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Q3UND0

- SKAP2_MOUSE

UniProt

Q3UND0 - SKAP2_MOUSE

Protein

Src kinase-associated phosphoprotein 2

Gene

Skap2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      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.3 Publications

    GO - Biological processi

    1. B cell activation Source: UniProtKB-KW
    2. negative regulation of cell proliferation Source: MGI

    Keywords - Biological processi

    B-cell activation

    Enzyme and pathway databases

    ReactomeiREACT_215628. Signal regulatory protein (SIRP) family interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Src kinase-associated phosphoprotein 2
    Alternative name(s):
    Pyk2/RAFTK-associated protein
    SKAP55 homolog
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1889206. Skap2.

    Subcellular locationi

    Cytoplasm 3 Publications
    Note: Membrane ruffles of macrophages. Perikarya and dendrites from neurons.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mice are healthy and do not display any obvious abnormality. They have normal T-cell, platelet and macrophage function, but show reduced levels of spontaneous immunoglobulins in the serum, and defects in B-cell proliferation.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi260 – 2601Y → F: Abolishes interaction with FYN, phosphorylation by FYN, and effects on cell growth. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Src kinase-associated phosphoprotein 2PRO_0000270180Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphotyrosine2 Publications
    Modified residuei151 – 1511Phosphotyrosine1 Publication
    Modified residuei260 – 2601Phosphotyrosine; by FYN3 Publications

    Post-translational modificationi

    Dephosphorylated on Tyr-75 by PTPN22 By similarity. Phosphorylated by FYN on Tyr-260. In case of infection with Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase yopH.By similarity5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ3UND0.
    PaxDbiQ3UND0.
    PRIDEiQ3UND0.

    Expressioni

    Tissue specificityi

    Expressed in kidney, lung, liver, spleen, bone marrow and testis. Present in T-cells, B-cells, and all cells of the myelomonocytic lineage. Present in all brain regions, with highest levels in neurons from the Purkinje cell layer, hippocampal gyrus, cortex and substantia nigra (at protein level).4 Publications

    Inductioni

    By IL-6 in myeloid cells.1 Publication

    Gene expression databases

    BgeeiQ3UND0.
    CleanExiMM_SKAP2.
    GenevestigatoriQ3UND0.

    Interactioni

    Subunit structurei

    Interacts with LAT, GRB2, PTK2B and PRAM1 By similarity. Homodimer. Interacts with FYB, which is required for SKAP2 protein stability. 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. May interact with FYN, HCK and LYN. Interacts with FASLG By similarity.By similarity

    Protein-protein interaction databases

    BioGridi207619. 1 interaction.
    IntActiQ3UND0. 1 interaction.
    MINTiMINT-263820.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 2915
    Turni30 – 345
    Helixi39 – 5517
    Helixi56 – 594
    Helixi61 – 633
    Helixi111 – 1133
    Beta strandi115 – 12612
    Beta strandi128 – 1303
    Turni132 – 1343
    Beta strandi136 – 14510
    Beta strandi148 – 1547
    Beta strandi161 – 1655
    Beta strandi170 – 1734
    Helixi175 – 1773
    Helixi183 – 1853
    Beta strandi186 – 1905
    Beta strandi192 – 1943
    Beta strandi196 – 2005
    Helixi204 – 21714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U5EX-ray2.60A/B14-222[»]
    1U5FX-ray1.90A111-248[»]
    1U5GX-ray2.10A/B/C/D103-222[»]
    2OTXX-ray2.60A/B12-222[»]
    ProteinModelPortaliQ3UND0.
    SMRiQ3UND0. Positions 14-222, 304-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ3UND0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini116 – 219104PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini296 – 35762SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Domaini

    The SH3 domain interacts with FYB and PTK2B.By similarity

    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.
    GeneTreeiENSGT00390000017856.
    HOGENOMiHOG000231109.
    HOVERGENiHBG052827.
    InParanoidiQ3UND0.
    OMAiWDCTGAL.
    OrthoDBiEOG7K6PVB.
    PhylomeDBiQ3UND0.
    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: Q3UND0-1) [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

    MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK    50
    KIKDVKSVYL QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP 100
    SDGNQFPPIA AQDLPFVIKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY 150
    YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD GKKDCCFEIC APDKRIYQFT 200
    AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV DHPAAVSSPQ 250
    RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF 300
    YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA 350
    YLMEMYDI 358
    Length:358
    Mass (Da):40,712
    Last modified:January 9, 2007 - v2
    Checksum:iB66973A656E44E05
    GO
    Isoform 2 (identifier: Q3UND0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         22-28: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:351
    Mass (Da):39,950
    Checksum:iA6C08305272498D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161E → K in BAE25817. (PubMed:16141072)Curated
    Sequence conflicti104 – 1041N → P AA sequence (PubMed:11207596)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei22 – 287Missing in isoform 2. 1 PublicationVSP_022184

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051324 mRNA. Translation: AAC99297.1.
    AB014485 mRNA. Translation: BAA77253.1.
    AK076000 mRNA. Translation: BAC36111.1.
    AK144289 mRNA. Translation: BAE25817.1.
    BC003711 mRNA. Translation: AAH03711.1.
    CCDSiCCDS20137.1. [Q3UND0-1]
    RefSeqiNP_061243.1. NM_018773.2. [Q3UND0-1]
    UniGeneiMm.221479.
    Mm.392558.

    Genome annotation databases

    EnsembliENSMUST00000078214; ENSMUSP00000077342; ENSMUSG00000059182. [Q3UND0-1]
    GeneIDi54353.
    KEGGimmu:54353.
    UCSCiuc009bxv.1. mouse. [Q3UND0-1]
    uc009bxw.1. mouse. [Q3UND0-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051324 mRNA. Translation: AAC99297.1 .
    AB014485 mRNA. Translation: BAA77253.1 .
    AK076000 mRNA. Translation: BAC36111.1 .
    AK144289 mRNA. Translation: BAE25817.1 .
    BC003711 mRNA. Translation: AAH03711.1 .
    CCDSi CCDS20137.1. [Q3UND0-1 ]
    RefSeqi NP_061243.1. NM_018773.2. [Q3UND0-1 ]
    UniGenei Mm.221479.
    Mm.392558.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U5E X-ray 2.60 A/B 14-222 [» ]
    1U5F X-ray 1.90 A 111-248 [» ]
    1U5G X-ray 2.10 A/B/C/D 103-222 [» ]
    2OTX X-ray 2.60 A/B 12-222 [» ]
    ProteinModelPortali Q3UND0.
    SMRi Q3UND0. Positions 14-222, 304-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207619. 1 interaction.
    IntActi Q3UND0. 1 interaction.
    MINTi MINT-263820.

    Proteomic databases

    MaxQBi Q3UND0.
    PaxDbi Q3UND0.
    PRIDEi Q3UND0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000078214 ; ENSMUSP00000077342 ; ENSMUSG00000059182 . [Q3UND0-1 ]
    GeneIDi 54353.
    KEGGi mmu:54353.
    UCSCi uc009bxv.1. mouse. [Q3UND0-1 ]
    uc009bxw.1. mouse. [Q3UND0-2 ]

    Organism-specific databases

    CTDi 8935.
    MGIi MGI:1889206. Skap2.

    Phylogenomic databases

    eggNOGi NOG46742.
    GeneTreei ENSGT00390000017856.
    HOGENOMi HOG000231109.
    HOVERGENi HBG052827.
    InParanoidi Q3UND0.
    OMAi WDCTGAL.
    OrthoDBi EOG7K6PVB.
    PhylomeDBi Q3UND0.
    TreeFami TF331055.

    Enzyme and pathway databases

    Reactomei REACT_215628. Signal regulatory protein (SIRP) family interactions.

    Miscellaneous databases

    EvolutionaryTracei Q3UND0.
    NextBioi 311138.
    PROi Q3UND0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3UND0.
    CleanExi MM_SKAP2.
    Genevestigatori Q3UND0.

    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. "Adaptor protein SKAP55R is associated with myeloid differentiation and growth arrest."
      Curtis D.J., Jane S.M., Hilton D.J., Dougherty L., Bodine D.M., Begley C.G.
      Exp. Hematol. 28:1250-1259(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN, PHOSPHORYLATION AT TYR-260, MUTAGENESIS OF TYR-260, FUNCTION.
      Tissue: Testis.
    2. "Mouse Saps, 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] (ISOFORM 1).
      Tissue: Liver.
    3. "RA70, retinoic acid responsive gene, is expressed specifically in spermatocyte in mouse testis."
      Momoi T., Urase K., Mukasa T., Fujita E., Kouroku Y., Miho Y., Soyama A., Momoi M.Y.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Lymph node.
    5. "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).
    6. "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: PROTEIN SEQUENCE OF 1-12.
      Tissue: T-cell.
    7. "The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages."
      Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.
      Cell. Microbiol. 2:401-414(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 93-114; 129-139 AND 147-158, PHOSPHORYLATION, INTERACTION WITH FYB, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1, IDENTIFICATION IN A COMPLEX WITH FYB AND LILRB3.
    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: INTERACTION WITH PTPNS1, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1.
    9. "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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "Macrophage colony-stimulating factor receptor induces tyrosine phosphorylation of SKAP55R adaptor and its association with actin."
      Bourette R.P., Therier J., Mouchiroud G.
      Cell. Signal. 17:941-949(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH ACTIN, FUNCTION.
    11. "Regulation of in vitro and in vivo immune functions by the cytosolic adaptor protein SKAP-HOM."
      Togni M., Swanson K.D., Reimann S., Kliche S., Pearce A.C., Simeoni L., Reinhold D., Wienands J., Neel B.G., Schraven B., Gerber A.
      Mol. Cell. Biol. 25:8052-8063(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75 AND TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-IX-V and other agonists."
      Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K., Ruggeri Z.M., Schraven B., Neel B.G., Koretzky G., Shattil S.J.
      Blood 109:1018-1025(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYB.
    14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-151 AND TYR-260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    15. "The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch."
      Swanson K.D., Tang Y., Ceccarelli D.F., Poy F., Sliwa J.P., Neel B.G., Eck M.J.
      Mol. Cell 32:564-575(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-222, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSKAP2_MOUSE
    AccessioniPrimary (citable) accession number: Q3UND0
    Secondary accession number(s): Q8BK74, Q9Z2K4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3