CD6_HUMAN - dbPTM
CD6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD6_HUMAN
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
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
28N-linked_GlycosylationPAPPDQLNTSSAESE
CCCCHHCCCCCCHHH
32.0826146185
48PhosphorylationERLPVRLTNGSSSCS
CCCCEEEECCCCCCC
27.28-
49N-linked_GlycosylationRLPVRLTNGSSSCSG
CCCEEEECCCCCCCC
53.6026146185
112N-linked_GlycosylationPPPPAAGNTSVAANA
CCCCCCCCCCHHHCC
25.18UniProtKB CARBOHYD
118N-linked_GlycosylationGNTSVAANATLAGAP
CCCCHHHCCCCCCCC
24.58UniProtKB CARBOHYD
229N-linked_GlycosylationPIHRDQVNCSGAEAY
CCCHHHCCCCCCEEE
14.4926146185
327PhosphorylationHSLSGRMYYSCNGEE
CCCCCCEEEEECCCE
7.2922817900
339N-linked_GlycosylationGEELTLSNCSWRFNN
CCEEEEECCEEECCC
27.27UniProtKB CARBOHYD
341PhosphorylationELTLSNCSWRFNNSN
EEEEECCEEECCCCC
26.0722817900
345N-linked_GlycosylationSNCSWRFNNSNLCSQ
ECCEEECCCCCCCCH
42.31UniProtKB CARBOHYD
365PhosphorylationVLCSASRSLHNLSTP
HHHHHHHHHCCCCCC
31.3322468782
368N-linked_GlycosylationSASRSLHNLSTPEVP
HHHHHHCCCCCCCCC
40.77UniProtKB CARBOHYD
380PhosphorylationEVPASVQTVTIESSV
CCCCCCEEEEEEEEE
19.9122468782
382PhosphorylationPASVQTVTIESSVTV
CCCCEEEEEEEEEEE
23.5522468782
385PhosphorylationVQTVTIESSVTVKIE
CEEEEEEEEEEEEEC
26.6824076635
388PhosphorylationVTIESSVTVKIENKE
EEEEEEEEEEECCHH
20.3024076635
396PhosphorylationVKIENKESRELMLLI
EEECCHHHHHHHHHH
32.4429759185
405PhosphorylationELMLLIPSIVLGILL
HHHHHHHHHHHHHHH
20.52-
430PhosphorylationLLRIKGKYALPVMVN
HHHHHCCCEEEEEEE
23.2622210691
443PhosphorylationVNHQHLPTTIPAGSN
EECCCCCCCCCCCCC
43.6629978859
444PhosphorylationNHQHLPTTIPAGSNS
ECCCCCCCCCCCCCC
24.0329978859
449PhosphorylationPTTIPAGSNSYQPVP
CCCCCCCCCCCCCCC
25.3929978859
451PhosphorylationTIPAGSNSYQPVPIT
CCCCCCCCCCCCCEE
27.1722210691
452PhosphorylationIPAGSNSYQPVPITI
CCCCCCCCCCCCEEE
22.5322210691
458PhosphorylationSYQPVPITIPKEVFM
CCCCCCEEECCEEEE
25.7529978859
480PhosphorylationPPPEDSDSGSDSDYE
CCCCCCCCCCCCCCC
44.12-
482PhosphorylationPEDSDSGSDSDYEHY
CCCCCCCCCCCCCCC
37.58-
484PhosphorylationDSDSGSDSDYEHYDF
CCCCCCCCCCCCCCC
43.73-
505PhosphorylationALTTFYNSQRHRVTD
EEEEEECCCCCCCCH
19.74-
511PhosphorylationNSQRHRVTDEEVQQS
CCCCCCCCHHHHHHH
37.34-
560PhosphorylationGPQYHPRSNSESSTS
CCCCCCCCCCCCCCC
49.51-
562PhosphorylationQYHPRSNSESSTSSG
CCCCCCCCCCCCCCC
39.85-
565PhosphorylationPRSNSESSTSSGEDY
CCCCCCCCCCCCCCC
28.40-
567PhosphorylationSNSESSTSSGEDYCN
CCCCCCCCCCCCCCC
37.99-
568PhosphorylationNSESSTSSGEDYCNS
CCCCCCCCCCCCCCC
46.41-
572PhosphorylationSTSSGEDYCNSPKSK
CCCCCCCCCCCCHHH
6.8225839225
629PhosphorylationSTSSGEWYQNFQPPP
CCCCCCHHHCCCCCC
6.8422817900
662PhosphorylationDSTDNDDYDDISAA-
CCCCCCCHHHCCCC-
20.551919444

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
480SPhosphorylationKinaseCSNK2A1P68400
GPS
482SPhosphorylationKinaseCSNK2A1P68400
GPS
484SPhosphorylationKinaseCSNK2A1P68400
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD6_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLYG_HUMANGYG1physical
21988832
NF2L1_HUMANNFE2L1physical
21988832

Drug and Disease Associations
Kegg Disease
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.
Regulatory Network of CD6_HUMAN

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Related Literatures of Post-Translational Modification

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