CPLM-009385

Genbank Nucleotide ID

Coatomer subunit zeta-1

Protein Synonyms/Alias

Zeta-1-coat protein; Zeta-1 COP

COPZ; CGI-120; HSPC181

Homo sapiens (Human)

Position	Peptide	Type	References
29	DGDRLFAKYYDDTYP	ubiquitination	[1, 2, 3, 4]
39	DDTYPSVKEQKAFEK	ubiquitination	[1, 2, 3, 4]
46	KEQKAFEKNIFNKTH	ubiquitination	[1, 2, 3, 4, 5]
51	FEKNIFNKTHRTDSE	ubiquitination	[1, 2, 3, 4]
168	SQVLQSAKEQIKWSL	ubiquitination	[2, 3, 4, 6, 7]
172	QSAKEQIKWSLLR**	ubiquitination	[1, 4]

[1] 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]
[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] 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]
[4] 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]
[5] 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]
[6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[7] 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).

MOD_RES 1 1 N-acetylmethionine.

3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:UniProtKB.

IPR022775; AP_mu_sigma_su.
IPR000804; Clathrin_sm-chain_CS.
IPR011012; Longin-like_dom.

PF01217; Clat_adaptor_s

PS00989; CLAT_ADAPTOR_S