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P43404

- ZAP70_MOUSE

UniProt

P43404 - ZAP70_MOUSE

Protein

Tyrosine-protein kinase ZAP-70

Gene

Zap70

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (14 Dec 2011)
      Previous versions | rss
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    Functioni

    Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR).4 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Activated by phosphorylation at Tyr-492 in the activation loop.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei368 – 3681ATPPROSITE-ProRule annotation
    Active sitei460 – 4601Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi343 – 3519ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: MGI
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    3. phosphotyrosine binding Source: MGI
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: MGI
    6. protein tyrosine kinase activity Source: MGI

    GO - Biological processi

    1. beta selection Source: MGI
    2. immune response Source: Ensembl
    3. intracellular signal transduction Source: MGI
    4. negative thymic T cell selection Source: MGI
    5. peptidyl-tyrosine phosphorylation Source: MGI
    6. positive regulation of alpha-beta T cell differentiation Source: MGI
    7. positive regulation of alpha-beta T cell proliferation Source: MGI
    8. positive regulation of calcium-mediated signaling Source: MGI
    9. positive regulation of T cell differentiation Source: MGI
    10. positive thymic T cell selection Source: MGI
    11. protein autophosphorylation Source: MGI
    12. protein phosphorylation Source: MGI
    13. T cell receptor signaling pathway Source: MGI
    14. thymic T cell selection Source: MGI

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_215414. Translocation of ZAP-70 to Immunological synapse.
    REACT_225768. Generation of second messenger molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase ZAP-70 (EC:2.7.10.2)
    Alternative name(s):
    70 kDa zeta-chain associated protein
    Syk-related tyrosine kinase
    Gene namesi
    Name:Zap70
    Synonyms:Srk, Zap-70
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:99613. Zap70.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein
    Note: In quiescent T-lymphocytes, ZAP70 is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD3Z. Colocalizes together with RHOH in the immunological synapse. RHOH is required for its proper localization to the cell membrane and cytoskeleton fractions in the thymocytes.

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: MGI
    4. immunological synapse Source: UniProtKB
    5. plasma membrane Source: UniProtKB
    6. T cell receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice lack both CD4 and CD8 positive mature T-lymphocytes. Displays a complete block in B-Cell development at the pro-B cell stage in the absence of both SYK and ZAP70.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 618618Tyrosine-protein kinase ZAP-70PRO_0000088169Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481PhosphotyrosineBy similarity
    Modified residuei287 – 2871PhosphoserineBy similarity
    Modified residuei290 – 2901PhosphotyrosineBy similarity
    Modified residuei314 – 3141Phosphotyrosine; by LCKBy similarity
    Modified residuei318 – 3181PhosphotyrosineBy similarity
    Modified residuei491 – 4911PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Phosphorylation of Tyr-314 and Tyr-314 are essential for ZAP70 positive function on T-lymphocyte activation whereas Tyr-290 has a negative regulatory role. Within the C-terminal kinase domain, Tyr-491 and Tyr-492 are phosphorylated after TCR induction, Tyr-491 playing a negative regulatory role and Tyr-492 a positive. Tyr-492 is dephosphorylated by PTN22.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP43404.
    PaxDbiP43404.
    PRIDEiP43404.

    PTM databases

    PhosphoSiteiP43404.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in thymus, spleen and lymph nodes.1 Publication

    Developmental stagei

    Isoform 2 is expressed in developing thymocytes from the CD44+CD25- stage up to mature T-cells. Isoform 1 is not expressed in thymocytes at the CD44+CD25- or CD44+CD25+ stages.1 Publication

    Gene expression databases

    BgeeiP43404.
    CleanExiMM_ZAP70.
    GenevestigatoriP43404.

    Interactioni

    Subunit structurei

    Interacts with CD3Z; this interaction docks ZAP70 at the stimulated TCR. Interacts with NFAM1. Interacts with adapter proteins SLA and SLA2; these interactions negatively regulates T-cell receptor signaling. Interacts with CBLB. Interacts with CBL; this interaction promotes ubiquitination, internalization and subsequent degradation of CD3Z. Identified in a complex with CBL and UBE2L3. Interacts with DEF6. Interacts (via SH2 domains) with RHOH; this interaction regulates ZAP70 subcellular localization. Interacts with FCRL3. Interacts with VAV1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP43404. 3 interactions.
    STRINGi10090.ENSMUSP00000027291.

    Structurei

    3D structure databases

    ProteinModelPortaliP43404.
    SMRiP43404. Positions 1-605.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 10293SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini163 – 25492SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini337 – 597261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni103 – 16260Interdomain AAdd
    BLAST
    Regioni255 – 33682Interdomain BAdd
    BLAST

    Domaini

    Composed of 2 N-terminal SH2 domains and a C-terminal kinase domain. The tandem SH2 domains bind to the doubly phosphorylated tyrosine-based activation motif (ITAM) of CD247/CD3Z and the non-canonical phosphorylated tyrosine-based activation motif (TAM) of RHOH By similarity. The interdomain B located between the second SH2 and the kinase domain has been implicated in binding to other signaling molecules including CBL or VAV1. Thus, ZAP70 can also function as a scaffold by recruiting additional factors to the stimulated TCR complex By similarity.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115195.
    HOGENOMiHOG000113264.
    HOVERGENiHBG001540.
    InParanoidiP43404.
    KOiK07360.
    OMAiMKGPEVI.
    OrthoDBiEOG7MWGWD.
    TreeFamiTF351629.

    Family and domain databases

    Gene3Di1.10.930.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProiIPR011009. Kinase-like_dom.
    IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000604. TyrPK_SYK. 1 hit.
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P43404-1) [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

    MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL    50
    VHDVRFHHFP IERQLNGTYA IAGGKAHCGP AELCQFYSQD PDGLPCNLRK 100
    PCNRPPGLEP QPGVFDCLRD AMVRDYVRQT WKLEGDALEQ AIISQAPQVE 150
    KLIATTAHER MPWYHSSLTR EEAERKLYSG QQTDGKFLLR PRKEQGTYAL 200
    SLVYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK LKADGLIYRL 250
    KEVCPNSSAS AAVAAPTLPA HPSTFTQPQR RVDTLNSDGY TPEPARLASS 300
    TDKPRPMPMD TSVYESPYSD PEELKDKKLF LKRENLLVAD IELGCGNFGS 350
    VRQGVYRMRK KQIDVAIKVL KQGTEKADKD EMMREAQIMH QLDNPYIVRL 400
    IGVCQAEALM LVMEMAGGGP LHKFLLGKKE EIPVSNVAEL LHQVAMGMKY 450
    LEEKNFVHRD LAARNVLLVN RHYAKISDFG LSKALGADDS YYTARSAGKW 500
    PLKWYAPECI NFRKFSSRSD VWSYGVTMWE AFSYGQKPYK KMKGPEVLDF 550
    IKQGKRMECP PECPPEMYAL MSDCWIYKWE DRPDFLTVEQ RMRNYYYSLA 600
    SRAEGPPQCE QVAEAACG 618
    Length:618
    Mass (Da):70,112
    Last modified:December 14, 2011 - v3
    Checksum:i9E0D18B240B28392
    GO
    Isoform 2 (identifier: P43404-2) [UniParc]FASTAAdd to Basket

    Also known as: TZK

    The sequence of this isoform differs from the canonical sequence as follows:
         1-306: Missing.

    Show »
    Length:312
    Mass (Da):35,883
    Checksum:i12CCA3AA2C3B1CF2
    GO
    Isoform 3 (identifier: P43404-3) [UniParc]FASTAAdd to Basket

    Also known as: TZK-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-309: Missing.
         310-360: DTSVYESPYS...VRQGVYRMRK → MAYGRVSGVS...MLSVASHLGR

    Note: No experimental confirmation available.

    Show »
    Length:309
    Mass (Da):35,255
    Checksum:iD1A230395CA2AFE4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241R → C in AAA19250. (PubMed:8196616)Curated
    Sequence conflicti526 – 5294VTMW → GHHV in BAC67015. 1 PublicationCurated
    Sequence conflicti546 – 5461E → Q in AAA19250. (PubMed:8196616)Curated
    Sequence conflicti599 – 5991L → P in AAA19250. (PubMed:8196616)Curated
    Sequence conflicti599 – 5991L → P in AAB36538. (PubMed:9208839)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti464 – 4641R → C in ST; causes an absence of mature T-cells due to thymocyte development being arrested at the CD4+CD8+ stage. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 309309Missing in isoform 3. 1 PublicationVSP_031160Add
    BLAST
    Alternative sequencei1 – 306306Missing in isoform 2. 1 PublicationVSP_031159Add
    BLAST
    Alternative sequencei310 – 36051DTSVY…YRMRK → MAYGRVSGVSELSRVLYVPF PPPPFLSNPGVHDTRMYTQH AMLSVASHLGR in isoform 3. 1 PublicationVSP_031161Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04379 mRNA. Translation: AAA19250.1.
    U77667 mRNA. Translation: AAB36538.1.
    AB083210 mRNA. Translation: BAC43746.1.
    AB084383 mRNA. Translation: BAC67015.1.
    AK039883 mRNA. Translation: BAC30471.1.
    AC084389 mRNA. No translation available.
    BC029727 mRNA. Translation: AAH29727.1.
    CCDSiCCDS14888.1. [P43404-1]
    PIRiI48914.
    RefSeqiNP_001276541.1. NM_001289612.1. [P43404-2]
    NP_001276694.1. NM_001289765.1. [P43404-1]
    NP_033565.2. NM_009539.3. [P43404-1]
    XP_006495959.1. XM_006495896.1. [P43404-1]
    UniGeneiMm.8038.

    Genome annotation databases

    EnsembliENSMUST00000027291; ENSMUSP00000027291; ENSMUSG00000026117. [P43404-1]
    GeneIDi22637.
    KEGGimmu:22637.
    UCSCiuc007aqz.1. mouse. [P43404-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04379 mRNA. Translation: AAA19250.1 .
    U77667 mRNA. Translation: AAB36538.1 .
    AB083210 mRNA. Translation: BAC43746.1 .
    AB084383 mRNA. Translation: BAC67015.1 .
    AK039883 mRNA. Translation: BAC30471.1 .
    AC084389 mRNA. No translation available.
    BC029727 mRNA. Translation: AAH29727.1 .
    CCDSi CCDS14888.1. [P43404-1 ]
    PIRi I48914.
    RefSeqi NP_001276541.1. NM_001289612.1. [P43404-2 ]
    NP_001276694.1. NM_001289765.1. [P43404-1 ]
    NP_033565.2. NM_009539.3. [P43404-1 ]
    XP_006495959.1. XM_006495896.1. [P43404-1 ]
    UniGenei Mm.8038.

    3D structure databases

    ProteinModelPortali P43404.
    SMRi P43404. Positions 1-605.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P43404. 3 interactions.
    STRINGi 10090.ENSMUSP00000027291.

    Chemistry

    ChEMBLi CHEMBL2034801.

    PTM databases

    PhosphoSitei P43404.

    Proteomic databases

    MaxQBi P43404.
    PaxDbi P43404.
    PRIDEi P43404.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027291 ; ENSMUSP00000027291 ; ENSMUSG00000026117 . [P43404-1 ]
    GeneIDi 22637.
    KEGGi mmu:22637.
    UCSCi uc007aqz.1. mouse. [P43404-1 ]

    Organism-specific databases

    CTDi 7535.
    MGIi MGI:99613. Zap70.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115195.
    HOGENOMi HOG000113264.
    HOVERGENi HBG001540.
    InParanoidi P43404.
    KOi K07360.
    OMAi MKGPEVI.
    OrthoDBi EOG7MWGWD.
    TreeFami TF351629.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_215414. Translocation of ZAP-70 to Immunological synapse.
    REACT_225768. Generation of second messenger molecules.

    Miscellaneous databases

    NextBioi 303021.
    PROi P43404.
    SOURCEi Search...

    Gene expression databases

    Bgeei P43404.
    CleanExi MM_ZAP70.
    Genevestigatori P43404.

    Family and domain databases

    Gene3Di 1.10.930.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProi IPR011009. Kinase-like_dom.
    IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000604. TyrPK_SYK. 1 hit.
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif."
      Gauen L.K.T., Zhu Y., Letourner F., Hu Q., Bolen J.B., Matis L.A., Klausner R.D., Shaw A.S.
      Mol. Cell. Biol. 14:3729-3741(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Thymus.
    2. "A spontaneously arising mutation in the DLAARN motif of murine ZAP-70 abrogates kinase activity and arrests thymocyte development."
      Wiest D.L., Ashe J.M., Howcroft T.K., Lee H.-M., Kemper D.M., Negishi I., Singer D.S., Singer A., Abe R.
      Immunity 6:663-671(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ST CYS-464.
      Strain: C57BL/6.
      Tissue: Thymocyte.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: C57BL/6.
      Tissue: Thymus.
    4. "Mouse TZK-2."
      Ikeda T., Kuroyama H.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    5. "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: Thymus.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. "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 1).
      Strain: FVB/N.
      Tissue: Salivary gland.
    8. "Essential role for ZAP-70 in both positive and negative selection of thymocytes."
      Negishi I., Motoyama N., Nakayama K., Nakayama K., Senju S., Hatakeyama S., Zhang Q., Chan A.C., Loh D.Y.
      Nature 376:435-438(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    9. "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
      Sosinowski T., Pandey A., Dixit V.M., Weiss A.
      J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA.
    10. Cited for: INTERACTION WITH CBLB.
    11. "A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling."
      Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M., Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.
      J. Biol. Chem. 277:19131-19138(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA2.
    12. "SWAP-70-like adapter of T cells, an adapter protein that regulates early TCR-initiated signaling in Th2 lineage cells."
      Tanaka Y., Bi K., Kitamura R., Hong S., Altman Y., Matsumoto A., Tabata H., Lebedeva S., Bushway P.J., Altman A.
      Immunity 18:403-414(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DEF6.
    13. "Unexpected requirement for ZAP-70 in pre-B cell development and allelic exclusion."
      Schweighoffer E., Vanes L., Mathiot A., Nakamura T., Tybulewicz V.L.
      Immunity 18:523-533(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    14. "NFAM1, an immunoreceptor tyrosine-based activation motif-bearing molecule that regulates B cell development and signaling."
      Ohtsuka M., Arase H., Takeuchi A., Yamasaki S., Shiina R., Suenaga T., Sakurai D., Yokosuka T., Arase N., Iwashima M., Kitamura T., Moriya H., Saito T.
      Proc. Natl. Acad. Sci. U.S.A. 101:8126-8131(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFAM1.
    15. "RhoH GTPase recruits and activates Zap70 required for T cell receptor signaling and thymocyte development."
      Gu Y., Chae H.-D., Siefring J.E., Jasti A.C., Hildeman D.A., Williams D.A.
      Nat. Immunol. 7:1182-1190(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHOH, DOMAIN.
    16. "Distinct roles for Syk and ZAP-70 during early thymocyte development."
      Palacios E.H., Weiss A.
      J. Exp. Med. 204:1703-1715(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THYMOCYTE DEVELOPMENT.

    Entry informationi

    Entry nameiZAP70_MOUSE
    AccessioniPrimary (citable) accession number: P43404
    Secondary accession number(s): P97455, Q80VV2, Q8CHJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: December 14, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3