COFA1_HUMAN - dbPTM
COFA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COFA1_HUMAN
UniProt AC P39059
Protein Name Collagen alpha-1(XV) chain
Gene Name COL15A1
Organism Homo sapiens (Human).
Sequence Length 1388
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.; Restin potently inhibits angiogenesis..
Protein Sequence MAPRRNNGQCWCLLMLLSVSTPLPAVTQTRGATETASQGHLDLTQLIGVPLPSSVSFVTGYGGFPAYSFGPGANVGRPARTLIPSTFFRDFAISVVVKPSSTRGGVLFAITDAFQKVIYLGLRLSGVEDGHQRIILYYTEPGSHVSQEAAAFSVPVMTHRWNRFAMIVQGEEVTLLVNCEEHSRIPFQRSSQALAFESSAGIFMGNAGATGLERFTGSLQQLTVHPDPRTPEELCDPEESSASGETSGLQEADGVAEILEAVTYTQASPKEAKVEPINTPPTPSSPFEDMELSGEPVPEGTLETTNMSIIQHSSPKQGSGEILNDTLEGVHSVDGDPITDSGSGAGAFLDIAEEKNLAATAAGLAEVPISTAGEAEASSVPTGGPTLSMSTENPEEGVTPGPDNEERLAATAAGEAEALASMPGEVEASGVAPGELDLSMSAQSLGEEATVGPSSEDSLTTAAAATEVSLSTFEDEEASGVPTDGLAPLTATMAPERAVTSGPGDEEDLAAATTEEPLITAGGEESGSPPPDGPPLPLPTVAPERWITPAQREHVGMKGQAGPKGEKGDAGEELPGPPEPSGPVGPTAGAEAEGSGLGWGSDVGSGSGDLVGSEQLLRGPPGPPGPPGLPGIPGKPGTDVFMGPPGSPGEDGPAGEPGPPGPEGQPGVDGATGLPGMKGEKGARGPNGSVGEKGDPGNRGLPGPPGKKGQAGPPGVMGPPGPPGPPGPPGPGCTMGLGFEDTEGSGSTQLLNEPKLSRPTAAIGLKGEKGDRGPKGERGMDGASIVGPPGPRGPPGHIKVLSNSLINITHGFMNFSDIPELVGPPGPDGLPGLPGFPGPRGPKGDTGLPGFPGLKGEQGEKGEPGAILTEDIPLERLMGKKGEPGMHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLNGLKGTKGDPGVIMQGPPGLPGPPGPPGPPGAVINIKGAIFPIPVRPHCKMPVDTAHPGSPELITFHGVKGEKGSWGLPGSKGEKGDQGAQGPPGPPLDLAYLRHFLNNLKGENGDKGFKGEKGEKGDINGSFLMSGPPGLPGNPGPAGQKGETVVGPQGPPGAPGLPGPPGFGRPGDPGPPGPPGPPGPPAILGAAVALPGPPGPPGQPGLPGSRNLVTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGELIPIPADSPPPPALSSNPHQLLPPPNPISSANYEKPALHLAALNMPFSGDIRADFQCFKQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSIFSGHGGQFNMHIPIYSFDGRDIMTDPSWPQKVIWHGSSPHGVRLVDNYCEAWRTADTAVTGLASPLSTGKILDQKAYSCANRLIVLCIENSFMTDARK
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
33O-linked_GlycosylationVTQTRGATETASQGH
HHCCCCCCCCCCCCC		36.37OGP
35O-linked_GlycosylationQTRGATETASQGHLD
CCCCCCCCCCCCCCC		27.53OGP
37O-linked_GlycosylationRGATETASQGHLDLT
CCCCCCCCCCCCCHH		44.08OGP
86PhosphorylationARTLIPSTFFRDFAI
HHHCCCCCHHCCEEE		22.8024719451
94PhosphorylationFFRDFAISVVVKPSS
HHCCEEEEEEECCCC		12.8724719451
263O-linked_GlycosylationAEILEAVTYTQASPK
HHHHHHHHHCCCCCC		28.09OGP
265O-linked_GlycosylationILEAVTYTQASPKEA
HHHHHHHCCCCCCCC		14.3222171320
279O-linked_GlycosylationAKVEPINTPPTPSSP
CCCCCCCCCCCCCCC		31.22OGP
282O-linked_GlycosylationEPINTPPTPSSPFED
CCCCCCCCCCCCCCC		36.69OGP
306N-linked_GlycosylationEGTLETTNMSIIQHS
CCCEEECCEEEEECC		29.62UniProtKB CARBOHYD
319PhosphorylationHSSPKQGSGEILNDT
CCCCCCCCCCCCCHH		30.6629759185
324N-linked_GlycosylationQGSGEILNDTLEGVH
CCCCCCCCHHHCCEE		45.97UniProtKB CARBOHYD
360O-linked_GlycosylationEEKNLAATAAGLAEV
HHCCHHHHHHHEEEC		16.07OGP
386O-linked_GlycosylationSVPTGGPTLSMSTEN
CCCCCCCEECCCCCC		34.44OGP
411O-linked_GlycosylationNEERLAATAAGEAEA
HHHHHHHHHHHHHHH		16.07OGP
513O-linked_GlycosylationEEDLAAATTEEPLIT
HHHHHHHCCCCCCEE		29.98OGP
514O-linked_GlycosylationEDLAAATTEEPLITA
HHHHHHCCCCCCEEC		33.36OGP
520O-linked_GlycosylationTTEEPLITAGGEESG
CCCCCCEECCCCCCC		27.25OGP
528O-linked_GlycosylationAGGEESGSPPPDGPP
CCCCCCCCCCCCCCC		43.44OGP
587PhosphorylationPSGPVGPTAGAEAEG
CCCCCCCCCCCCCCC		31.6222468782
687N-linked_GlycosylationEKGARGPNGSVGEKG
CCCCCCCCCCCCCCC		59.19UniProtKB CARBOHYD
807N-linked_GlycosylationVLSNSLINITHGFMN
EECCCCEEECCCCCC		38.10UniProtKB CARBOHYD
814N-linked_GlycosylationNITHGFMNFSDIPEL
EECCCCCCHHHCHHH		30.89UniProtKB CARBOHYD
971PhosphorylationHCKMPVDTAHPGSPE
CCCCCCCCCCCCCCC		27.4026657352
976PhosphorylationVDTAHPGSPELITFH
CCCCCCCCCCEEEEE		21.4729507054
1046N-linked_GlycosylationKGEKGDINGSFLMSG
CCCCCCCCCCEECCC		44.81UniProtKB CARBOHYD
1070PhosphorylationPAGQKGETVVGPQGP
CCCCCCCCEECCCCC		29.2123879269
1136PhosphorylationPGSRNLVTAFSNMDD
CCCHHHHHHHCCHHH		25.75-
1139PhosphorylationRNLVTAFSNMDDMLQ
HHHHHHHCCHHHHHH		28.87-
1188O-linked_GlycosylationLIPIPADSPPPPALS
EECCCCCCCCCCCCC		41.22OGP
1210O-linked_GlycosylationPPPNPISSANYEKPA
CCCCCCCCCCCCCCC		22.66OGP
1239UbiquitinationRADFQCFKQARAAGL
HHHHHHHHHHHHHHH		51.15-
1344PhosphorylationNYCEAWRTADTAVTG
HCHHHHHCCCHHHHC		20.41-
1350PhosphorylationRTADTAVTGLASPLS
HCCCHHHHCCCCCCC		24.82-
1360UbiquitinationASPLSTGKILDQKAY
CCCCCCCCCCCHHHH		39.94-
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 COFA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COFA1_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 COFA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of COFA1_HUMAN !!
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 COFA1_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-265, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.

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