH3 domain."
      Lee J.-S., Suh K.S., Burr J.G.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-202.
      Tissue: Pancreas.
    6. "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].
    7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    8. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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].
      Tissue: Lung and Testis.
    12. "Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin."
      Asazuma N., Wilde J.I., Berlanga O., Leduc M., Leo A., Schweighoffer E., Tybulewicz V., Bon C., Liu S.K., McGlade C.J., Schraven B., Watson S.P.
      J. Biol. Chem. 275:33427-33434(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH FYB; LAT AND GRB2, TISSUE SPECIFICITY.
    13. "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic leukemia cells."
      Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F., Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E., Koretzky G.
      J. Biol. Chem. 276:22375-22381(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, INTERACTION WITH PRAM1.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    16. "Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
      Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
      J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 71-79 IN COMPLEX WITH PTPN22, PHOSPHORYLATION AT TYR-75.

    Entry informationi

    Entry nameiSKAP2_HUMAN
    AccessioniPrimary (citable) accession number: O75563
    Secondary accession number(s): A4D173
    , Q53GP6, Q75MK6, Q75MZ4, Q9UBZ3, Q9UED8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 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 chromosome 7
      Human chromosome 7: 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

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