UniProt Accession

 COPA_HUMAN; P53621; Q5T201; Q8IXZ9 

Genbank Protein ID

 U24105; AL513282; AL445230; AL513282; AL445230; AL445230; AL513282; AL445230; AL513282; CH471121; CH471121; BC038447 

Genbank Nucleotide ID

 AAB70879.1; CAI12454.1; CAI12454.1; CAI12455.1; CAI12455.1; CAI15004.1; CAI15004.1; CAI15005.1; CAI15005.1; EAW52723.1; EAW52725.1; AAH38447.1 

Protein Name

 Coatomer subunit alpha 

Protein Synonyms/Alias

 Alpha-coat protein; Alpha-COP; HEP-COP; HEPCOP; Xenin; Xenopsin-related peptide; Proxenin 

Gene Name

 COPA 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
4	****MLTKFETKSAR	ubiquitination	[1]
8	MLTKFETKSARVKGL	ubiquitination	[2]
13	ETKSARVKGLSFHPK	ubiquitination	[1, 2, 3]
46	RMCTLIDKFDEHDGP	ubiquitination	[1, 3]
61	VRGIDFHKQQPLFVS	ubiquitination	[1, 2, 3, 4]
81	KIKVWNYKLRRCLFT	ubiquitination	[4]
169	WDISGLRKKNLSPGA	ubiquitination	[1, 3]
170	DISGLRKKNLSPGAV	ubiquitination	[1, 2, 3, 4]
198	GTTDAVVKHVLEGHD	ubiquitination	[1, 5]
230	GADDRQVKIWRMNES	ubiquitination	[1]
238	IWRMNESKAWEVDTC	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
271	ILSNSEDKSIRVWDM	acetylation	[3, 8]
271	ILSNSEDKSIRVWDM	ubiquitination	[1, 2, 3, 4]
280	IRVWDMSKRTGVQTF	ubiquitination	[1]
337	GNMLHYVKDRFLRQL	ubiquitination	[1, 2]
350	QLDFNSSKDVAVMQL	ubiquitination	[1, 2, 3, 7]
362	MQLRSGSKFPVFNMS	ubiquitination	[1, 2]
398	YDLYTIPKDADSQNP	ubiquitination	[1, 2, 5, 7]
411	NPDAPEGKRSSGLTA	ubiquitination	[2, 3, 5, 6, 7]
438	RMHSLLIKNLKNEIT	ubiquitination	[1, 2]
441	SLLIKNLKNEITKKV	ubiquitination	[1, 2, 3, 7]
446	NLKNEITKKVQVPNC	ubiquitination	[2]
447	LKNEITKKVQVPNCD	ubiquitination	[1, 3, 9]
480	TLFDVQQKRTLASVK	ubiquitination	[1, 2, 4, 7]
487	KRTLASVKISKVKYV	ubiquitination	[1]
517	AIVICNRKLDALCNI	ubiquitination	[1, 2]
531	IHENIRVKSGAWDES	ubiquitination	[1]
574	PIYVTRVKGNNVYCL	ubiquitination	[1, 2, 3, 5]
598	TIDPTEFKFKLALIN	ubiquitination	[1, 3, 4, 5, 6, 7]
600	DPTEFKFKLALINRK	ubiquitination	[1, 4]
607	KLALINRKYDEVLHM	ubiquitination	[1, 4]
619	LHMVRNAKLVGQSII	ubiquitination	[1, 2, 7]
631	SIIAYLQKKGYPEVA	ubiquitination	[4, 5, 7]
632	IIAYLQKKGYPEVAL	ubiquitination	[1]
643	EVALHFVKDEKTRFS	ubiquitination	[3]
671	AAKALDDKNCWEKLG	ubiquitination	[1, 3]
698	EMCYQRTKNFDKLSF	ubiquitination	[2]
715	LITGNLEKLRKMMKI	ubiquitination	[2]
721	EKLRKMMKIAEIRKD	ubiquitination	[1, 2]
727	MKIAEIRKDMSGHYQ	ubiquitination	[1, 4]
775	DEEAESLKETFDPEK	ubiquitination	[5]
782	KETFDPEKETIPDID	ubiquitination	[5]
825	FEGTIASKGKGGALA	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
827	GTIASKGKGGALAAD	ubiquitination	[1, 3]
988	GYPNRNWKDAGLKNG	ubiquitination	[1, 2, 3]
993	NWKDAGLKNGVPAVG	ubiquitination	[1, 2]
1028	KFEEAVEKFRSILLS	ubiquitination	[1, 4]
1150	KILSACEKNPTDAYQ	ubiquitination	[1, 5]
1184	YRGKPVEKCPLSGAC	ubiquitination	[1]
1197	ACYSPEFKGQICRVT	ubiquitination	[5]
1211	TTVTEIGKDVIGLRI	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 

Functional 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). 

Sequence Annotation

 REPEAT 7 37 WD 1.
 REPEAT 49 79 WD 2.
 REPEAT 91 121 WD 3.
 REPEAT 133 163 WD 4.
 REPEAT 203 233 WD 5.
 REPEAT 247 277 WD 6.
 MOD_RES 173 173 Phosphoserine.
 MOD_RES 185 185 Phosphothreonine.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 895 895 Phosphoserine.
 MOD_RES 1035 1035 Phosphoserine (By similarity).  

Keyword

 Alternative splicing; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Hormone; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; RNA editing; Secreted; Transport; WD repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1224 AA 

Protein Sequence

Gene Ontology

 GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005615; C:extracellular space; IDA:MGI.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0030157; P:pancreatic juice secretion; IDA:MGI.
 GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome. 

Interpro

 IPR016391; Coatomer_asu.
 IPR010714; Coatomer_asu_C.
 IPR006692; Coatomer_WD-assoc_reg.
 IPR020472; G-protein_beta_WD-40_rep.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 

Pfam

 PF04053; Coatomer_WDAD
 PF06957; COPI_C
 PF00400; WD40 

SMART

 SM00320; WD40 

PROSITE

 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 

PRINTS

 PR00320; GPROTEINBRPT.