GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

T-cell surface glycoprotein CD3 epsilon chain (T-cell surface antigen T3/Leu-4 epsilon chain) (CD antigen CD3e)

 CD3E_HUMAN              Reviewed;         207 AA.
P07766; A8K997;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
13-FEB-2019, entry version 201.
RecName: Full=T-cell surface glycoprotein CD3 epsilon chain;
AltName: Full=T-cell surface antigen T3/Leu-4 epsilon chain;
AltName: CD_antigen=CD3e;
Flags: Precursor;
Name=CD3E; Synonyms=T3E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3012357; DOI=10.1038/321431a0;
Gold D.P., Puck J.M., Pettey C.L., Cho M., Coligan J., Woody J.N.,
Terhorst C.;
"Isolation of cDNA clones encoding the 20K non-glycosylated
polypeptide chain of the human T-cell receptor/T3 complex.";
Nature 321:431-434(1986).
[2]
SEQUENCE REVISION.
Terhorst C.;
Submitted (JAN-1987) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=3267235; DOI=10.1073/pnas.85.21.8156;
Clevers H.C., Dunlap S., Wileman T.E., Terhorst C.;
"Human CD3-epsilon gene contains three miniexons and is transcribed
from a non-TATA promoter.";
Proc. Natl. Acad. Sci. U.S.A. 85:8156-8160(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND PHOSPHORYLATION BY LCK.
PubMed=2470098;
Barber E.K., Dasgupta J.D., Schlossman S.F., Trevillyan J.M.,
Rudd C.E.;
"The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase
(p56lck) that phosphorylates the CD3 complex.";
Proc. Natl. Acad. Sci. U.S.A. 86:3277-3281(1989).
[8]
TISSUE SPECIFICITY.
PubMed=1387664;
Lanier L.L., Chang C., Spits H., Phillips J.H.;
"Expression of cytoplasmic CD3 epsilon proteins in activated human
adult natural killer (NK) cells and CD3 gamma, delta, epsilon
complexes in fetal NK cells. Implications for the relationship of NK
and T lymphocytes.";
J. Immunol. 149:1876-1880(1992).
[9]
INVOLVEMENT IN IMD18, AND FUNCTION.
PubMed=8490660; DOI=10.1038/ng0193-77;
Soudais C., de Villartay J.P., Le Deist F., Fischer A.,
Lisowska-Grospierre B.;
"Independent mutations of the human CD3-epsilon gene resulting in a T
cell receptor/CD3 complex immunodeficiency.";
Nat. Genet. 3:77-81(1993).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10384095;
Borroto A., Lama J., Niedergang F., Dautry-Varsat A., Alarcon B.,
Alcover A.;
"The CD3 epsilon subunit of the TCR contains endocytosis signals.";
J. Immunol. 163:25-31(1999).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
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.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[13]
INVOLVEMENT IN IMD18, AND FUNCTION.
PubMed=15546002; DOI=10.1172/JCI22588;
de Saint Basile G., Geissmann F., Flori E., Uring-Lambert B.,
Soudais C., Cavazzana-Calvo M., Durandy A., Jabado N., Fischer A.,
Le Deist F.;
"Severe combined immunodeficiency caused by deficiency in either the
delta or the epsilon subunit of CD3.";
J. Clin. Invest. 114:1512-1517(2004).
[14]
FUNCTION, INTERACTION WITH CD6, AND SUBCELLULAR LOCATION.
PubMed=15294938; DOI=10.4049/jimmunol.173.4.2262;
Gimferrer I., Calvo M., Mittelbrunn M., Farnos M., Sarrias M.R.,
Enrich C., Vives J., Sanchez-Madrid F., Lozano F.;
"Relevance of CD6-mediated interactions in T cell activation and
proliferation.";
J. Immunol. 173:2262-2270(2004).
[15]
INTERACTION WITH NCK1.
PubMed=15972658;
Szymczak A.L., Workman C.J., Gil D., Dilioglou S., Vignali K.M.,
Palmer E., Vignali D.A.;
"The CD3epsilon proline-rich sequence, and its interaction with Nck,
is not required for T cell development and function.";
J. Immunol. 175:270-275(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
FUNCTION, INTERACTION WITH NUMB, AND REGION.
PubMed=26507128; DOI=10.1093/intimm/dxv060;
Martin-Blanco N., Jimenez Teja D., Bretones G., Borroto A.,
Caraballo M., Screpanti I., Leon J., Alarcon B., Canelles M.;
"CD3epsilon recruits Numb to promote TCR degradation.";
Int. Immunol. 28:127-137(2016).
[19]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 186-203 IN COMPLEX WITH SYK,
AND PHOSPHORYLATION AT TYR-188 AND TYR-199.
PubMed=9698567; DOI=10.1006/jmbi.1998.1964;
Fuetterer K., Wong J., Grucza R.A., Chan A.C., Waksman G.;
"Structural basis for Syk tyrosine kinase ubiquity in signal
transduction pathways revealed by the crystal structure of its
regulatory SH2 domains bound to a dually phosphorylated ITAM
peptide.";
J. Mol. Biol. 281:523-537(1998).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-118 IN COMPLEX WITH CD3G
AND ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
PubMed=15136729; DOI=10.1073/pnas.0402295101;
Kjer-Nielsen L., Dunstone M.A., Kostenko L., Ely L.K., Beddoe T.,
Mifsud N.A., Purcell A.W., Brooks A.G., McCluskey J., Rossjohn J.;
"Crystal structure of the human T cell receptor CD3 epsilon gamma
heterodimer complexed to the therapeutic mAb OKT3.";
Proc. Natl. Acad. Sci. U.S.A. 101:7675-7680(2004).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-126 IN COMPLEX WITH CD3D
AND ANTIBODY FRAGMENT, SUBUNIT, AND DISULFIDE BOND.
PubMed=15534202; DOI=10.1073/pnas.0407359101;
Arnett K.L., Harrison S.C., Wiley D.C.;
"Crystal structure of a human CD3-epsilon/delta dimer in complex with
a UCHT1 single-chain antibody fragment.";
Proc. Natl. Acad. Sci. U.S.A. 101:16268-16273(2004).
-!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
surface that plays an essential role in adaptive immune response.
When antigen presenting cells (APCs) activate T-cell receptor
(TCR), TCR-mediated signals are transmitted across the cell
membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3
chains contain immunoreceptor tyrosine-based activation motifs
(ITAMs) in their cytoplasmic domain. Upon TCR engagement, these
motifs become phosphorylated by Src family protein tyrosine
kinases LCK and FYN, resulting in the activation of downstream
signaling pathways (PubMed:2470098). In addition of this role of
signal transduction in T-cell activation, CD3E plays an essential
role in correct T-cell development. Initiates the TCR-CD3 complex
assembly by forming the two heterodimers CD3D/CD3E and CD3G/CD3E.
Participates also in internalization and cell surface down-
regulation of TCR-CD3 complexes via endocytosis sequences present
in CD3E cytosolic region (PubMed:10384095, PubMed:26507128).
{ECO:0000269|PubMed:10384095, ECO:0000269|PubMed:15294938,
ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:2470098,
ECO:0000269|PubMed:26507128, ECO:0000269|PubMed:8490660}.
-!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a
CD3G/CD3E heterodimers that preferentially associate with TCRalpha
and TCRbeta, respectively, to form TCRalpha/CD3E/CD3G and
TCRbeta/CD3G/CD3E trimers. In turn, the hexamer interacts with
CD3Z homodimer to form the TCR-CD3 complex. Alternatively,
TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta.
Interacts with CD6 (PubMed:15294938). Interacts with NCK1
(PubMed:15972658). Interacts with NUMB; this interaction is
important for TCR-CD3 internalization and subsequent degradation
(PubMed:26507128). {ECO:0000269|PubMed:15136729,
ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:15534202,
ECO:0000269|PubMed:15972658, ECO:0000269|PubMed:26507128,
ECO:0000269|PubMed:9698567}.
-!- INTERACTION:
Q8TE68:EPS8L1; NbExp=6; IntAct=EBI-1211297, EBI-7487998;
P16333:NCK1; NbExp=6; IntAct=EBI-1211297, EBI-389883;
O43639:NCK2; NbExp=3; IntAct=EBI-1211297, EBI-713635;
P43405:SYK; NbExp=6; IntAct=EBI-1211297, EBI-78302;
P43403:ZAP70; NbExp=3; IntAct=EBI-1211297, EBI-1211276;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10384095,
ECO:0000269|PubMed:15294938}; Single-pass type I membrane protein
{ECO:0000305}.
-!- PTM: Phosphorylated on Tyr residues after T-cell receptor
triggering by LCK in association with CD4/CD8.
{ECO:0000269|PubMed:2470098}.
-!- DISEASE: Immunodeficiency 18 (IMD18) [MIM:615615]: An autosomal
recessive primary immunodeficiency characterized by onset in
infancy or early childhood of recurrent infections. The severity
is variable, encompassing both a mild immunodeficiency and severe
combined immunodeficiency (SCID), resulting in early death without
bone marrow transplantation in some patients. Immunologic work-up
of the IMD18 SCID patients shows a T cell-negative, B cell-
positive, natural killer (NK) cell-positive phenotype, whereas T-
cell development is not impaired in the mild form of IMD18.
{ECO:0000269|PubMed:15546002, ECO:0000269|PubMed:8490660}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=CD3Ebase; Note=CD3E mutation db;
URL="http://structure.bmc.lu.se/idbase/CD3Ebase/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X03884; CAA27516.1; -; mRNA.
EMBL; M23323; AAA52295.1; -; Genomic_DNA.
EMBL; M23317; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23318; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23319; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23320; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23321; AAA52295.1; JOINED; Genomic_DNA.
EMBL; L34846; AAA52295.1; JOINED; Genomic_DNA.
EMBL; M23322; AAA52295.1; JOINED; Genomic_DNA.
EMBL; AK292612; BAF85301.1; -; mRNA.
EMBL; CH471065; EAW67364.1; -; Genomic_DNA.
EMBL; BC049847; AAH49847.1; -; mRNA.
CCDS; CCDS31685.1; -.
PIR; A32069; A32069.
RefSeq; NP_000724.1; NM_000733.3.
UniGene; Hs.3003; -.
PDB; 1A81; X-ray; 3.00 A; B/D/F/H/J/L=186-203.
PDB; 1SY6; X-ray; 2.10 A; A=21-118.
PDB; 1XIW; X-ray; 1.90 A; A/E=23-126.
PDB; 2ROL; NMR; -; B=181-192.
PDBsum; 1A81; -.
PDBsum; 1SY6; -.
PDBsum; 1XIW; -.
PDBsum; 2ROL; -.
DisProt; DP00506; -.
ProteinModelPortal; P07766; -.
SMR; P07766; -.
BioGrid; 107354; 25.
ELM; P07766; -.
IntAct; P07766; 21.
MINT; P07766; -.
STRING; 9606.ENSP00000354566; -.
ChEMBL; CHEMBL1975; -.
DrugBank; DB00075; Muromonab.
GuidetoPHARMACOLOGY; 2742; -.
iPTMnet; P07766; -.
PhosphoSitePlus; P07766; -.
BioMuta; CD3E; -.
DMDM; 1345708; -.
jPOST; P07766; -.
MaxQB; P07766; -.
PaxDb; P07766; -.
PeptideAtlas; P07766; -.
PRIDE; P07766; -.
ProteomicsDB; 52027; -.
DNASU; 916; -.
Ensembl; ENST00000361763; ENSP00000354566; ENSG00000198851.
GeneID; 916; -.
KEGG; hsa:916; -.
UCSC; uc001psq.5; human.
CTD; 916; -.
DisGeNET; 916; -.
EuPathDB; HostDB:ENSG00000198851.9; -.
GeneCards; CD3E; -.
HGNC; HGNC:1674; CD3E.
HPA; CAB000010; -.
HPA; CAB072863; -.
HPA; CAB072864; -.
HPA; HPA040957; -.
HPA; HPA043955; -.
MalaCards; CD3E; -.
MIM; 186830; gene.
MIM; 615615; phenotype.
neXtProt; NX_P07766; -.
OpenTargets; ENSG00000198851; -.
Orphanet; 169160; T-B+ severe combined immunodeficiency due to CD3delta/CD3epsilon/CD3zeta.
PharmGKB; PA26216; -.
eggNOG; ENOG410IYD1; Eukaryota.
eggNOG; ENOG41123JN; LUCA.
GeneTree; ENSGT00940000153312; -.
HOGENOM; HOG000290664; -.
HOVERGEN; HBG102121; -.
InParanoid; P07766; -.
KO; K06451; -.
OMA; VGAWGQE; -.
OrthoDB; 1362562at2759; -.
PhylomeDB; P07766; -.
TreeFam; TF335892; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-389948; PD-1 signaling.
SignaLink; P07766; -.
SIGNOR; P07766; -.
ChiTaRS; CD3E; human.
EvolutionaryTrace; P07766; -.
GeneWiki; T-cell_surface_glycoprotein_CD3_epsilon_chain; -.
GenomeRNAi; 916; -.
PRO; PR:P07766; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000198851; Expressed in 107 organ(s), highest expression level in leukocyte.
ExpressionAtlas; P07766; baseline and differential.
Genevisible; P07766; HS.
GO; GO:0042105; C:alpha-beta T cell receptor complex; IBA:GO_Central.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0042101; C:T cell receptor complex; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0019901; F:protein kinase binding; NAS:UniProtKB.
GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0042608; F:T cell receptor binding; NAS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Ensembl.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:BHF-UCL.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0002669; P:positive regulation of T cell anergy; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; IBA:GO_Central.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR015484; CD3_esu/gsu/dsu.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
PANTHER; PTHR10570; PTHR10570; 1.
Pfam; PF02189; ITAM; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00077; ITAM; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS51055; ITAM_1; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Disulfide bond; Immunity; Immunoglobulin domain; Membrane;
Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22
CHAIN 23 207 T-cell surface glycoprotein CD3 epsilon
chain.
/FTId=PRO_0000014607.
TOPO_DOM 23 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 152 Helical. {ECO:0000255}.
TOPO_DOM 153 207 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 112 Ig-like.
DOMAIN 178 205 ITAM. {ECO:0000255|PROSITE-
ProRule:PRU00379}.
REGION 175 192 NUMB-binding region.
{ECO:0000269|PubMed:26507128}.
MOD_RES 188 188 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:19690332,
ECO:0000255|PROSITE-ProRule:PRU00379,
ECO:0000269|PubMed:9698567}.
MOD_RES 199 199 Phosphotyrosine. {ECO:0000255|PROSITE-
ProRule:PRU00379,
ECO:0000269|PubMed:9698567}.
DISULFID 49 98 {ECO:0000269|PubMed:15136729,
ECO:0000269|PubMed:15534202}.
STRAND 37 41 {ECO:0000244|PDB:1XIW}.
STRAND 44 48 {ECO:0000244|PDB:1XIW}.
STRAND 57 61 {ECO:0000244|PDB:1XIW}.
STRAND 64 69 {ECO:0000244|PDB:1XIW}.
STRAND 75 78 {ECO:0000244|PDB:1XIW}.
STRAND 81 84 {ECO:0000244|PDB:1XIW}.
HELIX 89 92 {ECO:0000244|PDB:1XIW}.
STRAND 94 100 {ECO:0000244|PDB:1XIW}.
HELIX 105 107 {ECO:0000244|PDB:1XIW}.
STRAND 110 116 {ECO:0000244|PDB:1XIW}.
HELIX 193 195 {ECO:0000244|PDB:1A81}.
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


Related products :

Catalog number Product name Quantity
E1872h ELISA kit CD3E,Homo sapiens,Human,T3E,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
U1872h CLIA CD3E,Homo sapiens,Human,T3E,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
E1872h ELISA CD3E,Homo sapiens,Human,T3E,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
U1872h CLIA kit CD3E,Homo sapiens,Human,T3E,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
E1872m ELISA kit Cd3e,Mouse,Mus musculus,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
E1872m ELISA Cd3e,Mouse,Mus musculus,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
U1872m CLIA Cd3e,Mouse,Mus musculus,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
U1872m CLIA kit Cd3e,Mouse,Mus musculus,T-cell surface antigen T3_Leu-4 epsilon chain,T-cell surface glycoprotein CD3 epsilon chain 96T
H4325 T-cell surface glycoprotein CD3 epsilon chain (CD3E), Cat, ELISA Kit 96T
CSB-EL004931DO Dog T-cell surface glycoprotein CD3 epsilon chain(CD3E) ELISA kit 96T
H4329 T-cell surface glycoprotein CD3 epsilon chain (CD3E), Pig, ELISA Kit 96T
CSB-EL004931CA Cat T-cell surface glycoprotein CD3 epsilon chain(CD3E) ELISA kit 96T
H4327 T-cell surface glycoprotein CD3 epsilon chain (CD3E), Dog, ELISA Kit 96T
E1872p ELISA kit CD3E,Pig,Sus scrofa,T-cell surface glycoprotein CD3 epsilon chain 96T
CSB-EL004931HU Human T-cell surface glycoprotein CD3 epsilon chain(CD3E) ELISA kit 96T
CSB-EL004931CA Cat T-cell surface glycoprotein CD3 epsilon chain(CD3E) ELISA kit SpeciesCat 96T
U1872p CLIA kit CD3E,Pig,Sus scrofa,T-cell surface glycoprotein CD3 epsilon chain 96T
E1872p ELISA CD3E,Pig,Sus scrofa,T-cell surface glycoprotein CD3 epsilon chain 96T
H4324 T-cell surface glycoprotein CD3 epsilon chain (CD3E), Bovine, ELISA Kit 96T
CSB-EL004931PI Pig T-cell surface glycoprotein CD3 epsilon chain(CD3E) ELISA kit SpeciesPig 96T
H4330 T-cell surface glycoprotein CD3 epsilon chain (CD3E), Rabbit, ELISA Kit 96T
CSB-EL004931BO Bovine T-cell surface glycoprotein CD3 epsilon chain(CD3E) ELISA kit 96T
H4328 T-cell surface glycoprotein CD3 epsilon chain (CD3E), Human, ELISA Kit 96T
H4332 T-cell surface glycoprotein CD3 epsilon chain(CD3E T3E), Mouse, ELISA Kit 96T
U1872p CLIA CD3E,Pig,Sus scrofa,T-cell surface glycoprotein CD3 epsilon chain 96T

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1794: Cell surface interactions at the vascular wall
WP1833: Integrin cell surface interactions
WP2328: Allograft rejection
WP1011: T Cell Receptor Signaling Pathway
WP1130: T Cell Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP352: T Cell Receptor Signaling Pathway
WP480: T Cell Receptor Signaling Pathway
WP780: T Cell Receptor Signaling Pathway
WP894: T Cell Receptor Signaling Pathway
WP1002: Electron Transport Chain
WP1025: B Cell Receptor Signaling Pathway
WP1043: Calcium Regulation in the Cardiac Cell
WP1069: Integrin-mediated cell adhesion
WP1078: G1 to S cell cycle control
WP1083: Cell cycle
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1144: B Cell Receptor Signaling Pathway
WP1159: Calcium Regulation in the Cardiac Cell
WP1185: Integrin-mediated cell adhesion
WP1195: G1 to S cell cycle control
WP1200: Cell cycle
WP1339: Electron Transport Chain
WP1354: B Cell Receptor Signaling Pathway

Related Genes :
[CD3E T3E] T-cell surface glycoprotein CD3 epsilon chain (T-cell surface antigen T3/Leu-4 epsilon chain) (CD antigen CD3e)
[CD3G T3G] T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g)
[CD3D T3D] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[Cd3d T3d] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[Cd3g] T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g)
[Cd247 Cd3z Tcrz] T-cell surface glycoprotein CD3 zeta chain (T-cell receptor T3 zeta chain) (CD antigen CD247)
[Cd3d T3d] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[CD3G] T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g)
[CD3D] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[CD3D] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[Cd3g] T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g)
[CD3D] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[CD3G] T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g)
[CD3G] T-cell surface glycoprotein CD3 gamma chain (T-cell receptor T3 gamma chain) (CD antigen CD3g) (Fragment)
[CD3D] T-cell surface glycoprotein CD3 delta chain (T-cell receptor T3 delta chain) (CD antigen CD3d)
[Cd4] T-cell surface glycoprotein CD4 (T-cell differentiation antigen L3T4) (T-cell surface antigen T4/Leu-3) (CD antigen CD4)
[CD4] T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (CD antigen CD4)
[Cd4] T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (W3/25 antigen) (CD antigen CD4)
[CD8A MAL] T-cell surface glycoprotein CD8 alpha chain (T-lymphocyte differentiation antigen T8/Leu-2) (CD antigen CD8a)
[CD3E] T-cell surface glycoprotein CD3 epsilon chain (CD antigen CD3e)
[CD6] T-cell differentiation antigen CD6 (T12) (TP120) (CD antigen CD6) [Cleaved into: Soluble CD6]
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CD4] T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (CD antigen CD4)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CD1A] T-cell surface glycoprotein CD1a (T-cell surface antigen T6/Leu-6) (hTa1 thymocyte antigen) (CD antigen CD1a)
[B3GALNT1 B3GALT3 UNQ531/PRO1074] UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 (Beta-1,3-GalNAc-T1) (EC 2.4.1.79) (Beta-1,3-galactosyltransferase 3) (Beta-1,3-GalTase 3) (Beta3Gal-T3) (Beta3GalT3) (b3Gal-T3) (Beta-3-Gx-T3) (Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase) (Globoside synthase) (UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase)
[env gp160] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :
?>