P20963 (CD3Z_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Traceable author statement. Source: Reactome T cell receptor signaling pathway Traceable author statement. Source: Reactome regulation of defense response to virus by virus Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	T cell receptor complex Inferred from direct assay PubMed 8176201. Source: MGI alpha-beta T cell receptor complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay Ref.11. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	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

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-1165705,EBI-1165705
PTPN22	Q9Y2R2	4	EBI-1165705,EBI-1211241

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 164

143

T-cell surface glycoprotein CD3 zeta chain

PRO_0000016493

Regions

Topological domain

22 – 30

9

Extracellular Potential

Transmembrane

31 – 51

21

Helical; Potential

Topological domain

52 – 164

113

Cytoplasmic Potential

Domain

61 – 89

29

ITAM 1

Domain

100 – 128

29

ITAM 2

Domain

131 – 159

29

ITAM 3

Amino acid modifications

Modified residue

58

1

Phosphoserine Ref.14

Modified residue

64

1

Phosphotyrosine Ref.14 Ref.16 Ref.17

Modified residue

72

1

Phosphotyrosine Ref.14 Ref.16 Ref.17

Modified residue

83

1

Phosphotyrosine Ref.13

Modified residue

111

1

Phosphotyrosine Ref.13 Ref.14 Ref.16 Ref.17

Modified residue

123

1

Phosphotyrosine Ref.17

Modified residue

142

1

Phosphotyrosine Ref.13 Ref.14 Ref.16 Ref.17

Modified residue

153

1

Phosphotyrosine Ref.17

Disulfide bond

32

Interchain Potential

Natural variations

Alternative sequence

101

1

Missing in isoform 3.

VSP_036459

Experimental info

Sequence conflict

60 – 61

2

DA → EP in AAA60394. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

164

Helix Strand Turn

Details...

Helix

31 – 54

24

Helix

64 – 73

10

Turn

74 – 76

3

Helix

77 – 79

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CD-3-zeta) [UniParc]. Last modified October 10, 2002. Version 2. Checksum: 9408260374856EE9	FASTA	164	18,696
	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
	Isoform 2 (CD-3-eta) (Sequence not available).		–	–
	Isoform 3 [UniParc]. Checksum: 34898620B67167C7	FASTA	163	18,568
	10 20 30 40 50 60 MKWKALFTAA ILQAQLPITE AQSFGLLDPK LCYLLDGILF IYGVILTALF LRVKFSRSAD 70 80 90 100 110 120 APAYQQGQNQ LYNELNLGRR EEYDVLDKRR GRDPEMGGKP RRKNPQEGLY NELQKDKMAE 130 140 150 160 AYSEIGMKGE RRRGKGHDGL YQGLSTATKD TYDALHMQAL PPR

References

	« Hide 'large scale' referencesShow '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. , 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]	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 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, 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.

IPI

IPI00218634.
IPI00375504.

PIR

A31768.

RefSeq

NP_000725.1. NM_000734.3.
NP_932170.1. NM_198053.2.

UniGene

Hs.156445.

3D structure databases

PDBe
RCSB PDB
PDBj

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	30-60	[»]
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	[»]

DisProt

DP00200.

ProteinModelPortal

P20963.

ModBase

Search...

Protein-protein interaction databases

IntAct

P20963. 5 interactions.

STRING

9606.ENSP00000354782.

PTM databases

PhosphoSite

P20963.

Polymorphism databases

DMDM

23830999.

Proteomic databases

PaxDb

P20963.

PRIDE

P20963.

Protocols and materials databases

DNASU

919.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000362089; ENSP00000354782; ENSG00000198821.
ENST00000392122; ENSP00000375969; ENSG00000198821.

GeneID

919.

KEGG

hsa:919.

UCSC

uc001gei.4. human.
uc001gej.4. human.

Organism-specific databases

CTD

919.

GeneCards

GC01M167399.

HGNC

HGNC:1677. CD247.

HPA

CAB004651.
HPA008750.

MIM

186780. gene.
610163. phenotype.

neXtProt

NX_P20963.

Orphanet

169160. Severe combined immunodeficiency T- B+ due to CD3delta/CD3epsilon/CD3zeta.

PharmGKB

PA26219.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG87611.

HOGENOM

HOG000234398.

HOVERGEN

HBG005280.

KO

K06453.

OMA

EGLYNAL.

Enzyme and pathway databases

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
il12_stat4pathway. IL12 signaling mediated by STAT4.
il12_2pathway. IL12-mediated signaling events.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.

Reactome

REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P20963.

Bgee

P20963.

CleanEx

HS_CD247.

Genevestigator

P20963.

GermOnline

ENSG00000198821. Homo sapiens.

Family and domain databases

InterPro

IPR021663. CR3_zeta/IgE_Fc_rcpt_gamma.
IPR003110. Phos_immunorcpt_sig_ITAM.
IPR024128. T-cell_CD3_zeta/eta.
[Graphical view]

PANTHER

PTHR10035. PTHR10035. 1 hit.

Pfam

PF02189. ITAM. 3 hits.
PF11628. TCR_zetazeta. 1 hit.
[Graphical view]

SMART

SM00077. ITAM. 3 hits.
[Graphical view]

PROSITE

PS51055. ITAM_1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20963.

GenomeRNAi

919.

NextBio

3800.

SOURCE

Search...

Entry information

Entry name

CD3Z_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.