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P20963

- CD3Z_HUMAN

UniProt

P20963 - CD3Z_HUMAN

Protein

T-cell surface glycoprotein CD3 zeta chain

Gene

CD247

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (10 Oct 2002)
      Previous versions | rss
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    Functioni

    Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering.

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    2. innate immune response Source: Reactome
    3. regulation of defense response to virus by virus Source: Reactome
    4. regulation of immune response Source: Reactome
    5. T cell costimulation Source: Reactome
    6. T cell receptor signaling pathway Source: Reactome
    7. viral process Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_11068. Nef and signal transduction.
    REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12555. Downstream TCR signaling.
    REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_12596. Translocation of ZAP-70 to Immunological synapse.
    REACT_12623. Generation of second messenger molecules.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.
    REACT_19324. PD-1 signaling.
    SignaLinkiP20963.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T-cell surface glycoprotein CD3 zeta chain
    Alternative name(s):
    T-cell receptor T3 zeta chain
    CD_antigen: CD247
    Gene namesi
    Name:CD247
    Synonyms:CD3Z, T3Z, TCRZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1677. CD247.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-beta T cell receptor complex Source: Ensembl
    2. cytoplasm Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: MGI
    5. T cell receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency due to defect in CD3-zeta (CD3ZID) [MIM:610163]: An immunological deficiency characterized by T-cells impaired immune response to alloantigens, tetanus toxoid and mitogens.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi610163. phenotype.
    Orphaneti85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    169160. T-B+ severe combined immunodeficiency due to CD3delta/CD3epsilon/CD3zeta.
    PharmGKBiPA26219.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 164143T-cell surface glycoprotein CD3 zeta chainPRO_0000016493Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 – 32InterchainSequence Analysis
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei64 – 641Phosphotyrosine3 PublicationsPROSITE-ProRule annotation
    Modified residuei72 – 721Phosphotyrosine3 PublicationsPROSITE-ProRule annotation
    Modified residuei83 – 831Phosphotyrosine1 PublicationPROSITE-ProRule annotation
    Modified residuei111 – 1111Phosphotyrosine4 PublicationsPROSITE-ProRule annotation
    Modified residuei123 – 1231Phosphotyrosine1 PublicationPROSITE-ProRule annotation
    Modified residuei142 – 1421Phosphotyrosine4 PublicationsPROSITE-ProRule annotation
    Modified residuei153 – 1531Phosphotyrosine1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated on Tyr residues after T-cell receptor triggering.By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP20963.
    PaxDbiP20963.
    PRIDEiP20963.

    PTM databases

    PhosphoSiteiP20963.

    Expressioni

    Gene expression databases

    ArrayExpressiP20963.
    BgeeiP20963.
    CleanExiHS_CD247.
    GenevestigatoriP20963.

    Organism-specific databases

    HPAiCAB004651.
    HPA008750.

    Interactioni

    Subunit structurei

    The TCR/CD3 complex of T-lymphocytes consists of either a TCR alpha/beta or TCR gamma/delta heterodimer coexpressed at the cell surface with the invariant subunits of CD3 labeled gamma, delta, epsilon, zeta, and eta. CD3-zeta forms either homodimers or heterodimers with CD3-eta. Interacts with SLA and SLA2. Interacts with DOCK2 and TRAT1. Interacts with HIV-1; this interaction up-regulates the expression of the Fas ligand (FASLG) at the cell surface. Interacts with HIV-2 Nef protein; this interaction induces down-regulation of cell surface TCR/CD3 complexes. Interacts with SHB. Interacts with ZAP70. Interacts (tyrosine phosphorylated) with SHC1 (via SH2 domain). Interacts with PTPRC.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-1165705,EBI-1165705
    Ccr7P477742EBI-1165705,EBI-8038963From a different organism.
    NCK1P163332EBI-1165705,EBI-389883
    PTPN22Q9Y2R24EBI-1165705,EBI-1211241
    ZAP70P4340322EBI-1165705,EBI-1211276

    Protein-protein interaction databases

    BioGridi107357. 28 interactions.
    DIPiDIP-35404N.
    IntActiP20963. 12 interactions.
    MINTiMINT-1517020.
    STRINGi9606.ENSP00000354782.

    Structurei

    Secondary structure

    1
    164
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 5424
    Helixi64 – 7310
    Turni74 – 763
    Helixi77 – 793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TCENMR-B137-150[»]
    1YGRX-ray2.90C/D80-85[»]
    2HACNMR-A/B28-60[»]
    2OQ1X-ray1.90B69-87[»]
    3IK5X-ray2.05B/D63-80[»]
    3IOZX-ray3.70B51-93[»]
    DisProtiDP00200.
    ProteinModelPortaliP20963.
    SMRiP20963. Positions 28-60.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20963.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 309ExtracellularSequence Analysis
    Topological domaini52 – 164113CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei31 – 5121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 8929ITAM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini100 – 12829ITAM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini131 – 15929ITAM 3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The ITAM domains mediate interaction with SHB.

    Sequence similaritiesi

    Belongs to the CD3Z/FCER1G family.Curated
    Contains 3 ITAM domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG87611.
    HOGENOMiHOG000234398.
    HOVERGENiHBG005280.
    KOiK06453.
    OMAiLHMQTLP.
    OrthoDBiEOG78SQM7.
    PhylomeDBiP20963.
    TreeFamiTF330937.

    Family and domain databases

    InterProiIPR021663. CR3_zeta/IgE_Fc_rcpt_gamma.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    IPR024128. T-cell_CD3_zeta/eta.
    [Graphical view]
    PANTHERiPTHR10035. PTHR10035. 1 hit.
    PfamiPF02189. ITAM. 3 hits.
    PF11628. TCR_zetazeta. 1 hit.
    [Graphical view]
    SMARTiSM00077. ITAM. 3 hits.
    [Graphical view]
    PROSITEiPS51055. ITAM_1. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20963-1) [UniParc]FASTAAdd to Basket

    Also known as: CD-3-zeta

    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

    MKWKALFTAA ILQAQLPITE AQSFGLLDPK LCYLLDGILF IYGVILTALF    50
    LRVKFSRSAD APAYQQGQNQ LYNELNLGRR EEYDVLDKRR GRDPEMGGKP 100
    QRRKNPQEGL YNELQKDKMA EAYSEIGMKG ERRRGKGHDG LYQGLSTATK 150
    DTYDALHMQA LPPR 164
    Length:164
    Mass (Da):18,696
    Last modified:October 10, 2002 - v2
    Checksum:i9408260374856EE9
    GO
    Isoform 2 (identifier: P20963-2)

    Also known as: CD-3-eta

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 3 (identifier: P20963-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-101: Missing.

    Show »
    Length:163
    Mass (Da):18,568
    Checksum:i34898620B67167C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 612DA → EP in AAA60394. (PubMed:2974162)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei101 – 1011Missing in isoform 3. 2 PublicationsVSP_036459

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04132 mRNA. Translation: AAA60394.1.
    AK313946 mRNA. Translation: BAG36664.1.
    DQ072717 Genomic DNA. Translation: AAY57330.1.
    AL359962, AL031733 Genomic DNA. Translation: CAH69974.1.
    AL359962, AL031733 Genomic DNA. Translation: CAH69975.1.
    AL031733, AL359962 Genomic DNA. Translation: CAI21380.1.
    AL031733, AL359962 Genomic DNA. Translation: CAI21381.1.
    CH471067 Genomic DNA. Translation: EAW90792.1.
    BC025703 mRNA. Translation: AAH25703.1.
    CCDSiCCDS1260.1. [P20963-3]
    CCDS1261.1. [P20963-1]
    PIRiA31768.
    RefSeqiNP_000725.1. NM_000734.3. [P20963-3]
    NP_932170.1. NM_198053.2. [P20963-1]
    UniGeneiHs.156445.

    Genome annotation databases

    EnsembliENST00000362089; ENSP00000354782; ENSG00000198821. [P20963-1]
    ENST00000392122; ENSP00000375969; ENSG00000198821. [P20963-3]
    GeneIDi919.
    KEGGihsa:919.
    UCSCiuc001gei.4. human. [P20963-1]
    uc001gej.4. human. [P20963-3]

    Polymorphism databases

    DMDMi23830999.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    CD247base

    CD247 mutation db

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04132 mRNA. Translation: AAA60394.1 .
    AK313946 mRNA. Translation: BAG36664.1 .
    DQ072717 Genomic DNA. Translation: AAY57330.1 .
    AL359962 , AL031733 Genomic DNA. Translation: CAH69974.1 .
    AL359962 , AL031733 Genomic DNA. Translation: CAH69975.1 .
    AL031733 , AL359962 Genomic DNA. Translation: CAI21380.1 .
    AL031733 , AL359962 Genomic DNA. Translation: CAI21381.1 .
    CH471067 Genomic DNA. Translation: EAW90792.1 .
    BC025703 mRNA. Translation: AAH25703.1 .
    CCDSi CCDS1260.1. [P20963-3 ]
    CCDS1261.1. [P20963-1 ]
    PIRi A31768.
    RefSeqi NP_000725.1. NM_000734.3. [P20963-3 ]
    NP_932170.1. NM_198053.2. [P20963-1 ]
    UniGenei Hs.156445.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TCE NMR - B 137-150 [» ]
    1YGR X-ray 2.90 C/D 80-85 [» ]
    2HAC NMR - A/B 28-60 [» ]
    2OQ1 X-ray 1.90 B 69-87 [» ]
    3IK5 X-ray 2.05 B/D 63-80 [» ]
    3IOZ X-ray 3.70 B 51-93 [» ]
    DisProti DP00200.
    ProteinModelPortali P20963.
    SMRi P20963. Positions 28-60.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107357. 28 interactions.
    DIPi DIP-35404N.
    IntActi P20963. 12 interactions.
    MINTi MINT-1517020.
    STRINGi 9606.ENSP00000354782.

    PTM databases

    PhosphoSitei P20963.

    Polymorphism databases

    DMDMi 23830999.

    Proteomic databases

    MaxQBi P20963.
    PaxDbi P20963.
    PRIDEi P20963.

    Protocols and materials databases

    DNASUi 919.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000362089 ; ENSP00000354782 ; ENSG00000198821 . [P20963-1 ]
    ENST00000392122 ; ENSP00000375969 ; ENSG00000198821 . [P20963-3 ]
    GeneIDi 919.
    KEGGi hsa:919.
    UCSCi uc001gei.4. human. [P20963-1 ]
    uc001gej.4. human. [P20963-3 ]

    Organism-specific databases

    CTDi 919.
    GeneCardsi GC01M167399.
    HGNCi HGNC:1677. CD247.
    HPAi CAB004651.
    HPA008750.
    MIMi 186780. gene.
    610163. phenotype.
    neXtProti NX_P20963.
    Orphaneti 85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    169160. T-B+ severe combined immunodeficiency due to CD3delta/CD3epsilon/CD3zeta.
    PharmGKBi PA26219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87611.
    HOGENOMi HOG000234398.
    HOVERGENi HBG005280.
    KOi K06453.
    OMAi LHMQTLP.
    OrthoDBi EOG78SQM7.
    PhylomeDBi P20963.
    TreeFami TF330937.

    Enzyme and pathway databases

    Reactomei REACT_11068. Nef and signal transduction.
    REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12555. Downstream TCR signaling.
    REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_12596. Translocation of ZAP-70 to Immunological synapse.
    REACT_12623. Generation of second messenger molecules.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.
    REACT_19324. PD-1 signaling.
    SignaLinki P20963.

    Miscellaneous databases

    EvolutionaryTracei P20963.
    GeneWikii CD247.
    GenomeRNAii 919.
    NextBioi 3800.
    PROi P20963.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20963.
    Bgeei P20963.
    CleanExi HS_CD247.
    Genevestigatori P20963.

    Family and domain databases

    InterProi IPR021663. CR3_zeta/IgE_Fc_rcpt_gamma.
    IPR003110. Phos_immunorcpt_sig_ITAM.
    IPR024128. T-cell_CD3_zeta/eta.
    [Graphical view ]
    PANTHERi PTHR10035. PTHR10035. 1 hit.
    Pfami PF02189. ITAM. 3 hits.
    PF11628. TCR_zetazeta. 1 hit.
    [Graphical view ]
    SMARTi SM00077. ITAM. 3 hits.
    [Graphical view ]
    PROSITEi PS51055. ITAM_1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and chromosomal localization of the human T-cell receptor zeta chain: distinction from the molecular CD3 complex."
      Weissman A.M., Hou D., Orloff D.G., Modi W.S., Seuanez H., O'Brien S.J., Klausner R.D.
      Proc. Natl. Acad. Sci. U.S.A. 85:9709-9713(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. "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] (ISOFORM 3).
      Tissue: Skeletal muscle.
    3. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Pancreas.
    7. "Zeta chain of the T-cell receptor interacts with nef of simian immunodeficiency virus and human immunodeficiency virus type 2."
      Howe A.Y., Jung J.U., Desrosiers R.C.
      J. Virol. 72:9827-9834(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-2 NEF.
    8. "Stimulation through the T cell receptor leads to interactions between SHB and several signaling proteins."
      Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A., Karlsson T., Miyazaki M., Cantley L.C., Band H., Shoelson S.E.
      Oncogene 16:891-901(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    9. "Induction of Fas ligand expression by HIV involves the interaction of Nef with the T cell receptor zeta chain."
      Xu X.-N., Laffert B., Screaton G.R., Kraft M., Wolf D., Kolanus W., Mongkolsapay J., McMichael A.J., Baur A.S.
      J. Exp. Med. 189:1489-1496(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 NEF.
    10. "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 SLA.
    11. "The transmembrane adaptor protein TRIM regulates T-cell receptor (TCR) expression and TCR-mediated signaling via an association with the TCR zeta chain."
      Kirchgessner H., Dietrich J., Scherer J., Isomaeki P., Korinek V., Hilgert I., Bruyns E., Leo A., Cope A.P., Schraven B.
      J. Exp. Med. 193:1269-1284(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAT1.
    12. "DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription."
      Nishihara H., Maeda M., Tsuda M., Makino Y., Sawa H., Nagashima K., Tanaka S.
      Biochem. Biophys. Res. Commun. 296:716-720(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK2.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83; TYR-111 AND TYR-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-58; TYR-64; TYR-72; TYR-111 AND TYR-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Primary sooty mangabey simian immunodeficiency virus and human immunodeficiency virus type 2 nef alleles modulate cell surface expression of various human receptors and enhance viral infectivity and replication."
      Munch J., Schindler M., Wildum S., Rucker E., Bailer N., Knoop V., Novembre F.J., Kirchhoff F.
      J. Virol. 79:10547-10560(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-2 NEF.
    16. "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-64; TYR-72; TYR-111 AND TYR-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-64; TYR-72; TYR-111; TYR-123; TYR-142 AND TYR-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms."
      Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.
      Cell 72:779-790(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 136-149.
    19. "Inherited and somatic CD3zeta mutations in a patient with T-cell deficiency."
      Rieux-Laucat F., Hivroz C., Lim A., Mateo V., Pellier I., Selz F., Fischer A., Le Deist F.
      N. Engl. J. Med. 354:1913-1921(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CD3ZID.
    20. "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 69-87 IN COMPLEX WITH ZAP70, INTERACTION WITH ZAP70.
    21. "Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor."
      Zhou M.-M., Meadows R.P., Logan T.M., Yoon H.S., Wade W.S., Ravichandran K.S., Burakoff S.J., Fesik S.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:7784-7788(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 137-150 IN COMPLEX WITH SHC1, INTERACTION WITH SHC1.
    22. "Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45."
      Nam H.J., Poy F., Saito H., Frederick C.A.
      J. Exp. Med. 201:441-452(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 80-85 IN COMPLEX WITH PTPRC, INTERACTION WITH PTPRC.
    23. "The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor."
      Call M.E., Schnell J.R., Xu C., Lutz R.A., Chou J.J., Wucherpfennig K.W.
      Cell 127:355-368(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 30-60, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE T CELL RECEPTOR, SUBUNIT.

    Entry informationi

    Entry nameiCD3Z_HUMAN
    AccessioniPrimary (citable) accession number: P20963
    Secondary accession number(s): B1AK49, Q5VX13, Q8TAX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 10, 2002
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 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 cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3