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P20963 (CD3Z_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD3 zeta chain
Alternative name(s):
T-cell receptor T3 zeta chain
CD_antigen=CD247
Gene names
Name:CD247
Synonyms:CD3Z, T3Z, TCRZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.20 Ref.21 Ref.22 Ref.23

Subcellular location

Membrane; Single-pass type I membrane protein.

Domain

The ITAM domains mediate interaction with SHB.

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the CD3Z/FCER1G family.

Contains 3 ITAM domains.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

regulation of immune response

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentT cell receptor complex

Inferred from direct assay PubMed 8176201. Source: MGI

alpha-beta T cell receptor complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.11. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.11PubMed 1390434. Source: MGI

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.23. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11891219PubMed 7528772. Source: UniProtKB

protein homodimerization activity

Non-traceable author statement PubMed 12110186. Source: UniProtKB

transmembrane signaling receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20963-1)

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.
Isoform 2 (identifier: P20963-2)

Also known as: CD-3-eta;

The sequence of this isoform is not available.
Isoform 3 (identifier: P20963-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 164143T-cell surface glycoprotein CD3 zeta chain
PRO_0000016493

Regions

Topological domain22 – 309Extracellular Potential
Transmembrane31 – 5121Helical; Potential
Topological domain52 – 164113Cytoplasmic Potential
Domain61 – 8929ITAM 1
Domain100 – 12829ITAM 2
Domain131 – 15929ITAM 3

Amino acid modifications

Modified residue581Phosphoserine Ref.14
Modified residue641Phosphotyrosine Ref.14 Ref.16 Ref.17
Modified residue721Phosphotyrosine Ref.14 Ref.16 Ref.17
Modified residue831Phosphotyrosine Ref.13
Modified residue1111Phosphotyrosine Ref.13 Ref.14 Ref.16 Ref.17
Modified residue1231Phosphotyrosine Ref.17
Modified residue1421Phosphotyrosine Ref.13 Ref.14 Ref.16 Ref.17
Modified residue1531Phosphotyrosine Ref.17
Disulfide bond32Interchain Potential

Natural variations

Alternative sequence1011Missing in isoform 3.
VSP_036459

Experimental info

Sequence conflict60 – 612DA → EP in AAA60394. Ref.1

Secondary structure

....... 164
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CD-3-zeta) [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: 9408260374856EE9

FASTA16418,696
        10         20         30         40         50         60 
MKWKALFTAA ILQAQLPITE AQSFGLLDPK LCYLLDGILF IYGVILTALF LRVKFSRSAD 

        70         80         90        100        110        120 
APAYQQGQNQ LYNELNLGRR EEYDVLDKRR GRDPEMGGKP QRRKNPQEGL YNELQKDKMA 

       130        140        150        160 
EAYSEIGMKG ERRRGKGHDG LYQGLSTATK DTYDALHMQA LPPR 

« Hide

Isoform 2 (CD-3-eta) (Sequence not available).
Isoform 3 [UniParc].

Checksum: 34898620B67167C7
Show »

FASTA16318,568

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

CD247base

CD247 mutation db

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1260.1. [P20963-3]
CCDS1261.1. [P20963-1]
PIRA31768.
RefSeqNP_000725.1. NM_000734.3. [P20963-3]
NP_932170.1. NM_198053.2. [P20963-1]
UniGeneHs.156445.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00200.
ProteinModelPortalP20963.
SMRP20963. Positions 28-60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107357. 28 interactions.
DIPDIP-35404N.
IntActP20963. 10 interactions.
MINTMINT-1517020.
STRING9606.ENSP00000354782.

PTM databases

PhosphoSiteP20963.

Polymorphism databases

DMDM23830999.

Proteomic databases

MaxQBP20963.
PaxDbP20963.
PRIDEP20963.

Protocols and materials databases

DNASU919.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000362089; ENSP00000354782; ENSG00000198821. [P20963-1]
ENST00000392122; ENSP00000375969; ENSG00000198821. [P20963-3]
GeneID919.
KEGGhsa:919.
UCSCuc001gei.4. human. [P20963-1]
uc001gej.4. human. [P20963-3]

Organism-specific databases

CTD919.
GeneCardsGC01M167399.
HGNCHGNC:1677. CD247.
HPACAB004651.
HPA008750.
MIM186780. gene.
610163. phenotype.
neXtProtNX_P20963.
Orphanet85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
169160. T-B+ severe combined immunodeficiency due to CD3delta/CD3epsilon/CD3zeta.
PharmGKBPA26219.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87611.
HOGENOMHOG000234398.
HOVERGENHBG005280.
KOK06453.
OMALHMQTLP.
OrthoDBEOG78SQM7.
PhylomeDBP20963.
TreeFamTF330937.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP20963.

Gene expression databases

ArrayExpressP20963.
BgeeP20963.
CleanExHS_CD247.
GenevestigatorP20963.

Family and domain databases

InterProIPR021663. CR3_zeta/IgE_Fc_rcpt_gamma.
IPR003110. Phos_immunorcpt_sig_ITAM.
IPR024128. T-cell_CD3_zeta/eta.
[Graphical view]
PANTHERPTHR10035. PTHR10035. 1 hit.
PfamPF02189. ITAM. 3 hits.
PF11628. TCR_zetazeta. 1 hit.
[Graphical view]
SMARTSM00077. ITAM. 3 hits.
[Graphical view]
PROSITEPS51055. ITAM_1. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20963.
GeneWikiCD247.
GenomeRNAi919.
NextBio3800.
PROP20963.
SOURCESearch...

Entry information

Entry nameCD3Z_HUMAN
AccessionPrimary (citable) accession number: P20963
Secondary accession number(s): B1AK49, Q5VX13, Q8TAX4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 10, 2002
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries