COPB_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPB_RAT
• UniProt AC: P23514
• Protein Name: Coatomer subunit beta
• Gene Name: Copb1
• Organism: Rattus norvegicus (Rat).
• 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 compartmen
• 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. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in the axonal compartment of dorsal root ganglion (DRG) cells. 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: MTAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFENLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLVELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDSNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEVRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSQMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNVTDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPVHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSL

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	-
494	Acetylation	PIVESEIKKEAGELK CCCHHHHHHHHCCCC	40.27	-
521	Phosphorylation	LVTEMGTYATQSALS HHHHHHHHHHHHHHH	11.26	22276854
535	Succinylation	SSSRPTKKEEDRPPL HCCCCCCCCCCCCCC	69.67	26843850
562	Phosphorylation	ASLATTLTKIALRYV HHHHHHHHHHHHHHH	20.50	29779826
885	Phosphorylation	LTPEKALSGYCGFMA CCHHHHHHHHHHHHH	32.35	24945867
887	Phosphorylation	PEKALSGYCGFMAAN HHHHHHHHHHHHHHH	5.99	24945867
896	Phosphorylation	GFMAANLYARSIFGE HHHHHHCHHHHHHCC	10.36	24945867
933	Phosphorylation	HIRIRAKSQGMALSL EEEEEECCCCCEEHH	30.86	23984901

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

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

Functions of PTM Sites

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

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of COPB_RAT !!

Drug and Disease Associations

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