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 |
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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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
12 | Phosphorylation | FDKKDEESGGGSNPL CCCCCCCCCCCCCHH | 40.46 | 28432305 | |
16 | Phosphorylation | DEESGGGSNPLQHLE CCCCCCCCCHHHHHH | 38.25 | 28432305 | |
154 | Phosphorylation | AIVDKVPSVSSSALV HHHHCCCCCCHHHHH | 37.30 | 25575281 | |
156 | Phosphorylation | VDKVPSVSSSALVSS HHCCCCCCHHHHHHH | 23.94 | 25575281 | |
157 | Phosphorylation | DKVPSVSSSALVSSL HCCCCCCHHHHHHHH | 19.92 | 25575281 | |
158 | Phosphorylation | KVPSVSSSALVSSLH CCCCCCHHHHHHHHH | 20.37 | 25575281 | |
162 | Phosphorylation | VSSSALVSSLHLLKC CCHHHHHHHHHHHHH | 28.21 | 25575281 | |
163 | Phosphorylation | SSSALVSSLHLLKCS CHHHHHHHHHHHHHC | 16.60 | 25575281 | |
217 | Acetylation | AVSKMISKFTRHGLK HHHHHHHHHHHHCCC | 39.57 | 22902405 | |
290 | Phosphorylation | KELAPAVSVLQLFCS HHHHHHHHHHHHHHC | 21.15 | 28432305 | |
310 | Phosphorylation | LRYAAVRTLNKVAMK HHHHHHHHHHHHHHH | 28.25 | 23984901 | |
351 | Phosphorylation | AITTLLKTGSESSID HHHHHHHHCCHHHHH | 46.00 | 28432305 | |
353 | Phosphorylation | TTLLKTGSESSIDRL HHHHHHCCHHHHHHH | 39.27 | 28432305 | |
355 | Phosphorylation | LLKTGSESSIDRLMK HHHHCCHHHHHHHHH | 34.00 | 28432305 | |
356 | Phosphorylation | LKTGSESSIDRLMKQ HHHCCHHHHHHHHHH | 25.18 | 28432305 | |
538 | Ubiquitination | YLNVLEQKQKALNAG HHHHHHHHHHHHHCC | 44.37 | - | |
540 | Ubiquitination | NVLEQKQKALNAGYI HHHHHHHHHHHCCHH | 62.97 | - | |
572 | Acetylation | YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC | 56.15 | 22902405 | |
583 | Phosphorylation | LKSVPLATTPMTEQR CCCCCCCCCCCCCCC | 38.83 | 28432305 | |
584 | Phosphorylation | KSVPLATTPMTEQRP CCCCCCCCCCCCCCC | 12.88 | 30240740 | |
587 | Phosphorylation | PLATTPMTEQRPEST CCCCCCCCCCCCCCC | 30.12 | 22108457 | |
593 | Phosphorylation | MTEQRPESTSTAAVK CCCCCCCCCCCCHHC | 30.27 | 28432305 | |
594 | Phosphorylation | TEQRPESTSTAAVKQ CCCCCCCCCCCHHCC | 28.56 | 23984901 | |
595 | Phosphorylation | EQRPESTSTAAVKQP CCCCCCCCCCHHCCH | 25.90 | 22108457 | |
596 | Phosphorylation | QRPESTSTAAVKQPE CCCCCCCCCHHCCHH | 20.80 | 22108457 | |
640 | Phosphorylation | SPEPVALTESETEYV CCCCEECCCCCCEEE | 27.94 | 28432305 | |
642 | Phosphorylation | EPVALTESETEYVIR CCEECCCCCCEEEEE | 44.58 | 28432305 | |
644 | Phosphorylation | VALTESETEYVIRCT EECCCCCCEEEEEEE | 41.73 | 28432305 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COPG1_RAT !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of COPG1_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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