Search Results

Overview

Uniprot ID	P61923
Protein Name	Coatomer subunit zeta-1
Gene Name	COPZ1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
172	QSAKEQIKWSLLR**
29	DGDRLFAKYYDDTYP
51	FEKNIFNKTHRTDSE

Function

Component of the coatomer complex, involved in retrograde Golgi-to-ER transport (PubMed:39642330). 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 (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity)

Protein Sequence

10 MEALILEPSL 20 YTVKAILILD 30 NDGDRLFAKY 40 YDDTYPSVKE 50 QKAFEKNIFN 60 KTHRTDSEIA 70 LLEGLTVVYK 80 SSIDLYFYVI 90 GSSYENELML 100 MAVLNCLFDS 110 LSQMLRKNVE 120 KRALLENMEG 130 LFLAVDEIVD 140 GGVILESDPQ 150 QVVHRVALRG 160 EDVPLTEQTV 170 SQVLQSAKEQ IKWSLLR

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0030126	COPI vesicle coat
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005789	endoplasmic reticulum membrane
Cellular Component	GO:0000139	Golgi membrane
Cellular Component	GO:0030133	transport vesicle
Biological Process	GO:0006891	intra-Golgi vesicle-mediated transport
Biological Process	GO:0006886	intracellular protein transport
Biological Process	GO:0006890	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.