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P01730

- CD4_HUMAN

UniProt

P01730 - CD4_HUMAN

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
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    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 binding Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB
    8. protein kinase binding Source: UniProtKB
    9. receptor activity Source: ProtInc
    10. transmembrane signaling receptor activity Source: ProtInc
    11. 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

    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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi432 – 4321M → T: No effect. 2 Publications
    Mutagenesisi433 – 4331S → A: No effect. 2 Publications
    Mutagenesisi438 – 4392LL → AA: Loss of Nef-induced CD4 down-modulation. 1 Publication
    Mutagenesisi440 – 4401S → L: No effect. 2 Publications
    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

    ArrayExpressiP01730.
    BgeeiP01730.
    CleanExiHS_CD4.
    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. 79 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[»]
    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.
    HOGENOMiHOG000008696.
    HOVERGENiHBG005281.
    InParanoidiP01730.
    KOiK06454.
    OMAiPEAGMWQ.
    PhylomeDBiP01730.
    TreeFamiTF335974.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR000973. Ag_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

    MNRGVPFRHL LLVLQLALLP AATQGKKVVL GKKGDTVELT CTASQKKSIQ    50
    FHWKNSNQIK ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK 100
    IEDSDTYICE VEDQKEEVQL LVFGLTANSD THLLQGQSLT LTLESPPGSS 150
    PSVQCRSPRG KNIQGGKTLS VSQLELQDSG TWTCTVLQNQ KKVEFKIDIV 200
    VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW QAERASSSKS 250
    WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA 300
    LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK 350
    VSKREKAVWV LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQPMALI 400
    VLGGVAGLLL FIGLGIFFCV RCRHRRRQAE RMSQIKRLLS EKKTCQCPHR 450
    FQKTCSPI 458
    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 [» ]
    DisProti DP00123.
    ProteinModelPortali P01730.
    SMRi P01730. Positions 26-388, 393-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107358. 79 interactions.
    DIPi DIP-617N.
    IntActi P01730. 16 interactions.
    MINTi MINT-1130311.
    STRINGi 9606.ENSP00000011653.

    Chemistry

    BindingDBi P01730.
    ChEMBLi CHEMBL2754.

    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.
    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

    ArrayExpressi P01730.
    Bgeei P01730.
    CleanExi HS_CD4.
    Genevestigatori P01730.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR000973. Ag_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

    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 1, 2014
    This is version 177 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

    Dasty 3