COPA_HUMAN - dbPTM
COPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPA_HUMAN
UniProt AC P53621
Protein Name Coatomer subunit alpha
Gene Name COPA
Organism Homo sapiens (Human).
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..
Protein Sequence MLTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPTEDLVVSASLDQTVRVWDISGLRKKNLSPGAVESDVRGITGVDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKAWEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLFAAGHDGGMIVFKLERERPAYAVHGNMLHYVKDRFLRQLDFNSSKDVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRASNLENSTYDLYTIPKDADSQNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKVQVPNCDEIFYAGTGNLLLRDADSITLFDVQQKRTLASVKISKVKYVIWSADMSHVALLAKHAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHIKYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLTAATHGLDEEAESLKETFDPEKETIPDIDPNAKLLQPPAPIMPLDTNWPLLTVSKGFFEGTIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEDGFVEATEGLGDDALGKGQEEGGGWDVEEDLELPPELDISPGAAGGAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQALPCLPSMYGYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQQLITICREYIVGLSVETERKKLPKETLEQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLELGPKPEVAQQTRKILSACEKNPTDAYQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGKDVIGLRISPLQFR
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
4Acetylation----MLTKFETKSAR
----CCCCCCCCCCC		54.5627452117
4Ubiquitination----MLTKFETKSAR
----CCCCCCCCCCC		54.5629967540
8AcetylationMLTKFETKSARVKGL
CCCCCCCCCCCCCCC		34.6125953088
8UbiquitinationMLTKFETKSARVKGL
CCCCCCCCCCCCCCC		34.6133845483
13UbiquitinationETKSARVKGLSFHPK
CCCCCCCCCCCCCCC		48.8921906983
13 (in isoform 1)Ubiquitination-48.8921890473
13 (in isoform 2)Ubiquitination-48.8921890473
16PhosphorylationSARVKGLSFHPKRPW
CCCCCCCCCCCCCCE		30.12-
46AcetylationRMCTLIDKFDEHDGP
HHHHHHHHHCCCCCC		47.9625825284
46MalonylationRMCTLIDKFDEHDGP
HHHHHHHHHCCCCCC		47.9626320211
46UbiquitinationRMCTLIDKFDEHDGP
HHHHHHHHHCCCCCC		47.9624816145
61UbiquitinationVRGIDFHKQQPLFVS
CCCEEECCCCCEEEE		51.0923000965
61 (in isoform 1)Ubiquitination-51.0921890473
61 (in isoform 2)Ubiquitination-51.0921890473
68PhosphorylationKQQPLFVSGGDDYKI
CCCCEEEECCCCCEE		29.7130619164
73PhosphorylationFVSGGDDYKIKVWNY
EEECCCCCEEEEEHH		21.2530619164
74AcetylationVSGGDDYKIKVWNYK
EECCCCCEEEEEHHH		42.9468897
74UbiquitinationVSGGDDYKIKVWNYK
EECCCCCEEEEEHHH		42.9429967540
76UbiquitinationGGDDYKIKVWNYKLR
CCCCCEEEEEHHHHH		36.7323000965
80PhosphorylationYKIKVWNYKLRRCLF
CEEEEEHHHHHHHHH		8.83-
81UbiquitinationKIKVWNYKLRRCLFT
EEEEEHHHHHHHHHH		32.1023000965
81 (in isoform 1)Ubiquitination-32.1021890473
81 (in isoform 2)Ubiquitination-32.1021890473
95PhosphorylationTLLGHLDYIRTTFFH
HHHHCHHHHHHHCCC		9.92-
165PhosphorylationTVRVWDISGLRKKNL
EEEEEECCCCCCCCC		29.3324719451
169UbiquitinationWDISGLRKKNLSPGA
EECCCCCCCCCCCCC		51.5623000965
170UbiquitinationDISGLRKKNLSPGAV
ECCCCCCCCCCCCCC		57.6023000965
170 (in isoform 1)Ubiquitination-57.6021890473
170 (in isoform 2)Ubiquitination-57.6021890473
173PhosphorylationGLRKKNLSPGAVESD
CCCCCCCCCCCCCCC		30.5919664994
173 (in isoform 2)Phosphorylation-30.5924719451
179PhosphorylationLSPGAVESDVRGITG
CCCCCCCCCCCCCCC		34.5023927012
179 (in isoform 2)Phosphorylation-34.5024719451
182MethylationGAVESDVRGITGVDL
CCCCCCCCCCCCCCC		35.47-
185PhosphorylationESDVRGITGVDLFGT
CCCCCCCCCCCCCCC		33.7022199227
185 (in isoform 2)Phosphorylation-33.7027251275
192PhosphorylationTGVDLFGTTDAVVKH
CCCCCCCCCHHHHHH		17.7324719451
192 (in isoform 2)Phosphorylation-17.7324719451
193PhosphorylationGVDLFGTTDAVVKHV
CCCCCCCCHHHHHHH		23.4922199227
193 (in isoform 2)Phosphorylation-23.4924719451
198UbiquitinationGTTDAVVKHVLEGHD
CCCHHHHHHHHCCCC		22.7721963094
206MethylationHVLEGHDRGVNWAAF
HHHCCCCCCCCHHHC		45.33-
217SulfoxidationWAAFHPTMPLIVSGA
HHHCCCCCCEEEECC		2.7530846556
222PhosphorylationPTMPLIVSGADDRQV
CCCCEEEECCCHHHE		22.67-
230UbiquitinationGADDRQVKIWRMNES
CCCHHHEEEEEECCC		28.36-
238AcetylationIWRMNESKAWEVDTC
EEEECCCCCEEEEEC		51.8726051181
238UbiquitinationIWRMNESKAWEVDTC
EEEECCCCCEEEEEC		51.8723000965
238 (in isoform 1)Ubiquitination-51.8721890473
238 (in isoform 2)Ubiquitination-51.8721890473
244PhosphorylationSKAWEVDTCRGHYNN
CCCEEEEECCCCCCC		14.85-
245S-nitrosocysteineKAWEVDTCRGHYNNV
CCEEEEECCCCCCCE		4.20-
245S-nitrosylationKAWEVDTCRGHYNNV
CCEEEEECCCCCCCE		4.2022178444
246MethylationAWEVDTCRGHYNNVS
CEEEEECCCCCCCEE		36.70-
249PhosphorylationVDTCRGHYNNVSCAV
EEECCCCCCCEEEEE		15.9727155012
249 (in isoform 2)Phosphorylation-15.9727251275
253PhosphorylationRGHYNNVSCAVFHPR
CCCCCCEEEEEECCC		9.8528152594
266PhosphorylationPRQELILSNSEDKSI
CCCEEEECCCCCCCE		31.17-
271AcetylationILSNSEDKSIRVWDM
EECCCCCCCEEEEEC		43.6723749302
271UbiquitinationILSNSEDKSIRVWDM
EECCCCCCCEEEEEC		43.6723000965
271 (in isoform 1)Ubiquitination-43.6721890473
271 (in isoform 2)Ubiquitination-43.6721890473
272PhosphorylationLSNSEDKSIRVWDMS
ECCCCCCCEEEEECC		28.1328985074
279PhosphorylationSIRVWDMSKRTGVQT
CEEEEECCCCCCCCE		19.2628857561
280AcetylationIRVWDMSKRTGVQTF
EEEEECCCCCCCCEE		47.5525953088
280UbiquitinationIRVWDMSKRTGVQTF
EEEEECCCCCCCCEE		47.55-
286PhosphorylationSKRTGVQTFRRDHDR
CCCCCCCEEECCCCC		19.3927251275
286 (in isoform 2)Phosphorylation-19.3927251275
332SulfoxidationAYAVHGNMLHYVKDR
EEEEECCHHHHHHHH		2.6330846556
337UbiquitinationGNMLHYVKDRFLRQL
CCHHHHHHHHHHHHC		35.7021906983
337 (in isoform 1)Ubiquitination-35.7021890473
337 (in isoform 2)Ubiquitination-35.7021890473
348PhosphorylationLRQLDFNSSKDVAVM
HHHCCCCCCCCEEEE		38.4620873877
349PhosphorylationRQLDFNSSKDVAVMQ
HHCCCCCCCCEEEEE		33.7020873877
350UbiquitinationQLDFNSSKDVAVMQL
HCCCCCCCCEEEEEE		56.9221906983
350 (in isoform 1)Ubiquitination-56.9221890473
350 (in isoform 2)Ubiquitination-56.9221890473
355SulfoxidationSSKDVAVMQLRSGSK
CCCCEEEEEECCCCC		1.9321406390
358MethylationDVAVMQLRSGSKFPV
CEEEEEECCCCCCCE		23.29-
359PhosphorylationVAVMQLRSGSKFPVF
EEEEEECCCCCCCEE		56.8828857561
361PhosphorylationVMQLRSGSKFPVFNM
EEEECCCCCCCEEEE		32.1628857561
362UbiquitinationMQLRSGSKFPVFNMS
EEECCCCCCCEEEEC		58.1621906983
362 (in isoform 1)Ubiquitination-58.1621890473
362 (in isoform 2)Ubiquitination-58.1621890473
368SulfoxidationSKFPVFNMSYNPAEN
CCCCEEEECCCHHHC		2.8230846556
370PhosphorylationFPVFNMSYNPAENAV
CCEEEECCCHHHCEE		17.88-
389PhosphorylationRASNLENSTYDLYTI
EHHHCCCCEEEEEEC		20.9729214152
390PhosphorylationASNLENSTYDLYTIP
HHHCCCCEEEEEECC		32.4128152594
390 (in isoform 2)Phosphorylation-32.4127251275
391PhosphorylationSNLENSTYDLYTIPK
HHCCCCEEEEEECCC		12.0828796482
394PhosphorylationENSTYDLYTIPKDAD
CCCEEEEEECCCCCC		10.3428796482
394 (in isoform 2)Phosphorylation-10.3427642862
395PhosphorylationNSTYDLYTIPKDADS
CCEEEEEECCCCCCC		37.7928796482
398UbiquitinationYDLYTIPKDADSQNP
EEEEECCCCCCCCCC		62.7921906983
398 (in isoform 1)Ubiquitination-62.7921890473
398 (in isoform 2)Ubiquitination-62.7921890473
402PhosphorylationTIPKDADSQNPDAPE
ECCCCCCCCCCCCCC		33.3123401153
402 (in isoform 2)Phosphorylation-33.3124719451
411AcetylationNPDAPEGKRSSGLTA
CCCCCCCCCCCCCEE		47.6626051181
411UbiquitinationNPDAPEGKRSSGLTA
CCCCCCCCCCCCCEE		47.6621906983
411 (in isoform 1)Ubiquitination-47.6621890473
411 (in isoform 2)Ubiquitination-47.6621890473
413PhosphorylationDAPEGKRSSGLTAVW
CCCCCCCCCCCEEEE		32.0423312004
413 (in isoform 2)Phosphorylation-32.0424719451
414PhosphorylationAPEGKRSSGLTAVWV
CCCCCCCCCCEEEEE		41.6828348404
414 (in isoform 2)Phosphorylation-41.6827251275
417PhosphorylationGKRSSGLTAVWVARN
CCCCCCCEEEEEECC		23.7723312004
423MethylationLTAVWVARNRFAVLD
CEEEEEECCHHHHHH		25.82-
434PhosphorylationAVLDRMHSLLIKNLK
HHHHHHHHHHHHHHH		18.6128450419
434 (in isoform 2)Phosphorylation-18.6124719451
438UbiquitinationRMHSLLIKNLKNEIT
HHHHHHHHHHHHHHH		57.0823000965
438 (in isoform 1)Ubiquitination-57.0821890473
438 (in isoform 2)Ubiquitination-57.0821890473
441AcetylationSLLIKNLKNEITKKV
HHHHHHHHHHHHHCC		63.0325953088
441MalonylationSLLIKNLKNEITKKV
HHHHHHHHHHHHHCC		63.0326320211
441UbiquitinationSLLIKNLKNEITKKV
HHHHHHHHHHHHHCC		63.0323000965
441 (in isoform 1)Ubiquitination-63.0321890473
441 (in isoform 2)Ubiquitination-63.0321890473
446UbiquitinationNLKNEITKKVQVPNC
HHHHHHHHCCCCCCC		57.5221906983
446 (in isoform 1)Ubiquitination-57.5221890473
446 (in isoform 2)Ubiquitination-57.5221890473
447MalonylationLKNEITKKVQVPNCD
HHHHHHHCCCCCCCC		29.2926320211
447UbiquitinationLKNEITKKVQVPNCD
HHHHHHHCCCCCCCC		29.2922053931
458PhosphorylationPNCDEIFYAGTGNLL
CCCCEEEEECCCCEE		15.13-
471PhosphorylationLLLRDADSITLFDVQ
EEEECCCEEEEEECC		21.1320873877
473PhosphorylationLRDADSITLFDVQQK
EECCCEEEEEECCCC		25.8920873877
480AcetylationTLFDVQQKRTLASVK
EEEECCCCCCEEEEE		30.2025953088
480UbiquitinationTLFDVQQKRTLASVK
EEEECCCCCCEEEEE		30.2027667366
480 (in isoform 1)Ubiquitination-30.2021890473
480 (in isoform 2)Ubiquitination-30.2021890473
487UbiquitinationKRTLASVKISKVKYV
CCCEEEEEECCCEEE		38.4729967540
489O-linked_GlycosylationTLASVKISKVKYVIW
CEEEEEECCCEEEEE		26.1928411811
497PhosphorylationKVKYVIWSADMSHVA
CCEEEEECCCHHHHH		11.85-
501PhosphorylationVIWSADMSHVALLAK
EEECCCHHHHHHHHH		18.50-
517UbiquitinationAIVICNRKLDALCNI
HHEECCCHHHHHCCC		36.4121906983
517 (in isoform 1)Ubiquitination-36.4121890473
526UbiquitinationDALCNIHENIRVKSG
HHHCCCCCCCEECCC		51.0224816145
526 (in isoform 2)Ubiquitination-51.0221890473
531UbiquitinationIHENIRVKSGAWDES
CCCCCEECCCCCCCC		33.07-
551PhosphorylationTTSNHIKYAVTTGDH
ECCCCEEEEEECCCC		13.0028152594
554PhosphorylationNHIKYAVTTGDHGII
CCEEEEEECCCCCEE		19.5228152594
563PhosphorylationGDHGIIRTLDLPIYV
CCCCEEEECCCCEEE		17.7625690035
569PhosphorylationRTLDLPIYVTRVKGN
EECCCCEEEEEEECC		8.2028152594
571PhosphorylationLDLPIYVTRVKGNNV
CCCCEEEEEEECCEE		16.8728152594
574MalonylationPIYVTRVKGNNVYCL
CEEEEEEECCEEEEE		53.2626320211
574UbiquitinationPIYVTRVKGNNVYCL
CEEEEEEECCEEEEE		53.2621963094
574 (in isoform 1)Ubiquitination-53.2621890473
579PhosphorylationRVKGNNVYCLDRECR
EEECCEEEEECCCCC		6.8728152594
583UbiquitinationNNVYCLDRECRPRVL
CEEEEECCCCCCCEE		31.7821963094
583 (in isoform 2)Ubiquitination-31.7821890473
588 (in isoform 2)Phosphorylation-19.4125147952
591PhosphorylationECRPRVLTIDPTEFK
CCCCCEEEECCCHHH		22.0719664994
595PhosphorylationRVLTIDPTEFKFKLA
CEEEECCCHHHHHHH		50.7530266825
598AcetylationTIDPTEFKFKLALIN
EECCCHHHHHHHHHC		35.0425953088
598UbiquitinationTIDPTEFKFKLALIN
EECCCHHHHHHHHHC		35.0423000965
598 (in isoform 1)Ubiquitination-35.0421890473
600UbiquitinationDPTEFKFKLALINRK
CCCHHHHHHHHHCCC		33.1823000965
600 (in isoform 1)Ubiquitination-33.1821890473
600 (in isoform 2)Phosphorylation-33.1824719451
607MalonylationKLALINRKYDEVLHM
HHHHHCCCHHHHHHH		53.1926320211
607UbiquitinationKLALINRKYDEVLHM
HHHHHCCCHHHHHHH		53.1923000965
607 (in isoform 2)Ubiquitination-53.1921890473
609UbiquitinationALINRKYDEVLHMVR
HHHCCCHHHHHHHHH		42.4323000965
609 (in isoform 2)Ubiquitination-42.4321890473
614SulfoxidationKYDEVLHMVRNAKLV
CHHHHHHHHHCCHHH		2.3730846556
616UbiquitinationDEVLHMVRNAKLVGQ
HHHHHHHHCCHHHHH		29.7933845483
617 (in isoform 2)Phosphorylation-29.9827642862
619AcetylationLHMVRNAKLVGQSII
HHHHHCCHHHHHHHH		47.4525953088
619UbiquitinationLHMVRNAKLVGQSII
HHHHHCCHHHHHHHH		47.4521906983
619 (in isoform 1)Ubiquitination-47.4521890473
624PhosphorylationNAKLVGQSIIAYLQK
CCHHHHHHHHHHHHH		15.2728152594
628PhosphorylationVGQSIIAYLQKKGYP
HHHHHHHHHHHCCCC		10.1528152594
628UbiquitinationVGQSIIAYLQKKGYP
HHHHHHHHHHHCCCC		10.1533845483
628 (in isoform 2)Ubiquitination-10.1521890473
631UbiquitinationSIIAYLQKKGYPEVA
HHHHHHHHCCCCCEE		45.6421963094
631 (in isoform 1)Ubiquitination-45.6421890473
632UbiquitinationIIAYLQKKGYPEVAL
HHHHHHHCCCCCEEE		51.2033845483
640UbiquitinationGYPEVALHFVKDEKT
CCCCEEEEEECCCCC		18.7321963094
640 (in isoform 2)Ubiquitination-18.7321890473
641UbiquitinationYPEVALHFVKDEKTR
CCCEEEEEECCCCCC		8.3233845483
643AcetylationEVALHFVKDEKTRFS
CEEEEEECCCCCCEE		60.2626051181
643UbiquitinationEVALHFVKDEKTRFS
CEEEEEECCCCCCEE		60.2632015554
652UbiquitinationEKTRFSLALECGNIE
CCCCEEEEEECCCHH		10.5032015554
671AcetylationAAKALDDKNCWEKLG
HHHHCCCCCHHHHHH		54.3926822725
671UbiquitinationAAKALDDKNCWEKLG
HHHHCCCCCHHHHHH		54.3929967540
676UbiquitinationDDKNCWEKLGEVALL
CCCCHHHHHHHHHHH		36.9729967540
680UbiquitinationCWEKLGEVALLQGNH
HHHHHHHHHHHCCCH		4.2829967540
685UbiquitinationGEVALLQGNHQIVEM
HHHHHHCCCHHHHHH		33.2929967540
692SulfoxidationGNHQIVEMCYQRTKN
CCHHHHHHHHHHCCC		1.4630846556
698UbiquitinationEMCYQRTKNFDKLSF
HHHHHHCCCCCHHHH		58.786983
698 (in isoform 1)Ubiquitination-58.7821890473
702UbiquitinationQRTKNFDKLSFLYLI
HHCCCCCHHHHHHHH		41.72-
707UbiquitinationFDKLSFLYLITGNLE
CCHHHHHHHHHCCHH		8.2727667366
707 (in isoform 2)Ubiquitination-8.2721890473
715UbiquitinationLITGNLEKLRKMMKI
HHHCCHHHHHHHHHH		57.6821906983
715 (in isoform 1)Ubiquitination-57.6821890473
721AcetylationEKLRKMMKIAEIRKD
HHHHHHHHHHHHHHH		34.9525953088
721UbiquitinationEKLRKMMKIAEIRKD
HHHHHHHHHHHHHHH		34.9523000965
721 (in isoform 1)Ubiquitination-34.9521890473
724 (in isoform 2)Ubiquitination-46.9621890473
727UbiquitinationMKIAEIRKDMSGHYQ
HHHHHHHHHCCCCCC		64.5423000965
727 (in isoform 1)Ubiquitination-64.5421890473
729SulfoxidationIAEIRKDMSGHYQNA
HHHHHHHCCCCCCCC		6.0830846556
730PhosphorylationAEIRKDMSGHYQNAL
HHHHHHCCCCCCCCE		32.3327080861
730UbiquitinationAEIRKDMSGHYQNAL
HHHHHHCCCCCCCCE		32.3323000965
730 (in isoform 2)Ubiquitination-32.3321890473
733PhosphorylationRKDMSGHYQNALYLG
HHHCCCCCCCCEECC		13.6417360941
736UbiquitinationMSGHYQNALYLGDVS
CCCCCCCCEECCCHH		5.0923000965
736 (in isoform 2)Ubiquitination-5.0921890473
738PhosphorylationGHYQNALYLGDVSER
CCCCCCEECCCHHHH		13.2627080861
739 (in isoform 2)Phosphorylation-4.9927251275
743PhosphorylationALYLGDVSERVRILK
CEECCCHHHHHHHHH		25.1527080861
750AcetylationSERVRILKNCGQKSL
HHHHHHHHHCCCHHH		48.0625953088
750UbiquitinationSERVRILKNCGQKSL
HHHHHHHHHCCCHHH		48.0633845483
755UbiquitinationILKNCGQKSLAYLTA
HHHHCCCHHHHHHHH		32.4932015554
756PhosphorylationLKNCGQKSLAYLTAA
HHHCCCHHHHHHHHH		15.4528348404
759UbiquitinationCGQKSLAYLTAATHG
CCCHHHHHHHHHHHC		15.1833845483
764UbiquitinationLAYLTAATHGLDEEA
HHHHHHHHHCCHHHH		17.6332015554
765 (in isoform 2)Phosphorylation-30.0527251275
773PhosphorylationGLDEEAESLKETFDP
CCHHHHHHHHHHCCC		52.3628348404
775UbiquitinationDEEAESLKETFDPEK
HHHHHHHHHHCCCCC		65.0821963094
777PhosphorylationEAESLKETFDPEKET
HHHHHHHHCCCCCCC		31.5827251275
782UbiquitinationKETFDPEKETIPDID
HHHCCCCCCCCCCCC		66.6021963094
782 (in isoform 2)Phosphorylation-66.6027251275
784UbiquitinationTFDPEKETIPDIDPN
HCCCCCCCCCCCCCC		49.2121963094
791UbiquitinationTIPDIDPNAKLLQPP
CCCCCCCCCCCCCCC		46.0621963094
793UbiquitinationPDIDPNAKLLQPPAP
CCCCCCCCCCCCCCC		57.2729967540
802SulfoxidationLQPPAPIMPLDTNWP
CCCCCCCCCCCCCCC		2.3428183972
802UbiquitinationLQPPAPIMPLDTNWP
CCCCCCCCCCCCCCC		2.3429967540
812PhosphorylationDTNWPLLTVSKGFFE
CCCCCEEEEECCCCE		30.3428348404
814PhosphorylationNWPLLTVSKGFFEGT
CCCEEEEECCCCEEE		23.0928348404
815UbiquitinationWPLLTVSKGFFEGTI
CCEEEEECCCCEEEE		56.24-
821O-linked_GlycosylationSKGFFEGTIASKGKG
ECCCCEEEEECCCCC		13.2328411811
821PhosphorylationSKGFFEGTIASKGKG
ECCCCEEEEECCCCC		13.2320873877
823 (in isoform 2)Phosphorylation-12.6727251275
824PhosphorylationFFEGTIASKGKGGAL
CCEEEEECCCCCCEE		37.7825850435
825AcetylationFEGTIASKGKGGALA
CEEEEECCCCCCEEE		56.4725953088
825UbiquitinationFEGTIASKGKGGALA
CEEEEECCCCCCEEE		56.4721906983
825 (in isoform 1)Ubiquitination-56.4721890473
827UbiquitinationGTIASKGKGGALAAD
EEEECCCCCCEEEEE		58.8923503661
830 (in isoform 2)Phosphorylation-11.6027251275
833 (in isoform 2)Phosphorylation-18.3624719451
834UbiquitinationKGGALAADIDIDTVG
CCCEEEEEEECCCCC		33.2221963094
834 (in isoform 2)Ubiquitination-33.2221890473
836UbiquitinationGALAADIDIDTVGTE
CEEEEEEECCCCCCC		33.0023503661
895PhosphorylationLPPELDISPGAAGGA
CCCCCCCCCCCCCCC		19.5625159151
904 (in isoform 2)Phosphorylation-59.6827251275
911PhosphorylationDGFFVPPTKGTSPTQ
CCCCCCCCCCCCCCE		35.7220068231
914PhosphorylationFVPPTKGTSPTQIWC
CCCCCCCCCCCEEEE		32.8423663014
915PhosphorylationVPPTKGTSPTQIWCN
CCCCCCCCCCEEEEC		34.3223663014
917PhosphorylationPTKGTSPTQIWCNNS
CCCCCCCCEEEECCC		32.2423663014
923 (in isoform 2)Phosphorylation-28.1727251275
924 (in isoform 2)Phosphorylation-21.0724719451
955PhosphorylationGVIQFGPYKQLFLQT
CEEEECCCHHHHHHH		16.2526074081
956AcetylationVIQFGPYKQLFLQTY
EEEECCCHHHHHHHH		43.5924847213
962PhosphorylationYKQLFLQTYARGRTT
CHHHHHHHHCCCCCH		22.6926074081
963PhosphorylationKQLFLQTYARGRTTY
HHHHHHHHCCCCCHH		4.9526074081
965MethylationLFLQTYARGRTTYQA
HHHHHHCCCCCHHHH		25.3924129315
978PhosphorylationQALPCLPSMYGYPNR
HHCCCCHHHHCCCCC		16.2229759185
980PhosphorylationLPCLPSMYGYPNRNW
CCCCHHHHCCCCCCH		20.1828985074
982PhosphorylationCLPSMYGYPNRNWKD
CCHHHHCCCCCCHHH		4.6529759185
988SuccinylationGYPNRNWKDAGLKNG
CCCCCCHHHCCCCCC		41.0523954790
988UbiquitinationGYPNRNWKDAGLKNG
CCCCCCHHHCCCCCC		41.0527667366
993MalonylationNWKDAGLKNGVPAVG
CHHHCCCCCCCCCHH		51.2226320211
993UbiquitinationNWKDAGLKNGVPAVG
CHHHCCCCCCCCCHH		51.2232015554
997UbiquitinationAGLKNGVPAVGLKLN
CCCCCCCCCHHHCHH		23.7227667366
1002UbiquitinationGVPAVGLKLNDLIQR
CCCCHHHCHHHHHHH		39.0432015554
1028AcetylationKFEEAVEKFRSILLS
CHHHHHHHHHHHHHH		39.2127452117
1028UbiquitinationKFEEAVEKFRSILLS
CHHHHHHHHHHHHHH		39.2122817900
1028 (in isoform 1)Ubiquitination-39.2121890473
1035PhosphorylationKFRSILLSVPLLVVD
HHHHHHHHCCEEEEC		20.4621082442
1037UbiquitinationRSILLSVPLLVVDNK
HHHHHHCCEEEECCH		19.3233845483
1037 (in isoform 2)Ubiquitination-19.3221890473
1072UbiquitinationSVETERKKLPKETLE
CHHHHHHCCCHHHHH		76.0129967540
1075UbiquitinationTERKKLPKETLEQQK
HHHHCCCHHHHHHHH		74.0024816145
1081UbiquitinationPKETLEQQKRICEMA
CHHHHHHHHHHHHHH		27.8529967540
1084UbiquitinationTLEQQKRICEMAAYF
HHHHHHHHHHHHHHH		2.7624816145
1119AcetylationFFKLKNFKTAATFAR
HHHCCCHHHHHHHHH		46.8025953088
1119UbiquitinationFFKLKNFKTAATFAR
HHHCCCHHHHHHHHH		46.8029967540
1128UbiquitinationAATFARRLLELGPKP
HHHHHHHHHHHCCCH		3.4829967540
1134AcetylationRLLELGPKPEVAQQT
HHHHHCCCHHHHHHH		52.6026051181
1134MalonylationRLLELGPKPEVAQQT
HHHHHCCCHHHHHHH		52.6026320211
1134UbiquitinationRLLELGPKPEVAQQT
HHHHHCCCHHHHHHH		52.6024816145
1141PhosphorylationKPEVAQQTRKILSAC
CHHHHHHHHHHHHHH		23.1128857561
1143MalonylationEVAQQTRKILSACEK
HHHHHHHHHHHHHHH		51.9226320211
1143UbiquitinationEVAQQTRKILSACEK
HHHHHHHHHHHHHHH		51.9224816145
1146PhosphorylationQQTRKILSACEKNPT
HHHHHHHHHHHHCCC		34.0522673903
1150AcetylationKILSACEKNPTDAYQ
HHHHHHHHCCCCCHH		69.0225953088
1150UbiquitinationKILSACEKNPTDAYQ
HHHHHHHHCCCCCHH		69.0221963094
1152UbiquitinationLSACEKNPTDAYQLN
HHHHHHCCCCCHHCC		42.6029967540
1159UbiquitinationPTDAYQLNYDMHNPF
CCCCHHCCCCCCCCH		18.4221963094
1162SulfoxidationAYQLNYDMHNPFDIC
CHHCCCCCCCCHHHE		2.0230846556
1180UbiquitinationYRPIYRGKPVEKCPL
CCCEECCCCCCCCCC		36.5729967540
1184UbiquitinationYRGKPVEKCPLSGAC
ECCCCCCCCCCCCCC		41.1929967540
1188PhosphorylationPVEKCPLSGACYSPE
CCCCCCCCCCCCCCC		14.9728152594
1189UbiquitinationVEKCPLSGACYSPEF
CCCCCCCCCCCCCCC		27.6129967540
1192PhosphorylationCPLSGACYSPEFKGQ
CCCCCCCCCCCCCCC		27.0828152594
1193PhosphorylationPLSGACYSPEFKGQI
CCCCCCCCCCCCCCE		20.1725159151
1193UbiquitinationPLSGACYSPEFKGQI
CCCCCCCCCCCCCCE		20.1729967540
1197AcetylationACYSPEFKGQICRVT
CCCCCCCCCCEEEEE		48.5226051181
1197UbiquitinationACYSPEFKGQICRVT
CCCCCCCCCCEEEEE		48.5221963094
1202 (in isoform 2)Phosphorylation-30.3724719451
1204PhosphorylationKGQICRVTTVTEIGK
CCCEEEEEEEEECCC		9.01-
1205PhosphorylationGQICRVTTVTEIGKD
CCEEEEEEEEECCCC		23.6728857561
1206UbiquitinationQICRVTTVTEIGKDV
CEEEEEEEEECCCCE		3.1021963094
1207PhosphorylationICRVTTVTEIGKDVI
EEEEEEEEECCCCEE		21.57-
1211AcetylationTTVTEIGKDVIGLRI
EEEEECCCCEEEEEE		55.2626051181
1211UbiquitinationTTVTEIGKDVIGLRI
EEEEECCCCEEEEEE		55.2624816145
1217MethylationGKDVIGLRISPLQFR
CCCEEEEEECCCCCC		23.33-
1219PhosphorylationDVIGLRISPLQFR--
CEEEEEECCCCCC--		17.0828348404
1220UbiquitinationVIGLRISPLQFR---
EEEEEECCCCCC---		28.0124816145
1228 (in isoform 2)Phosphorylation-27251275
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPA_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 COPA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPE_HUMANCOPEphysical
10921873
COPB_HUMANCOPB1physical
10921873
ARFG1_HUMANARFGAP1physical
12379802
PGFRB_HUMANPDGFRBphysical
9207175
COPE_HUMANCOPEphysical
8858162
SMN_HUMANSMN1physical
21300694
GEMI2_HUMANGEMIN2physical
21300694
DDX20_HUMANDDX20physical
21300694
TMEDA_HUMANTMED10physical
9751720
COPA_HUMANCOPAphysical
9751720
COPB_HUMANCOPB1physical
9751720
COPB2_HUMANCOPB2physical
9751720
COPG1_HUMANCOPG1physical
9751720
COPD_HUMANARCN1physical
9751720
COPE_HUMANCOPEphysical
9751720
COPZ1_HUMANCOPZ1physical
9751720
COPA_HUMANCOPAphysical
9482852
COPB2_HUMANCOPB2physical
9482852
COPE_HUMANCOPEphysical
9482852
COPB2_HUMANCOPB2physical
22939629
COPE_HUMANCOPEphysical
22939629
COPB_HUMANCOPB1physical
22939629
COPD_HUMANARCN1physical
22939629
COPG1_HUMANCOPG1physical
22939629
COPG2_HUMANCOPG2physical
22939629
COPZ1_HUMANCOPZ1physical
22939629
SC24C_HUMANSEC24Cphysical
22939629
SC23A_HUMANSEC23Aphysical
22939629
SEPT9_HUMANSEPT9physical
22939629
COPD_HUMANARCN1physical
22863883
TCPG_HUMANCCT3physical
22863883
COPZ1_HUMANCOPZ1physical
22863883
TCPA_HUMANTCP1physical
22863883
CCD97_HUMANCCDC97physical
26344197
SF3B3_HUMANSF3B3physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616414Autoimmune interstitial lung, joint, and kidney disease (AILJK)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COPA_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-173, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, 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-173 AND SER-402, ANDMASS SPECTROMETRY.
"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-173 AND SER-895, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND MASSSPECTROMETRY.

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