COPE_HUMAN - dbPTM
COPE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPE_HUMAN
UniProt AC O14579
Protein Name Coatomer subunit epsilon
Gene Name COPE
Organism Homo sapiens (Human).
Sequence Length 308
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 side o
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. The 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 with 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 MAPPAPGPASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKLSSPERDVERDVFLYRAYLAQRKFGVVLDEIKPSSAPELQAVRMFADYLAHESRRDSIVAELDREMSRSVDVTNTTFLLMAASIYLHDQNPDAALRALHQGDSLECTAMTVQILLKLDRLDLARKELKRMQDLDEDATLTQLATAWVSLATGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHMAQGRWEAAEGLLQEALDKDSGYPETLVNLIVLSQHLGKPPEVTNRYLSQLKDAHRSHPFIKEYQAKENDFDRLVLQYAPSA
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
10PhosphorylationPPAPGPASGGSGEVD
CCCCCCCCCCCCCCC		46.9825159151
13PhosphorylationPGPASGGSGEVDELF
CCCCCCCCCCCCCHH		34.9925159151
23UbiquitinationVDELFDVKNAFYIGS
CCCHHCCCCCEEEEC		44.39-
23SumoylationVDELFDVKNAFYIGS
CCCHHCCCCCEEEEC		44.39-
30PhosphorylationKNAFYIGSYQQCINE
CCCEEEECHHHHHHH		15.3728348404
31PhosphorylationNAFYIGSYQQCINEA
CCEEEECHHHHHHHH		9.4427251275
42UbiquitinationINEAQRVKLSSPERD
HHHHHCCCCCCCCCH		44.86-
44PhosphorylationEAQRVKLSSPERDVE
HHHCCCCCCCCCHHH		37.8225159151
45PhosphorylationAQRVKLSSPERDVER
HHCCCCCCCCCHHHH		41.0125159151
52MethylationSPERDVERDVFLYRA
CCCCHHHHHHHHHHH		45.28-
57PhosphorylationVERDVFLYRAYLAQR
HHHHHHHHHHHHHHH		5.0323186163
65UbiquitinationRAYLAQRKFGVVLDE
HHHHHHHHHCEEECC		34.1021890473
65UbiquitinationRAYLAQRKFGVVLDE
HHHHHHHHHCEEECC		34.1021890473
65AcetylationRAYLAQRKFGVVLDE
HHHHHHHHHCEEECC		34.1025953088
65UbiquitinationRAYLAQRKFGVVLDE
HHHHHHHHHCEEECC		34.1021890473
65UbiquitinationRAYLAQRKFGVVLDE
HHHHHHHHHCEEECC		34.1021890473
74UbiquitinationGVVLDEIKPSSAPEL
CEEECCCCCCCCHHH		36.4821906983
86SulfoxidationPELQAVRMFADYLAH
HHHHHHHHHHHHHHH		2.3330846556
90PhosphorylationAVRMFADYLAHESRR
HHHHHHHHHHHHHHH		11.4523312004
95PhosphorylationADYLAHESRRDSIVA
HHHHHHHHHHHHHHH		23.8125849741
97 (in isoform 2)Phosphorylation-51.8420068231
98 (in isoform 2)Phosphorylation-41.4220068231
98PhosphorylationLAHESRRDSIVAELD
HHHHHHHHHHHHHHH		41.4227251275
99PhosphorylationAHESRRDSIVAELDR
HHHHHHHHHHHHHHH		19.7029255136
101PhosphorylationESRRDSIVAELDREM
HHHHHHHHHHHHHHH		3.8127251275
101 (in isoform 2)Phosphorylation-3.8120068231
108SulfoxidationVAELDREMSRSVDVT
HHHHHHHHHCCCCCC		4.1421406390
109PhosphorylationAELDREMSRSVDVTN
HHHHHHHHCCCCCCH		19.3623403867
151SulfoxidationDSLECTAMTVQILLK
CCHHHHHHHHHHHHH		1.7130846556
170UbiquitinationDLARKELKRMQDLDE
HHHHHHHHHCCCCCC		47.09-
172SulfoxidationARKELKRMQDLDEDA
HHHHHHHCCCCCCCH		3.3030846556
202PhosphorylationGEKLQDAYYIFQEMA
CCHHHHHHHHHHHHH		12.8425147952
203PhosphorylationEKLQDAYYIFQEMAD
CHHHHHHHHHHHHHH		9.29-
213UbiquitinationQEMADKCSPTLLLLN
HHHHHHCCCEEEECC		27.0221890473
214UbiquitinationEMADKCSPTLLLLNG
HHHHHCCCEEEECCC		36.2121890473
226UbiquitinationLNGQAACHMAQGRWE
CCCCHHHHHHHCCHH		15.1921890473
227UbiquitinationNGQAACHMAQGRWEA
CCCHHHHHHHCCHHH		2.7521890473
247PhosphorylationQEALDKDSGYPETLV
HHHHHCCCCCCHHHH		46.0620071362
260PhosphorylationLVNLIVLSQHLGKPP
HHHHHHHHHHCCCCH		12.5020071362
265UbiquitinationVLSQHLGKPPEVTNR
HHHHHCCCCHHHHHH		64.8521890473
265UbiquitinationVLSQHLGKPPEVTNR
HHHHHCCCCHHHHHH		64.8521890473
270PhosphorylationLGKPPEVTNRYLSQL
CCCCHHHHHHHHHHH		16.5920071362
275PhosphorylationEVTNRYLSQLKDAHR
HHHHHHHHHHHHHHH		25.2424719451
278UbiquitinationNRYLSQLKDAHRSHP
HHHHHHHHHHHHHCH		45.2721890473
278AcetylationNRYLSQLKDAHRSHP
HHHHHHHHHHHHHCH		45.2725953088
2782-HydroxyisobutyrylationNRYLSQLKDAHRSHP
HHHHHHHHHHHHHCH		45.27-
278UbiquitinationNRYLSQLKDAHRSHP
HHHHHHHHHHHHHCH		45.2721890473
283PhosphorylationQLKDAHRSHPFIKEY
HHHHHHHHCHHHHHH		26.1628555341
288UbiquitinationHRSHPFIKEYQAKEN
HHHCHHHHHHHHHCC		51.23-
293UbiquitinationFIKEYQAKENDFDRL
HHHHHHHHCCCHHHH		41.3421890473
299MethylationAKENDFDRLVLQYAP
HHCCCHHHHHHHHCC		27.04-
307PhosphorylationLVLQYAPSA------
HHHHHCCCC------		38.1430108239
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
-KUbiquitinationE3 ubiquitin ligaseRCHY1Q96PM5
PMID:17721809
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPE_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 COPE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPA_HUMANCOPAphysical
16169070
ZN363_HUMANRCHY1physical
17721809
TMEDA_HUMANTMED10physical
9751720
COPA_HUMANCOPAphysical
9482852
COPE_HUMANCOPEphysical
9482852
COPG1_HUMANCOPG1physical
22939629
COPG2_HUMANCOPG2physical
22939629
SEPT2_HUMANSEPT2physical
22863883
RBGP1_HUMANRABGAP1physical
22863883
EFHC2_HUMANEFHC2physical
25416956
COPA_HUMANCOPAphysical
26344197
COPG1_HUMANCOPG1physical
26344197
COPG2_HUMANCOPG2physical
26344197
DTBP1_HUMANDTNBP1physical
26344197
MCFD2_HUMANMCFD2physical
26344197
OSBL9_HUMANOSBPL9physical
26344197
PSD12_HUMANPSMD12physical
26344197
SF3B3_HUMANSF3B3physical
26344197
SF3B4_HUMANSF3B4physical
26344197
SF3B5_HUMANSF3B5physical
26344197
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 COPE_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-99, AND MASSSPECTROMETRY.

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