COPG2_HUMAN - dbPTM
COPG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPG2_HUMAN
UniProt AC Q9UBF2
Protein Name Coatomer subunit gamma-2
Gene Name COPG2
Organism Homo sapiens (Human).
Sequence Length 871
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 (By similarity)..
Protein Sequence MIKKFDKKDEESGSGSNPFQHLEKSAVLQEARIFNETPINPRRCLHILTKILYLLNQGEHFGTTEATEAFFAMTRLFQSNDQTLRRMCYLTIKEMATISEDVIIVTSSLTKDMTGKEDVYRGPAIRALCRITDGTMLQAIERYMKQAIVDKVSSVSSSALVSSLHMMKISYDVVKRWINEAQEAASSDNIMVQYHALGVLYHLRKNDRLAVSKMLNKFTKSGLKSQFAYCMLIRIASRLLKETEDGHESPLFDFIESCLRNKHEMVIYEAASAIIHLPNCTARELAPAVSVLQLFCSSPKPALRYAAVRTLNKVAMKHPSAVTACNLDLENLITDSNRSIATLAITTLLKTGSESSVDRLMKQISSFVSEISDEFKVVVVQAISALCQKYPRKHSVMMTFLSNMLRDDGGFEYKRAIVDCIISIVEENPESKEAGLAHLCEFIEDCEHTVLATKILHLLGKEGPRTPVPSKYIRFIFNRVVLENEAVRAAAVSALAKFGAQNESLLPSILVLLQRCMMDTDDEVRDRATFYLNVLQQRQMALNATYIFNGLTVSVPGMEKALHQYTLEPSEKPFDMKSIPLAMAPVFEQKAEITLVATKPEKLAPSRQDIFQEQLAAIPEFLNIGPLFKSSEPVQLTEAETEYFVRCIKHMFTNHIVFQFDCTNTLNDQLLEKVTVQMEPSDSYEVLSCIPAPSLPYNQPGICYTLVRLPDDDPTAVAGSFSCTMKFTVRDCDPNTGVPDEDGYDDEYVLEDLEVTVSDHIQKVLKPNFAAAWEEVGDTFEKEETFALSSTKTLEEAVNNIITFLGMQPCERSDKVPENKNSHSLYLAGIFRGGYDLLVRSRLALADGVTMQVTVRSKERTPVDVILASVG
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
12PhosphorylationFDKKDEESGSGSNPF
CCCCCCCCCCCCCHH
35.8920873877
14PhosphorylationKKDEESGSGSNPFQH
CCCCCCCCCCCHHHH
48.6120873877
16PhosphorylationDEESGSGSNPFQHLE
CCCCCCCCCHHHHHH
42.9223186163
25PhosphorylationPFQHLEKSAVLQEAR
HHHHHHHHHHHHHHH
17.7722199227
32MethylationSAVLQEARIFNETPI
HHHHHHHHHHCCCCC
33.02-
67PhosphorylationHFGTTEATEAFFAMT
CCCCHHHHHHHHHHH
22.93-
83PhosphorylationLFQSNDQTLRRMCYL
HHHCCHHHHHHHHHH
25.7025599653
89PhosphorylationQTLRRMCYLTIKEMA
HHHHHHHHHHHHHHC
9.5029116813
99PhosphorylationIKEMATISEDVIIVT
HHHHCCCCCCEEEEE
24.32-
106PhosphorylationSEDVIIVTSSLTKDM
CCCEEEEECCCCCCC
11.37-
107PhosphorylationEDVIIVTSSLTKDMT
CCEEEEECCCCCCCC
16.68-
108PhosphorylationDVIIVTSSLTKDMTG
CEEEEECCCCCCCCC
30.60-
110PhosphorylationIIVTSSLTKDMTGKE
EEEECCCCCCCCCCC
27.26-
114PhosphorylationSSLTKDMTGKEDVYR
CCCCCCCCCCCCHHC
56.06-
136SulfoxidationCRITDGTMLQAIERY
HHCCCCHHHHHHHHH
2.9821406390
143PhosphorylationMLQAIERYMKQAIVD
HHHHHHHHHHHHHHH
8.8927251275
145MethylationQAIERYMKQAIVDKV
HHHHHHHHHHHHHHH
27.87-
145AcetylationQAIERYMKQAIVDKV
HHHHHHHHHHHHHHH
27.8725953088
145MalonylationQAIERYMKQAIVDKV
HHHHHHHHHHHHHHH
27.8726320211
145UbiquitinationQAIERYMKQAIVDKV
HHHHHHHHHHHHHHH
27.87-
153PhosphorylationQAIVDKVSSVSSSAL
HHHHHHHHCCCHHHH
30.6627251275
154PhosphorylationAIVDKVSSVSSSALV
HHHHHHHCCCHHHHH
29.0727251275
156PhosphorylationVDKVSSVSSSALVSS
HHHHHCCCHHHHHHH
22.1127251275
157PhosphorylationDKVSSVSSSALVSSL
HHHHCCCHHHHHHHH
19.9227251275
158PhosphorylationKVSSVSSSALVSSLH
HHHCCCHHHHHHHHH
20.3727251275
201PhosphorylationYHALGVLYHLRKNDR
HHHHHHHHHHHHCCH
9.0820068231
213AcetylationNDRLAVSKMLNKFTK
CCHHHHHHHHHHHHH
40.5925953088
229PhosphorylationGLKSQFAYCMLIRIA
CHHHHHHHHHHHHHH
4.62-
249PhosphorylationETEDGHESPLFDFIE
HCCCCCCCHHHHHHH
22.6418452278
257PhosphorylationPLFDFIESCLRNKHE
HHHHHHHHHHCCCCH
17.4018452278
290PhosphorylationRELAPAVSVLQLFCS
HHHHHHHHHHHHHHC
21.1524719451
296GlutathionylationVSVLQLFCSSPKPAL
HHHHHHHHCCCCHHH
5.5322555962
296S-nitrosocysteineVSVLQLFCSSPKPAL
HHHHHHHHCCCCHHH
5.53-
296S-nitrosylationVSVLQLFCSSPKPAL
HHHHHHHHCCCCHHH
5.5319483679
297PhosphorylationSVLQLFCSSPKPALR
HHHHHHHCCCCHHHH
42.2028348404
298PhosphorylationVLQLFCSSPKPALRY
HHHHHHCCCCHHHHH
37.8228348404
305PhosphorylationSPKPALRYAAVRTLN
CCCHHHHHHHHHHHH
10.3622210691
310PhosphorylationLRYAAVRTLNKVAMK
HHHHHHHHHHHHHHH
28.2528857561
313AcetylationAAVRTLNKVAMKHPS
HHHHHHHHHHHHCCC
34.1927452117
317AcetylationTLNKVAMKHPSAVTA
HHHHHHHHCCCHHCC
42.5026051181
320PhosphorylationKVAMKHPSAVTACNL
HHHHHCCCHHCCCCC
34.78-
325S-nitrosylationHPSAVTACNLDLENL
CCCHHCCCCCCHHHH
3.6719483679
325GlutathionylationHPSAVTACNLDLENL
CCCHHCCCCCCHHHH
3.6722555962
325S-nitrosocysteineHPSAVTACNLDLENL
CCCHHCCCCCCHHHH
3.67-
339PhosphorylationLITDSNRSIATLAIT
HHCCCCHHHHHHHHH
22.3321712546
350UbiquitinationLAITTLLKTGSESSV
HHHHHHHHHCCHHHH
54.69-
366PhosphorylationRLMKQISSFVSEISD
HHHHHHHHHHHHCCH
31.15-
414UbiquitinationDDGGFEYKRAIVDCI
CCCCCCHHHHHHHHH
28.31-
420GlutathionylationYKRAIVDCIISIVEE
HHHHHHHHHHHHHHH
1.7422555962
461UbiquitinationKILHLLGKEGPRTPV
HHHHHHCCCCCCCCC
60.5121890473
461UbiquitinationKILHLLGKEGPRTPV
HHHHHHCCCCCCCCC
60.5121890473
471AcetylationPRTPVPSKYIRFIFN
CCCCCCHHHHHHHHH
38.3325953088
471UbiquitinationPRTPVPSKYIRFIFN
CCCCCCHHHHHHHHH
38.33-
472PhosphorylationRTPVPSKYIRFIFNR
CCCCCHHHHHHHHHH
11.15-
504PhosphorylationKFGAQNESLLPSILV
HCCCCCCCHHHHHHH
42.6323401153
508PhosphorylationQNESLLPSILVLLQR
CCCCHHHHHHHHHHH
28.6423401153
529PhosphorylationDEVRDRATFYLNVLQ
HHHHHHHHHHHHHHH
17.4426074081
531PhosphorylationVRDRATFYLNVLQQR
HHHHHHHHHHHHHHH
7.9426074081
545PhosphorylationRQMALNATYIFNGLT
HHHHHCCEEEECCEE
18.9726074081
546PhosphorylationQMALNATYIFNGLTV
HHHHCCEEEECCEEE
10.9126074081
552PhosphorylationTYIFNGLTVSVPGME
EEEECCEEEECCCHH
16.4826074081
554PhosphorylationIFNGLTVSVPGMEKA
EECCEEEECCCHHHH
19.8426074081
572UbiquitinationYTLEPSEKPFDMKSI
CCCCCCCCCCCCCCC
56.1521890473
572UbiquitinationYTLEPSEKPFDMKSI
CCCCCCCCCCCCCCC
56.1521890473
576SulfoxidationPSEKPFDMKSIPLAM
CCCCCCCCCCCCCCH
3.6230846556
583SulfoxidationMKSIPLAMAPVFEQK
CCCCCCCHHHHCCCC
5.9621406390
594PhosphorylationFEQKAEITLVATKPE
CCCCEEEEEEECCHH
13.49-
599UbiquitinationEITLVATKPEKLAPS
EEEEEECCHHHCCCC
41.25-
630PhosphorylationNIGPLFKSSEPVQLT
CCCCCCCCCCCEECC
32.3820068231
631PhosphorylationIGPLFKSSEPVQLTE
CCCCCCCCCCEECCH
46.6520068231
637PhosphorylationSSEPVQLTEAETEYF
CCCCEECCHHHHHHH
18.9620068231
641PhosphorylationVQLTEAETEYFVRCI
EECCHHHHHHHHHHH
42.9320068231
643PhosphorylationLTEAETEYFVRCIKH
CCHHHHHHHHHHHHH
18.1320068231
715PhosphorylationRLPDDDPTAVAGSFS
ECCCCCCCCCCEEEE
40.5321406692
720PhosphorylationDPTAVAGSFSCTMKF
CCCCCCEEEEEEEEE
12.3021406692
722PhosphorylationTAVAGSFSCTMKFTV
CCCCEEEEEEEEEEE
15.4621406692
724PhosphorylationVAGSFSCTMKFTVRD
CCEEEEEEEEEEEEC
23.3821406692
826PhosphorylationNKNSHSLYLAGIFRG
CCCCCCCHHHHHHHC
9.4925839225
835PhosphorylationAGIFRGGYDLLVRSR
HHHHHCCHHHHHHHH
13.27-
850PhosphorylationLALADGVTMQVTVRS
HHHCCCCEEEEEECC
13.8629759185
854PhosphorylationDGVTMQVTVRSKERT
CCCEEEEEECCCCCC
8.0329759185
857PhosphorylationTMQVTVRSKERTPVD
EEEEEECCCCCCCCE
34.2418491316

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 COPG2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPG2_HUMAN !!

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 COPG2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPA_HUMANCOPAphysical
14729954
COPB_HUMANCOPB1physical
14729954
COPB2_HUMANCOPB2physical
14729954
COPG2_HUMANCOPG2physical
14729954
COPD_HUMANARCN1physical
14729954
COPG1_HUMANCOPG1physical
22939629
COPZ1_HUMANCOPZ1physical
22939629
NDUB8_HUMANNDUFB8physical
22939629

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.
Regulatory Network of COPG2_HUMAN

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Related Literatures of Post-Translational Modification

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