COPZ1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPZ1_HUMAN
• UniProt AC: P61923
• Protein Name: Coatomer subunit zeta-1
• Gene Name: COPZ1
• Organism: Homo sapiens (Human).
• 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	Sulfoxidation	-------MEALILEP -------CCCEECCC	6.49	28465586
1	Acetylation	-------MEALILEP -------CCCEECCC	6.49	22223895
7 (in isoform 3)	Phosphorylation	-	26.33	23663014
8 (in isoform 3)	Phosphorylation	-	26.62	23663014
9	Phosphorylation	EALILEPSLYTVKAI CCEECCCCCEEEEEE	25.32	28348404
11 (in isoform 3)	Phosphorylation	-	17.52	23663014
11	Phosphorylation	LILEPSLYTVKAILI EECCCCCEEEEEEEE	17.52	28348404
12 (in isoform 3)	Phosphorylation	-	22.33	23663014
12	Phosphorylation	ILEPSLYTVKAILIL ECCCCCEEEEEEEEE	22.33	28348404
14 (in isoform 3)	Phosphorylation	-	23.16	23663014
16	Ubiquitination	SLYTVKAILILDNDG CCEEEEEEEEECCCC	1.72	21890473
19	Ubiquitination	TVKAILILDNDGDRL EEEEEEEECCCCCCE	4.51	-
23	Ubiquitination	ILILDNDGDRLFAKY EEEECCCCCCEEHHH	28.35	21890473
25	Methylation	ILDNDGDRLFAKYYD EECCCCCCEEHHHCC	36.92	-
28	Ubiquitination	NDGDRLFAKYYDDTY CCCCCEEHHHCCCCC	11.97	21890473
29	2-Hydroxyisobutyrylation	DGDRLFAKYYDDTYP CCCCEEHHHCCCCCC	36.69	-
29	Ubiquitination	DGDRLFAKYYDDTYP CCCCEEHHHCCCCCC	36.69	-
29	Acetylation	DGDRLFAKYYDDTYP CCCCEEHHHCCCCCC	36.69	26822725
29	Ubiquitination	DGDRLFAKYYDDTYP CCCCEEHHHCCCCCC	36.69	21890473
30	Phosphorylation	GDRLFAKYYDDTYPS CCCEEHHHCCCCCCC	14.54	28152594
31	Phosphorylation	DRLFAKYYDDTYPSV CCEEHHHCCCCCCCH	13.46	28152594
34	Phosphorylation	FAKYYDDTYPSVKEQ EHHHCCCCCCCHHHH	34.14	-
35	Phosphorylation	AKYYDDTYPSVKEQK HHHCCCCCCCHHHHH	10.66	23663014
39	Acetylation	DDTYPSVKEQKAFEK CCCCCCHHHHHHHHC	59.78	26051181
39	2-Hydroxyisobutyrylation	DDTYPSVKEQKAFEK CCCCCCHHHHHHHHC	59.78	-
39	Ubiquitination	DDTYPSVKEQKAFEK CCCCCCHHHHHHHHC	59.78	21890473
39	Ubiquitination	DDTYPSVKEQKAFEK CCCCCCHHHHHHHHC	59.78	-
39	Sumoylation	DDTYPSVKEQKAFEK CCCCCCHHHHHHHHC	59.78	-
42	Ubiquitination	YPSVKEQKAFEKNIF CCCHHHHHHHHCCCC	57.02	-
46	Acetylation	KEQKAFEKNIFNKTH HHHHHHHCCCCCCCC	49.22	26822725
46	Ubiquitination	KEQKAFEKNIFNKTH HHHHHHHCCCCCCCC	49.22	21890473
51	Ubiquitination	FEKNIFNKTHRTDSE HHCCCCCCCCCCHHH	34.65	21890473
117	Ubiquitination	EKRALLENMEGLFLA HHHHHHHHCCHHHEE	33.50	21890473
121	Ubiquitination	LLENMEGLFLAVDEI HHHHCCHHHEEEEEE	1.71	21890473
145	Ubiquitination	DPQQVVHRVALRGED CHHHHEEEEECCCCC	12.09	21890473
149	Methylation	VVHRVALRGEDVPLT HEEEEECCCCCCCCC	36.40	-
149	Ubiquitination	VVHRVALRGEDVPLT HEEEEECCCCCCCCC	36.40	21890473
156	Phosphorylation	RGEDVPLTEQTVSQV CCCCCCCCHHHHHHH	21.70	27050516
159	Phosphorylation	DVPLTEQTVSQVLQS CCCCCHHHHHHHHHH	18.85	29523821
161	Phosphorylation	PLTEQTVSQVLQSAK CCCHHHHHHHHHHHH	20.26	17525332
166	Phosphorylation	TVSQVLQSAKEQIKW HHHHHHHHHHHHHHH	36.83	25159151
168	Ubiquitination	SQVLQSAKEQIKWSL HHHHHHHHHHHHHHH	56.23	21906983
169	Phosphorylation	QVLQSAKEQIKWSLL HHHHHHHHHHHHHHC	58.20	27251275
172	Ubiquitination	QSAKEQIKWSLLR-- HHHHHHHHHHHCC--	30.35	21906983
174	Phosphorylation	AKEQIKWSLLR---- HHHHHHHHHCC----	16.72	25159151
182	Phosphorylation	LLR------------ HCC------------		27251275

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

Oops, there are no upstream regulatory protein records of COPZ1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPZ1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COPG1_HUMAN	COPG1	physical	8858162
TMEDA_HUMAN	TMED10	physical	9751720
COPG1_HUMAN	COPG1	physical	9482852
COPZ1_HUMAN	COPZ1	physical	9482852
COPZ1_HUMAN	COPZ1	physical	14729954
A4_HUMAN	APP	physical	21832049
GOPC_HUMAN	GOPC	physical	22939629
TMED9_HUMAN	TMED9	physical	9472029
TMEDA_HUMAN	TMED10	physical	9472029
UD11_HUMAN	UGT1A1	physical	9472029
COPD_HUMAN	ARCN1	physical	22863883
COPB_HUMAN	COPB1	physical	22863883
DIAP1_HUMAN	DIAPH1	physical	22863883
KLC1_HUMAN	KLC1	physical	22863883
RUFY1_HUMAN	RUFY1	physical	22863883
TTI1_HUMAN	TTI1	physical	22863883
COPA_HUMAN	COPA	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
COPG1_HUMAN	COPG1	physical	26344197
COPG2_HUMAN	COPG2	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
SARNP_HUMAN	SARNP	physical	27173435
CHRD1_HUMAN	CHORDC1	physical	27173435
DRG1_HUMAN	DRG1	physical	27173435
SEPT7_HUMAN	SEPT7	physical	27173435
PRCC_HUMAN	PRCC	physical	27173435
ZCCHV_HUMAN	ZC3HAV1	physical	27173435

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.
PubMed: 17525332