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P01730

- CD4_HUMAN

UniProt

P01730 - CD4_HUMAN

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Protein

T-cell surface glycoprotein CD4

Gene

CD4

Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

  1. coreceptor activity Source: UniProtKB
  2. enzyme binding Source: UniProtKB
  3. extracellular matrix structural constituent Source: UniProtKB
  4. glycoprotein binding Source: UniProtKB
  5. MHC class II protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. protein kinase binding Source: UniProtKB
  8. receptor activity Source: ProtInc
  9. transmembrane signaling receptor activity Source: ProtInc
  10. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: InterPro
  2. cell surface receptor signaling pathway Source: ProtInc
  3. cytokine production Source: Ensembl
  4. defense response to Gram-negative bacterium Source: Ensembl
  5. entry into host cell Source: Reactome
  6. enzyme linked receptor protein signaling pathway Source: ProtInc
  7. immune response Source: UniProtKB
  8. induction by virus of host cell-cell fusion Source: UniProtKB
  9. innate immune response Source: Reactome
  10. maintenance of protein location in cell Source: MGI
  11. positive regulation of calcium-mediated signaling Source: Ensembl
  12. positive regulation of interleukin-2 biosynthetic process Source: UniProtKB
  13. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  14. positive regulation of protein kinase activity Source: UniProtKB
  15. protein palmitoleylation Source: MGI
  16. regulation of defense response to virus by virus Source: Reactome
  17. regulation of T cell activation Source: UniProtKB
  18. signal transduction Source: ProtInc
  19. T cell costimulation Source: Reactome
  20. T cell differentiation Source: UniProtKB
  21. T cell receptor signaling pathway Source: Reactome
  22. T cell selection Source: UniProtKB
  23. transmembrane receptor protein tyrosine kinase signaling pathway Source: UniProtKB
  24. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Host-virus interaction, Immunity

Enzyme and pathway databases

ReactomeiREACT_11166. Nef Mediated CD4 Down-regulation.
REACT_115574. Alpha-defensins.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.
REACT_6903. Binding and entry of HIV virion.
REACT_9031. Vpu mediated degradation of CD4.
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
ProteomesiUP000005640: 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.

GO - Cellular componenti

  1. early endosome Source: Reactome
  2. endoplasmic reticulum lumen Source: Ensembl
  3. endoplasmic reticulum membrane Source: Reactome
  4. external side of plasma membrane Source: MGI
  5. integral component of membrane Source: UniProtKB-KW
  6. membrane raft Source: Ensembl
  7. plasma membrane Source: UniProtKB
  8. T cell receptor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi432 – 4321M → T: No effect. 1 Publication
Mutagenesisi433 – 4331S → A: No effect. 1 Publication
Mutagenesisi438 – 4392LL → AA: Loss of Nef-induced CD4 down-modulation. 1 Publication
Mutagenesisi440 – 4401S → L: No effect. 1 Publication
Mutagenesisi457 – 4582Missing: Abolished interaction with SPG21 and induced T-cell activation. 1 Publication

Organism-specific databases

MIMi613949. phenotype.
PharmGKBiPA26220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25252 PublicationsAdd
BLAST
Chaini26 – 458433T-cell surface glycoprotein CD4PRO_0000014621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 1091 PublicationPROSITE-ProRule annotation
Disulfide bondi155 ↔ 1841 PublicationPROSITE-ProRule annotation
Glycosylationi296 – 2961N-linked (GlcNAc...)2 PublicationsCAR_000053
Glycosylationi325 – 3251N-linked (GlcNAc...)1 PublicationCAR_000054
Disulfide bondi328 ↔ 3701 PublicationPROSITE-ProRule annotation
Lipidationi419 – 4191S-palmitoyl cysteine1 Publication
Lipidationi422 – 4221S-palmitoyl cysteine1 Publication

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

PhosphoSiteiP01730.
UniCarbKBiP01730.

Expressioni

Gene expression databases

BgeeiP01730.
CleanExiHS_CD4.
ExpressionAtlasiP01730. baseline and differential.
GenevestigatoriP01730.

Organism-specific databases

HPAiCAB000011.
HPA004252.
HPA004472.

Interactioni

Subunit structurei

Associates with LCK. Binds to HIV-1 gp120 and to P4HB/PDI and upon HIV-1 binding to the cell membrane, is part of P4HB/PDI-CD4-CXCR4-gp120 complex. Interacts with HIV-1 Envelope polyprotein gp160 and protein Vpu. Interacts with Human Herpes virus 7 capsid proteins. Interacts with PTK2/FAK1; this interaction requires the presence of HIV-1 gp120.6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107358. 80 interactions.
DIPiDIP-617N.
IntActiP01730. 16 interactions.
MINTiMINT-1130311.
STRINGi9606.ENSP00000011653.

Structurei

Secondary structure

1
458
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 326
Beta strandi37 – 393
Beta strandi44 – 474
Beta strandi51 – 555
Beta strandi56 – 583
Beta strandi60 – 656
Beta strandi68 – 714
Beta strandi73 – 764
Helixi77 – 793
Helixi84 – 896
Beta strandi94 – 963
Helixi101 – 1033
Beta strandi105 – 1117
Beta strandi114 – 12916
Beta strandi131 – 1344
Beta strandi135 – 1373
Beta strandi139 – 1446
Beta strandi152 – 1565
Beta strandi158 – 1603
Beta strandi162 – 1643
Beta strandi166 – 1716
Helixi176 – 1783
Beta strandi180 – 1889
Beta strandi191 – 20010
Helixi398 – 42124
Beta strandi426 – 4283
Helixi432 – 4387
Beta strandi440 – 4423

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
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[»]
4R4HX-ray4.28B26-203[»]
DisProtiDP00123.
ProteinModelPortaliP01730.
SMRiP01730. Positions 26-388, 393-458.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01730.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 396371ExtracellularSequence AnalysisAdd
BLAST
Topological domaini419 – 45840CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei397 – 41822HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 125100Ig-like V-typeAdd
BLAST
Domaini126 – 20378Ig-like C2-type 1Add
BLAST
Domaini204 – 317114Ig-like C2-type 2Add
BLAST
Domaini318 – 37457Ig-like C2-type 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni427 – 45529HIV-1 Vpu-susceptibility domainAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47205.
GeneTreeiENSGT00390000001745.
HOGENOMiHOG000008696.
HOVERGENiHBG005281.
InParanoidiP01730.
KOiK06454.
OMAiPEAGMWQ.
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.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR021963. Tcell_CD4_Cterm.
[Graphical view]
PfamiPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR00692. CD4TCANTIGEN.
SMARTiSM00409. IG. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
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].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911K → E.1 Publication
Corresponds to variant rs28917504 [ dbSNP | Ensembl ].
VAR_023459
Natural varianti227 – 2271F → S.1 Publication
Corresponds to variant rs11064419 [ dbSNP | Ensembl ].
VAR_023460
Natural varianti265 – 2651R → W in OKT4-negative populations. 3 Publications
Corresponds to variant rs28919570 [ dbSNP | Ensembl ].
VAR_003906

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.2. human.

Polymorphism databases

DMDMi116013.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

CD4 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8562.1.
PIRi A90872. RWHUT4.
RefSeqi NP_000607.1. NM_000616.4.
UniGenei Hs.631659.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CDH X-ray 2.30 A 26-203 [» ]
1CDI X-ray 2.90 A 26-203 [» ]
1CDJ X-ray 2.50 A 26-203 [» ]
1CDU X-ray 2.70 A 26-203 [» ]
1CDY X-ray 2.00 A 26-203 [» ]
1G9M X-ray 2.20 C 26-208 [» ]
1G9N X-ray 2.90 C 26-208 [» ]
1GC1 X-ray 2.50 C 26-206 [» ]
1JL4 X-ray 4.30 D 26-203 [» ]
1OPN model - C 26-206 [» ]
1OPT model - C 26-206 [» ]
1OPW model - C 26-206 [» ]
1Q68 NMR - A 421-458 [» ]
1RZJ X-ray 2.20 C 26-208 [» ]
1RZK X-ray 2.90 C 26-208 [» ]
1WBR NMR - A 428-444 [» ]
1WIO X-ray 3.90 A/B 26-388 [» ]
1WIP X-ray 4.00 A/B 26-388 [» ]
1WIQ X-ray 5.00 A/B 26-388 [» ]
2B4C X-ray 3.30 C 26-206 [» ]
2JKR X-ray 2.98 P/Q 431-441 [» ]
2JKT X-ray 3.40 P/Q 435-441 [» ]
2KLU NMR - A 397-458 [» ]
2NXY X-ray 2.00 B 26-208 [» ]
2NXZ X-ray 2.04 B 26-208 [» ]
2NY0 X-ray 2.20 B 26-208 [» ]
2NY1 X-ray 1.99 B 26-208 [» ]
2NY2 X-ray 2.00 B 26-208 [» ]
2NY3 X-ray 2.00 B 26-208 [» ]
2NY4 X-ray 2.00 B 26-208 [» ]
2NY5 X-ray 2.50 C 26-208 [» ]
2NY6 X-ray 2.80 B 26-208 [» ]
2QAD X-ray 3.30 B/F 26-206 [» ]
3B71 X-ray 2.82 D/E/F 428-450 [» ]
3CD4 X-ray 2.20 A 26-207 [» ]
3JWD X-ray 2.61 C/D 26-208 [» ]
3JWO X-ray 3.51 C 26-208 [» ]
3LQA X-ray 3.40 C 26-207 [» ]
3O2D X-ray 2.19 A 26-207 [» ]
3S4S X-ray 2.40 G/H 26-203 [» ]
3S5L X-ray 2.10 G/H 26-203 [» ]
3T0E X-ray 4.00 E 26-388 [» ]
4H8W X-ray 1.85 C 26-208 [» ]
4JM2 X-ray 3.10 F 26-208 [» ]
4P9H X-ray 3.00 C 26-207 [» ]
4Q6I X-ray 3.65 C/I/J/K 1-208 [» ]
4R4H X-ray 4.28 B 26-203 [» ]
DisProti DP00123.
ProteinModelPortali P01730.
SMRi P01730. Positions 26-388, 393-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107358. 80 interactions.
DIPi DIP-617N.
IntActi P01730. 16 interactions.
MINTi MINT-1130311.
STRINGi 9606.ENSP00000011653.

Chemistry

BindingDBi P01730.
ChEMBLi CHEMBL2754.
DrugBanki DB00098. Antithymocyte globulin.

PTM databases

PhosphoSitei P01730.
UniCarbKBi P01730.

Polymorphism databases

DMDMi 116013.

Proteomic databases

MaxQBi P01730.
PaxDbi P01730.
PeptideAtlasi P01730.
PRIDEi P01730.

Protocols and materials databases

DNASUi 920.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000011653 ; ENSP00000011653 ; ENSG00000010610 .
GeneIDi 920.
KEGGi hsa:920.
UCSCi uc001qqv.2. human.

Organism-specific databases

CTDi 920.
GeneCardsi GC12P006899.
HGNCi HGNC:1678. CD4.
HPAi CAB000011.
HPA004252.
HPA004472.
MIMi 186940. gene.
613949. phenotype.
neXtProti NX_P01730.
PharmGKBi PA26220.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47205.
GeneTreei ENSGT00390000001745.
HOGENOMi HOG000008696.
HOVERGENi HBG005281.
InParanoidi P01730.
KOi K06454.
OMAi PEAGMWQ.
PhylomeDBi P01730.
TreeFami TF335974.

Enzyme and pathway databases

Reactomei REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_115574. Alpha-defensins.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_19324. PD-1 signaling.
REACT_6903. Binding and entry of HIV virion.
REACT_9031. Vpu mediated degradation of CD4.
SignaLinki P01730.

Miscellaneous databases

ChiTaRSi CD4. human.
EvolutionaryTracei P01730.
GeneWikii CD4.
GenomeRNAii 920.
NextBioi 3806.
PROi P01730.
SOURCEi Search...

Gene expression databases

Bgeei P01730.
CleanExi HS_CD4.
ExpressionAtlasi P01730. baseline and differential.
Genevestigatori P01730.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
InterProi IPR000973. CD4.
IPR015274. CD4-extracel.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR021963. Tcell_CD4_Cterm.
[Graphical view ]
Pfami PF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
PRINTSi PR00692. CD4TCANTIGEN.
SMARTi SM00409. IG. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family."
    Maddon P.J., Littman D.R., Godfrey M., Maddon D.E., Chess L., Axel R.
    Cell 42:93-104(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: SEQUENCE REVISION TO 26.
  3. "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13."
    Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.
    Genome Res. 6:314-326(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
    Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
    Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  5. "Humans with OKT4-epitope deficiency have a single nucleotide base change in the CD4 gene, resulting in substitution of TRP240 for ARG240."
    Hodge T.W., Sasso D.R., McDougal J.S.
    Hum. Immunol. 30:99-104(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM, VARIANT TRP-265.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "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].
    Tissue: Thymus.
  8. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-191; SER-227 AND TRP-265.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
    Tissue: Pancreas.
  11. "Cloning and sequences of primate CD4 molecules: diversity of the cellular receptor for simian immunodeficiency virus/human immunodeficiency virus."
    Fomsgaard A., Hirsch V.M., Johnson P.R.
    Eur. J. Immunol. 22:2973-2981(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-424.
    Tissue: Blood.
  12. "Protein and carbohydrate structural analysis of a recombinant soluble CD4 receptor by mass spectrometry."
    Carr S.A., Hemling M.E., Folena-Wasserman G., Sweet R.W., Anumula K., Barr J.R., Huddleston M.J., Taylor P.
    J. Biol. Chem. 264:21286-21295(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-394, DISULFIDE BOND.
  13. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-40.
  14. "A single amino acid substitution in a common African allele of the CD4 molecule ablates binding of the monoclonal antibody, OKT4."
    Lederman S., DeMartino J.A., Daugherty B.L., Foeldvari I., Yellin M.J., Cleary A.M., Berkowitz N., Lowy I., Braunstein N.S., Mark G.E.
    Mol. Immunol. 28:1171-1181(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 250-280, POLYMORPHISM, VARIANT TRP-265.
  15. "CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor."
    Crise B., Buonocore L., Rose J.K.
    J. Virol. 64:5585-5593(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 ENVELOPE POLYPROTEIN GP160.
  16. "Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells."
    Spellman M.W., Leonard C.K., Basa L.J., Gelineo I., van Halbeek H.
    Biochemistry 30:2395-2406(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-296 AND ASN-325.
  17. "Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor."
    Crise B., Rose J.K.
    J. Biol. Chem. 267:13593-13597(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-419 AND CYS-422.
  18. "Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain."
    Aiken C., Konner J., Landau N.R., Lenburg M.E., Trono D.
    Cell 76:853-864(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REMOVAL FROM CELL SURFACE BY HIV-1 NEF, MUTAGENESIS OF MET-432; SER-433; 438-LEU-LEU-439 AND SER-440.
  19. "CD4 is a critical component of the receptor for human herpesvirus 7: interference with human immunodeficiency virus."
    Lusso P., Secchiero P., Crowley R.W., Garzino-Demo A., Berneman Z.N., Gallo R.C.
    Proc. Natl. Acad. Sci. U.S.A. 91:3872-3876(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HERPESVIRUS 7 CAPSID PROTEINS.
  20. "Cloning of ACP33 as a novel intracellular ligand of CD4."
    Zeitlmann L., Sirim P., Kremmer E., Kolanus W.
    J. Biol. Chem. 276:9123-9132(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPG21, MUTAGENESIS OF 457-PRO-ILE-458.
  21. "Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling."
    Fragoso R., Ren D., Zhang X., Su M.W., Burakoff S.J., Jin Y.J.
    J. Immunol. 170:913-921(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  22. Cited for: INTERACTION WITH HIV-1 SURFACE PROTEIN GP120.
  23. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296.
    Tissue: Liver.
  24. "Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains."
    Wang J., Yan Y., Garrett T.P., Liu J., Rodgers D.W., Garlick R.L., Tarr G.E., Husain Y., Reinherz E.L., Harrison S.C.
    Nature 348:411-418(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-208.
  25. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-208.
  26. "Dimeric association and segmental variability in the structure of human CD4."
    Wu H., Kwong P.D., Hendrickson W.A.
    Nature 387:527-530(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 26-388.
  27. "Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody."
    Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A.
    Nature 393:648-659(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-208 IN COMPLEX WITH HIV SURFACE PROTEIN GP120.
  28. "Structural basis for the interaction between focal adhesion kinase and CD4."
    Garron M.L., Arthos J., Guichou J.F., McNally J., Cicala C., Arold S.T.
    J. Mol. Biol. 375:1320-1328(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 428-450 IN COMPLEX WITH PTK2/FAK1, INTERACTION WITH PTK2/FAK1.

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: October 29, 2014
This is version 178 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

External Data

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