COPZ1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPZ1_MOUSE
• UniProt AC: P61924
• Protein Name: Coatomer subunit zeta-1
• Gene Name: Copz1
• Organism: Mus musculus (Mouse).
• Sequence Length: 177
• 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).; 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..
• Protein Sequence: MEALILEPSLYTVKAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMAVLNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVALRGEDVPLTEQTVSQVLQSAKEQIKWSLLR

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
1	Acetylation	-------MEALILEP -------CCCEECCC	6.49	-
11	Phosphorylation	LILEPSLYTVKAILI EECCCCCEEEEEEEE	17.52	29899451
12	Phosphorylation	ILEPSLYTVKAILIL ECCCCCEEEEEEEEE	22.33	29899451
29	Acetylation	DGDRLFAKYYDDTYP CCCCEEHHHCCCCCC	36.69	22826441
39	Ubiquitination	DDTYPSVKEQKAFEK CCCCCCHHHHHHHHC	59.78	22790023
46	Acetylation	KEQKAFEKNIFNKTH HHHHHHHCCCCCCCC	49.22	23954790
46	Ubiquitination	KEQKAFEKNIFNKTH HHHHHHHCCCCCCCC	49.22	22790023
51	Ubiquitination	FEKNIFNKTHRTDSE HHCCCCCCCCCCHHH	34.65	22790023
69	Phosphorylation	LEGLTVVYKSSIDLY HCCCEEEEECCCEEE	10.79	21454597
161	Phosphorylation	PLTEQTVSQVLQSAK CCCHHHHHHHHHHHH	20.26	30352176
166	Phosphorylation	TVSQVLQSAKEQIKW HHHHHHHHHHHHHHH	36.83	30352176
168	Ubiquitination	SQVLQSAKEQIKWSL HHHHHHHHHHHHHHH	56.23	22790023
172	Ubiquitination	QSAKEQIKWSLLR-- HHHHHHHHHHHCC--	30.35	22790023
174	Phosphorylation	AKEQIKWSLLR---- HHHHHHHHHCC----	16.72	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of COPZ1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPZ1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of COPZ1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of COPZ1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.