Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01730 (CD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD4
Alternative name(s):
T-cell surface antigen T4/Leu-3
CD_antigen=CD4
Gene names
Name:CD4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.

Subunit structure

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. Ref.15 Ref.19 Ref.20 Ref.22 Ref.28

Subcellular location

Cell membrane; Single-pass type I membrane protein. 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. Ref.21

Post-translational modification

Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. Ref.17

Polymorphism

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 [MIM:613949].

Miscellaneous

Primary receptor for HIV-1.

Sequence similarities

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Host-virus interaction
Immunity
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Traceable author statement. Source: Reactome

T cell differentiation

Inferred from direct assay PubMed 1533274. Source: UniProtKB

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

T cell selection

Inferred from direct assay PubMed 9551897. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: InterPro

cell surface receptor signaling pathway

Traceable author statement PubMed 9780207. Source: ProtInc

cytokine production

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-negative bacterium

Inferred from electronic annotation. Source: Ensembl

entry into host cell

Traceable author statement. Source: Reactome

enzyme linked receptor protein signaling pathway

Traceable author statement PubMed 10358157. Source: ProtInc

immune response

Non-traceable author statement PubMed 8512039. Source: UniProtKB

induction by virus of host cell-cell fusion

Inferred from direct assay PubMed 9166430. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

maintenance of protein location in cell

Inferred from direct assay PubMed 15128768. Source: MGI

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-2 biosynthetic process

Non-traceable author statement PubMed 1901411. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase activity

Inferred from direct assay PubMed 2118992. Source: UniProtKB

protein palmitoleylation

Inferred from direct assay PubMed 15128768. Source: MGI

regulation of T cell activation

Inferred from direct assay PubMed 1533274. Source: UniProtKB

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement PubMed 10358157PubMed 9558100. Source: ProtInc

transmembrane receptor protein tyrosine kinase signaling pathway

Non-traceable author statement PubMed 8512039. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentT cell receptor complex

Non-traceable author statement PubMed 8512039. Source: UniProtKB

early endosome

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from direct assay PubMed 17213291. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 19333378Ref.18. Source: UniProtKB

   Molecular_functionMHC class II protein binding

Non-traceable author statement PubMed 8512039. Source: UniProtKB

coreceptor activity

Non-traceable author statement PubMed 8512039. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 19333378. Source: UniProtKB

extracellular matrix structural constituent

Non-traceable author statement PubMed 12444132. Source: UniProtKB

glycoprotein binding

Inferred from physical interaction PubMed 10922058. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 12444132. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 7486703. Source: UniProtKB

receptor activity

Traceable author statement PubMed 10413516. Source: ProtInc

transmembrane signaling receptor activity

Traceable author statement PubMed 10358157. Source: ProtInc

zinc ion binding

Inferred from direct assay PubMed 9668045. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LCKP062392EBI-353826,EBI-1348
NR3C1P041502EBI-353826,EBI-493507
vpuP059193EBI-353826,EBI-6248147From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.12 Ref.13
Chain26 – 458433T-cell surface glycoprotein CD4
PRO_0000014621

Regions

Topological domain26 – 396371Extracellular Potential
Transmembrane397 – 41822Helical; Potential
Topological domain419 – 45840Cytoplasmic Potential
Domain26 – 125100Ig-like V-type
Domain126 – 20378Ig-like C2-type 1
Domain204 – 317114Ig-like C2-type 2
Domain318 – 37457Ig-like C2-type 3
Region427 – 45529HIV-1 Vpu-susceptibility domain

Amino acid modifications

Lipidation4191S-palmitoyl cysteine Ref.17
Lipidation4221S-palmitoyl cysteine Ref.17
Glycosylation2961N-linked (GlcNAc...) Ref.16 Ref.23
CAR_000053
Glycosylation3251N-linked (GlcNAc...) Ref.16
CAR_000054
Disulfide bond41 ↔ 109 Ref.12
Disulfide bond155 ↔ 184 Ref.12
Disulfide bond328 ↔ 370 Ref.12

Natural variations

Natural variant1911K → E. Ref.8
Corresponds to variant rs28917504 [ dbSNP | Ensembl ].
VAR_023459
Natural variant2271F → S. Ref.8
Corresponds to variant rs11064419 [ dbSNP | Ensembl ].
VAR_023460
Natural variant2651R → W in OKT4-negative populations. Ref.5 Ref.8 Ref.14
Corresponds to variant rs28919570 [ dbSNP | Ensembl ].
VAR_003906

Experimental info

Mutagenesis4321M → T: No effect. Ref.18 Ref.20
Mutagenesis4331S → A: No effect. Ref.18 Ref.20
Mutagenesis438 – 4392LL → AA: Loss of Nef-induced CD4 down-modulation. Ref.20
Mutagenesis4401S → L: No effect. Ref.18 Ref.20
Mutagenesis457 – 4582Missing: Abolished interaction with SPG21 and induced T-cell activation. Ref.20

Secondary structure

.................................................... 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01730 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 20ED893F9E56D236

FASTA45851,111
        10         20         30         40         50         60 
MNRGVPFRHL LLVLQLALLP AATQGKKVVL GKKGDTVELT CTASQKKSIQ FHWKNSNQIK 

        70         80         90        100        110        120 
ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK IEDSDTYICE VEDQKEEVQL 

       130        140        150        160        170        180 
LVFGLTANSD THLLQGQSLT LTLESPPGSS PSVQCRSPRG KNIQGGKTLS VSQLELQDSG 

       190        200        210        220        230        240 
TWTCTVLQNQ KKVEFKIDIV VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW 

       250        260        270        280        290        300 
QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA 

       310        320        330        340        350        360 
LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK VSKREKAVWV 

       370        380        390        400        410        420 
LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQPMALI VLGGVAGLLL FIGLGIFFCV 

       430        440        450 
RCRHRRRQAE RMSQIKRLLS EKKTCQCPHR FQKTCSPI 

« Hide

References

« Hide 'large scale' references
[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]"Corrected CD4 sequence."
Littman D.R., Maddon P.J., Axel R.
Cell 55:541-541(1988) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Protein minimization of the gp120 binding region of human CD4."
Sharma D., Balamurali M.M., Chakraborty K., Kumaran S., Jeganathan S., Rashid U., Ingallinella P., Varadarajan R.
Biochemistry 44:16192-16202(2005) [PubMed] [Europe PMC] [Abstract]
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]"Crystal structure of an HIV-binding recombinant fragment of human CD4."
Ryu S.-E., Kwong P.D., Truneh A., Porter T.G., Arthos J., Rosenberg M., Dai X., Xuong N.-H., Axel R., Sweet R.W., Hendrickson W.A.
Nature 348:419-426(1990) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRWHUT4. A90872.
RefSeqNP_000607.1. NM_000616.4.
UniGeneHs.631659.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray2.50C26-208[»]
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/Q431-441[»]
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[»]
4JM2X-ray3.10F26-208[»]
DisProtDP00123.
ProteinModelPortalP01730.
SMRP01730. Positions 26-388, 393-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107358. 78 interactions.
DIPDIP-617N.
IntActP01730. 16 interactions.
MINTMINT-1130311.
STRING9606.ENSP00000011653.

Chemistry

BindingDBP01730.
ChEMBLCHEMBL2754.

PTM databases

PhosphoSiteP01730.
UniCarbKBP01730.

Polymorphism databases

DMDM116013.

Proteomic databases

PaxDbP01730.
PeptideAtlasP01730.
PRIDEP01730.

Protocols and materials databases

DNASU920.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000011653; ENSP00000011653; ENSG00000010610.
ENST00000594128; ENSP00000469397; ENSG00000268779.
GeneID920.
KEGGhsa:920.
UCSCuc001qqv.2. human.

Organism-specific databases

CTD920.
GeneCardsGC12P006899.
HGNCHGNC:1678. CD4.
HPACAB000011.
HPA004252.
HPA004472.
MIM186940. gene.
613949. phenotype.
neXtProtNX_P01730.
PharmGKBPA26220.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47205.
HOGENOMHOG000008696.
HOVERGENHBG005281.
InParanoidP01730.
KOK06454.
OMAWQCLLSD.
PhylomeDBP01730.
TreeFamTF335974.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP01730.

Gene expression databases

ArrayExpressP01730.
BgeeP01730.
CleanExHS_CD4.
GenevestigatorP01730.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR000973. 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]
PfamPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR00692. CD4TCANTIGEN.
SMARTSM00409. IG. 2 hits.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD4. human.
EvolutionaryTraceP01730.
GeneWikiCD4.
GenomeRNAi920.
NextBio3806.
PROP01730.
SOURCESearch...

Entry information

Entry nameCD4_HUMAN
AccessionPrimary (citable) accession number: P01730
Secondary accession number(s): B2R737 expand/collapse secondary AC list , D3DUS5, Q4ZGK2, Q5U066, Q9UDE5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: April 16, 2014
This is version 172 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries