COPG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPG1_MOUSE
• UniProt AC: Q9QZE5
• Protein Name: Coatomer subunit gamma-1
• Gene Name: Copg1
• Organism: Mus musculus (Mouse).
• 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 cytop
• 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 (By similarity). 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..
• Protein Sequence: MLKKFDKKDEESGGGSNPLQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAVERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVSKMISKFTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTNNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLEKALQQYTLEPSEKPFDLKSVPLATTPMAEQRPESTATAAVKQPEKVAATRQEIFQEQLAAVPEFQGLGPLFKSSPEPVALTESETEYVIRCTKHTFSDHLVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLSYVPARSLPYNQPGTCYTLVALPTEDPTAVACTFSCVMKFTVKDCDPNTGEIDEEGYEDEYVLEDLEVTVADHIQKVMKVNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPENKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSSEELPVDIILASVG

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
12	Phosphorylation	FDKKDEESGGGSNPL CCCCCCCCCCCCCHH	40.46	29472430
16	Phosphorylation	DEESGGGSNPLQHLE CCCCCCCCCHHHHHH	38.25	28066266
163	Phosphorylation	SSSALVSSLHLLKCS CHHHHHHHHHHHHHC	16.60	29899451
213	Acetylation	NDRLAVSKMISKFTR CCHHHHHHHHHHHHH	33.38	22826441
213	Malonylation	NDRLAVSKMISKFTR CCHHHHHHHHHHHHH	33.38	26320211
217	Malonylation	AVSKMISKFTRHGLK HHHHHHHHHHHHCCC	39.57	26320211
246	Phosphorylation	QLEEEDGSRDSPLFD HHHHCCCCCCCHHHH	45.28	-
258	S-palmitoylation	LFDFIESCLRNKHEM HHHHHHHHHCCCCHH	2.41	28526873
317	Acetylation	TLNKVAMKHPSAVTA HHHHHHHHCCCHHEE	42.50	-
355	Phosphorylation	LLKTGSESSIDRLMK HHHHCCHHHHHHHHH	34.00	27841257
389	Acetylation	AISALCQKYPRKHAV HHHHHHHHCCHHHHH	57.11	22826441
420	Glutathionylation	YKRAIVDCIISIIEE HHHHHHHHHHHHHHH	1.74	24333276
471	Acetylation	PKTNNPSKYIRFIYN CCCCCHHHHHHHHHC	46.05	23954790
538	Ubiquitination	YLNVLEQKQKALNAG HHHHHHHHHHHHHCC	44.37	-
540	Ubiquitination	NVLEQKQKALNAGYI HHHHHHHHHHHCCHH	62.97	-
554	Phosphorylation	ILNGLTVSIPGLEKA HHCCEEEECCCHHHH	20.17	30352176
572	Ubiquitination	YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC	56.15	-
572	Acetylation	YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC	56.15	23236377
578	Phosphorylation	EKPFDLKSVPLATTP CCCCCCCCCCCCCCC	35.94	26643407
583	Phosphorylation	LKSVPLATTPMAEQR CCCCCCCCCCHHHHC	38.83	26824392
584	Phosphorylation	KSVPLATTPMAEQRP CCCCCCCCCHHHHCC	12.88	26824392
593	Phosphorylation	MAEQRPESTATAAVK HHHHCCCCCCCHHHC	26.48	29472430
594	Phosphorylation	AEQRPESTATAAVKQ HHHCCCCCCCHHHCC	26.77	26643407
596	Phosphorylation	QRPESTATAAVKQPE HCCCCCCCHHHCCHH	18.42	26643407
600	Ubiquitination	STATAAVKQPEKVAA CCCCHHHCCHHHHHH	56.24	-
604	Malonylation	AAVKQPEKVAATRQE HHHCCHHHHHHHHHH	43.80	26320211
604	Ubiquitination	AAVKQPEKVAATRQE HHHCCHHHHHHHHHH	43.80	-
640	Phosphorylation	SPEPVALTESETEYV CCCCEECCCCCCEEE	27.94	26525534
642	Phosphorylation	EPVALTESETEYVIR CCEECCCCCCEEEEE	44.58	26525534
644	Phosphorylation	VALTESETEYVIRCT EECCCCCCEEEEEEE	41.73	30635358

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of COPG1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPG1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of COPG1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of COPG1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.