COPA_MOUSE - dbPTM
COPA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPA_MOUSE
UniProt AC Q8CIE6
Protein Name Coatomer subunit alpha
Gene Name Copa
Organism Mus musculus (Mouse).
Sequence Length 1224
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. 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).; Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity)..
Protein Sequence MLTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWDISGLRKKNLSPGAVESDVRGITGVDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKAWEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLFAAGHDGGMIVFKLERERPAYAVHGNMLHYVKDRFLRQLDFNSSKDVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRASNLENSTYDLYTIPKDADSQNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKIQVPNCDEIFYAGTGNLLLRDADSITLFDVQQKRTLASVKISKVKYVIWSADMSHVALLAKHAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHIKYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLSAATHGLDEEAESLKETFDPEKETIPDIDPNAKLLQPPAPIMPLDTNWPLLTVSKGFFEGSIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEDGFVEAPEGLGEDVLGKGQEEGGGWDVEEDLELPPELDVPSGVSGSAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQALPCLPSMYSYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQQLITICREYIVGLCMEIERKKLPKETLDQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLELGPKPEVAQQTRKILSACEKNPTDACQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGKDVIGLRISPLQFR
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
41S-palmitoylationQLWDYRMCTLIDKFD
ECCCHHHHHHHHHHC		1.7528526873
41S-nitrosocysteineQLWDYRMCTLIDKFD
ECCCHHHHHHHHHHC		1.75-
46UbiquitinationRMCTLIDKFDEHDGP
HHHHHHHHHCCCCCC		47.9622790023
46AcetylationRMCTLIDKFDEHDGP
HHHHHHHHHCCCCCC		47.9623806337
61UbiquitinationVRGIDFHKQQPLFVS
CCCEEECCCCCEEEE		51.0922790023
61AcetylationVRGIDFHKQQPLFVS
CCCEEECCCCCEEEE		51.0922826441
74UbiquitinationVSGGDDYKIKVWNYK
EECCCCCEEEEEHHH		42.9422790023
170UbiquitinationDISGLRKKNLSPGAV
ECCCCCCCCCCCCCC		57.6022790023
173PhosphorylationGLRKKNLSPGAVESD
CCCCCCCCCCCCCCC		30.5927087446
179PhosphorylationLSPGAVESDVRGITG
CCCCCCCCCCCCCCC		34.5028833060
185PhosphorylationESDVRGITGVDLFGT
CCCCCCCCCCCCCCC		33.7026745281
238UbiquitinationIWRMNESKAWEVDTC
EEEECCCCCEEEEEC		51.8722790023
244PhosphorylationSKAWEVDTCRGHYNN
CCCEEEEECCCCCCC		14.8525367039
245S-nitrosocysteineKAWEVDTCRGHYNNV
CCEEEEECCCCCCCE		4.20-
245S-palmitoylationKAWEVDTCRGHYNNV
CCEEEEECCCCCCCE		4.2028526873
249PhosphorylationVDTCRGHYNNVSCAV
EEECCCCCCCEEEEE		15.9717242355
254S-nitrosocysteineGHYNNVSCAVFHPRQ
CCCCCEEEEEECCCC		3.05-
254S-palmitoylationGHYNNVSCAVFHPRQ
CCCCCEEEEEECCCC		3.0528526873
271AcetylationILSNSEDKSIRVWDM
EECCCCCCCEEEEEC		43.6723954790
271MalonylationILSNSEDKSIRVWDM
EECCCCCCCEEEEEC		43.6726320211
271UbiquitinationILSNSEDKSIRVWDM
EECCCCCCCEEEEEC		43.67-
279PhosphorylationSIRVWDMSKRTGVQT
CEEEEECCCCCCCCE		19.2622817900
326PhosphorylationLERERPAYAVHGNML
EEECCCEEEEECCHH		16.3125293948
350UbiquitinationQLDFNSSKDVAVMQL
HCCCCCCCCEEEEEE		56.9222790023
362UbiquitinationMQLRSGSKFPVFNMS
EEECCCCCCCEEEEC		58.1622790023
380S-palmitoylationAENAVLLCTRASNLE
HHCEEEEEEEHHHCC		1.8028526873
398AcetylationYDLYTIPKDADSQNP
EEEEECCCCCCCCCC		62.7923954790
398UbiquitinationYDLYTIPKDADSQNP
EEEEECCCCCCCCCC		62.7922790023
402PhosphorylationTIPKDADSQNPDAPE
ECCCCCCCCCCCCCC		33.3125521595
411AcetylationNPDAPEGKRSSGLTA
CCCCCCCCCCCCCEE		47.662373583
434PhosphorylationAVLDRMHSLLIKNLK
HHHHHHHHHHHHHHH		18.6122942356
438AcetylationRMHSLLIKNLKNEIT
HHHHHHHHHHHHHHH		57.0822826441
441UbiquitinationSLLIKNLKNEITKKI
HHHHHHHHHHHHHCC		63.03-
441MalonylationSLLIKNLKNEITKKI
HHHHHHHHHHHHHCC		63.0326320211
446AcetylationNLKNEITKKIQVPNC
HHHHHHHHCCCCCCC		54.242373591
447UbiquitinationLKNEITKKIQVPNCD
HHHHHHHCCCCCCCC		29.7122790023
453S-palmitoylationKKIQVPNCDEIFYAG
HCCCCCCCCEEEEEC		3.9828526873
480UbiquitinationTLFDVQQKRTLASVK
EEEECCCCCCEEEEE		30.20-
480SuccinylationTLFDVQQKRTLASVK
EEEECCCCCCEEEEE		30.2023954790
480AcetylationTLFDVQQKRTLASVK
EEEECCCCCCEEEEE		30.2023236377
522S-nitrosocysteineNRKLDALCNIHENIR
CCHHHHHCCCCCCCE		4.88-
574UbiquitinationPIYVTRVKGNNVYCL
CEEEEEEECCEEEEE		53.26-
574MalonylationPIYVTRVKGNNVYCL
CEEEEEEECCEEEEE		53.2626320211
579PhosphorylationRVKGNNVYCLDRECR
EEECCEEEEECCCCC		6.8718563927
580S-palmitoylationVKGNNVYCLDRECRP
EECCEEEEECCCCCC		2.5128526873
591PhosphorylationECRPRVLTIDPTEFK
CCCCCEEEECCCHHH		22.0727180971
598AcetylationTIDPTEFKFKLALIN
EECCCHHHHHHHHHC		35.0423236377
598UbiquitinationTIDPTEFKFKLALIN
EECCCHHHHHHHHHC		35.0422790023
600AcetylationDPTEFKFKLALINRK
CCCHHHHHHHHHCCC		33.1822826441
600UbiquitinationDPTEFKFKLALINRK
CCCHHHHHHHHHCCC		33.1822790023
607AcetylationKLALINRKYDEVLHM
HHHHHCCCHHHHHHH		53.1922826441
619UbiquitinationLHMVRNAKLVGQSII
HHHHHCCHHHHHHHH		47.4522790023
631UbiquitinationSIIAYLQKKGYPEVA
HHHHHHHHCCCCCEE		45.6422790023
631AcetylationSIIAYLQKKGYPEVA
HHHHHHHHCCCCCEE		45.6422826441
643UbiquitinationEVALHFVKDEKTRFS
CEEEEEECCCCCCEE		60.26-
646UbiquitinationLHFVKDEKTRFSLAL
EEEECCCCCCEEEEE		55.95-
702UbiquitinationQRTKNFDKLSFLYLI
HHCCCCCHHHHHHHH		41.72-
715UbiquitinationLITGNLEKLRKMMKI
HHHCCHHHHHHHHHH		57.68-
727UbiquitinationMKIAEIRKDMSGHYQ
HHHHHHHHHCCCCCC		64.5422790023
750UbiquitinationSERVRILKNCGQKSL
HHHHHHHHHCCCHHH		48.0622790023
821PhosphorylationSKGFFEGSIASKGKG
ECCCCCCCHHCCCCC		14.0528833060
824PhosphorylationFFEGSIASKGKGGAL
CCCCCHHCCCCCCCE		40.0328833060
825UbiquitinationFEGSIASKGKGGALA
CCCCHHCCCCCCCEE		56.4722790023
914PhosphorylationFVPPTKGTSPTQIWC
ECCCCCCCCCCEEEE		32.8426643407
915PhosphorylationVPPTKGTSPTQIWCN
CCCCCCCCCCEEEEC		34.3226824392
917PhosphorylationPTKGTSPTQIWCNNS
CCCCCCCCEEEECCC		32.2423984901
924PhosphorylationTQIWCNNSQLPVDHI
CEEEECCCCCCCCCC		21.0726643407
935PhosphorylationVDHILAGSFETAMRL
CCCCCCCCHHHHHHH		17.8226643407
938PhosphorylationILAGSFETAMRLLHD
CCCCCHHHHHHHHHH		24.6026643407
965MethylationLFLQTYARGRTTYQA
HHHHHHCCCCCHHHC		25.39-
993UbiquitinationNWKDAGLKNGVPAVG
CHHHCCCCCCCCCHH		51.22-
993MalonylationNWKDAGLKNGVPAVG
CHHHCCCCCCCCCHH		51.2226320211
1013S-palmitoylationLIQRLQLCYQLTTVG
HHHHHHHHHHHHCCC		1.0028526873
1028UbiquitinationKFEEAVEKFRSILLS
CHHHHHHHHHHHHHH		39.2122790023
1028AcetylationKFEEAVEKFRSILLS
CHHHHHHHHHHHHHH		39.2122826441
1035PhosphorylationKFRSILLSVPLLVVD
HHHHHHHHCCEEEEC		20.4617203969
1057S-palmitoylationAQQLITICREYIVGL
HHHHHHHHHHHHHHH		1.7028526873
1075MalonylationIERKKLPKETLDQQK
HHHHCCCHHHHHHHH		74.0026320211
1082AcetylationKETLDQQKRICEMAA
HHHHHHHHHHHHHHH		37.792383475
1134MalonylationRLLELGPKPEVAQQT
HHHHHCCCHHHHHHH		52.6026320211
1134AcetylationRLLELGPKPEVAQQT
HHHHHCCCHHHHHHH		52.6023236377
1143MalonylationEVAQQTRKILSACEK
HHHHHHHHHHHHHHH		51.9226320211
1184AcetylationYRGKPVEKCPLSGAC
ECCCCCCCCCCCCCC		41.1922826441
1184UbiquitinationYRGKPVEKCPLSGAC
ECCCCCCCCCCCCCC		41.1922790023
1192PhosphorylationCPLSGACYSPEFKGQ
CCCCCCCCCCCCCCC		27.0828066266
1193PhosphorylationPLSGACYSPEFKGQI
CCCCCCCCCCCCCCE		20.1726745281
1211AcetylationTTVTEIGKDVIGLRI
EEEEECCCCEEEEEE		55.2622826441
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 COPA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPA_MOUSE !!
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 COPA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPE_HUMANCOPEphysical
20360068
ATLA2_HUMANATL2physical
20360068
COPZ1_HUMANCOPZ1physical
20360068
COPA_HUMANCOPAphysical
20360068
COPB2_HUMANCOPB2physical
20360068
ERGI2_HUMANERGIC2physical
20360068
SI1L3_HUMANSIPA1L3physical
20360068
COPG1_HUMANCOPG1physical
20360068
BAP31_HUMANBCAP31physical
20360068
COPB_HUMANCOPB1physical
20360068
COPD_HUMANARCN1physical
20360068
COPD_HUMANARCN1physical
26496610
COPB_HUMANCOPB1physical
26496610
BACD2_HUMANTNFAIP1physical
26496610
COPB2_HUMANCOPB2physical
26496610
BAP31_HUMANBCAP31physical
26496610
COPE_HUMANCOPEphysical
26496610
COPZ1_HUMANCOPZ1physical
26496610
COPG1_HUMANCOPG1physical
26496610
SI1L3_HUMANSIPA1L3physical
26496610
N4BP3_HUMANN4BP3physical
26496610
UBR4_HUMANUBR4physical
26496610
COPG2_HUMANCOPG2physical
26496610
BAP29_HUMANBCAP29physical
26496610
BACD3_HUMANKCTD10physical
26496610
LZTS2_HUMANLZTS2physical
26496610
TM263_HUMANTMEM263physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COPA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1035, AND MASSSPECTROMETRY.

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