COPG1_RAT - dbPTM
COPG1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPG1_RAT
UniProt AC Q4AEF8
Protein Name Coatomer subunit gamma-1
Gene Name Copg1
Organism Rattus norvegicus (Rat).
Sequence Length 874
Subcellular Localization Cytoplasm, cytosol. Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasm
Protein Description The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity)..
Protein Sequence MLKKFDKKDEESGGGSNPLQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAVERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVSKMISKFTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTNNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLEKALQQYTLEPSEKPFDLKSVPLATTPMTEQRPESTSTAAVKQPEKVAATRQEIFQEQLAAVPEFQGLGPLFKSSPEPVALTESETEYVIRCTKHTFSDHLVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLSYVPVRSLPYNQPGTCYTLVALPKEDPTAVACTFSCVMKFTVKDCDPNTGEIDEEGYEDEYVLEDLEVTVADHIQKVMKVNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPENKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSSEELPVDIILASVG
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
12PhosphorylationFDKKDEESGGGSNPL
CCCCCCCCCCCCCHH
40.4628432305
16PhosphorylationDEESGGGSNPLQHLE
CCCCCCCCCHHHHHH
38.2528432305
154PhosphorylationAIVDKVPSVSSSALV
HHHHCCCCCCHHHHH
37.3025575281
156PhosphorylationVDKVPSVSSSALVSS
HHCCCCCCHHHHHHH
23.9425575281
157PhosphorylationDKVPSVSSSALVSSL
HCCCCCCHHHHHHHH
19.9225575281
158PhosphorylationKVPSVSSSALVSSLH
CCCCCCHHHHHHHHH
20.3725575281
162PhosphorylationVSSSALVSSLHLLKC
CCHHHHHHHHHHHHH
28.2125575281
163PhosphorylationSSSALVSSLHLLKCS
CHHHHHHHHHHHHHC
16.6025575281
217AcetylationAVSKMISKFTRHGLK
HHHHHHHHHHHHCCC
39.5722902405
290PhosphorylationKELAPAVSVLQLFCS
HHHHHHHHHHHHHHC
21.1528432305
310PhosphorylationLRYAAVRTLNKVAMK
HHHHHHHHHHHHHHH
28.2523984901
351PhosphorylationAITTLLKTGSESSID
HHHHHHHHCCHHHHH
46.0028432305
353PhosphorylationTTLLKTGSESSIDRL
HHHHHHCCHHHHHHH
39.2728432305
355PhosphorylationLLKTGSESSIDRLMK
HHHHCCHHHHHHHHH
34.0028432305
356PhosphorylationLKTGSESSIDRLMKQ
HHHCCHHHHHHHHHH
25.1828432305
538UbiquitinationYLNVLEQKQKALNAG
HHHHHHHHHHHHHCC
44.37-
540UbiquitinationNVLEQKQKALNAGYI
HHHHHHHHHHHCCHH
62.97-
572AcetylationYTLEPSEKPFDLKSV
CCCCCCCCCCCCCCC
56.1522902405
583PhosphorylationLKSVPLATTPMTEQR
CCCCCCCCCCCCCCC
38.8328432305
584PhosphorylationKSVPLATTPMTEQRP
CCCCCCCCCCCCCCC
12.8830240740
587PhosphorylationPLATTPMTEQRPEST
CCCCCCCCCCCCCCC
30.1222108457
593PhosphorylationMTEQRPESTSTAAVK
CCCCCCCCCCCCHHC
30.2728432305
594PhosphorylationTEQRPESTSTAAVKQ
CCCCCCCCCCCHHCC
28.5623984901
595PhosphorylationEQRPESTSTAAVKQP
CCCCCCCCCCHHCCH
25.9022108457
596PhosphorylationQRPESTSTAAVKQPE
CCCCCCCCCHHCCHH
20.8022108457
640PhosphorylationSPEPVALTESETEYV
CCCCEECCCCCCEEE
27.9428432305
642PhosphorylationEPVALTESETEYVIR
CCEECCCCCCEEEEE
44.5828432305
644PhosphorylationVALTESETEYVIRCT
EECCCCCCEEEEEEE
41.7328432305

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 COPG1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPG1_RAT !!

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 COPG1_RAT !!

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

Oops, there are no PPI records of COPG1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COPG1_RAT

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Related Literatures of Post-Translational Modification

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