CD3E_HUMAN
ID CD3E_HUMAN Reviewed; 207 AA.
AC P07766; A8K997;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
DE AltName: Full=T-cell surface antigen T3/Leu-4 epsilon chain;
DE AltName: CD_antigen=CD3e;
DE Flags: Precursor;
GN Name=CD3E; Synonyms=T3E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3012357; DOI=10.1038/321431a0;
RA Gold D.P., Puck J.M., Pettey C.L., Cho M., Coligan J., Woody J.N.,
RA Terhorst C.;
RT "Isolation of cDNA clones encoding the 20K non-glycosylated polypeptide
RT chain of the human T-cell receptor/T3 complex.";
RL Nature 321:431-434(1986).
RN [2]
RP SEQUENCE REVISION.
RA Terhorst C.;
RL Submitted (JAN-1987) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=3267235; DOI=10.1073/pnas.85.21.8156;
RA Clevers H.C., Dunlap S., Wileman T.E., Terhorst C.;
RT "Human CD3-epsilon gene contains three miniexons and is transcribed from a
RT non-TATA promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8156-8160(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION BY LCK.
RX PubMed=2470098; DOI=10.1073/pnas.86.9.3277;
RA Barber E.K., Dasgupta J.D., Schlossman S.F., Trevillyan J.M., Rudd C.E.;
RT "The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p56lck)
RT that phosphorylates the CD3 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3277-3281(1989).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=1387664;
RA Lanier L.L., Chang C., Spits H., Phillips J.H.;
RT "Expression of cytoplasmic CD3 epsilon proteins in activated human adult
RT natural killer (NK) cells and CD3 gamma, delta, epsilon complexes in fetal
RT NK cells. Implications for the relationship of NK and T lymphocytes.";
RL J. Immunol. 149:1876-1880(1992).
RN [9]
RP INVOLVEMENT IN IMD18, AND FUNCTION.
RX PubMed=8490660; DOI=10.1038/ng0193-77;
RA Soudais C., de Villartay J.P., Le Deist F., Fischer A.,
RA Lisowska-Grospierre B.;
RT "Independent mutations of the human CD3-epsilon gene resulting in a T cell
RT receptor/CD3 complex immunodeficiency.";
RL Nat. Genet. 3:77-81(1993).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10384095;
RA Borroto A., Lama J., Niedergang F., Dautry-Varsat A., Alarcon B.,
RA Alcover A.;
RT "The CD3 epsilon subunit of the TCR contains endocytosis signals.";
RL J. Immunol. 163:25-31(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=12522270; DOI=10.1073/pnas.2436191100;
RA Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C.,
RA Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
RT "Profiling of tyrosine phosphorylation pathways in human cells using mass
RT spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP INVOLVEMENT IN IMD18, AND FUNCTION.
RX PubMed=15546002; DOI=10.1172/jci200422588;
RA de Saint Basile G., Geissmann F., Flori E., Uring-Lambert B., Soudais C.,
RA Cavazzana-Calvo M., Durandy A., Jabado N., Fischer A., Le Deist F.;
RT "Severe combined immunodeficiency caused by deficiency in either the delta
RT or the epsilon subunit of CD3.";
RL J. Clin. Invest. 114:1512-1517(2004).
RN [14]
RP FUNCTION, INTERACTION WITH CD6, AND SUBCELLULAR LOCATION.
RX PubMed=15294938; DOI=10.4049/jimmunol.173.4.2262;
RA Gimferrer I., Calvo M., Mittelbrunn M., Farnos M., Sarrias M.R., Enrich C.,
RA Vives J., Sanchez-Madrid F., Lozano F.;
RT "Relevance of CD6-mediated interactions in T cell activation and
RT proliferation.";
RL J. Immunol. 173:2262-2270(2004).
RN [15]
RP INTERACTION WITH NCK1.
RX PubMed=15972658; DOI=10.4049/jimmunol.175.1.270;
RA Szymczak A.L., Workman C.J., Gil D., Dilioglou S., Vignali K.M., Palmer E.,
RA Vignali D.A.;
RT "The CD3epsilon proline-rich sequence, and its interaction with Nck, is not
RT required for T cell development and function.";
RL J. Immunol. 175:270-275(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP FUNCTION, INTERACTION WITH NUMB, AND REGION.
RX PubMed=26507128; DOI=10.1093/intimm/dxv060;
RA Martin-Blanco N., Jimenez Teja D., Bretones G., Borroto A., Caraballo M.,
RA Screpanti I., Leon J., Alarcon B., Canelles M.;
RT "CD3epsilon recruits Numb to promote TCR degradation.";
RL Int. Immunol. 28:127-137(2016).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 186-203 IN COMPLEX WITH SYK, AND
RP PHOSPHORYLATION AT TYR-188 AND TYR-199.
RX PubMed=9698567; DOI=10.1006/jmbi.1998.1964;
RA Fuetterer K., Wong J., Grucza R.A., Chan A.C., Waksman G.;
RT "Structural basis for Syk tyrosine kinase ubiquity in signal transduction
RT pathways revealed by the crystal structure of its regulatory SH2 domains
RT bound to a dually phosphorylated ITAM peptide.";
RL J. Mol. Biol. 281:523-537(1998).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-118 IN COMPLEX WITH CD3G AND
RP ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=15136729; DOI=10.1073/pnas.0402295101;
RA Kjer-Nielsen L., Dunstone M.A., Kostenko L., Ely L.K., Beddoe T.,
RA Mifsud N.A., Purcell A.W., Brooks A.G., McCluskey J., Rossjohn J.;
RT "Crystal structure of the human T cell receptor CD3 epsilon gamma
RT heterodimer complexed to the therapeutic mAb OKT3.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7675-7680(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-126 IN COMPLEX WITH CD3D AND
RP ANTIBODY FRAGMENT, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=15534202; DOI=10.1073/pnas.0407359101;
RA Arnett K.L., Harrison S.C., Wiley D.C.;
RT "Crystal structure of a human CD3-epsilon/delta dimer in complex with a
RT UCHT1 single-chain antibody fragment.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16268-16273(2004).
CC -!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
CC surface that plays an essential role in adaptive immune response. When
CC antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-
CC mediated signals are transmitted across the cell membrane by the CD3
CC chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor
CC tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain.
CC Upon TCR engagement, these motifs become phosphorylated by Src family
CC protein tyrosine kinases LCK and FYN, resulting in the activation of
CC downstream signaling pathways (PubMed:2470098). In addition of this
CC role of signal transduction in T-cell activation, CD3E plays an
CC essential role in correct T-cell development. Initiates the TCR-CD3
CC complex assembly by forming the two heterodimers CD3D/CD3E and
CC CD3G/CD3E. Participates also in internalization and cell surface down-
CC regulation of TCR-CD3 complexes via endocytosis sequences present in
CC CD3E cytosolic region (PubMed:10384095, PubMed:26507128).
CC {ECO:0000269|PubMed:10384095, ECO:0000269|PubMed:15294938,
CC ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:2470098,
CC ECO:0000269|PubMed:26507128, ECO:0000269|PubMed:8490660}.
CC -!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E
CC heterodimers that preferentially associate with TCRalpha and TCRbeta,
CC respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers.
CC In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3
CC complex. Alternatively, TCRalpha and TCRbeta can be replaced by
CC TCRgamma and TCRdelta. Interacts with CD6 (PubMed:15294938). Interacts
CC with NCK1 (PubMed:15972658). Interacts with NUMB; this interaction is
CC important for TCR-CD3 internalization and subsequent degradation
CC (PubMed:26507128). {ECO:0000269|PubMed:15136729,
CC ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:15534202,
CC ECO:0000269|PubMed:15972658, ECO:0000269|PubMed:26507128,
CC ECO:0000269|PubMed:9698567}.
CC -!- INTERACTION:
CC P07766; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-1211297, EBI-10225815;
CC P07766; Q12983: BNIP3; NbExp=3; IntAct=EBI-1211297, EBI-749464;
CC P07766; Q8TE68: EPS8L1; NbExp=6; IntAct=EBI-1211297, EBI-7487998;
CC P07766; Q8N387: MUC15; NbExp=3; IntAct=EBI-1211297, EBI-17937277;
CC P07766; P16333: NCK1; NbExp=6; IntAct=EBI-1211297, EBI-389883;
CC P07766; O43639: NCK2; NbExp=4; IntAct=EBI-1211297, EBI-713635;
CC P07766; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-1211297, EBI-12257782;
CC P07766; P43405: SYK; NbExp=6; IntAct=EBI-1211297, EBI-78302;
CC P07766; P43403: ZAP70; NbExp=3; IntAct=EBI-1211297, EBI-1211276;
CC P07766; O95159: ZFPL1; NbExp=3; IntAct=EBI-1211297, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10384095,
CC ECO:0000269|PubMed:15294938}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC LCK in association with CD4/CD8. {ECO:0000269|PubMed:2470098}.
CC -!- DISEASE: Immunodeficiency 18 (IMD18) [MIM:615615]: An autosomal
CC recessive primary immunodeficiency characterized by onset in infancy or
CC early childhood of recurrent infections. The severity is variable,
CC encompassing both a mild immunodeficiency and severe combined
CC immunodeficiency (SCID), resulting in early death without bone marrow
CC transplantation in some patients. Immunologic work-up of the IMD18 SCID
CC patients shows a T cell-negative, B cell-positive, natural killer (NK)
CC cell-positive phenotype, whereas T-cell development is not impaired in
CC the mild form of IMD18. {ECO:0000269|PubMed:15546002,
CC ECO:0000269|PubMed:8490660}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=CD3Ebase; Note=CD3E mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CD3Ebase/";
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DR EMBL; X03884; CAA27516.1; -; mRNA.
DR EMBL; M23323; AAA52295.1; -; Genomic_DNA.
DR EMBL; M23317; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; M23318; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; M23319; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; M23320; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; M23321; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; L34846; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; M23322; AAA52295.1; JOINED; Genomic_DNA.
DR EMBL; AK292612; BAF85301.1; -; mRNA.
DR EMBL; CH471065; EAW67364.1; -; Genomic_DNA.
DR EMBL; BC049847; AAH49847.1; -; mRNA.
DR CCDS; CCDS31685.1; -.
DR PIR; A32069; A32069.
DR RefSeq; NP_000724.1; NM_000733.3.
DR PDB; 1A81; X-ray; 3.00 A; B/D/F/H/J/L=186-203.
DR PDB; 1SY6; X-ray; 2.10 A; A=21-118.
DR PDB; 1XIW; X-ray; 1.90 A; A/E=23-126.
DR PDB; 2ROL; NMR; -; B=181-192.
DR PDB; 5QU2; X-ray; 1.04 A; D/E=180-188.
DR PDB; 6JXR; EM; 3.70 A; e/f=1-207.
DR PDBsum; 1A81; -.
DR PDBsum; 1SY6; -.
DR PDBsum; 1XIW; -.
DR PDBsum; 2ROL; -.
DR PDBsum; 5QU2; -.
DR PDBsum; 6JXR; -.
DR AlphaFoldDB; P07766; -.
DR BMRB; P07766; -.
DR SMR; P07766; -.
DR BioGRID; 107354; 67.
DR ComplexPortal; CPX-6482; Alpha-beta T cell receptor complex, TRBC2 variant.
DR ComplexPortal; CPX-6581; Alpha-beta T cell receptor complex, TRBC1 variant.
DR ComplexPortal; CPX-6582; Gamma-delta T cell receptor complex, TRGC1 variant.
DR ComplexPortal; CPX-6603; Gamma-delta T cell receptor complex, TRGC2 variant.
DR ELM; P07766; -.
DR IntAct; P07766; 27.
DR MINT; P07766; -.
DR STRING; 9606.ENSP00000354566; -.
DR ChEMBL; CHEMBL1975; -.
DR DrugBank; DB06607; Catumaxomab.
DR DrugBank; DB00075; Muromonab.
DR DrugBank; DB06606; Teplizumab.
DR DrugCentral; P07766; -.
DR GuidetoPHARMACOLOGY; 2742; -.
DR TCDB; 8.A.128.1.10; the signaling adaptor protein karap/dap12/tyrobp (sap) family.
DR GlyGen; P07766; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07766; -.
DR PhosphoSitePlus; P07766; -.
DR BioMuta; CD3E; -.
DR DMDM; 1345708; -.
DR jPOST; P07766; -.
DR MassIVE; P07766; -.
DR MaxQB; P07766; -.
DR PaxDb; P07766; -.
DR PeptideAtlas; P07766; -.
DR PRIDE; P07766; -.
DR ProteomicsDB; 52027; -.
DR ABCD; P07766; 183 sequenced antibodies.
DR Antibodypedia; 3494; 7099 antibodies from 58 providers.
DR DNASU; 916; -.
DR Ensembl; ENST00000361763.9; ENSP00000354566.4; ENSG00000198851.10.
DR GeneID; 916; -.
DR KEGG; hsa:916; -.
DR MANE-Select; ENST00000361763.9; ENSP00000354566.4; NM_000733.4; NP_000724.1.
DR UCSC; uc001psq.5; human.
DR CTD; 916; -.
DR DisGeNET; 916; -.
DR GeneCards; CD3E; -.
DR HGNC; HGNC:1674; CD3E.
DR HPA; ENSG00000198851; Tissue enriched (lymphoid).
DR MalaCards; CD3E; -.
DR MIM; 186830; gene.
DR MIM; 615615; phenotype.
DR neXtProt; NX_P07766; -.
DR OpenTargets; ENSG00000198851; -.
DR Orphanet; 169160; T-B+ severe combined immunodeficiency due to CD3delta/CD3epsilon/CD3zeta.
DR PharmGKB; PA26216; -.
DR VEuPathDB; HostDB:ENSG00000198851; -.
DR eggNOG; ENOG502S8KB; Eukaryota.
DR GeneTree; ENSGT00940000153312; -.
DR InParanoid; P07766; -.
DR OMA; RVCENCV; -.
DR OrthoDB; 1362562at2759; -.
DR PhylomeDB; P07766; -.
DR TreeFam; TF335892; -.
DR PathwayCommons; P07766; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-389948; PD-1 signaling.
DR SignaLink; P07766; -.
DR SIGNOR; P07766; -.
DR BioGRID-ORCS; 916; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; CD3E; human.
DR EvolutionaryTrace; P07766; -.
DR GeneWiki; T-cell_surface_glycoprotein_CD3_epsilon_chain; -.
DR GenomeRNAi; 916; -.
DR Pharos; P07766; Tclin.
DR PRO; PR:P07766; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P07766; protein.
DR Bgee; ENSG00000198851; Expressed in granulocyte and 104 other tissues.
DR ExpressionAtlas; P07766; baseline and differential.
DR Genevisible; P07766; HS.
DR GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0042106; C:gamma-delta T cell receptor complex; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042101; C:T cell receptor complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0019901; F:protein kinase binding; NAS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0042608; F:T cell receptor binding; NAS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0046631; P:alpha-beta T cell activation; IC:ComplexPortal.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0046629; P:gamma-delta T cell activation; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:BHF-UCL.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0002669; P:positive regulation of T cell anergy; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR GO; GO:0002870; P:T cell anergy; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR DisProt; DP00506; -.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR015484; CD3_esu/gsu/dsu.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR PANTHER; PTHR10570; PTHR10570; 1.
DR Pfam; PF02189; ITAM; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00077; ITAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS51055; ITAM_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT CHAIN 23..207
FT /note="T-cell surface glycoprotein CD3 epsilon chain"
FT /id="PRO_0000014607"
FT TOPO_DOM 23..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..112
FT /note="Ig-like"
FT DOMAIN 178..205
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT REGION 161..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..192
FT /note="NUMB-binding region"
FT /evidence="ECO:0000269|PubMed:26507128"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379,
FT ECO:0000269|PubMed:9698567, ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 199
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379,
FT ECO:0000269|PubMed:9698567"
FT DISULFID 49..98
FT /evidence="ECO:0000269|PubMed:15136729,
FT ECO:0000269|PubMed:15534202"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1XIW"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1XIW"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1XIW"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1XIW"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1A81"
SQ SEQUENCE 207 AA; 23147 MW; A1603D01CE9957D7 CRC64;
MQSGTHWRVL GLCLLSVGVW GQDGNEEMGG ITQTPYKVSI SGTTVILTCP QYPGSEILWQ
HNDKNIGGDE DDKNIGSDED HLSLKEFSEL EQSGYYVCYP RGSKPEDANF YLYLRARVCE
NCMEMDVMSV ATIVIVDICI TGGLLLLVYY WSKNRKAKAK PVTRGAGAGG RQRGQNKERP
PPVPNPDYEP IRKGQRDLYS GLNQRRI
