COPB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPB_MOUSE
• UniProt AC: Q9JIF7
• Protein Name: Coatomer subunit beta
• Gene Name: Copb1
• Organism: Mus musculus (Mouse).
• Sequence Length: 953
• Subcellular Localization: Cytoplasm . Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasmic vesicle, COPI-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Cell membrane . Endoplasmic reticulum-Golgi intermediate compartme
• 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. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis..
• Protein Sequence: MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFEHLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLVELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDSNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEVRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSQMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNMTDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPVHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSL

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
2	Acetylation	------MTAAENVCY ------CCHHHHHEE	34.28	-
88	Phosphorylation	FWEIVPKTTPDGRLL HHHCCCCCCCCCCHH	37.17	-
102	Glutathionylation	LHEMILVCDAYRKDL HHHHHHHHHHHHCCC	1.91	24333276
105	Phosphorylation	MILVCDAYRKDLQHP HHHHHHHHHCCCCCC	12.63	-
107	Ubiquitination	LVCDAYRKDLQHPNE HHHHHHHCCCCCCCH	50.55	27667366
128	Ubiquitination	LRFLCKLKEAELLEP HHHHHHCCHHHHHHC	40.13	22790023
128	Acetylation	LRFLCKLKEAELLEP HHHHHHCCHHHHHHC	40.13	22826441
248	S-nitrosocysteine	ERARFIRCIYNLLQS HHHHHHHHHHHHHHC	3.11	-
248	S-nitrosylation	ERARFIRCIYNLLQS HHHHHHHHHHHHHHC	3.11	20925432
250	Phosphorylation	ARFIRCIYNLLQSSS HHHHHHHHHHHHCCC	11.90	28542873
255	Phosphorylation	CIYNLLQSSSPAVKY HHHHHHHCCCCCCCC	32.52	28542873
256	Phosphorylation	IYNLLQSSSPAVKYE HHHHHHCCCCCCCCE	27.64	28542873
298	Ubiquitination	KESDNNVKLIVLDRL EECCCCEEEEEEEHH	34.32	22790023
330	Phosphorylation	MDILRVLSTPDLEVR HHHHHHHCCCCHHHH	34.73	25195567
366	Acetylation	VLKKEVIKTNNVSEH EEEEHHHHCCCCCCC	50.83	23954790
386	Phosphorylation	YRQLLVRTLHSCSVR HHHHHHHHHHHCCCC	22.73	-
466	S-palmitoylation	LWILGEYCSTKEDIQ HHHHHHHCCCHHHHH	3.47	28526873
482	Phosphorylation	VMTEVRRSLGEIPIV HHHHHHHHHCCCCCC	30.11	26370283
494	Ubiquitination	PIVESEIKKEAGELK CCCHHHHHHHHCCCC	40.27	27667366
494	Acetylation	PIVESEIKKEAGELK CCCHHHHHHHHCCCC	40.27	23806337
501	Acetylation	KKEAGELKPEEEITV HHHHCCCCCHHHEEC	46.19	23954790
516	Phosphorylation	GPVQKLVTEMGTYAT CHHHHHHHHHHHHHH	30.59	25367039
520	Phosphorylation	KLVTEMGTYATQSAL HHHHHHHHHHHHHHH	14.52	25367039
521	Phosphorylation	LVTEMGTYATQSALS HHHHHHHHHHHHHHH	11.26	22817900
534	Ubiquitination	LSSSRPTKKEEDRPP HHCCCCCCCCCCCCC	61.95	22790023
603	Ubiquitination	GKSSLPKKPITDDDV CCCCCCCCCCCHHCH	39.45	22790023
623	S-palmitoylation	CLKVLSECSPLMNDI HHHHHHHCCHHHHHH	4.57	28526873
640	Phosphorylation	KECRQSLSQMLSAKL HHHHHHHHHHHHHHH	20.84	28285833
644	Phosphorylation	QSLSQMLSAKLEEEK HHHHHHHHHHHHHHH	20.29	22942356
651	Malonylation	SAKLEEEKLSQKKES HHHHHHHHHHHHHHH	57.63	26073543
653	Phosphorylation	KLEEEKLSQKKESEK HHHHHHHHHHHHHHH	51.53	28066266
684	Glutathionylation	TAKNEMNCKEDQFQL CCCCCCCCCCHHHHH	5.01	24333276
773	Phosphorylation	LKLVEKPSPLTLAPH CEEECCCCCCCCCCC	43.54	29899451
786	Ubiquitination	PHDFANIKANVKVAS CCCCCCCCCCEEEEE	33.44	22790023
786	Acetylation	PHDFANIKANVKVAS CCCCCCCCCCEEEEE	33.44	23954790
879	Phosphorylation	STNMKCLTPEKALSG HCCCCCCCHHHHHHH	38.58	-
933	Phosphorylation	HIRIRAKSQGMALSL EEEEEECCCCCEEHH	30.86	28507225
939	Phosphorylation	KSQGMALSLGDKINL CCCCCEEHHHCCCCH	22.29	29472430

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COPB_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 COPB_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of COPB_MOUSE !!

Drug and Disease Associations

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