CO4A1_HUMAN - dbPTM
CO4A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO4A1_HUMAN
UniProt AC P02462
Protein Name Collagen alpha-1(IV) chain
Gene Name COL4A1
Organism Homo sapiens (Human).
Sequence Length 1669
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane .
Protein Description Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin..
Protein Sequence MGPRLSVWLLLLPAALLLHEEHSRAAAKGGCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVPGMLLKGERGFPGIPGTPGPPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGLSFQGPKGDKGDQGVSGPPGVPGQAQVQEKGDFATKGEKGQKGEPGFQGMPGVGEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEAGPPGPPGIVIGTGPLGEKGERGYPGTPGPRGEPGPKGFPGLPGQPGPPGLPVPGQAGAPGFPGERGEKGDRGFPGTSLPGPSGRDGLPGPPGSPGPPGQPGYTNGIVECQPGPPGDQGPPGIPGQPGFIGEIGEKGQKGESCLICDIDGYRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGVAGVPGPQGTPGLIGQPGAKGEPGEFYFDLRLKGDKGDPGFPGQPGMPGRAGSPGRDGHPGLPGPKGSPGSVGLKGERGPPGGVGFPGSRGDTGPPGPPGYGPAGPIGDKGQAGFPGGPGSPGLPGPKGEPGKIVPLPGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGAVGQPGIGFPGPPGPKGVDGLPGDMGPPGTPGRPGFNGLPGNPGVQGQKGEPGVGLPGLKGLPGLPGIPGTPGEKGSIGVPGVPGEHGAIGPPGLQGIRGEPGPPGLPGSVGSPGVPGIGPPGARGPPGGQGPPGLSGPPGIKGEKGFPGFPGLDMPGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGSMDKVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKGEVGFPGLAGSPGIPGSKGEQGFMGPPGPQGQPGLPGSPGHATEGPKGDRGPQGQPGLPGLPGPMGPPGLPGIDGVKGDKGNPGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGPKGLPGLQGIKGDQGDQGVPGAKGLPGPPGPPGPYDIIKGEPGLPGPEGPPGLKGLQGLPGPKGQQGVTGLVGIPGPPGIPGFDGAPGQKGEMGPAGPTGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPITGENIRPFISRCAVCEAPAMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
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
6Phosphorylation--MGPRLSVWLLLLP
--CCHHHHHHHHHHH		16.72-
23PhosphorylationLLLHEEHSRAAAKGG
HHHCHHHHHHHHHCC		27.2224043423
126N-linked_GlycosylationPPGIPGCNGTKGERG
CCCCCCCCCCCCCCC		68.06UniProtKB CARBOHYD
204HydroxylationGPPGFTGPPGPPGPP
CCCCCCCCCCCCCCC		27.84-
207HydroxylationGFTGPPGPPGPPGPP
CCCCCCCCCCCCCCC		36.13-
210HydroxylationGPPGPPGPPGPPGEK
CCCCCCCCCCCCCCC		36.13-
348PhosphorylationGEKGERGYPGTPGPR
CCCCCCCCCCCCCCC		12.5218083107
348NitrationGEKGERGYPGTPGPR
CCCCCCCCCCCCCCC		12.52-
534NitrationKGEPGEFYFDLRLKG
CCCCCCEEEEEEECC		7.59-
587HydroxylationGLKGERGPPGGVGFP
CCCCCCCCCCCCCCC		30.50-
602HydroxylationGSRGDTGPPGPPGYG
CCCCCCCCCCCCCCC		32.54-
603HydroxylationSRGDTGPPGPPGYGP
CCCCCCCCCCCCCCC		70.08-
605HydroxylationGDTGPPGPPGYGPAG
CCCCCCCCCCCCCCC		25.56-
606HydroxylationDTGPPGPPGYGPAGP
CCCCCCCCCCCCCCC		55.33-
623HydroxylationDKGQAGFPGGPGSPG
CCCCCCCCCCCCCCC		46.01-
626HydroxylationQAGFPGGPGSPGLPG
CCCCCCCCCCCCCCC		46.10-
629HydroxylationFPGGPGSPGLPGPKG
CCCCCCCCCCCCCCC		55.01-
632HydroxylationGPGSPGLPGPKGEPG
CCCCCCCCCCCCCCC		64.06-
647HydroxylationKIVPLPGPPGAEGLP
CEECCCCCCCCCCCC		23.39-
892PhosphorylationGTPGQPGSPGPVGAP
CCCCCCCCCCCCCCC		33.1124719451
1012PhosphorylationGLPGPKGSVGGMGLP
CCCCCCCCCCCCCCC		24.58-
1077PhosphorylationGIAGFPGSPGEKGEK
CCCCCCCCCCCCCCC		29.9423312004
1095PhosphorylationGIPGMPGSPGLKGSP
CCCCCCCCCCCCCCC		15.2124719451
1214HydroxylationGEQGFMGPPGPQGQP
CCCCCCCCCCCCCCC		20.91-
1226PhosphorylationGQPGLPGSPGHATEG
CCCCCCCCCCCCCCC		26.26-
1231PhosphorylationPGSPGHATEGPKGDR
CCCCCCCCCCCCCCC		35.48-
1265O-linked_GlycosylationLPGIDGVKGDKGNPG
CCCCCCCCCCCCCCC		67.916434307
1424HydroxylationGPRGFPGPPGPDGLP
CCCCCCCCCCCCCCC		30.80-
1433PhosphorylationGPDGLPGSMGPPGTP
CCCCCCCCCCCCCCC		20.7328857561
1439PhosphorylationGSMGPPGTPSVDHGF
CCCCCCCCCCCCCCE		20.4028857561
1460S-palmitoylationQTIDDPQCPSGTKIL
CCCCCCCCCCCCEEE		3.3521044946
1493S-palmitoylationDLGTAGSCLRKFSTM
CCCCHHHHHHHHCCC		4.1021044946
1496GlycationTAGSCLRKFSTMPFL
CHHHHHHHHCCCCEE		30.62-
1519PhosphorylationNFASRNDYSYWLSTP
CCCCCCCCCEEECCC		13.7524275569
1525O-linked_GlycosylationDYSYWLSTPEPMPMS
CCCEEECCCCCCCCC		29.51OGP
1532O-linked_GlycosylationTPEPMPMSMAPITGE
CCCCCCCCCCCCCCC		13.11OGP
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 CO4A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO4A1_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 CO4A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NID1_HUMANNID1physical
9733643
NID1_MOUSENid1physical
9733643
NID2_HUMANNID2physical
9733643
CO4A1_HUMANCOL4A1physical
12011424
PDGFA_HUMANPDGFAphysical
8900172
PDGFB_HUMANPDGFBphysical
8900172
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607595Brain small vessel disease with or without ocular anomalies (BSVD)
611773Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC)
175780Porencephaly 1 (POREN1)
614519Intracerebral hemorrhage (ICH)
180000Tortuosity of retinal arteries (RATOR)
269160Schizencephaly (SCHZC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO4A1_HUMAN

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Related Literatures of Post-Translational Modification

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