CO6A1_HUMAN - dbPTM
CO6A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO6A1_HUMAN
UniProt AC P12109
Protein Name Collagen alpha-1(VI) chain
Gene Name COL6A1
Organism Homo sapiens (Human).
Sequence Length 1028
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Collagen VI acts as a cell-binding protein..
Protein Sequence MRAARALLPLLLQACWTAAQDEPETPRAVAFQDCPVDLFFVLDTSESVALRLKPYGALVDKVKSFTKRFIDNLRDRYYRCDRNLVWNAGALHYSDEVEIIQGLTRMPGGRDALKSSVDAVKYFGKGTYTDCAIKKGLEQLLVGGSHLKENKYLIVVTDGHPLEGYKEPCGGLEDAVNEAKHLGVKVFSVAITPDHLEPRLSIIATDHTYRRNFTAADWGQSRDAEEAISQTIDTIVDMIKNNVEQVCCSFECQPARGPPGLRGDPGFEGERGKPGLPGEKGEAGDPGRPGDLGPVGYQGMKGEKGSRGEKGSRGPKGYKGEKGKRGIDGVDGVKGEMGYPGLPGCKGSPGFDGIQGPPGPKGDPGAFGLKGEKGEPGADGEAGRPGSSGPSGDEGQPGEPGPPGEKGEAGDEGNPGPDGAPGERGGPGERGPRGTPGTRGPRGDPGEAGPQGDQGREGPVGVPGDPGEAGPIGPKGYRGDEGPPGSEGARGAPGPAGPPGDPGLMGERGEDGPAGNGTEGFPGFPGYPGNRGAPGINGTKGYPGLKGDEGEAGDPGDDNNDIAPRGVKGAKGYRGPEGPQGPPGHQGPPGPDECEILDIIMKMCSCCECKCGPIDLLFVLDSSESIGLQNFEIAKDFVVKVIDRLSRDELVKFEPGQSYAGVVQYSHSQMQEHVSLRSPSIRNVQELKEAIKSLQWMAGGTFTGEALQYTRDQLLPPSPNNRIALVITDGRSDTQRDTTPLNVLCSPGIQVVSVGIKDVFDFIPGSDQLNVISCQGLAPSQGRPGLSLVKENYAELLEDAFLKNVTAQICIDKKCPDYTCPITFSSPADITILLDGSASVGSHNFDTTKRFAKRLAERFLTAGRTDPAHDVRVAVVQYSGTGQQRPERASLQFLQNYTALASAVDAMDFINDATDVNDALGYVTRFYREASSGAAKKRLLLFSDGNSQGATPAAIEKAVQEAQRAGIEIFVVVVGRQVNEPHIRVLVTGKTAEYDVAYGESHLFRVPSYQALLRGVFHQTVSRKVALG
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
64PhosphorylationALVDKVKSFTKRFID
HHHHHHHHHHHHHHH
40.9324719451
93PhosphorylationWNAGALHYSDEVEII
ECCCCCCCCCHHHHH
20.7624275569
104PhosphorylationVEIIQGLTRMPGGRD
HHHHHHHHCCCCCHH
31.57-
115PhosphorylationGGRDALKSSVDAVKY
CCHHHHHHHHHHHHH
36.1223312004
116PhosphorylationGRDALKSSVDAVKYF
CHHHHHHHHHHHHHH
23.5623312004
121AcetylationKSSVDAVKYFGKGTY
HHHHHHHHHHCCCCH
36.26129835
121UbiquitinationKSSVDAVKYFGKGTY
HHHHHHHHHHCCCCH
36.26-
125AcetylationDAVKYFGKGTYTDCA
HHHHHHCCCCHHHHH
37.8727178108
129PhosphorylationYFGKGTYTDCAIKKG
HHCCCCHHHHHHHHC
25.1729759185
134AcetylationTYTDCAIKKGLEQLL
CHHHHHHHHCHHHHH
23.4330587825
148AcetylationLVGGSHLKENKYLIV
HCCCHHCCCCCEEEE
54.5427178108
152PhosphorylationSHLKENKYLIVVTDG
HHCCCCCEEEEEECC
17.16-
157PhosphorylationNKYLIVVTDGHPLEG
CCEEEEEECCCCCCC
25.93-
165PhosphorylationDGHPLEGYKEPCGGL
CCCCCCCCCCCCCCH
11.64-
201PhosphorylationDHLEPRLSIIATDHT
CCCCCCEEEEEECCC
17.1523312004
212N-linked_GlycosylationTDHTYRRNFTAADWG
ECCCHHCCCCHHHHC
29.6219159218
301UbiquitinationPVGYQGMKGEKGSRG
CCCCCCCCCCCCCCC
71.402190698
348PhosphorylationGLPGCKGSPGFDGIQ
CCCCCCCCCCCCCCC
13.8225159151
387PhosphorylationGEAGRPGSSGPSGDE
CCCCCCCCCCCCCCC
34.5023663014
388PhosphorylationEAGRPGSSGPSGDEG
CCCCCCCCCCCCCCC
61.7123663014
391PhosphorylationRPGSSGPSGDEGQPG
CCCCCCCCCCCCCCC
63.5023663014
477PhosphorylationGPIGPKGYRGDEGPP
CCCCCCCCCCCCCCC
19.97-
486PhosphorylationGDEGPPGSEGARGAP
CCCCCCCCCCCCCCC
38.3321902226
505SulfoxidationPPGDPGLMGERGEDG
CCCCCCCCCCCCCCC
6.9430846556
516N-linked_GlycosylationGEDGPAGNGTEGFPG
CCCCCCCCCCCCCCC
57.2119159218
537N-linked_GlycosylationNRGAPGINGTKGYPG
CCCCCCCCCCCCCCC
58.98UniProtKB CARBOHYD
601SulfoxidationCEILDIIMKMCSCCE
HHHHHHHHHHHCCCC
2.0130846556
640AcetylationIAKDFVVKVIDRLSR
HCHHHHHHHHHHCCH
28.3327178108
670SulfoxidationVQYSHSQMQEHVSLR
EEECHHHHHHHCCCC
5.9030846556
688AcetylationIRNVQELKEAIKSLQ
CCCHHHHHHHHHHCH
44.3327178108
688UbiquitinationIRNVQELKEAIKSLQ
CCCHHHHHHHHHHCH
44.33-
701O-linked_GlycosylationLQWMAGGTFTGEALQ
CHHHHCCCCCHHHHH
19.67OGP
701PhosphorylationLQWMAGGTFTGEALQ
CHHHHCCCCCHHHHH
19.6727251275
703O-linked_GlycosylationWMAGGTFTGEALQYT
HHHCCCCCHHHHHHC
33.67OGP
703PhosphorylationWMAGGTFTGEALQYT
HHHCCCCCHHHHHHC
33.6727251275
746PhosphorylationTPLNVLCSPGIQVVS
CCCCEEECCCEEEEE
23.2328348404
766PhosphorylationVFDFIPGSDQLNVIS
HHHCCCCCCCEEEEE
19.4826657352
787PhosphorylationSQGRPGLSLVKENYA
CCCCCCHHHHHHHHH
36.7124719451
793PhosphorylationLSLVKENYAELLEDA
HHHHHHHHHHHHHHH
11.5327642862
804N-linked_GlycosylationLEDAFLKNVTAQICI
HHHHHHHCCEEEEEC
38.2219159218
878PhosphorylationVRVAVVQYSGTGQQR
EEEEEEEECCCCCCC
9.47-
896N-linked_GlycosylationASLQFLQNYTALASA
HHHHHHHHHHHHHHH
37.9719159218
1008PhosphorylationSHLFRVPSYQALLRG
CCCCCCHHHHHHHHH
27.3323312004
1009PhosphorylationHLFRVPSYQALLRGV
CCCCCHHHHHHHHHH
7.5523312004
1020PhosphorylationLRGVFHQTVSRKVAL
HHHHHHHHHCCHHHC
16.3323312004

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

Oops, there are no upstream regulatory protein records of CO6A1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO6A1_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 CO6A1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDGFA_HUMANPDGFAphysical
8900172
PDGFB_HUMANPDGFBphysical
8900172

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
158810Bethlem myopathy 1 (BTHLM1)
254090Ullrich congenital muscular dystrophy 1 (UCMD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO6A1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-516; ASN-804 ANDASN-896, AND MASS SPECTROMETRY.

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