CO4A1_MOUSE - dbPTM
CO4A1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO4A1_MOUSE
UniProt AC P02463
Protein Name Collagen alpha-1(IV) chain
Gene Name Col4a1
Organism Mus musculus (Mouse).
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 MGPRLSVWLLLLFAALLLHEERSRAAAKGDCGGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFSGNPGPPGLPGMKGDPGEILGHVPGTLLKGERGFPGIPGMPGSPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQAQVKEKGDFAPTGEKGQKGEPGFPGVPGYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPLGEKGDRGYPGAPGLRGEPGPKGFPGTPGQPGPPGFPTPGQAGAPGFPGERGEKGDQGFPGVSLPGPSGRDGAPGPPGPPGPPGQPGHTNGIVECQPGPPGDQGPPGTPGQPGLTGEVGQKGQKGESCLACDTEGLRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGLEGLPGPQGSPGLIGQPGAKGEPGEIFFDMRLKGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGERGPPGGVGFPGSRGDIGPPGPPGVGPIGPVGEKGQAGFPGGPGSPGLPGPKGEAGKVVPLPGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPGIGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPPGVPGIGPPGAMGPPGGQGPPGSSGPPGIKGEKGFPGFPGLDMPGPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGMPGSMEHVDMGSMKGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRGFPGFPGSKGDKGSKGEVGFPGLAGSPGIPGVKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGINGPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGLPGVPGFQGQKGLPGLQGVKGDQGDQGVPGPKGLQGPPGPPGPYDVIKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGSVGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPISGDNIRPFISRCAVCEAPAMVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
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
126N-linked_GlycosylationPPGIPGCNGTKGERG
CCCCCCCCCCCCCCC
68.06-
204HydroxylationGPPGFTGPPGPPGPP
CCCCCCCCCCCCCCC
27.84-
207HydroxylationGFTGPPGPPGPPGPP
CCCCCCCCCCCCCCC
36.13-
210HydroxylationGPPGPPGPPGPPGEK
CCCCCCCCCCCCCCC
36.13-
587HydroxylationGLKGERGPPGGVGFP
CCCCCCCCCCCCCCC
30.50-
602HydroxylationGSRGDIGPPGPPGVG
CCCCCCCCCCCCCCC
30.8925645914
603HydroxylationSRGDIGPPGPPGVGP
CCCCCCCCCCCCCCC
63.8125645914
605HydroxylationGDIGPPGPPGVGPIG
CCCCCCCCCCCCCCC
28.3925645914
606HydroxylationDIGPPGPPGVGPIGP
CCCCCCCCCCCCCCC
56.8925645914
623HydroxylationEKGQAGFPGGPGSPG
CCCCCCCCCCCCCCC
46.0125645914
626HydroxylationQAGFPGGPGSPGLPG
CCCCCCCCCCCCCCC
46.1025645914
629HydroxylationFPGGPGSPGLPGPKG
CCCCCCCCCCCCCCC
55.0125645914
632HydroxylationGPGSPGLPGPKGEAG
CCCCCCCCCCCCCCC
64.0625645914
647HydroxylationKVVPLPGPPGAAGLP
CEECCCCCCCCCCCC
23.39-
656PhosphorylationGAAGLPGSPGFPGPQ
CCCCCCCCCCCCCCC
21.6526824392
979AcetylationGTPGVPGKDGQAGHP
CCCCCCCCCCCCCCC
53.257630809
1086PhosphorylationGEKGEKGSAGTPGMP
CCCCCCCCCCCCCCC
34.2926239621
1089PhosphorylationGEKGSAGTPGMPGSP
CCCCCCCCCCCCCCC
19.1826239621
1095PhosphorylationGTPGMPGSPGPRGSP
CCCCCCCCCCCCCCC
22.3226239621
1110PhosphorylationGNIGHPGSPGLPGEK
CCCCCCCCCCCCCCC
21.90-
1214HydroxylationGEQGFMGPPGPQGQP
CCCCCCCCCCCCCCC
20.91-
1303PhosphorylationGSPGITGSKGDMGLP
CCCCCCCCCCCCCCC
25.4728973931
1328AcetylationLPGLQGVKGDQGDQG
CCCCCCCCCCCCCCC
64.697611573
1352PhosphorylationPPGPPGPYDVIKGEP
CCCCCCCCCCCCCCC
28.85-
1424HydroxylationGPRGFPGPPGPDGLP
CCCCCCCCCCCCCCC
30.80-
1433PhosphorylationGPDGLPGSMGPPGTP
CCCCCCCCCCCCCCC
20.7326060331
1439PhosphorylationGSMGPPGTPSVDHGF
CCCCCCCCCCCCCCE
20.4026060331
1441PhosphorylationMGPPGTPSVDHGFLV
CCCCCCCCCCCCEEE
39.7626060331
1460S-nitrosocysteineQTTDDPLCPPGTKIL
CCCCCCCCCCCCEEE
4.68-
1460S-nitrosylationQTTDDPLCPPGTKIL
CCCCCCCCCCCCEEE
4.6821278135
1493S-nitrosocysteineDLGTAGSCLRKFSTM
CCCCHHHHHHHHCCC
4.10-
1493GlutathionylationDLGTAGSCLRKFSTM
CCCCHHHHHHHHCCC
4.1024333276
1493S-nitrosylationDLGTAGSCLRKFSTM
CCCCHHHHHHHHCCC
4.1021278135

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO4A1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CO4A1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO4A1_MOUSE

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Related Literatures of Post-Translational Modification

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