UniProt ID | CD6_HUMAN | |
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UniProt AC | P30203 | |
Protein Name | T-cell differentiation antigen CD6 | |
Gene Name | CD6 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 668 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . 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 t |
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Protein Description | Cell adhesion molecule that mediates cell-cell contacts and regulates T-cell responses via its interaction with ALCAM/CD166. [PubMed: 15048703] | |
Protein Sequence | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
28 | N-linked_Glycosylation | PAPPDQLNTSSAESE CCCCHHCCCCCCHHH | 32.08 | 26146185 | |
48 | Phosphorylation | ERLPVRLTNGSSSCS CCCCEEEECCCCCCC | 27.28 | - | |
49 | N-linked_Glycosylation | RLPVRLTNGSSSCSG CCCEEEECCCCCCCC | 53.60 | 26146185 | |
112 | N-linked_Glycosylation | PPPPAAGNTSVAANA CCCCCCCCCCHHHCC | 25.18 | UniProtKB CARBOHYD | |
118 | N-linked_Glycosylation | GNTSVAANATLAGAP CCCCHHHCCCCCCCC | 24.58 | UniProtKB CARBOHYD | |
229 | N-linked_Glycosylation | PIHRDQVNCSGAEAY CCCHHHCCCCCCEEE | 14.49 | 26146185 | |
327 | Phosphorylation | HSLSGRMYYSCNGEE CCCCCCEEEEECCCE | 7.29 | 22817900 | |
339 | N-linked_Glycosylation | GEELTLSNCSWRFNN CCEEEEECCEEECCC | 27.27 | UniProtKB CARBOHYD | |
341 | Phosphorylation | ELTLSNCSWRFNNSN EEEEECCEEECCCCC | 26.07 | 22817900 | |
345 | N-linked_Glycosylation | SNCSWRFNNSNLCSQ ECCEEECCCCCCCCH | 42.31 | UniProtKB CARBOHYD | |
365 | Phosphorylation | VLCSASRSLHNLSTP HHHHHHHHHCCCCCC | 31.33 | 22468782 | |
368 | N-linked_Glycosylation | SASRSLHNLSTPEVP HHHHHHCCCCCCCCC | 40.77 | UniProtKB CARBOHYD | |
380 | Phosphorylation | EVPASVQTVTIESSV CCCCCCEEEEEEEEE | 19.91 | 22468782 | |
382 | Phosphorylation | PASVQTVTIESSVTV CCCCEEEEEEEEEEE | 23.55 | 22468782 | |
385 | Phosphorylation | VQTVTIESSVTVKIE CEEEEEEEEEEEEEC | 26.68 | 24076635 | |
388 | Phosphorylation | VTIESSVTVKIENKE EEEEEEEEEEECCHH | 20.30 | 24076635 | |
396 | Phosphorylation | VKIENKESRELMLLI EEECCHHHHHHHHHH | 32.44 | 29759185 | |
405 | Phosphorylation | ELMLLIPSIVLGILL HHHHHHHHHHHHHHH | 20.52 | - | |
430 | Phosphorylation | LLRIKGKYALPVMVN HHHHHCCCEEEEEEE | 23.26 | 22210691 | |
443 | Phosphorylation | VNHQHLPTTIPAGSN EECCCCCCCCCCCCC | 43.66 | 29978859 | |
444 | Phosphorylation | NHQHLPTTIPAGSNS ECCCCCCCCCCCCCC | 24.03 | 29978859 | |
449 | Phosphorylation | PTTIPAGSNSYQPVP CCCCCCCCCCCCCCC | 25.39 | 29978859 | |
451 | Phosphorylation | TIPAGSNSYQPVPIT CCCCCCCCCCCCCEE | 27.17 | 22210691 | |
452 | Phosphorylation | IPAGSNSYQPVPITI CCCCCCCCCCCCEEE | 22.53 | 22210691 | |
458 | Phosphorylation | SYQPVPITIPKEVFM CCCCCCEEECCEEEE | 25.75 | 29978859 | |
480 | Phosphorylation | PPPEDSDSGSDSDYE CCCCCCCCCCCCCCC | 44.12 | - | |
482 | Phosphorylation | PEDSDSGSDSDYEHY CCCCCCCCCCCCCCC | 37.58 | - | |
484 | Phosphorylation | DSDSGSDSDYEHYDF CCCCCCCCCCCCCCC | 43.73 | - | |
505 | Phosphorylation | ALTTFYNSQRHRVTD EEEEEECCCCCCCCH | 19.74 | - | |
511 | Phosphorylation | NSQRHRVTDEEVQQS CCCCCCCCHHHHHHH | 37.34 | - | |
560 | Phosphorylation | GPQYHPRSNSESSTS CCCCCCCCCCCCCCC | 49.51 | - | |
562 | Phosphorylation | QYHPRSNSESSTSSG CCCCCCCCCCCCCCC | 39.85 | - | |
565 | Phosphorylation | PRSNSESSTSSGEDY CCCCCCCCCCCCCCC | 28.40 | - | |
567 | Phosphorylation | SNSESSTSSGEDYCN CCCCCCCCCCCCCCC | 37.99 | - | |
568 | Phosphorylation | NSESSTSSGEDYCNS CCCCCCCCCCCCCCC | 46.41 | - | |
572 | Phosphorylation | STSSGEDYCNSPKSK CCCCCCCCCCCCHHH | 6.82 | 25839225 | |
629 | Phosphorylation | STSSGEWYQNFQPPP CCCCCCHHHCCCCCC | 6.84 | 22817900 | |
662 | Phosphorylation | DSTDNDDYDDISAA- CCCCCCCHHHCCCC- | 20.55 | 1919444 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of CD6_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CD6_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GLYG_HUMAN | GYG1 | physical | 21988832 | |
NF2L1_HUMAN | NFE2L1 | physical | 21988832 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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