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UniProtKB/Swiss-Prot entry P01730


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CD4_HUMAN
Primary accession number P01730
Secondary accession numbers Q4ZGK2 Q5U066
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 1, 1988 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 124)
Name and origin of the protein
Protein name T-cell surface glycoprotein CD4 [Precursor]
Synonyms T-cell surface antigen T4/Leu-3
CD4 antigen
Gene name
Name: CD4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0092-8674(85)80105-7; PubMed=2990730 [NCBI, ExPASy, EBI, Israel, Japan]
Maddon P.J., Littman D.R., Godfrey M., Maddon D.E., Chess L., Axel R.;
"The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family.";
Cell 42:93-104(1985).
[2]
SEQUENCE REVISION TO 26.
DOI=10.1016/0092-8674(88)90211-5; PubMed=3263213 [NCBI, ExPASy, EBI, Israel, Japan]
Littman D.R., Maddon P.J., Axel R.;
"Corrected CD4 sequence.";
Cell 55:541-541(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8723724 [NCBI, ExPASy, EBI, Israel, Japan]
Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.;
"A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13.";
Genome Res. 6:314-326(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=9074930 [NCBI, ExPASy, EBI, Israel, Japan]
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination.";
Genome Res. 7:268-280(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TRP-265.
DOI=10.1016/0198-8859(91)90077-M; PubMed=1708753 [NCBI, ExPASy, EBI, Israel, Japan]
Hodge T.W., Sasso D.R., McDougal J.S.;
"Humans with OKT4-epitope deficiency have a single nucleotide base change in the CD4 gene, resulting in substitution of TRP240 for ARG240.";
Hum. Immunol. 30:99-104(1991).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-191; SER-227 AND TRP-265.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-424.
TISSUE=Blood;
DOI=10.1002/eji.1830221132; PubMed=1425921 [NCBI, ExPASy, EBI, Israel, Japan]
Fomsgaard A., Hirsch V.M., Johnson P.R.;
"Cloning and sequences of primate CD4 molecules: diversity of the cellular receptor for simian immunodeficiency virus/human immunodeficiency virus.";
Eur. J. Immunol. 22:2973-2981(1992).
[10]
PROTEIN SEQUENCE OF 26-394, AND DISULFIDE BOND.
PubMed=2592374 [NCBI, ExPASy, EBI, Israel, Japan]
Carr S.A., Hemling M.E., Folena-Wasserman G., Sweet R.W., Anumula K., Barr J.R., Huddleston M.J., Taylor P.;
"Protein and carbohydrate structural analysis of a recombinant soluble CD4 receptor by mass spectrometry.";
J. Biol. Chem. 264:21286-21295(1989).
[11]
PROTEIN SEQUENCE OF 26-40.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[12]
INTERACTION WITH HIV-1 ENVELOPE POLYPROTEIN GP160.
PubMed=2214026 [NCBI, ExPASy, EBI, Israel, Japan]
Crise B., Buonocore L., Rose J.K.;
"CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor.";
J. Virol. 64:5585-5593(1990).
[13]
PALMITOYLATION AT CYS-419 AND CYS-422.
PubMed=1618861 [NCBI, ExPASy, EBI, Israel, Japan]
Crise B., Rose J.K.;
"Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.";
J. Biol. Chem. 267:13593-13597(1992).
[14]
REMOVAL FROM CELL SURFACE BY HIV-1 NEF, AND MUTAGENESIS OF MET-432; SER-433; 438-LEU-LEU-439 AND SER-440.
DOI=10.1016/0092-8674(94)90360-3; PubMed=8124721 [NCBI, ExPASy, EBI, Israel, Japan]
Aiken C., Konner J., Landau N.R., Lenburg M.E., Trono D.;
"Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain.";
Cell 76:853-864(1994).
[15]
INTERACTION WITH HUMAN HERPESVIRUS 7 CAPSID PROTEINS.
DOI=10.1073/pnas.91.9.3872; PubMed=7909607 [NCBI, ExPASy, EBI, Israel, Japan]
Lusso P., Secchiero P., Crowley R.W., Garzino-Demo A., Berneman Z.N., Gallo R.C.;
"CD4 is a critical component of the receptor for human herpesvirus 7: interference with human immunodeficiency virus.";
Proc. Natl. Acad. Sci. U.S.A. 91:3872-3876(1994).
[16]
INTERACTION WITH SPG21, AND MUTAGENESIS OF 457-PRO-ILE-458.
DOI=10.1074/jbc.M009270200; PubMed=11113139 [NCBI, ExPASy, EBI, Israel, Japan]
Zeitlmann L., Sirim P., Kremmer E., Kolanus W.;
"Cloning of ACP33 as a novel intracellular ligand of CD4.";
J. Biol. Chem. 276:9123-9132(2001).
[17]
SUBCELLULAR LOCATION.
PubMed=12517957 [NCBI, ExPASy, EBI, Israel, Japan]
Fragoso R., Ren D., Zhang X., Su M.W., Burakoff S.J., Jin Y.J.;
"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.";
J. Immunol. 170:913-921(2003).
[18]
INTERACTION WITH HIV-1 SURFACE PROTEIN GP120.
DOI=10.1021/bi051120s; PubMed=16331979 [NCBI, ExPASy, EBI, Israel, Japan]
Sharma D., Balamurali M.M., Chakraborty K., Kumaran S., Jeganathan S., Rashid U., Ingallinella P., Varadarajan R.;
"Protein minimization of the gp120 binding region of human CD4.";
Biochemistry 44:16192-16202(2005).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-208.
DOI=10.1038/348411a0; PubMed=1701030 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains.";
Nature 348:411-418(1990).
[21]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-208.
DOI=10.1038/348419a0; PubMed=2247146 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Crystal structure of an HIV-binding recombinant fragment of human CD4.";
Nature 348:419-426(1990).
[22]
X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 26-388.
DOI=10.1038/387527a0; PubMed=9168119 [NCBI, ExPASy, EBI, Israel, Japan]
Wu H., Kwong P.D., Hendrickson W.A.;
"Dimeric association and segmental variability in the structure of human CD4.";
Nature 387:527-530(1997).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-208 IN COMPLEX WITH HIV SURFACE PROTEIN GP120.
DOI=10.1038/31405; PubMed=9641677 [NCBI, ExPASy, EBI, Israel, Japan]
Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A.;
"Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody.";
Nature 393:648-659(1998).
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: 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.
  • 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.
  • PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts.
  • MISCELLANEOUS: Primary receptor for HIV-1.
  • SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like) domains.
  • SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) domain.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cd4/";.
  • WEB RESOURCE: Name=Wikipedia; Note=CD4 entry; URL="http://en.wikipedia.org/wiki/CD4";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M12807; AAA35572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47924; AAB51309.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35160; AAA16069.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019791; AAV38594.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019811; AAV38614.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ012936; AAY22175.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025782; AAH25782.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00003983; -.
PIR A90872; RWHUT4.
RefSeq NP_000607.1; -.
UniGene Hs.631659
3D structure databases
PDB
1CDH; X-ray; 2.30 A; A=26-203.[ExPASy / RCSB / EBI]
1CDI; X-ray; 2.90 A; A=26-203.[ExPASy / RCSB / EBI]
1CDJ; X-ray; 2.50 A; A=26-203.[ExPASy / RCSB / EBI]
1CDU; X-ray; 2.70 A; A=26-203.[ExPASy / RCSB / EBI]
1CDY; X-ray; 2.00 A; A=26-203.[ExPASy / RCSB / EBI]
1G9M; X-ray; 2.20 A; C=26-208.[ExPASy / RCSB / EBI]
1G9N; X-ray; 2.90 A; C=26-208.[ExPASy / RCSB / EBI]
1GC1; X-ray; 2.50 A; C=26-208.[ExPASy / RCSB / EBI]
1JL4; X-ray; 4.30 A; D=26-203.[ExPASy / RCSB / EBI]
1OPN; Model; -; C=26-206.[ExPASy / RCSB / EBI]
1OPT; Model; -; C=26-206.[ExPASy / RCSB / EBI]
1OPW; Model; -; C=26-206.[ExPASy / RCSB / EBI]
1Q68; NMR; -; A=421-458.[ExPASy / RCSB / EBI]
1RZJ; X-ray; 2.20 A; C=26-208.[ExPASy / RCSB / EBI]
1RZK; X-ray; 2.90 A; C=26-208.[ExPASy / RCSB / EBI]
1WBR; NMR; -; A=428-444.[ExPASy / RCSB / EBI]
1WIO; X-ray; 3.90 A; A/B=26-388.[ExPASy / RCSB / EBI]
1WIP; X-ray; 4.00 A; A/B=26-388.[ExPASy / RCSB / EBI]
1WIQ; X-ray; 5.00 A; A/B=26-388.[ExPASy / RCSB / EBI]
2B4C; X-ray; 3.30 A; C=26-206.[ExPASy / RCSB / EBI]
2JKR; X-ray; 2.98 A; P/Q=431-441.[ExPASy / RCSB / EBI]
2JKT; X-ray; 3.40 A; P/Q=431-441.[ExPASy / RCSB / EBI]
2NXY; X-ray; 2.00 A; B=26-208.[ExPASy / RCSB / EBI]
2NXZ; X-ray; 2.04 A; B=26-208.[ExPASy / RCSB / EBI]
2NY0; X-ray; 2.20 A; B=26-208.[ExPASy / RCSB / EBI]
2NY1; X-ray; 1.99 A; B=26-208.[ExPASy / RCSB / EBI]
2NY2; X-ray; 2.00 A; B=26-208.[ExPASy / RCSB / EBI]
2NY3; X-ray; 2.00 A; B=26-208.[ExPASy / RCSB / EBI]
2NY4; X-ray; 2.00 A; B=26-208.[ExPASy / RCSB / EBI]
2NY5; X-ray; 2.50 A; C=26-208.[ExPASy / RCSB / EBI]
2NY6; X-ray; 2.80 A; B=26-208.[ExPASy / RCSB / EBI]
2QAD; X-ray; 3.30 A; B/F=26-206.[ExPASy / RCSB / EBI]
3B71; X-ray; 2.82 A; D/E/F=428-450.[ExPASy / RCSB / EBI]
3CD4; X-ray; 2.20 A; A=26-207.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CDH; -.
1CDI; -.
1CDJ; -.
1CDU; -.
1CDY; -.
1G9M; -.
1G9N; -.
1GC1; -.
1JL4; -.
1OPN; -.
1OPT; -.
1OPW; -.
1Q68; -.
1RZJ; -.
1RZK; -.
1WBR; -.
1WIO; -.
1WIP; -.
1WIQ; -.
2B4C; -.
2JKR; -.
2JKT; -.
2NXY; -.
2NXZ; -.
2NY0; -.
2NY1; -.
2NY2; -.
2NY3; -.
2NY4; -.
2NY5; -.
2NY6; -.
2QAD; -.
3B71; -.
3CD4; -.
DisProt DP00123; -.
ModBase P01730.
Protein-protein interaction databases
DIP DIP:617N; -.
PTM databases
GlycoSuiteDB P01730; -.
PhosphoSite P01730; -.
Enzyme and pathway databases
Pathway_Interaction_DB arf_3pathway; Arf1 pathway.
il12_stat4pathway; IL12 signaling mediated by STAT4.
il12_2pathway; IL12-mediated signaling events.
il23pathway; IL23-mediated signaling events.
tcrpathway; TCR signaling in naive CD4+ T cells.
Reactome REACT_6185; HIV Infection.
REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC12P006769; -.
H-InvDB HIX0023001; -.
HGNC HGNC:1678; CD4.
GenAtlas CD4.
HPA CAB000011; -.
HPA004252; -.
HPA004472; -.
MIM 186940; gene+phenotype. [NCBI / EBI]
PharmGKB PA24403; -.
Gene expression databases
ArrayExpress P01730; -.
Bgee P01730; -.
CleanEx HS_CD4; -.
GermOnline ENSG00000010610; Homo sapiens.
Ontologies
GO
GO:0005769; Cellular component: early endosome (inferred from experiment from Reactome).
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from experiment from Reactome).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042101; Cellular component: T cell receptor complex (non-traceable author statement from UniProtKB).
GO:0015026; Molecular function: coreceptor activity (non-traceable author statement from UniProtKB).
GO:0005201; Molecular function: extracellular matrix structural constituent (non-traceable author statement from UniProtKB).
GO:0001948; Molecular function: glycoprotein binding (inferred from physical interaction from UniProtKB).
GO:0042289; Molecular function: MHC class II protein binding (non-traceable author statement from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0019901; Molecular function: protein kinase binding (inferred from physical interaction from UniProtKB).
GO:0004888; Molecular function: transmembrane receptor activity (traceable author statement from ProtInc).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0007155; Biological process: cell adhesion (inferred from electronic annotation from InterPro).
GO:0000747; Biological process: conjugation with cellular fusion (inferred from direct assay from UniProtKB).
GO:0006955; Biological process: immune response (non-traceable author statement from UniProtKB).
GO:0019059; Biological process: initiation of viral infection (inferred from experiment from Reactome).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0045086; Biological process: positive regulation of interleukin-2 biosynthetic process (non-traceable author statement from UniProtKB).
GO:0045860; Biological process: positive regulation of protein kinase activity (inferred from direct assay from UniProtKB).
GO:0045058; Biological process: T cell selection (inferred from direct assay from UniProtKB).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000973; Ag_CD4.
IPR015274; CD4-extracel.
IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR008424; Ig_C2-set.
IPR003599; Ig_sub.
IPR003596; Ig_V-set_sub.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 4.
Pfam PF05790; C2-set; 2.
PF09191; CD4-extracel; 1.
PF00047; ig; 1.
Pfam graphical view of domain structure.
PRINTS PR00692; CD4TCANTIGEN.
SMART SM00409; IG; 2.
SM00406; IGv; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 1.
PROSITE graphical view of domain structure (profiles).
Other
SWISS-3DIMAGE P01730.
Proteomic databases
PeptideAtlas P01730; -.
PRIDE P01730; -.
Genome annotation databases
Ensembl ENSG00000010610; Homo sapiens. [Contig view]
GeneID 920; -.
KEGG hsa:920; -.
Phylogenomic databases
HOGENOM P01730; -.
HOVERGEN P01730; -.
OMA P01730; QAERMSQ.
Other
NextBio 3806; -.
SOURCE CD4; Homo sapiens.
ProtoNet P01730.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; Host-virus interaction; Immune response; Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Polymorphism; Repeat; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25      
CHAIN   26   458  433     T-cell surface glycoprotein CD4. PRO_0000014621
TOPO_DOM   26   396  371     Extracellular (Potential). 
TRANSMEM   397   418  22     Potential. 
TOPO_DOM   419   458  40     Cytoplasmic (Potential). 
DOMAIN   26   125  100     Ig-like V-type. 
DOMAIN   126   203  78     Ig-like C2-type 1. 
DOMAIN   204   317  114     Ig-like C2-type 2. 
DOMAIN   318   374  57     Ig-like C2-type 3. 
REGION   427   455  29     HIV-1 Vpu-susceptibility domain. 
LIPID   419   419        S-palmitoyl cysteine. 
LIPID   422   422        S-palmitoyl cysteine. 
CARBOHYD   296   296        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000053
CARBOHYD   325   325        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000054
DISULFID   41   109         
DISULFID   155   184         
DISULFID   328   370         
VARIANT   191   191  1     K -> E (in dbSNP:rs28917504 [NCBI]). VAR_023459 [3D]
VARIANT   227   227  1     F -> S (in dbSNP:rs11064419 [NCBI]). VAR_023460 
VARIANT   265   265  1     R -> W (in OKT4-negative populations; dbSNP:rs28919570 [NCBI]). VAR_003906 
MUTAGEN   432   432        M->T: No effect. 
MUTAGEN   433   433        S->A: No effect. 
MUTAGEN   438   439        LL->AA: Loss of Nef-induced CD4 down-modulation. 
MUTAGEN   440   440        S->L: No effect. 
MUTAGEN   457   458        Missing: Abolished interaction with SPG21 and induced T-cell activation. 
STRAND   27    32  6      
STRAND   37    39  3      
STRAND   45    48  4      
STRAND   50    55  6      
STRAND   60    63  4      
TURN   75    79  5      
HELIX   87    89  3      
STRAND   94    96  3      
HELIX   101   103  3      
STRAND   105   111  7      
STRAND   114   129  16      
STRAND   131   134  4      
STRAND   141   144  4      
STRAND   152   156  5      
STRAND   162   168  7      
STRAND   171   173  3      
STRAND   182   187  6      
STRAND   192   197  6      
STRAND   200   202  3      
STRAND   207   214  8      
STRAND   219   222  4      
STRAND   234   244  11      
STRAND   251   256  6      
STRAND   261   267  7      
STRAND   276   279  4      
STRAND   281   287  7      
HELIX   289   291  3      
STRAND   293   299  7      
TURN   302   305  4      
STRAND   308   319  12      
STRAND   323   333  11      
STRAND   340   343  4      
STRAND   345   348  4      
STRAND   350   362  13      
STRAND   365   372  8      
STRAND   374   377  4      
STRAND   380   386  7      
HELIX   432   438  7      
Sequence information
Length: 458 AA [This is the length of the unprocessed precursor] Molecular weight: 51111 Da [This is the MW of the unprocessed precursor] CRC64: 20ED893F9E56D236 [This is a checksum on the sequence]
        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 

P01730 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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