CPLM-000248

Genbank Nucleotide ID

Coatomer subunit epsilon

Protein Synonyms/Alias

Epsilon-coat protein; Epsilon-COP

Homo sapiens (Human)

Position	Peptide	Type	References
42	INEAQRVKLSSPERD	ubiquitination	[1]
65	RAYLAQRKFGVVLDE	ubiquitination	[1, 2, 3, 4, 5]
74	GVVLDEIKPSSAPEL	ubiquitination	[1, 3]
265	VLSQHLGKPPEVTNR	ubiquitination	[2, 3, 4, 5, 6, 7]
278	NRYLSQLKDAHRSHP	ubiquitination	[1, 2, 3, 4, 5, 7]
288	HRSHPFIKEYQAKEN	ubiquitination	[1, 7]
293	FIKEYQAKENDFDRL	ubiquitination	[1, 3]

[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] 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]
[3] 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]
[4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[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]

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).

Alternative splicing; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005198; F:structural molecule activity; IEA:InterPro.
GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.

IPR006822; Coatomer_esu.
IPR011990; TPR-like_helical.