CD4
entrez
920
canonical
uniprot
P01730
canonical
ensembl
ENSG00000010610
resolver
ensp
ENSP00000011653
resolver
ensp
ENSP00000542118
resolver
ensp
ENSP00000542119
resolver
enst
ENST00000011653
resolver
enst
ENST00000872060
resolver
genesymbol
CD4
resolver
hgnc
HGNC:1678
resolver
uniprot
A0A4Y5UGE4
resolver
uniprot
B0AZV7
resolver
uniprot
B2R737
resolver
uniprot
B4DT49
resolver
uniprot
D3DUS5
resolver
uniprot
Q4ZGK2
resolver
uniprot
Q5U066
resolver
uniprot
Q9UDE5
resolver
uniprot_entry
A0A4Y5UGE4_HUMAN
resolver
uniprot_entry
B0AZV7_HUMAN
resolver
uniprot_entry
B4DT49_HUMAN
resolver
uniprot_entry
CD4_HUMAN
resolver
uniprot_sec
B2R737
resolver
uniprot_sec
D3DUS5
resolver
uniprot_sec
Q4ZGK2
resolver
uniprot_sec
Q5U066
resolver
uniprot_sec
Q9UDE5
resolver
amino_acid_sequence
MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 79 (IMD79) [MIM:619238]: An autosomal recessive disorder characterized by childhood onset of recurrent and recalcitrant skin warts due to uncontrolled viral infection with human papillomavirus (HPV). Some patients may also have recurrent respiratory infections. Laboratory studies show a complete absence of CD4+ T cells. {ECO:0000269|PubMed:31781092, ECO:0000269|PubMed:33471124}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages. {ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:16951326, ECO:0000269|PubMed:24942581, ECO:0000269|PubMed:2823150, ECO:0000269|PubMed:7604010}.; FUNCTION: (Microbial infection) Primary receptor for human immunodeficiency virus-1 (HIV-1) (PubMed:12089508, PubMed:16331979, PubMed:2214026, PubMed:9641677). Down-regulated by HIV-1 Vpu (PubMed:17346169). Acts as a receptor for Human Herpes virus 7/HHV-7 (PubMed:7909607). {ECO:0000269|PubMed:12089508, ECO:0000269|PubMed:16331979, ECO:0000269|PubMed:17346169, ECO:0000269|PubMed:2214026, ECO:0000269|PubMed:7909607, ECO:0000269|PubMed:9641677}.
uniprot
proteins
mass_dalton
51111
uniprot
proteins
mutagenesis
MUTAGEN 65; /note="Q->Y: Increases the affinity for MHCII; when associated with W-70; R-85 and R-88."; /evidence="ECO:0000269|PubMed:21900604"; MUTAGEN 68; /note="F->I: Abrogates the interaction with MHCII and T cell activation."; /evidence="ECO:0000269|PubMed:7604010"; MUTAGEN 70; /note="T->W: Increases the affinity for MHCII; when associated with Y-65; R-85 and R-88."; /evidence="ECO:0000269|PubMed:21900604"; MUTAGEN 85; /note="S->R: Increases the affinity for MHCII; when associated with Y-65; W-70 and R-88."; /evidence="ECO:0000269|PubMed:21900604"; MUTAGEN 88; /note="D->R: Increases the affinity for MHCII; when associated with Y-65; W-70 and R-85."; /evidence="ECO:0000269|PubMed:21900604"; MUTAGEN 265; /note="R->A: Has no effect on the interaction with MHCII. Impairs recognition by OKT4 antibody."; /evidence="ECO:0000269|PubMed:7604010"; MUTAGEN 432; /note="M->T: No effect."; /evidence="ECO:0000269|PubMed:8124721"; MUTAGEN 433; /note="S->A: About 75% loss of internalization."; /evidence="ECO:0000269|PubMed:2105883"; MUTAGEN 433; /note="S->A: No effect."; /evidence="ECO:0000269|PubMed:8124721"; MUTAGEN 438..439; /note="LL->AA: Loss of Nef-induced CD4 down-modulation."; /evidence="ECO:0000269|PubMed:8124721"; MUTAGEN 440; /note="S->L: No effect."; /evidence="ECO:0000269|PubMed:8124721"; MUTAGEN 445; /note="C->A: Loss of homodimerization; when associated with A-447."; /evidence="ECO:0000269|PubMed:9168119"; MUTAGEN 447; /note="C->A: Loss of homodimerization; when associated with A-445."; /evidence="ECO:0000269|PubMed:9168119"; MUTAGEN 457..458; /note="Missing: Abolished interaction with SPG21 and induced T-cell activation."; /evidence="ECO:0000269|PubMed:11113139
uniprot
proteins
post_translational_modification
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000269|PubMed:1618861}.; PTM: Phosphorylated by PKC; phosphorylation at Ser-433 plays an important role for CD4 internalization. {ECO:0000269|PubMed:2105883, ECO:0000269|PubMed:2512251}.
uniprot
proteins
pubmed
11113139
uniprot
proteins
pubmed
12089508
uniprot
proteins
pubmed
12517957
uniprot
proteins
pubmed
1425921
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1618861
uniprot
proteins
pubmed
16331979
uniprot
proteins
pubmed
1673145
uniprot
proteins
pubmed
16888650
uniprot
proteins
pubmed
16951326
uniprot
proteins
pubmed
1701030
uniprot
proteins
pubmed
1708753
uniprot
proteins
pubmed
17346169
uniprot
proteins
pubmed
18078954
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
1961196
uniprot
proteins
pubmed
2001369
uniprot
proteins
pubmed
2105883
uniprot
proteins
pubmed
21900604
uniprot
proteins
pubmed
2214026
uniprot
proteins
pubmed
2247146
uniprot
proteins
pubmed
24696433
uniprot
proteins
pubmed
24942581
uniprot
proteins
pubmed
2512251
uniprot
proteins
pubmed
2592374
uniprot
proteins
pubmed
27114505
uniprot
proteins
pubmed
2823150
uniprot
proteins
pubmed
2990730
uniprot
proteins
pubmed
31781092
uniprot
proteins
pubmed
3263213
uniprot
proteins
pubmed
33471124
uniprot
proteins
pubmed
36070318
uniprot
proteins
pubmed
7604010
uniprot
proteins
pubmed
7909607
uniprot
proteins
pubmed
8088877
uniprot
proteins
pubmed
8124721
uniprot
proteins
pubmed
8723724
uniprot
proteins
pubmed
9074930
uniprot
proteins
pubmed
9168119
uniprot
proteins
pubmed
9641677
uniprot
proteins
sequence_length
458
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12089508, ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:2823150, ECO:0000269|PubMed:2990730}; Single-pass type I membrane protein {ECO:0000269|PubMed:12517957, ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:1708753}. Note=Localizes to lipid rafts (PubMed:12517957, PubMed:9168119). 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.
uniprot
proteins
transmembrane_region
TRANSMEM 397..418; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins