dbPTM

COPG_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COPG_SCHPO
UniProt AC	P87140
Protein Name	Probable coatomer subunit gamma
Gene Name	sec21
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	905
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 (By similarity)..
Protein Sequence	MSYSKKDDDGDESIFANVNQVTVTQDARAFNSSSISPRKSRRLLSKIAYLIYTGEHFQEKQATELFFGITKLFQHKDPSLRQFVYIIIKELSVVAEDVIMITSSIMKDTATGRETIYRPNAIRSLIRVIDANTVPAIERILTTGIVDPISAVASAALVSAYHLYPVAKDIVSRWNNEVQDAVTSHNVGRKVASSPFFTSTLGYTPNASGISQYHALGLLYRIRRHDSIAMNKLLQLLVSNLGTVSNSHAFVMLIRYISSLMDQNTQFRDQMVPFLHGWLKSKGDMVNLEVARNMVRLKNISDDDLQPVVSVLKIFLSSHRSATRFSAIRTLNELAMTRPHLVHSCNLNIESLITDVNRSIATYAITTLLKTGNDESVDRLMKQIVTFMSDISDNFKIIVVDAIRSLCLKFPRKQDSMLTFLSNILCDEGGYEFKRAAVDAISDMIKYIPESKERALAELCEFIEDCEYPKIAVRILSILGEEGPKASEPTRFIRYIYNRIMLENAIVRSAAVSALTKFGLNAEDKFVQRSVKVILTRCLEDADDEVRDRAAFSVKALEDRDAFLPVVKSDKIPSLPALERSLVIYISERKFGQGFDIKSVPVLSQEEIDAENLRIKKATTEVEFTEVTPAEDQNALASSNIETEFLNALESVSEFNEYGPVLKSSPSPIELTEQETEFVVKVVKHVFKDHLVVQFQLHNTLSEVILENAVVVSTPSTDDLVEECVVPAAIVSGEPVSIFVSFKFNDSVPYPLTTLTNTLQFTTKEIDIHTGEPEEEGYEDEYKIDDLDVSAGDFISPAYESNFDGLFDSLEHEASEVYVLSLLDSFRSTCSRVAELLQMQPLEGTENPTDKPVHVMKLSGKLVNGEKVLALVKMAHSKDGEGITIKVIARGESDSSVELVVGGIA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	DARAFNSSSISPRKS CHHHHCCCCCCHHHH	32.56	25720772
36	Phosphorylation	AFNSSSISPRKSRRL HHCCCCCCHHHHHHH	22.17	28889911
599	Phosphorylation	GQGFDIKSVPVLSQE CCCCCCCCCCCCCHH	31.80	29996109
604	Phosphorylation	IKSVPVLSQEEIDAE CCCCCCCCHHHHCHH	35.46	28889911
664	Phosphorylation	EYGPVLKSSPSPIEL HCCCCCCCCCCCCCC	43.23	25720772
665	Phosphorylation	YGPVLKSSPSPIELT CCCCCCCCCCCCCCC	28.01	25720772
754	Phosphorylation	SVPYPLTTLTNTLQF CCCCCEEECCCEEEE	38.99	27738172
762	Phosphorylation	LTNTLQFTTKEIDIH CCCEEEEEECEEECC	24.81	27738172

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of COPG_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of COPG_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of COPG_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of COPG_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of COPG_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND MASSSPECTROMETRY.	18257517 [Abstract]