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P43403

- ZAP70_HUMAN

UniProt

P43403 - ZAP70_HUMAN

Protein

Tyrosine-protein kinase ZAP-70

Gene

ZAP70

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 CD247/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-CD247/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).6 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Enzyme regulationi

    Activated by phosphorylation at Tyr-493 in the activation loop. Inhibited by staurosporine.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei369 – 3691ATP
    Active sitei461 – 4611Proton acceptor2 PublicationsPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi345 – 3528ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

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

    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. 2681.
    ReactomeiREACT_12596. Translocation of ZAP-70 to Immunological synapse.
    REACT_12623. Generation of second messenger molecules.
    SignaLinkiP43403.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12858. ZAP70.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: In quiescent T-lymphocytes, it is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD247/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 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytosol Source: Reactome
    3. immunological synapse Source: Ensembl
    4. plasma membrane Source: UniProtKB
    5. T cell receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Selective T-cell defect (STCD) [MIM:269840]: A form of severe combined immunodeficiency characterized by a selective absence of CD8+ T-cells.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti337 – 3371L → R in STCD. 1 Publication
    VAR_065623
    Natural varianti465 – 4651R → C in STCD. 1 Publication
    VAR_065624
    Natural varianti465 – 4651R → H in STCD. 1 Publication
    VAR_015538
    Natural varianti507 – 5071A → V in STCD. 1 Publication
    VAR_065625
    Natural varianti518 – 5181S → R in STCD. 1 Publication
    VAR_006351
    Natural varianti541 – 5411K → KLEQ in STCD. 1 Publication
    VAR_038688
    Natural varianti564 – 5641C → R in STCD. 1 Publication
    VAR_065626

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311W → A: Increased constitutive kinase activity. 1 Publication
    Mutagenesisi133 – 1331L → A: Increased constitutive kinase activity. 1 Publication
    Mutagenesisi141 – 1411A → E: Increased constitutive kinase activity. 1 Publication
    Mutagenesisi144 – 1441S → A: Increased kinase activity after activation by LCK. 1 Publication
    Mutagenesisi145 – 1451Q → A: Increased kinase activity after activation by LCK. 1 Publication
    Mutagenesisi147 – 1471P → A: Increased kinase activity after activation by LCK. 1 Publication
    Mutagenesisi292 – 2921Y → F: Induces constitutive TCR stimulation-independent NFAT induction. 1 Publication
    Mutagenesisi314 – 3141V → A: Increased constitutive kinase activity.
    Mutagenesisi315 – 3151Y → A: Increased constitutive kinase activity; when associated with F-319. 4 Publications
    Mutagenesisi315 – 3151Y → F: Increased constitutive kinase activity; when associated with F-319. About 75% loss of CD247/CD3Z-binding in stimulated TCR and complete loss of VAV1 interaction. 4 Publications
    Mutagenesisi319 – 3191Y → A: Increased constitutive kinase activity; when associated with F-315. 2 Publications
    Mutagenesisi319 – 3191Y → F: Increased constitutive kinase activity; when associated with F-315. About 80% loss of TCR-induced NFAT activation. 2 Publications
    Mutagenesisi461 – 4611D → N: Abolishes kinase activity. 1 Publication
    Mutagenesisi479 – 4791D → N: Abolishes kinase activity. 1 Publication
    Mutagenesisi492 – 4921Y → F: Increases kinase activity. 1 Publication
    Mutagenesisi493 – 4931Y → F: Impairs kinase activity. 1 Publication
    Mutagenesisi597 – 5971Y → A: Increased kinase activity after activation by LCK. 1 Publication
    Mutagenesisi598 – 5981Y → A: Increased kinase activity after activation by LCK. 1 Publication

    Keywords - Diseasei

    Disease mutation, SCID

    Organism-specific databases

    MIMi269840. phenotype.
    Orphaneti911. Combined immunodeficiency due to ZAP70 deficiency.
    PharmGKBiPA37447.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 619619Tyrosine-protein kinase ZAP-70PRO_0000088168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481Phosphotyrosine1 Publication
    Modified residuei289 – 2891Phosphoserine1 Publication
    Modified residuei292 – 2921Phosphotyrosine2 Publications
    Modified residuei315 – 3151Phosphotyrosine; by LCK1 Publication
    Modified residuei319 – 3191Phosphotyrosine1 Publication
    Modified residuei492 – 4921Phosphotyrosine
    Modified residuei603 – 6031N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Phosphorylation of Tyr-315 and Tyr-319 are essential for ZAP70 positive function on T-lymphocyte activation whereas Tyr-292 has a negative regulatory role. Within the C-terminal kinase domain, Tyr-492 and Tyr-493 are phosphorylated after TCR induction, Tyr-492 playing a negative regulatory role and Tyr-493 a positive. Tyr-493 is dephosphorylated by PTN22.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP43403.
    PaxDbiP43403.
    PRIDEiP43403.

    PTM databases

    PhosphoSiteiP43403.

    Miscellaneous databases

    PMAP-CutDBP43403.

    Expressioni

    Tissue specificityi

    Expressed in T- and natural killer cells. Also present in early thymocytes and pro/pre B-cells.3 Publications

    Gene expression databases

    ArrayExpressiP43403.
    BgeeiP43403.
    CleanExiHS_ZAP70.
    GenevestigatoriP43403.

    Organism-specific databases

    HPAiCAB002625.
    HPA003134.

    Interactioni

    Subunit structurei

    Interacts with NFAM1. Interacts with adapter proteins SLA and SLA2; these interactions negatively regulates T-cell receptor signaling. Interacts with CBLB By similarity. Interacts with DEF6. Interacts (via SH2 domains) with RHOH; this interaction regulates ZAP70 subcellular localization By similarity. Interacts with FCRL3. Interacts with VAV1. Interacts with CD247/CD3Z; this interaction docks ZAP70 at the stimulated TCR. Interacts with CBL; this interaction promotes ubiquitination, internalization and subsequent degradation of CD247/CD3Z. Identified in a complex with CBL and UBE2L3.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CD247P2096322EBI-1211276,EBI-1165705
    CD3EP077663EBI-1211276,EBI-1211297
    KITP107212EBI-1211276,EBI-1379503
    LCKP062392EBI-1211276,EBI-1348
    METP085812EBI-1211276,EBI-1039152
    PTPN22Q9Y2R24EBI-1211276,EBI-1211241
    Ubash3bQ8BGG710EBI-1211276,EBI-8846415From a different organism.

    Protein-protein interaction databases

    BioGridi113367. 49 interactions.
    DIPiDIP-38781N.
    IntActiP43403. 19 interactions.
    MINTiMINT-110540.
    STRINGi9606.ENSP00000264972.

    Structurei

    Secondary structure

    1
    619
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 74
    Beta strandi11 – 144
    Helixi17 – 2610
    Beta strandi34 – 385
    Beta strandi40 – 423
    Beta strandi46 – 527
    Beta strandi55 – 639
    Beta strandi69 – 713
    Beta strandi77 – 793
    Helixi80 – 8910
    Beta strandi94 – 963
    Helixi114 – 13118
    Helixi135 – 15622
    Helixi157 – 1604
    Helixi170 – 1789
    Turni179 – 1813
    Beta strandi186 – 1916
    Beta strandi197 – 2048
    Beta strandi207 – 2159
    Beta strandi221 – 2233
    Beta strandi229 – 2313
    Helixi232 – 24110
    Beta strandi246 – 2483
    Helixi309 – 3113
    Beta strandi316 – 3205
    Helixi322 – 3265
    Helixi334 – 3363
    Beta strandi337 – 3459
    Beta strandi350 – 3578
    Beta strandi364 – 3718
    Helixi377 – 39216
    Beta strandi401 – 41515
    Helixi422 – 4265
    Turni430 – 4323
    Helixi435 – 45420
    Helixi464 – 4663
    Beta strandi467 – 4715
    Beta strandi474 – 4774
    Turni482 – 4854
    Helixi503 – 5053
    Helixi508 – 5136
    Helixi518 – 53316
    Turni534 – 5363
    Turni539 – 5424
    Helixi546 – 5538
    Helixi566 – 5749
    Helixi580 – 5823
    Helixi586 – 60116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FBVX-ray2.90B289-297[»]
    1M61X-ray2.50A1-256[»]
    1U59X-ray2.30A327-606[»]
    2CBLX-ray2.10B286-297[»]
    2OQ1X-ray1.90A3-256[»]
    2OZOX-ray2.60A1-606[»]
    2Y1NX-ray2.00B/D286-297[»]
    3ZNIX-ray2.21B/F/J/N286-297[»]
    4A4BX-ray2.79B286-297[»]
    4A4CX-ray2.70B286-297[»]
    4K2RX-ray3.00A1-606[»]
    ProteinModelPortaliP43403.
    SMRiP43403. Positions 1-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43403.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 10293SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini163 – 25492SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini338 – 600263Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni103 – 16260Interdomain AAdd
    BLAST
    Regioni255 – 33783Interdomain 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 contains 3 tyrosines (Tyr-292, Tyr-315, Tyr-319) that are phosphorylated following TCR activation. These sites have 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 similarity1 Publication

    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.
    HOGENOMiHOG000113264.
    HOVERGENiHBG001540.
    InParanoidiP43403.
    KOiK07360.
    OMAiMKGPEVI.
    OrthoDBiEOG7MWGWD.
    PhylomeDBiP43403.
    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: P43403-1) [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 AELCEFYSRD PDGLPCNLRK 100
    PCNRPSGLEP QPGVFDCLRD AMVRDYVRQT WKLEGEALEQ AIISQAPQVE 150
    KLIATTAHER MPWYHSSLTR EEAERKLYSG AQTDGKFLLR PRKEQGTYAL 200
    SLIYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK LKADGLIYCL 250
    KEACPNSSAS NASGAAAPTL PAHPSTLTHP QRRIDTLNSD GYTPEPARIT 300
    SPDKPRPMPM DTSVYESPYS DPEELKDKKL FLKRDNLLIA DIELGCGNFG 350
    SVRQGVYRMR KKQIDVAIKV LKQGTEKADT EEMMREAQIM HQLDNPYIVR 400
    LIGVCQAEAL MLVMEMAGGG PLHKFLVGKR EEIPVSNVAE LLHQVSMGMK 450
    YLEEKNFVHR DLAARNVLLV NRHYAKISDF GLSKALGADD SYYTARSAGK 500
    WPLKWYAPEC INFRKFSSRS DVWSYGVTMW EALSYGQKPY KKMKGPEVMA 550
    FIEQGKRMEC PPECPPELYA LMSDCWIYKW EDRPDFLTVE QRMRACYYSL 600
    ASKVEGPPGS TQKAEAACA 619
    Length:619
    Mass (Da):69,872
    Last modified:November 1, 1995 - v1
    Checksum:iD1E1A8EC66FA116F
    GO
    Isoform 2 (identifier: P43403-2) [UniParc]FASTAAdd to Basket

    Also known as: TZK

    The sequence of this isoform differs from the canonical sequence as follows:
         1-307: Missing.

    Show »
    Length:312
    Mass (Da):35,647
    Checksum:iB1D7A63A61D63215
    GO
    Isoform 3 (identifier: P43403-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-126: Missing.
         127-134: VRQTWKLE → MRLGPRWK

    Note: No experimental confirmation available.

    Show »
    Length:493
    Mass (Da):55,873
    Checksum:i14F1841C3F898EEF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751R → L.1 Publication
    Corresponds to variant rs55964305 [ dbSNP | Ensembl ].
    VAR_041846
    Natural varianti191 – 1911P → L.1 Publication
    Corresponds to variant rs56403250 [ dbSNP | Ensembl ].
    VAR_041847
    Natural varianti337 – 3371L → R in STCD. 1 Publication
    VAR_065623
    Natural varianti448 – 4481G → E in a head and neck squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041848
    Natural varianti465 – 4651R → C in STCD. 1 Publication
    VAR_065624
    Natural varianti465 – 4651R → H in STCD. 1 Publication
    VAR_015538
    Natural varianti507 – 5071A → V in STCD. 1 Publication
    VAR_065625
    Natural varianti518 – 5181S → R in STCD. 1 Publication
    VAR_006351
    Natural varianti523 – 5231W → L.1 Publication
    Corresponds to variant rs56189815 [ dbSNP | Ensembl ].
    VAR_041849
    Natural varianti541 – 5411K → KLEQ in STCD. 1 Publication
    VAR_038688
    Natural varianti564 – 5641C → R in STCD. 1 Publication
    VAR_065626

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 307307Missing in isoform 2. 1 PublicationVSP_031156Add
    BLAST
    Alternative sequencei1 – 126126Missing in isoform 3. 1 PublicationVSP_031157Add
    BLAST
    Alternative sequencei127 – 1348VRQTWKLE → MRLGPRWK in isoform 3. 1 PublicationVSP_031158

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05148 mRNA. No translation available.
    AB083211 mRNA. Translation: BAC43747.1.
    AC016699 Genomic DNA. Translation: AAX93187.1.
    BC039039 mRNA. Translation: AAH39039.1.
    BC053878 mRNA. Translation: AAH53878.1.
    CCDSiCCDS33254.1. [P43403-1]
    CCDS33255.1. [P43403-2]
    PIRiA44266.
    A49955.
    RefSeqiNP_001070.2. NM_001079.3. [P43403-1]
    NP_997402.1. NM_207519.1. [P43403-2]
    XP_006712792.1. XM_006712729.1. [P43403-2]
    UniGeneiHs.234569.

    Genome annotation databases

    EnsembliENST00000264972; ENSP00000264972; ENSG00000115085. [P43403-1]
    ENST00000451498; ENSP00000400475; ENSG00000115085. [P43403-2]
    GeneIDi7535.
    KEGGihsa:7535.
    UCSCiuc002syd.1. human. [P43403-1]
    uc002sye.1. human. [P43403-3]

    Polymorphism databases

    DMDMi1177044.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    ZAP70base

    ZAP70 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05148 mRNA. No translation available.
    AB083211 mRNA. Translation: BAC43747.1 .
    AC016699 Genomic DNA. Translation: AAX93187.1 .
    BC039039 mRNA. Translation: AAH39039.1 .
    BC053878 mRNA. Translation: AAH53878.1 .
    CCDSi CCDS33254.1. [P43403-1 ]
    CCDS33255.1. [P43403-2 ]
    PIRi A44266.
    A49955.
    RefSeqi NP_001070.2. NM_001079.3. [P43403-1 ]
    NP_997402.1. NM_207519.1. [P43403-2 ]
    XP_006712792.1. XM_006712729.1. [P43403-2 ]
    UniGenei Hs.234569.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FBV X-ray 2.90 B 289-297 [» ]
    1M61 X-ray 2.50 A 1-256 [» ]
    1U59 X-ray 2.30 A 327-606 [» ]
    2CBL X-ray 2.10 B 286-297 [» ]
    2OQ1 X-ray 1.90 A 3-256 [» ]
    2OZO X-ray 2.60 A 1-606 [» ]
    2Y1N X-ray 2.00 B/D 286-297 [» ]
    3ZNI X-ray 2.21 B/F/J/N 286-297 [» ]
    4A4B X-ray 2.79 B 286-297 [» ]
    4A4C X-ray 2.70 B 286-297 [» ]
    4K2R X-ray 3.00 A 1-606 [» ]
    ProteinModelPortali P43403.
    SMRi P43403. Positions 1-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113367. 49 interactions.
    DIPi DIP-38781N.
    IntActi P43403. 19 interactions.
    MINTi MINT-110540.
    STRINGi 9606.ENSP00000264972.

    Chemistry

    BindingDBi P43403.
    ChEMBLi CHEMBL2803.
    GuidetoPHARMACOLOGYi 2285.

    PTM databases

    PhosphoSitei P43403.

    Polymorphism databases

    DMDMi 1177044.

    Proteomic databases

    MaxQBi P43403.
    PaxDbi P43403.
    PRIDEi P43403.

    Protocols and materials databases

    DNASUi 7535.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264972 ; ENSP00000264972 ; ENSG00000115085 . [P43403-1 ]
    ENST00000451498 ; ENSP00000400475 ; ENSG00000115085 . [P43403-2 ]
    GeneIDi 7535.
    KEGGi hsa:7535.
    UCSCi uc002syd.1. human. [P43403-1 ]
    uc002sye.1. human. [P43403-3 ]

    Organism-specific databases

    CTDi 7535.
    GeneCardsi GC02P098331.
    GeneReviewsi ZAP70.
    HGNCi HGNC:12858. ZAP70.
    HPAi CAB002625.
    HPA003134.
    MIMi 176947. gene.
    269840. phenotype.
    neXtProti NX_P43403.
    Orphaneti 911. Combined immunodeficiency due to ZAP70 deficiency.
    PharmGKBi PA37447.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000113264.
    HOVERGENi HBG001540.
    InParanoidi P43403.
    KOi K07360.
    OMAi MKGPEVI.
    OrthoDBi EOG7MWGWD.
    PhylomeDBi P43403.
    TreeFami TF351629.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_12596. Translocation of ZAP-70 to Immunological synapse.
    REACT_12623. Generation of second messenger molecules.
    SignaLinki P43403.

    Miscellaneous databases

    EvolutionaryTracei P43403.
    GeneWikii ZAP70.
    GenomeRNAii 7535.
    NextBioi 29481.
    PMAP-CutDB P43403.
    PROi P43403.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43403.
    Bgeei P43403.
    CleanExi HS_ZAP70.
    Genevestigatori P43403.

    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. "ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain."
      Chan A.C., Iwashima M., Turck C.W., Weiss A.
      Cell 71:649-662(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CD3Z, TISSUE SPECIFICITY, PHOSPHORYLATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Leukocyte.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS 1 AND 3).
      Tissue: Blood and Brain.
    5. "Defective T cell receptor signaling and CD8+ thymic selection in humans lacking zap-70 kinase."
      Arpaia E., Shahar M., Dadi H., Cohen A., Roifman C.M.
      Cell 76:947-958(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 521-547, VARIANT STCD LEU-GLU-GLN-541 INS, FUNCTION.
      Tissue: Lymphoid tissue.
    6. "ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity."
      Isakov N., Wange R.L., Burgess W.H., Watts J.D., Aebersold R., Samelson L.E.
      J. Exp. Med. 181:375-380(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF TAM-BINDING.
    7. "Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function."
      Chan A.C., Dalton M., Johnson R., Kong G.H., Wang T., Thoma R., Kurosaki T.
      EMBO J. 14:2499-2508(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-492 AND TYR-493.
    8. "Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function."
      Bubeck Wardenburg J., Fu C., Jackman J.K., Flotow H., Wilkinson S.E., Williams D.H., Johnson R., Kong G., Chan A.C., Findell P.R.
      J. Biol. Chem. 271:19641-19644(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LCP2.
    9. "Enhancement of lymphocyte responsiveness by a gain-of-function mutation of ZAP-70."
      Zhao Q., Weiss A.
      Mol. Cell. Biol. 16:6765-6774(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-292, MUTAGENESIS OF TYR-292.
    10. "The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction."
      Wu J., Zhao Q., Kurosaki T., Weiss A.
      J. Exp. Med. 185:1877-1882(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VAV1, MUTAGENESIS OF TYR-315.
    11. "In vivo association of CD5 with tyrosine-phosphorylated ZAP-70 and p21 phospho-zeta molecules in human CD3+ thymocytes."
      Gary-Gouy H., Lang V., Sarun S., Boumsell L., Bismuth G.
      J. Immunol. 159:3739-3747(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
      Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
      Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LAT.
    13. "ZAP-70 association with T cell receptor zeta (TCRzeta): fluorescence imaging of dynamic changes upon cellular stimulation."
      Sloan-Lancaster J., Presley J., Ellenberg J., Yamazaki T., Lippincott-Schwartz J., Samelson L.E.
      J. Cell Biol. 143:613-624(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Tyrosine 319, a newly identified phosphorylation site of ZAP-70, plays a critical role in T cell antigen receptor signaling."
      Di Bartolo V., Mege D., Germain V., Pelosi M., Dufour E., Michel F., Magistrelli G., Isacchi A., Acuto O.
      J. Biol. Chem. 274:6285-6294(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-315 AND TYR-319, MUTAGENESIS OF TYR-315 AND TYR-319.
    15. "SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling."
      Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.
      Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL AND SLA.
    16. "Cbl promotes ubiquitination of the T cell receptor zeta through an adaptor function of Zap-70."
      Wang H.Y., Altman Y., Fang D., Elly C., Dai Y., Shao Y., Liu Y.C.
      J. Biol. Chem. 276:26004-26011(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CD3Z UBIQUITINATION.
    17. "SPAP2, an Ig family receptor containing both ITIMs and ITAMs."
      Xu M.-J., Zhao R., Cao H., Zhao Z.J.
      Biochem. Biophys. Res. Commun. 293:1037-1046(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FCRL3.
    18. "Tyrosine 315 determines optimal recruitment of ZAP-70 to the T cell antigen receptor."
      Di Bartolo V., Malissen M., Dufour E., Sechet E., Malissen B., Acuto O.
      Eur. J. Immunol. 32:568-575(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-315.
    19. "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
      Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
      Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "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.
    23. "T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315."
      Gelkop S., Gish G.D., Babichev Y., Pawson T., Isakov N.
      J. Immunol. 175:8123-8132(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY LCK.
    24. "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-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "ZAP-70 expression in normal pro/pre B cells, mature B cells, and in B-cell acute lymphoblastic leukemia."
      Crespo M., Villamor N., Gine E., Muntanola A., Colomer D., Marafioti T., Jones M., Camos M., Campo E., Montserrat E., Bosch F.
      Clin. Cancer Res. 12:726-734(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    26. Cited for: DEPHOSPHORYLATION BY PTN22.
    27. Cited for: REVIEW ON FUNCTION.
    28. "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-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: FUNCTION, DOMAIN.
    31. "Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor."
      Hatada M.H., Lu X., Laird E.R., Green J., Morgenstern J.P., Lou M., Marr C.S., Phillips T.B., Ram M.K., Theriault K., Zoller M.J., Karas L.K.
      Nature 377:32-38(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-256 IN COMPLEX WITH CD247, INTERACTION WITH CD247.
    32. "Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase."
      Meng W., Sawasdikosol S., Burakoff S.J., Eck M.J.
      Nature 398:84-90(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 286-297 IN COMPLEX WITH CBL, INTERACTION WITH CBL.
    33. "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases."
      Zheng N., Wang P., Jeffrey P.D., Pavletich N.P.
      Cell 102:533-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 289-297 IN COMPLEX WITH CBL AND UBE2L3.
    34. "Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem."
      Folmer R.H., Geschwindner S., Xue Y.
      Biochemistry 41:14176-14184(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-256.
    35. "The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors."
      Jin L., Pluskey S., Petrella E.C., Cantin S.M., Gorga J.C., Rynkiewicz M.J., Pandey P., Strickler J.E., Babine R.E., Weaver D.T., Seidl K.J.
      J. Biol. Chem. 279:42818-42825(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 327-606 IN COMPLEX WITH STAUROSPORINE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-479, ENZYME REGULATION.
    36. "Structural basis for the inhibition of tyrosine kinase activity of ZAP-70."
      Deindl S., Kadlecek T.A., Brdicka T., Cao X., Weiss A., Kuriyan J.
      Cell 129:735-746(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-606 OF MUTANT ASN-461 IN COMPLEX WITH MAGNESIUM AND ATP ANALOG, ACTIVE SITE, MUTAGENESIS OF TRP-131; LEU-133; ALA-141; SER-144; GLN-145; PRO-147; TYR-315; TYR-319; ASP-461; TYR-597 AND TYR-598.
    37. "ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency."
      Chan A.C., Kadlecek T.A., Elder M.E., Filipovich A.H., Kuo W.-L., Iwashima M., Parslow T.G., Weiss A.
      Science 264:1599-1601(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT STCD ARG-518.
    38. "Specific immunoglobulin E responses in ZAP-70-deficient patients are mediated by Syk-dependent T-cell receptor signalling."
      Toyabe S., Watanabe A., Harada W., Karasawa T., Uchiyama M.
      Immunology 103:164-171(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT STCD HIS-465.
    39. "Distinct T cell developmental consequences in humans and mice expressing identical mutations in the DLAARN motif of ZAP-70."
      Elder M.E., Skoda-Smith S., Kadlecek T.A., Wang F., Wu J., Weiss A.
      J. Immunol. 166:656-661(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT STCD CYS-465.
    40. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-175; LEU-191; GLU-448 AND LEU-523.
    41. "Clinical heterogeneity can hamper the diagnosis of patients with ZAP70 deficiency."
      Turul T., Tezcan I., Artac H., de Bruin-Versteeg S., Barendregt B.H., Reisli I., Sanal O., van Dongen J.J., van der Burg M.
      Eur. J. Pediatr. 168:87-93(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS STCD ARG-337; VAL-507 AND ARG-564.

    Entry informationi

    Entry nameiZAP70_HUMAN
    AccessioniPrimary (citable) accession number: P43403
    Secondary accession number(s): A6NFP4
    , Q6PIA4, Q8IXD6, Q9UBS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 175 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 2
      Human chromosome 2: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3