CO6A2_HUMAN - dbPTM
CO6A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO6A2_HUMAN
UniProt AC P12110
Protein Name Collagen alpha-2(VI) chain
Gene Name COL6A2
Organism Homo sapiens (Human).
Sequence Length 1019
Subcellular Localization Secreted, extracellular space, extracellular matrix . Membrane
Peripheral membrane protein . Recruited on membranes by CSPG4.
Protein Description Collagen VI acts as a cell-binding protein..
Protein Sequence MLQGTCSVLLLWGILGAIQAQQQEVISPDTTERNNNCPEKTDCPIHVYFVLDTSESVTMQSPTDILLFHMKQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQVEVFSPPGSDRASFIKNLQGISSFRRGTFTDCALANMTEQIRQDRSKGTVHFAVVITDGHVTGSPCGGIKLQAERAREEGIRLFAVAPNQNLKEQGLRDIASTPHELYRNDYATMLPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPSGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGADGRKGAPGLAGKNGTDGQKGKLGRIGPPGCKGDPGNRGPDGYPGEAGSPGERGDQGGKGDPGRPGRRGPPGEIGAKGSKGYQGNSGAPGSPGVKGAKGGPGPRGPKGEPGRRGDPGTKGSPGSDGPKGEKGDPGPEGPRGLAGEVGNKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGAPGEKGEPGPRGPEGGRGDFGLKGEPGRKGEKGEPADPGPPGEPGPRGPRGVPGPEGEPGPPGDPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIQLDDERIDSLSSFKEAVKNLEWIAGGTWTPSALKFAYDRLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHEKHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPDLPCQTELSVAQCTQRPVDIVFLLDGSERLGEQNFHKARRFVEQVARRLTLARRDDDPLNARVALLQFGGPGEQQVAFPLSHNLTAIHEALETTQYLNSFSHVGAGVVHAINAIVRSPRGGARRHAELSFVFLTDGVTGNDSLHESAHSMRKQNVVPTVLALGSDVDMDVLTTLSLGDRAAVFHEKDYDSLAQPGFFDRFIRWIC
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
58O-linked_GlycosylationLDTSESVTMQSPTDI
EECCCCCCCCCCCHH		20.83OGP
93PhosphorylationYLDQVALSWRYGGLH
HHHHHHHHHEECCEE		10.3624719451
117PhosphorylationPPGSDRASFIKNLQG
CCCCCHHHHHHHHHC		28.5324719451
120 (in isoform 2)Ubiquitination-49.9821906983
120 (in isoform 1)Ubiquitination-49.9821906983
120UbiquitinationSDRASFIKNLQGISS
CCHHHHHHHHHCCCH		49.9821906983
120 (in isoform 3)Ubiquitination-49.9821906983
126PhosphorylationIKNLQGISSFRRGTF
HHHHHCCCHHHCCCC		30.1923911959
127PhosphorylationKNLQGISSFRRGTFT
HHHHCCCHHHCCCCH		22.3523911959
140N-linked_GlycosylationFTDCALANMTEQIRQ
CHHHHHHHHHHHHHH		38.4719159218
197 (in isoform 2)Ubiquitination-56.3821906983
197 (in isoform 1)Ubiquitination-56.3821906983
197UbiquitinationVAPNQNLKEQGLRDI
ECCCCCHHHHCHHHH		56.3821906983
197 (in isoform 3)Ubiquitination-56.3821906983
206PhosphorylationQGLRDIASTPHELYR
HCHHHHHCCHHHHHH		42.6924043423
207PhosphorylationGLRDIASTPHELYRN
CHHHHHCCHHHHHHC		21.4623312004
212PhosphorylationASTPHELYRNDYATM
HCCHHHHHHCCCCCC		12.3724043423
216PhosphorylationHELYRNDYATMLPDS
HHHHHCCCCCCCCCC		13.9224043423
218PhosphorylationLYRNDYATMLPDSTE
HHHCCCCCCCCCCCC		17.0124043423
218O-linked_GlycosylationLYRNDYATMLPDSTE
HHHCCCCCCCCCCCC		17.01OGP
223PhosphorylationYATMLPDSTEIDQDT
CCCCCCCCCCCCHHH		26.4626657352
224PhosphorylationATMLPDSTEIDQDTI
CCCCCCCCCCCHHHH		44.3224043423
230PhosphorylationSTEIDQDTINRIIKV
CCCCCHHHHHHHHHH		17.9624043423
239AcetylationNRIIKVMKHEAYGEC
HHHHHHHHHHHCCEE		41.0827178108
327N-linked_GlycosylationAPGLAGKNGTDGQKG
CCCCCCCCCCCCCCC		58.65UniProtKB CARBOHYD
393UbiquitinationEIGAKGSKGYQGNSG
CCCCCCCCCCCCCCC		71.01-
399PhosphorylationSKGYQGNSGAPGSPG
CCCCCCCCCCCCCCC		43.06-
597PhosphorylationTECDVMTYVRETCGC
CCCCHHHHHHHHCCC		4.5722817900
609AcetylationCGCCDCEKRCGALDV
CCCCCHHHCCCCCCE		60.367668199
630N-linked_GlycosylationSESIGYTNFTLEKNF
CCCCCCCCEEECCCC		21.30UniProtKB CARBOHYD
665PhosphorylationTRVGVVQYSHEGTFE
CEEEEEEECCCCEEE		10.6117053785
666PhosphorylationRVGVVQYSHEGTFEA
EEEEEEECCCCEEEE		9.66-
683PhosphorylationLDDERIDSLSSFKEA
CCHHHHHCHHHHHHH		27.9824275569
685PhosphorylationDERIDSLSSFKEAVK
HHHHHCHHHHHHHHH		37.37-
688 (in isoform 2)Ubiquitination-46.8721906983
688 (in isoform 1)Ubiquitination-46.8721906983
688 (in isoform 3)Ubiquitination-46.8721906983
688UbiquitinationIDSLSSFKEAVKNLE
HHCHHHHHHHHHCCH		46.8721906983
692 (in isoform 2)Ubiquitination-63.9621906983
692 (in isoform 1)Ubiquitination-63.9621906983
692 (in isoform 3)Ubiquitination-63.9621906983
692UbiquitinationSSFKEAVKNLEWIAG
HHHHHHHHCCHHHHC		63.9621906983
701PhosphorylationLEWIAGGTWTPSALK
CHHHHCCCCCHHHHH		25.8322817900
703PhosphorylationWIAGGTWTPSALKFA
HHHCCCCCHHHHHHH		13.7522817900
705PhosphorylationAGGTWTPSALKFAYD
HCCCCCHHHHHHHHH		38.5723040494
708UbiquitinationTWTPSALKFAYDRLI
CCCHHHHHHHHHHHH		27.89-
708 (in isoform 2)Ubiquitination-27.89-
773PhosphorylationKHESENLYSIACDKP
CCCCCCCEEEECCCC		15.0426657352
785N-linked_GlycosylationDKPQQVRNMTLFSDL
CCCHHHCCCCHHHHH		29.0019159218
787O-linked_GlycosylationPQQVRNMTLFSDLVA
CHHHCCCCHHHHHHH		28.3528657654
851UbiquitinationLGEQNFHKARRFVEQ
HHCCCHHHHHHHHHH		39.18-
851AcetylationLGEQNFHKARRFVEQ
HHCCCHHHHHHHHHH		39.1827178108
864PhosphorylationEQVARRLTLARRDDD
HHHHHHHHHHHCCCC		19.2924719451
897N-linked_GlycosylationVAFPLSHNLTAIHEA
EEEECCCCHHHHHHH		35.3919159218
954N-linked_GlycosylationLTDGVTGNDSLHESA
ECCCCCCCHHHHHHH		26.7419159218
1000AcetylationRAAVFHEKDYDSLAQ
CEEEECCCCHHHHCC		53.6827178108
1000 (in isoform 1)Ubiquitination-53.6821906983
1000UbiquitinationRAAVFHEKDYDSLAQ
CEEEECCCCHHHHCC		53.682190698
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 CO6A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO6A2_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 CO6A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CX6A2_HUMANCOX6A2physical
21988832
S38A3_HUMANSLC38A3physical
21988832
Drug and Disease Associations
Kegg Disease
H00590 Congenital muscular dystrophies (CMD/MDC), including: Merosin-deficient CMD (MDC1A); Ullrich CMD (UC
OMIM Disease
158810Bethlem myopathy 1 (BTHLM1)
254090Ullrich congenital muscular dystrophy 1 (UCMD1)
255600Myosclerosis autosomal recessive (MYOSAR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO6A2_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-140; ASN-785; ASN-897 ANDASN-954, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-597, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-665, AND MASSSPECTROMETRY.

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