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Protein

T-cell surface glycoprotein CD4

Gene

CD4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.
(Microbial infection) Acts as a receptor for human immunodeficiency virus-1 (PubMed:2214026, PubMed:16331979, PubMed:9641677). Down-regulated by HIV-1 Vpu (PubMed:17346169). Acts as a receptor for Human Herpes virus 7/HHV-7 (PubMed:7909607).5 Publications

GO - Molecular functioni

  • coreceptor activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • extracellular matrix structural constituent Source: UniProtKB
  • glycoprotein binding Source: UniProtKB
  • MHC class II protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • receptor activity Source: ProtInc
  • transmembrane signaling receptor activity Source: ProtInc
  • virus receptor activity Source: UniProtKB-KW
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Adaptive immunity, Host-virus interaction, Immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000010610-MONOMER.
ReactomeiR-HSA-1462054. Alpha-defensins.
R-HSA-167590. Nef Mediated CD4 Down-regulation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-202424. Downstream TCR signaling.
R-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-202430. Translocation of ZAP-70 to Immunological synapse.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-389948. PD-1 signaling.
R-HSA-449147. Signaling by Interleukins.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP01730.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface glycoprotein CD4
Alternative name(s):
T-cell surface antigen T4/Leu-3
CD_antigen: CD4
Gene namesi
Name:CD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1678. CD4.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Localizes to lipid rafts. Removed from plasma membrane by HIV-1 Nef protein that increases clathrin-dependent endocytosis of this antigen to target it to lysosomal degradation. Cell surface expression is also down-modulated by HIV-1 Envelope polyprotein gp160 that interacts with, and sequesters CD4 in the endoplasmic reticulum.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 396ExtracellularSequence analysisAdd BLAST371
Transmembranei397 – 418HelicalSequence analysisAdd BLAST22
Topological domaini419 – 458CytoplasmicSequence analysisAdd BLAST40

GO - Cellular componenti

  • early endosome Source: Reactome
  • endoplasmic reticulum lumen Source: Ensembl
  • endoplasmic reticulum membrane Source: Reactome
  • external side of plasma membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • T cell receptor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi432M → T: No effect. 1 Publication1
Mutagenesisi433S → A: No effect. 1 Publication1
Mutagenesisi438 – 439LL → AA: Loss of Nef-induced CD4 down-modulation. 1 Publication2
Mutagenesisi440S → L: No effect. 1 Publication1
Mutagenesisi457 – 458Missing : Abolished interaction with SPG21 and induced T-cell activation. 1 Publication2

Organism-specific databases

DisGeNETi920.
MalaCardsiCD4.
MIMi613949. phenotype.
OpenTargetsiENSG00000010610.
PharmGKBiPA26220.

Chemistry databases

ChEMBLiCHEMBL2754.
DrugBankiDB00098. Anti-thymocyte Globulin (Rabbit).

Polymorphism and mutation databases

BioMutaiCD4.
DMDMi116013.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 252 PublicationsAdd BLAST25
ChainiPRO_000001462126 – 458T-cell surface glycoprotein CD4Add BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 109PROSITE-ProRule annotation1 Publication
Disulfide bondi155 ↔ 184PROSITE-ProRule annotation1 Publication
GlycosylationiCAR_000053296N-linked (GlcNAc...)2 Publications1
GlycosylationiCAR_000054325N-linked (GlcNAc...)1 Publication1
Disulfide bondi328 ↔ 370PROSITE-ProRule annotation1 Publication
Lipidationi419S-palmitoyl cysteine1 Publication1
Lipidationi422S-palmitoyl cysteine1 Publication1

Post-translational modificationi

Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP01730.
PaxDbiP01730.
PeptideAtlasiP01730.
PRIDEiP01730.

PTM databases

iPTMnetiP01730.
PhosphoSitePlusiP01730.
SwissPalmiP01730.
UniCarbKBiP01730.

Expressioni

Gene expression databases

BgeeiENSG00000010610.
CleanExiHS_CD4.
ExpressionAtlasiP01730. baseline and differential.
GenevisibleiP01730. HS.

Organism-specific databases

HPAiCAB000011.
CAB068180.
HPA004252.
HPA004472.

Interactioni

Subunit structurei

Associates with LCK. Interacts with PTK2/FAK1. Binds to P4HB/PDI.2 Publications
(Microbial infection) Interacts with HIV-1 Envelope polyprotein gp160 and protein Vpu (PubMed:2214026, PubMed:16331979, PubMed:9641677).3 Publications
(Microbial infection) Interacts with Human Herpes virus 7 surface proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CCR5P516812EBI-353826,EBI-489374
LCKP062392EBI-353826,EBI-1348
NR3C1P041502EBI-353826,EBI-493507
vpuP059193EBI-353826,EBI-6248147From a different organism.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • MHC class II protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107358. 90 interactors.
DIPiDIP-617N.
IntActiP01730. 17 interactors.
MINTiMINT-1130311.
STRINGi9606.ENSP00000011653.

Chemistry databases

BindingDBiP01730.

Structurei

Secondary structure

1458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 32Combined sources6
Beta strandi37 – 39Combined sources3
Beta strandi44 – 47Combined sources4
Beta strandi51 – 55Combined sources5
Beta strandi56 – 58Combined sources3
Beta strandi60 – 65Combined sources6
Beta strandi68 – 71Combined sources4
Beta strandi73 – 76Combined sources4
Helixi77 – 79Combined sources3
Helixi84 – 89Combined sources6
Beta strandi94 – 96Combined sources3
Helixi101 – 103Combined sources3
Beta strandi105 – 111Combined sources7
Beta strandi114 – 129Combined sources16
Beta strandi131 – 134Combined sources4
Beta strandi135 – 137Combined sources3
Beta strandi139 – 144Combined sources6
Beta strandi152 – 156Combined sources5
Beta strandi158 – 160Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi166 – 171Combined sources6
Helixi176 – 178Combined sources3
Beta strandi180 – 188Combined sources9
Beta strandi191 – 200Combined sources10
Helixi398 – 421Combined sources24
Beta strandi426 – 428Combined sources3
Helixi432 – 438Combined sources7
Beta strandi440 – 442Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDHX-ray2.30A26-203[»]
1CDIX-ray2.90A26-203[»]
1CDJX-ray2.50A26-203[»]
1CDUX-ray2.70A26-203[»]
1CDYX-ray2.00A26-203[»]
1G9MX-ray2.20C26-208[»]
1G9NX-ray2.90C26-208[»]
1GC1X-ray2.50C26-206[»]
1JL4X-ray4.30D26-203[»]
1OPNmodel-C26-206[»]
1OPTmodel-C26-206[»]
1OPWmodel-C26-206[»]
1Q68NMR-A421-458[»]
1RZJX-ray2.20C26-208[»]
1RZKX-ray2.90C26-208[»]
1WBRNMR-A428-444[»]
1WIOX-ray3.90A/B26-388[»]
1WIPX-ray4.00A/B26-388[»]
1WIQX-ray5.00A/B26-388[»]
2B4CX-ray3.30C26-206[»]
2JKRX-ray2.98P/Q431-441[»]
2JKTX-ray3.40P/Q435-441[»]
2KLUNMR-A397-458[»]
2NXYX-ray2.00B26-208[»]
2NXZX-ray2.04B26-208[»]
2NY0X-ray2.20B26-208[»]
2NY1X-ray1.99B26-208[»]
2NY2X-ray2.00B26-208[»]
2NY3X-ray2.00B26-208[»]
2NY4X-ray2.00B26-208[»]
2NY5X-ray2.50C26-208[»]
2NY6X-ray2.80B26-208[»]
2QADX-ray3.30B/F26-206[»]
3B71X-ray2.82D/E/F428-450[»]
3CD4X-ray2.20A26-207[»]
3J70electron microscopy-C/O/T26-208[»]
3JWDX-ray2.61C/D26-208[»]
3JWOX-ray3.51C26-208[»]
3LQAX-ray3.40C26-207[»]
3O2DX-ray2.19A26-207[»]
3S4SX-ray2.40G/H26-203[»]
3S5LX-ray2.10G/H26-203[»]
3T0EX-ray4.00E26-388[»]
4H8WX-ray1.85C26-208[»]
4JM2X-ray3.10F26-208[»]
4P9HX-ray3.00C26-207[»]
4Q6IX-ray3.65C/I/J/K1-208[»]
4R2GX-ray3.28B/F/H/L26-208[»]
4R4HX-ray4.28B26-203[»]
4RQSX-ray4.49B26-208[»]
5A7Xelectron microscopy17.00B/F/J26-206[»]
5A8Helectron microscopy23.00B/H/N26-208[»]
5CAYX-ray3.00B26-208[»]
DisProtiDP00123.
ProteinModelPortaliP01730.
SMRiP01730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01730.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 125Ig-like V-typeAdd BLAST100
Domaini126 – 203Ig-like C2-type 1Add BLAST78
Domaini204 – 317Ig-like C2-type 2Add BLAST114
Domaini318 – 374Ig-like C2-type 3Add BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni427 – 455HIV-1 Vpu-susceptibility domainAdd BLAST29

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IK9F. Eukaryota.
ENOG410YWI4. LUCA.
GeneTreeiENSGT00390000001745.
HOGENOMiHOG000008696.
HOVERGENiHBG005281.
InParanoidiP01730.
KOiK06454.
OMAiPEAGMWQ.
OrthoDBiEOG091G0AZL.
PhylomeDBiP01730.
TreeFamiTF335974.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR000973. CD4.
IPR015274. CD4-extracel.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
IPR021963. Tcell_CD4_Cterm.
[Graphical view]
PANTHERiPTHR11422:SF0. PTHR11422:SF0. 1 hit.
PfamiPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF00047. ig. 1 hit.
PF12104. Tcell_CD4_C. 1 hit.
[Graphical view]
PRINTSiPR00692. CD4TCANTIGEN.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01730-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRGVPFRHL LLVLQLALLP AATQGKKVVL GKKGDTVELT CTASQKKSIQ
60 70 80 90 100
FHWKNSNQIK ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK
110 120 130 140 150
IEDSDTYICE VEDQKEEVQL LVFGLTANSD THLLQGQSLT LTLESPPGSS
160 170 180 190 200
PSVQCRSPRG KNIQGGKTLS VSQLELQDSG TWTCTVLQNQ KKVEFKIDIV
210 220 230 240 250
VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW QAERASSSKS
260 270 280 290 300
WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA
310 320 330 340 350
LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK
360 370 380 390 400
VSKREKAVWV LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQPMALI
410 420 430 440 450
VLGGVAGLLL FIGLGIFFCV RCRHRRRQAE RMSQIKRLLS EKKTCQCPHR

FQKTCSPI
Length:458
Mass (Da):51,111
Last modified:November 1, 1988 - v1
Checksum:i20ED893F9E56D236
GO

Polymorphismi

The OKT monoclonal antibodies are widely used for the analysis of human peripheral blood T-lymphocytes. OKT4 reacts with T-helper/inducer lymphocytes. The OKT4 epitope of the CD4 cell-surface protein is polymorphic in white, black, and Japanese populations. The variable phenotypic expression is due a CD4 polymorphism. OKT4 positive individuals carry Arg-265 and OKT4 negative individuals carry Trp-265 [MIMi:613949].2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023459191K → E.1 PublicationCorresponds to variant rs28917504dbSNPEnsembl.1
Natural variantiVAR_023460227F → S.1 PublicationCorresponds to variant rs11064419dbSNPEnsembl.1
Natural variantiVAR_003906265R → W in OKT4-negative populations. 3 PublicationsCorresponds to variant rs28919570dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12807 mRNA. Translation: AAA35572.1.
U47924 Genomic DNA. Translation: AAB51309.1.
M35160 mRNA. Translation: AAA16069.1.
BT019791 mRNA. Translation: AAV38594.1.
BT019811 mRNA. Translation: AAV38614.1.
DQ012936 Genomic DNA. Translation: AAY22175.1.
AK312828 mRNA. Translation: BAG35684.1.
CH471116 Genomic DNA. Translation: EAW88738.1.
CH471116 Genomic DNA. Translation: EAW88739.1.
BC025782 mRNA. Translation: AAH25782.1.
CCDSiCCDS8562.1.
PIRiA90872. RWHUT4.
RefSeqiNP_000607.1. NM_000616.4.
UniGeneiHs.631659.

Genome annotation databases

EnsembliENST00000011653; ENSP00000011653; ENSG00000010610.
GeneIDi920.
KEGGihsa:920.
UCSCiuc001qqv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

CD4 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12807 mRNA. Translation: AAA35572.1.
U47924 Genomic DNA. Translation: AAB51309.1.
M35160 mRNA. Translation: AAA16069.1.
BT019791 mRNA. Translation: AAV38594.1.
BT019811 mRNA. Translation: AAV38614.1.
DQ012936 Genomic DNA. Translation: AAY22175.1.
AK312828 mRNA. Translation: BAG35684.1.
CH471116 Genomic DNA. Translation: EAW88738.1.
CH471116 Genomic DNA. Translation: EAW88739.1.
BC025782 mRNA. Translation: AAH25782.1.
CCDSiCCDS8562.1.
PIRiA90872. RWHUT4.
RefSeqiNP_000607.1. NM_000616.4.
UniGeneiHs.631659.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CDHX-ray2.30A26-203[»]
1CDIX-ray2.90A26-203[»]
1CDJX-ray2.50A26-203[»]
1CDUX-ray2.70A26-203[»]
1CDYX-ray2.00A26-203[»]
1G9MX-ray2.20C26-208[»]
1G9NX-ray2.90C26-208[»]
1GC1X-ray2.50C26-206[»]
1JL4X-ray4.30D26-203[»]
1OPNmodel-C26-206[»]
1OPTmodel-C26-206[»]
1OPWmodel-C26-206[»]
1Q68NMR-A421-458[»]
1RZJX-ray2.20C26-208[»]
1RZKX-ray2.90C26-208[»]
1WBRNMR-A428-444[»]
1WIOX-ray3.90A/B26-388[»]
1WIPX-ray4.00A/B26-388[»]
1WIQX-ray5.00A/B26-388[»]
2B4CX-ray3.30C26-206[»]
2JKRX-ray2.98P/Q431-441[»]
2JKTX-ray3.40P/Q435-441[»]
2KLUNMR-A397-458[»]
2NXYX-ray2.00B26-208[»]
2NXZX-ray2.04B26-208[»]
2NY0X-ray2.20B26-208[»]
2NY1X-ray1.99B26-208[»]
2NY2X-ray2.00B26-208[»]
2NY3X-ray2.00B26-208[»]
2NY4X-ray2.00B26-208[»]
2NY5X-ray2.50C26-208[»]
2NY6X-ray2.80B26-208[»]
2QADX-ray3.30B/F26-206[»]
3B71X-ray2.82D/E/F428-450[»]
3CD4X-ray2.20A26-207[»]
3J70electron microscopy-C/O/T26-208[»]
3JWDX-ray2.61C/D26-208[»]
3JWOX-ray3.51C26-208[»]
3LQAX-ray3.40C26-207[»]
3O2DX-ray2.19A26-207[»]
3S4SX-ray2.40G/H26-203[»]
3S5LX-ray2.10G/H26-203[»]
3T0EX-ray4.00E26-388[»]
4H8WX-ray1.85C26-208[»]
4JM2X-ray3.10F26-208[»]
4P9HX-ray3.00C26-207[»]
4Q6IX-ray3.65C/I/J/K1-208[»]
4R2GX-ray3.28B/F/H/L26-208[»]
4R4HX-ray4.28B26-203[»]
4RQSX-ray4.49B26-208[»]
5A7Xelectron microscopy17.00B/F/J26-206[»]
5A8Helectron microscopy23.00B/H/N26-208[»]
5CAYX-ray3.00B26-208[»]
DisProtiDP00123.
ProteinModelPortaliP01730.
SMRiP01730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107358. 90 interactors.
DIPiDIP-617N.
IntActiP01730. 17 interactors.
MINTiMINT-1130311.
STRINGi9606.ENSP00000011653.

Chemistry databases

BindingDBiP01730.
ChEMBLiCHEMBL2754.
DrugBankiDB00098. Anti-thymocyte Globulin (Rabbit).

PTM databases

iPTMnetiP01730.
PhosphoSitePlusiP01730.
SwissPalmiP01730.
UniCarbKBiP01730.

Polymorphism and mutation databases

BioMutaiCD4.
DMDMi116013.

Proteomic databases

MaxQBiP01730.
PaxDbiP01730.
PeptideAtlasiP01730.
PRIDEiP01730.

Protocols and materials databases

DNASUi920.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000011653; ENSP00000011653; ENSG00000010610.
GeneIDi920.
KEGGihsa:920.
UCSCiuc001qqv.3. human.

Organism-specific databases

CTDi920.
DisGeNETi920.
GeneCardsiCD4.
HGNCiHGNC:1678. CD4.
HPAiCAB000011.
CAB068180.
HPA004252.
HPA004472.
MalaCardsiCD4.
MIMi186940. gene.
613949. phenotype.
neXtProtiNX_P01730.
OpenTargetsiENSG00000010610.
PharmGKBiPA26220.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK9F. Eukaryota.
ENOG410YWI4. LUCA.
GeneTreeiENSGT00390000001745.
HOGENOMiHOG000008696.
HOVERGENiHBG005281.
InParanoidiP01730.
KOiK06454.
OMAiPEAGMWQ.
OrthoDBiEOG091G0AZL.
PhylomeDBiP01730.
TreeFamiTF335974.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000010610-MONOMER.
ReactomeiR-HSA-1462054. Alpha-defensins.
R-HSA-167590. Nef Mediated CD4 Down-regulation.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-202424. Downstream TCR signaling.
R-HSA-202427. Phosphorylation of CD3 and TCR zeta chains.
R-HSA-202430. Translocation of ZAP-70 to Immunological synapse.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-389948. PD-1 signaling.
R-HSA-449147. Signaling by Interleukins.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP01730.

Miscellaneous databases

ChiTaRSiCD4. human.
EvolutionaryTraceiP01730.
GeneWikiiCD4.
GenomeRNAii920.
PROiP01730.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000010610.
CleanExiHS_CD4.
ExpressionAtlasiP01730. baseline and differential.
GenevisibleiP01730. HS.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR000973. CD4.
IPR015274. CD4-extracel.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
IPR021963. Tcell_CD4_Cterm.
[Graphical view]
PANTHERiPTHR11422:SF0. PTHR11422:SF0. 1 hit.
PfamiPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF00047. ig. 1 hit.
PF12104. Tcell_CD4_C. 1 hit.
[Graphical view]
PRINTSiPR00692. CD4TCANTIGEN.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 1 hit.
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ProtoNetiSearch...

Entry informationi

Entry nameiCD4_HUMAN
AccessioniPrimary (citable) accession number: P01730
Secondary accession number(s): B2R737
, D3DUS5, Q4ZGK2, Q5U066, Q9UDE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: November 2, 2016
This is version 198 of the entry and version 1 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

Miscellaneous

Primary receptor for HIV-1.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.