CD6
entrez
923
canonical
uniprot
P30203
canonical
ensembl
ENSG00000013725
resolver
ensp
ENSP00000323280
resolver
ensp
ENSP00000340628
resolver
ensp
ENSP00000390676
resolver
ensp
ENSP00000569081
resolver
ensp
ENSP00000569085
resolver
ensp
ENSP00000569089
resolver
ensp
ENSP00000569090
resolver
ensp
ENSP00000569091
resolver
ensp
ENSP00000569092
resolver
genesymbol
CD6
resolver
hgnc
HGNC:1691
resolver
uniprot
A4KAD4
resolver
uniprot
A4KAD5
resolver
uniprot
Q6AZ88
resolver
uniprot
Q8N4Q7
resolver
uniprot
Q8WWJ3
resolver
uniprot
Q8WWJ4
resolver
uniprot
Q8WWJ5
resolver
uniprot
Q8WWJ6
resolver
uniprot
Q8WWJ7
resolver
uniprot
Q9UMF2
resolver
uniprot
Q9Y4K7
resolver
uniprot
Q9Y4K8
resolver
uniprot
Q9Y4K9
resolver
uniprot
Q9Y4L0
resolver
uniprot_entry
CD6_HUMAN
resolver
uniprot_entry
Q6AZ88_HUMAN
resolver
uniprot_entry
Q8N4Q7_HUMAN
resolver
uniprot_sec
A4KAD4
resolver
uniprot_sec
A4KAD5
resolver
uniprot_sec
Q8WWJ3
resolver
uniprot_sec
Q8WWJ4
resolver
uniprot_sec
Q8WWJ5
resolver
uniprot_sec
Q8WWJ6
resolver
uniprot_sec
Q8WWJ7
resolver
uniprot_sec
Q9UMF2
resolver
uniprot_sec
Q9Y4K7
resolver
uniprot_sec
Q9Y4K8
resolver
uniprot_sec
Q9Y4K9
resolver
uniprot_sec
Q9Y4L0
resolver
amino_acid_sequence
MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA
uniprot
proteins
function
FUNCTION: Cell adhesion molecule that mediates cell-cell contacts and regulates T-cell responses via its interaction with ALCAM/CD166 (PubMed:15048703, PubMed:15294938, PubMed:16352806, PubMed:16914752, PubMed:24584089, PubMed:24945728). Contributes to signaling cascades triggered by activation of the TCR/CD3 complex (PubMed:24584089). Functions as a costimulatory molecule; promotes T-cell activation and proliferation (PubMed:15294938, PubMed:16352806, PubMed:16914752). Contributes to the formation and maturation of the immunological synapse (PubMed:15294938, PubMed:16352806). Functions as a calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria (PubMed:17601777). LPS binding leads to the activation of signaling cascades and down-stream MAP kinases (PubMed:17601777). Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS (PubMed:17601777). {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:17601777, ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:24945728}.
uniprot
proteins
mass_dalton
71801
uniprot
proteins
mutagenesis
MUTAGEN 291; /note="D->A: Strongly reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 293; /note="E->A: Reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 295; /note="Y->A: Abolishes interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 298; /note="E->A: Nearly abolishes interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 314; /note="R->A: Reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 327; /note="Y->A: Nearly abolishes interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 329; /note="S->A: Reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 346; /note="N->A: Strongly reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 349; /note="L->A: Reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 352; /note="Q->A: Reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 353; /note="S->A: Reduces interaction with ALCAM."; /evidence="ECO:0000269|PubMed:26146185"; MUTAGEN 662; /note="Y->F: Reduces tyrosine phosphorylation. Reduces affinity for LCP2. Impairs activation of T-cells."; /evidence="ECO:0000269|PubMed:16914752
uniprot
proteins
post_translational_modification
PTM: After T-cell activation, becomes hyperphosphorylated on Ser and Thr residues and phosphorylated on Tyr residues. {ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:2016320, ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:7678115}.; PTM: Glycosylated. {ECO:0000305|PubMed:24945728}.
uniprot
proteins
pubmed
15048703
uniprot
proteins
pubmed
15294938
uniprot
proteins
pubmed
16352806
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16914752
uniprot
proteins
pubmed
17371992
uniprot
proteins
pubmed
17601777
uniprot
proteins
pubmed
1919444
uniprot
proteins
pubmed
2016320
uniprot
proteins
pubmed
24584089
uniprot
proteins
pubmed
24945728
uniprot
proteins
pubmed
26146185
uniprot
proteins
pubmed
7678115
uniprot
proteins
pubmed
9013954
uniprot
proteins
sequence_length
668
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:17371992, ECO:0000269|PubMed:17601777, ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:9013954}; Single-pass type I membrane protein {ECO:0000269|PubMed:17371992}. Note=Detected at the immunological synapse, i.e, at the contact zone between antigen-presenting dendritic cells and T-cells (PubMed:15294938, PubMed:16352806). Colocalizes with the TCR/CD3 complex at the immunological synapse (PubMed:15294938). {ECO:0000269|PubMed:15294938}.; SUBCELLULAR LOCATION: [Soluble CD6]: Secreted {ECO:0000269|PubMed:17601777}. Note=The origins of the secreted form are not clear, but it might be created by proteolytic shedding of the ectodomain. {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 403..423; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins