COPG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPG1_HUMAN
• UniProt AC: Q9Y678
• Protein Name: Coatomer subunit gamma-1
• Gene Name: COPG1
• Organism: Homo sapiens (Human).
• Sequence Length: 874
• Subcellular Localization: Cytoplasm . 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 cytoplasmic si
• 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: MLKKFDKKDEESGGGSNPFQHLEKSAVLQEARVFNETPINPRKCAHILTKILYLINQGEHLGTTEATEAFFAMTKLFQSNDPTLRRMCYLTIKEMSCIAEDVIIVTSSLTKDMTGKEDNYRGPAVRALCQITDSTMLQAIERYMKQAIVDKVPSVSSSALVSSLHLLKCSFDVVKRWVNEAQEAASSDNIMVQYHALGLLYHVRKNDRLAVNKMISKVTRHGLKSPFAYCMMIRVASKQLEEEDGSRDSPLFDFIESCLRNKHEMVVYEAASAIVNLPGCSAKELAPAVSVLQLFCSSPKAALRYAAVRTLNKVAMKHPSAVTACNLDLENLVTDSNRSIATLAITTLLKTGSESSIDRLMKQISSFMSEISDEFKVVVVQAISALCQKYPRKHAVLMNFLFTMLREEGGFEYKRAIVDCIISIIEENSESKETGLSHLCEFIEDCEFTVLATRILHLLGQEGPKTTNPSKYIRFIYNRVVLEHEEVRAGAVSALAKFGAQNEEMLPSILVLLKRCVMDDDNEVRDRATFYLNVLEQKQKALNAGYILNGLTVSIPGLERALQQYTLEPSEKPFDLKSVPLATAPMAEQRTESTPITAVKQPEKVAATRQEIFQEQLAAVPEFRGLGPLFKSSPEPVALTESETEYVIRCTKHTFTNHMVFQFDCTNTLNDQTLENVTVQMEPTEAYEVLCYVPARSLPYNQPGTCYTLVALPKEDPTAVACTFSCMMKFTVKDCDPTTGETDDEGYEDEYVLEDLEVTVADHIQKVMKLNFEAAWDEVGDEFEKEETFTLSTIKTLEEAVGNIVKFLGMHPCERSDKVPDNKNTHTLLLAGVFRGGHDILVRSRLLLLDTVTMQVTARSLEELPVDIILASVG

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
4	Ubiquitination	----MLKKFDKKDEE ----CCCCCCCCCCC	55.63	24816145
7	Ubiquitination	-MLKKFDKKDEESGG -CCCCCCCCCCCCCC	66.32	29967540
8	Ubiquitination	MLKKFDKKDEESGGG CCCCCCCCCCCCCCC	72.69	29967540
12	Phosphorylation	FDKKDEESGGGSNPF CCCCCCCCCCCCCHH	40.46	25159151
16	Phosphorylation	DEESGGGSNPFQHLE CCCCCCCCCHHHHHH	44.60	20873877
24	Ubiquitination	NPFQHLEKSAVLQEA CHHHHHHHHHHHHHH	50.50	21906983
25	Phosphorylation	PFQHLEKSAVLQEAR HHHHHHHHHHHHHHH	17.77	28674419
37	Phosphorylation	EARVFNETPINPRKC HHHCCCCCCCCHHHH	30.49	23312004
79	Phosphorylation	AMTKLFQSNDPTLRR HHHHHHHCCCHHHHH	35.55	26552605
83	Phosphorylation	LFQSNDPTLRRMCYL HHHCCCHHHHHHHHH	35.44	26552605
89	Phosphorylation	PTLRRMCYLTIKEMS HHHHHHHHHHHHHHH	9.50	26552605
91	Phosphorylation	LRRMCYLTIKEMSCI HHHHHHHHHHHHHHE	11.97	26552605
106	Phosphorylation	AEDVIIVTSSLTKDM EECEEEEECCCCCCC	11.37	-
107	Phosphorylation	EDVIIVTSSLTKDMT ECEEEEECCCCCCCC	16.68	27362937
108	Phosphorylation	DVIIVTSSLTKDMTG CEEEEECCCCCCCCC	30.60	27362937
110	Phosphorylation	IIVTSSLTKDMTGKE EEEECCCCCCCCCCC	27.26	-
111	Ubiquitination	IVTSSLTKDMTGKED EEECCCCCCCCCCCC	51.28	22817900
114	Phosphorylation	SSLTKDMTGKEDNYR CCCCCCCCCCCCCCC	56.06	-
116	Ubiquitination	LTKDMTGKEDNYRGP CCCCCCCCCCCCCCH	53.37	21906983
136	Sulfoxidation	CQITDSTMLQAIERY HHCCCHHHHHHHHHH	2.78	21406390
143	Phosphorylation	MLQAIERYMKQAIVD HHHHHHHHHHHHHHH	8.89	-
145	2-Hydroxyisobutyrylation	QAIERYMKQAIVDKV HHHHHHHHHHHHHCC	27.87	-
145	Malonylation	QAIERYMKQAIVDKV HHHHHHHHHHHHHCC	27.87	26320211
145	Methylation	QAIERYMKQAIVDKV HHHHHHHHHHHHHCC	27.87	-
145	Ubiquitination	QAIERYMKQAIVDKV HHHHHHHHHHHHHCC	27.87	21906983
162	Phosphorylation	VSSSALVSSLHLLKC CCHHHHHHHHHHHHH	28.21	-
163	Phosphorylation	SSSALVSSLHLLKCS CHHHHHHHHHHHHHC	16.60	24719451
191	Sulfoxidation	AASSDNIMVQYHALG HHCCCCHHHHHHHHH	1.60	30846556
213	Acetylation	NDRLAVNKMISKVTR CCHHHHHHHHHHHHH	30.89	25953088
213	Malonylation	NDRLAVNKMISKVTR CCHHHHHHHHHHHHH	30.89	26320211
213	Ubiquitination	NDRLAVNKMISKVTR CCHHHHHHHHHHHHH	30.89	24816145
217	Acetylation	AVNKMISKVTRHGLK HHHHHHHHHHHHCCC	36.38	25953088
217	Malonylation	AVNKMISKVTRHGLK HHHHHHHHHHHHCCC	36.38	26320211
219	Phosphorylation	NKMISKVTRHGLKSP HHHHHHHHHHCCCCH	22.23	24719451
237	Phosphorylation	CMMIRVASKQLEEED HHHHHHHHHHHHHCC	20.34	-
238	Acetylation	MMIRVASKQLEEEDG HHHHHHHHHHHHCCC	49.52	27452117
238	Ubiquitination	MMIRVASKQLEEEDG HHHHHHHHHHHHCCC	49.52	21906983
246	Phosphorylation	QLEEEDGSRDSPLFD HHHHCCCCCCCHHHH	45.28	24719451
257	Phosphorylation	PLFDFIESCLRNKHE HHHHHHHHHHCCCCH	17.40	18452278
290	Phosphorylation	KELAPAVSVLQLFCS HHHHHHHHHHHHHHC	21.15	21406692
297	Phosphorylation	SVLQLFCSSPKAALR HHHHHHHCCHHHHHH	42.20	21406692
298	Phosphorylation	VLQLFCSSPKAALRY HHHHHHCCHHHHHHH	31.44	27050516
300	Ubiquitination	QLFCSSPKAALRYAA HHHHCCHHHHHHHHH	48.52	-
304	Methylation	SSPKAALRYAAVRTL CCHHHHHHHHHHHHH	17.83	-
310	Phosphorylation	LRYAAVRTLNKVAMK HHHHHHHHHHHHHHH	28.25	28857561
317	Acetylation	TLNKVAMKHPSAVTA HHHHHHHHCCCHHEE	42.50	27452117
317	Malonylation	TLNKVAMKHPSAVTA HHHHHHHHCCCHHEE	42.50	26320211
320	Phosphorylation	KVAMKHPSAVTACNL HHHHHCCCHHEECCC	34.78	28348404
339	Phosphorylation	LVTDSNRSIATLAIT HCCCCCHHHHHHHHH	22.33	21712546
350	Ubiquitination	LAITTLLKTGSESSI HHHHHHHHHCCHHHH	54.69	23503661
356	Phosphorylation	LKTGSESSIDRLMKQ HHHCCHHHHHHHHHH	25.18	-
359	Methylation	GSESSIDRLMKQISS CCHHHHHHHHHHHHH	34.70	-
365	Phosphorylation	DRLMKQISSFMSEIS HHHHHHHHHHHHHCC	18.28	30631047
366	Phosphorylation	RLMKQISSFMSEISD HHHHHHHHHHHHCCH	26.97	30631047
414	2-Hydroxyisobutyrylation	EEGGFEYKRAIVDCI HCCCCCHHHHHHHHH	28.31	-
414	Acetylation	EEGGFEYKRAIVDCI HCCCCCHHHHHHHHH	28.31	26822725
465	Ubiquitination	LLGQEGPKTTNPSKY HHCCCCCCCCCHHHH	78.00	21906983
471	Ubiquitination	PKTTNPSKYIRFIYN CCCCCHHHHHHHHHC	46.05	21906983
488	Methylation	VLEHEEVRAGAVSAL HCCCHHHHHHHHHHH	30.50	-
508	Phosphorylation	QNEEMLPSILVLLKR CCHHHHHHHHHHHHH	25.29	28258704
514	Ubiquitination	PSILVLLKRCVMDDD HHHHHHHHHHHCCCC	39.32	21906983
531	Phosphorylation	VRDRATFYLNVLEQK HHHHHHHHHHHHHHH	7.94	27642862
538	Ubiquitination	YLNVLEQKQKALNAG HHHHHHHHHHHHHHC	44.37	21906983
540	Ubiquitination	NVLEQKQKALNAGYI HHHHHHHHHHHHCHH	62.97	21890473
540	Ubiquitination	NVLEQKQKALNAGYI HHHHHHHHHHHHCHH	62.97	21890473
540	Ubiquitination	NVLEQKQKALNAGYI HHHHHHHHHHHHCHH	62.97	21890473
540	Ubiquitination	NVLEQKQKALNAGYI HHHHHHHHHHHHCHH	62.97	22817900
552	Phosphorylation	GYILNGLTVSIPGLE CHHHCCEEEECCCHH	17.38	28348404
554	Phosphorylation	ILNGLTVSIPGLERA HHCCEEEECCCHHHH	20.17	28102081
572	Ubiquitination	YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC	56.15	21890473
572	Ubiquitination	YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC	56.15	21890473
572	Ubiquitination	YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC	56.15	21890473
572	Ubiquitination	YTLEPSEKPFDLKSV CCCCCCCCCCCCCCC	56.15	23000965
577	Ubiquitination	SEKPFDLKSVPLATA CCCCCCCCCCCEECC	51.78	23000965
578	Phosphorylation	EKPFDLKSVPLATAP CCCCCCCCCCEECCC	35.94	22199227
583	Phosphorylation	LKSVPLATAPMAEQR CCCCCEECCCCCCCC	38.69	26074081
586	Sulfoxidation	VPLATAPMAEQRTES CCEECCCCCCCCCCC	6.26	21406390
591	Phosphorylation	APMAEQRTESTPITA CCCCCCCCCCCCCCC	33.70	22199227
593	Phosphorylation	MAEQRTESTPITAVK CCCCCCCCCCCCCCC	38.58	25159151
594	Phosphorylation	AEQRTESTPITAVKQ CCCCCCCCCCCCCCC	16.69	14690497
597	Phosphorylation	RTESTPITAVKQPEK CCCCCCCCCCCCHHH	26.97	30576142
600	Acetylation	STPITAVKQPEKVAA CCCCCCCCCHHHHHH	58.64	25953088
600	Ubiquitination	STPITAVKQPEKVAA CCCCCCCCCHHHHHH	58.64	21906983
604	Ubiquitination	TAVKQPEKVAATRQE CCCCCHHHHHHHHHH	43.80	27667366
631	Ubiquitination	RGLGPLFKSSPEPVA CCCCCCCCCCCCCEE	58.68	21906983
632	Phosphorylation	GLGPLFKSSPEPVAL CCCCCCCCCCCCEEC	43.73	25159151
633	Phosphorylation	LGPLFKSSPEPVALT CCCCCCCCCCCEECC	33.60	25159151
640	Phosphorylation	SPEPVALTESETEYV CCCCEECCCCCEEEE	27.94	22199227
642	Phosphorylation	EPVALTESETEYVIR CCEECCCCCEEEEEE	44.58	26657352
644	Phosphorylation	VALTESETEYVIRCT EECCCCCEEEEEEEE	41.73	27732954
646	Phosphorylation	LTESETEYVIRCTKH CCCCCEEEEEEEECC	14.48	27732954
697	Phosphorylation	LCYVPARSLPYNQPG EEEEECCCCCCCCCC	35.48	28152594
700	Phosphorylation	VPARSLPYNQPGTCY EECCCCCCCCCCCEE	31.55	28152594
718	Phosphorylation	ALPKEDPTAVACTFS ECCCCCCCCEEECEE	46.19	-
723	Phosphorylation	DPTAVACTFSCMMKF CCCCEEECEECEEEE	14.62	-
725	O-linked_Glycosylation	TAVACTFSCMMKFTV CCEEECEECEEEEEE	5.28	23301498
725	Phosphorylation	TAVACTFSCMMKFTV CCEEECEECEEEEEE	5.28	-
738	Phosphorylation	TVKDCDPTTGETDDE EECCCCCCCCCCCCC	33.89	28102081
739	Phosphorylation	VKDCDPTTGETDDEG ECCCCCCCCCCCCCC	38.11	28102081
742	Phosphorylation	CDPTTGETDDEGYED CCCCCCCCCCCCCCC	50.52	28102081
747	Phosphorylation	GETDDEGYEDEYVLE CCCCCCCCCCCCHHC	20.40	28348404
751	Phosphorylation	DEGYEDEYVLEDLEV CCCCCCCCHHCCEEE	23.74	28348404
788	Phosphorylation	DEFEKEETFTLSTIK HHHHHCEEEEHHHHH	24.02	21815630
795	Ubiquitination	TFTLSTIKTLEEAVG EEEHHHHHHHHHHHH	47.33	32015554
806	Ubiquitination	EAVGNIVKFLGMHPC HHHHHHHHHHCCCCC	30.95	21906983
818	Ubiquitination	HPCERSDKVPDNKNT CCCCCCCCCCCCCCC	57.84	33845483
823	Malonylation	SDKVPDNKNTHTLLL CCCCCCCCCCEEEEE	71.28	26320211
823	Ubiquitination	SDKVPDNKNTHTLLL CCCCCCCCCCEEEEE	71.28	33845483
854	Sulfoxidation	LLLDTVTMQVTARSL HHHHHCCHHHHHHCH	2.34	30846556
860	Phosphorylation	TMQVTARSLEELPVD CHHHHHHCHHHCCCC	37.35	25693802
872	Phosphorylation	PVDIILASVG----- CCCEEEEECC-----	24.75	20068231

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

Oops, there are no upstream regulatory protein records of COPG1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPG1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COPG2_HUMAN	COPG2	physical	11056392
COPZ1_HUMAN	COPZ1	physical	11056392
COPZ2_HUMAN	COPZ2	physical	11056392
ARF1_HUMAN	ARF1	physical	10720466
COPE_HUMAN	COPE	physical	10921873
SAC1_HUMAN	SACM1L	physical	14527956
TMEDA_HUMAN	TMED10	physical	9751720
COPA_HUMAN	COPA	physical	9751720
COPB_HUMAN	COPB1	physical	9751720
COPB2_HUMAN	COPB2	physical	9751720
COPG1_HUMAN	COPG1	physical	9751720
COPD_HUMAN	ARCN1	physical	9751720
COPE_HUMAN	COPE	physical	9751720
COPZ1_HUMAN	COPZ1	physical	9751720
COPA_HUMAN	COPA	physical	14729954
COPB_HUMAN	COPB1	physical	14729954
COPB2_HUMAN	COPB2	physical	14729954
COPG1_HUMAN	COPG1	physical	14729954
COPD_HUMAN	ARCN1	physical	14729954
COPZ1_HUMAN	COPZ1	physical	22939629
CXCL7_HUMAN	PPBP	physical	21988832
COPD_HUMAN	ARCN1	physical	22863883
COPB_HUMAN	COPB1	physical	22863883
COPB2_HUMAN	COPB2	physical	22863883
COPE_HUMAN	COPE	physical	22863883
COPZ1_HUMAN	COPZ1	physical	22863883
DDB2_HUMAN	DDB2	physical	22863883
RBGP1_HUMAN	RABGAP1	physical	22863883
RUFY1_HUMAN	RUFY1	physical	22863883
TCPA_HUMAN	TCP1	physical	22863883
TELO2_HUMAN	TELO2	physical	22863883
TTI1_HUMAN	TTI1	physical	22863883
COPA_HUMAN	COPA	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
GCN1_HUMAN	GCN1L1	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
COPA_HUMAN	COPA	physical	28514442
COPB2_HUMAN	COPB2	physical	28514442
COPB_HUMAN	COPB1	physical	28514442
COPD_HUMAN	ARCN1	physical	28514442
COPE_HUMAN	COPE	physical	28514442
ERGI2_HUMAN	ERGIC2	physical	28514442
COPZ1_HUMAN	COPZ1	physical	28514442
ATLA2_HUMAN	ATL2	physical	28514442
NUDC1_HUMAN	NUDCD1	physical	28514442
COPG2_HUMAN	COPG2	physical	28514442

Drug and Disease Associations

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