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P20963

- CD3Z_HUMAN

UniProt

P20963 - CD3Z_HUMAN

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Protein
T-cell surface glycoprotein CD3 zeta chain
Gene
CD247, CD3Z, T3Z, TCRZ
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. T cell costimulation Source: Reactome
  3. T cell receptor signaling pathway Source: Reactome
  4. innate immune response Source: Reactome
  5. regulation of defense response to virus by virus Source: Reactome
  6. regulation of immune response Source: Reactome
  7. viral process Source: Reactome
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 309Extracellular Reviewed prediction
Transmembranei31 – 5121Helical; Reviewed prediction
Add
BLAST
Topological domaini52 – 164113Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 2121
Add
BLAST
Chaini22 – 164143T-cell surface glycoprotein CD3 zeta chain
PRO_0000016493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 – 32Interchain Reviewed prediction
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei64 – 641Phosphotyrosine3 Publications
Modified residuei72 – 721Phosphotyrosine3 Publications
Modified residuei83 – 831Phosphotyrosine1 Publication
Modified residuei111 – 1111Phosphotyrosine4 Publications
Modified residuei123 – 1231Phosphotyrosine1 Publication
Modified residuei142 – 1421Phosphotyrosine4 Publications
Modified residuei153 – 1531Phosphotyrosine1 Publication

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. 10 interactions.
MINTiMINT-1517020.
STRINGi9606.ENSP00000354782.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP20963.

Family & Domainsi

Domains and Repeats

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

Domaini

The ITAM domains mediate interaction with SHB.

Sequence similaritiesi

Belongs to the CD3Z/FCER1G family.
Contains 3 ITAM domains.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 1011Missing in isoform 3.
VSP_036459

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 612DA → EP in AAA60394. 1 Publication

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. 10 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 161 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

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