CO7A1_HUMAN - dbPTM
CO7A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO7A1_HUMAN
UniProt AC Q02388
Protein Name Collagen alpha-1(VII) chain
Gene Name COL7A1
Organism Homo sapiens (Human).
Sequence Length 2944
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane.
Protein Description Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen..
Protein Sequence MTLRLLVAALCAGILAEAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD
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
28DimethylationVRAQHRERVTCTRLY
HHHHHHHHCCHHHHE		29.06-
35PhosphorylationRVTCTRLYAADIVFL
HCCHHHHEECEEEEE		9.1019835603
47PhosphorylationVFLLDGSSSIGRSNF
EEEECCCCCCCCCCH		31.3519835603
117PhosphorylationLSYKGGNTRTGAAIL
HHCCCCCCCCCEEEE		32.65-
202PhosphorylationFFFVNDFSILRTLLP
EEEECHHHHHHHHHH		24.47-
278PhosphorylationGLGQPLPSERQEVNV
CCCCCCCCCCCCCCC		53.7624719451
301PhosphorylationLRGLRPLTEYQVTVI
ECCCCCCCCCEEEEE		35.0224043423
303PhosphorylationGLRPLTEYQVTVIAL
CCCCCCCCEEEEEEE		11.7524043423
311PhosphorylationQVTVIALYANSIGEA
EEEEEEEEECCHHHH		8.5024043423
314PhosphorylationVIALYANSIGEAVSG
EEEEEECCHHHHHCC		24.6524043423
320PhosphorylationNSIGEAVSGTARTTA
CCHHHHHCCCCCCCC		37.1624043423
322PhosphorylationIGEAVSGTARTTALE
HHHHHCCCCCCCCCC		12.8824043423
337N-linked_GlycosylationGPELTIQNTTAHSLL
CCCEEEECCCCCEEE		35.23UniProtKB CARBOHYD
354PhosphorylationWRSVPGATGYRVTWR
ECCCCCCCCEEEEEE		40.43-
356PhosphorylationSVPGATGYRVTWRVL
CCCCCCCEEEEEEEE		9.50-
402PhosphorylationVSTLFGRSVGPATSL
EEHHHCCCCCCCHHH		31.63-
408PhosphorylationRSVGPATSLMARTDA
CCCCCCHHHHHCCCC		20.4627251275
585PhosphorylationRVGPREGSASVLTVR
EECCCCCCCEEEEEE		16.7728464451
587PhosphorylationGPREGSASVLTVRRE
CCCCCCCEEEEEECC		21.2528464451
597PhosphorylationTVRREPETPLAVPGL
EEECCCCCCCCCCCE		34.03-
691PhosphorylationDPLGPVRTVHVTQAS
CCCCCCEEEEEEECC		18.39-
695PhosphorylationPVRTVHVTQASSSSV
CCEEEEEEECCCCCE		11.98-
703PhosphorylationQASSSSVTITWTRVP
ECCCCCEEEEEEECC		18.03-
786N-linked_GlycosylationVSRLQILNASSDVLR
EEEHHHHHCCCCEEE		39.13UniProtKB CARBOHYD
788PhosphorylationRLQILNASSDVLRIT
EHHHHHCCCCEEEEE		26.4623403867
788O-linked_GlycosylationRLQILNASSDVLRIT
EHHHHHCCCCEEEEE		26.4630059200
789PhosphorylationLQILNASSDVLRITW
HHHHHCCCCEEEEEE		29.3623403867
826PhosphorylationHQILPGNTDSAEIRG
CCCCCCCCCCHHHCC		36.9326657352
828PhosphorylationILPGNTDSAEIRGLE
CCCCCCCCHHHCCCC		26.2623312004
952PhosphorylationSAEVTARTESPRVPS
CCEEEECCCCCCCCC		38.0523403867
954PhosphorylationEVTARTESPRVPSIE
EEEECCCCCCCCCEE		19.8623403867
959PhosphorylationTESPRVPSIELRVVD
CCCCCCCCEEEEEEE		26.3223403867
988PhosphorylationRASSYILSWRPLRGP
CCCCEEEEECCCCCC		16.1024719451
1045PhosphorylationPEASVTQTPVCPRGL
CCCCCCCCCCCCCCC		14.3424719451
1062PhosphorylationVVFLPHATQDNAHRA
EEEECCCCCCHHHHH		33.1624719451
1098PhosphorylationVQVGLLSYSHRPSPL
EEEECCCCCCCCCCC		14.4122210691
1099PhosphorylationQVGLLSYSHRPSPLF
EEECCCCCCCCCCCC		15.0522210691
1109N-linked_GlycosylationPSPLFPLNGSHDLGI
CCCCCCCCCCCCHHH		50.59UniProtKB CARBOHYD
1309PhosphorylationGADGRPGSPGRAGNP
CCCCCCCCCCCCCCC		27.1928674419
1318PhosphorylationGRAGNPGTPGAPGLK
CCCCCCCCCCCCCCC		21.5826055452
1327PhosphorylationGAPGLKGSPGLPGPR
CCCCCCCCCCCCCCC		17.7626055452
1396PhosphorylationGPPGLPGTAMKGDKG
CCCCCCCCCCCCCCC		22.9528348404
1470MethylationSPGEQGPRGPPGAIG
CCCCCCCCCCCCCCC		76.66-
1686PhosphorylationGEDGRNGSPGSSGPK
CCCCCCCCCCCCCCC		29.6322817900
1690PhosphorylationRNGSPGSSGPKGDRG
CCCCCCCCCCCCCCC		66.1022817900
1918PhosphorylationPKGDRGETGSKGEQG
CCCCCCCCCCCCCCC		49.9729759185
1920PhosphorylationGDRGETGSKGEQGLP
CCCCCCCCCCCCCCC		44.9329759185
1938PhosphorylationGLRGEPGSVPNVDRL
CCCCCCCCCCCHHHH		45.1525404012
2030PhosphorylationERGPPGPSGLAGEPG
CCCCCCCCCCCCCCC		52.9728064214
2036HydroxylationPSGLAGEPGKPGIPG
CCCCCCCCCCCCCCC		56.012537292
2039HydroxylationLAGEPGKPGIPGLPG
CCCCCCCCCCCCCCC		52.432537292
2083PhosphorylationGPPGLPGTPGPPGPP
CCCCCCCCCCCCCCC		24.1128555341
2084HydroxylationPPGLPGTPGPPGPPG
CCCCCCCCCCCCCCC		60.242537292
2087HydroxylationLPGTPGPPGPPGPKV
CCCCCCCCCCCCCCC		74.062537292
2090HydroxylationTPGPPGPPGPKVSVD
CCCCCCCCCCCCCCC		77.092537292
2121PhosphorylationGAKGEPGSNGDQGPK
CCCCCCCCCCCCCCC		48.6429396449
2167HydroxylationMAGPEGKPGLQGPRG
CCCCCCCCCCCCCCC		60.632537292
2176HydroxylationLQGPRGPPGPVGGHG
CCCCCCCCCCCCCCC		63.642537292
2185HydroxylationPVGGHGDPGPPGAPG
CCCCCCCCCCCCCCC		62.882537292
2188HydroxylationGHGDPGPPGAPGLAG
CCCCCCCCCCCCCCC		58.452537292
2273PhosphorylationGKDGDRGSPGVPGSP
CCCCCCCCCCCCCCC		21.2626425664
2279PhosphorylationGSPGVPGSPGLPGPV
CCCCCCCCCCCCCCC		15.1026425664
2492MethylationRPGQEGPRGLTGPPG
CCCCCCCCCCCCCCC		64.71-
2504MethylationPPGSRGERGEKGDVG
CCCCCCCCCCCCCCC		62.49-
2512PhosphorylationGEKGDVGSAGLKGDK
CCCCCCCCCCCCCCC		21.0024719451
2625O-linked_GlycosylationFMGPRGLKGERGVKG
CCCCCCCCCCCCCCC		62.64-
2625HydroxylationFMGPRGLKGERGVKG
CCCCCCCCCCCCCCC		62.642537292
2631HydroxylationLKGERGVKGACGLDG
CCCCCCCCCCCCCCC		43.552537292
2631O-linked_GlycosylationLKGERGVKGACGLDG
CCCCCCCCCCCCCCC		43.55-
2664HydroxylationHKGEMGEPGVPGQSG
CCCCCCCCCCCCCCC		43.272537292
2667HydroxylationEMGEPGVPGQSGAPG
CCCCCCCCCCCCCCC		40.812537292
2673HydroxylationVPGQSGAPGKEGLIG
CCCCCCCCCCCCCCC		58.892537292
2682AcetylationKEGLIGPKGDRGFDG
CCCCCCCCCCCCCCC		69.138273277
2889PhosphorylationEGSCTAYTLRWYHRA
CCCEEEEEEEEHHHH		13.8424719451
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 CO7A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO7A1_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 CO7A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAMA5_HUMANLAMA5physical
9245798
CO1A1_HUMANCOL1A1physical
9169408
CO4A1_HUMANCOL4A1physical
9169408
FINC_HUMANFN1physical
9169408
LAMB3_HUMANLAMB3physical
9989793
LAMC2_HUMANLAMC2physical
9989793
LRC57_HUMANLRRC57physical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen.
131750
226600Epidermolysis bullosa dystrophica, autosomal recessive (RDEB)
131750Epidermolysis bullosa dystrophica, Pasini type (P-DEB)
226600Epidermolysis bullosa dystrophica, Hallopeau-Siemens type (HS-DEB)
131705Transient bullous dermolysis of the newborn (TBDN)
131850Epidermolysis bullosa dystrophica, pretibial type (PR-DEB)
132000Epidermolysis bullosa dystrophica, Bart type (B-DEB)
604129Epidermolysis bullosa pruriginosa (EBP)
607523Nail disorder, non-syndromic congenital, 8 (NDNC8)
131750Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO7A1_HUMAN

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Related Literatures of Post-Translational Modification

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