COPA_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COPA_SCHPO
• UniProt AC: Q96WV5
• Protein Name: Putative coatomer subunit alpha
• Gene Name: SPBPJ4664.04
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1207
• Subcellular Localization: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
• 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: MEMLTKFESRSSRAKGVAFHPTQPWILTSLHNGRIQLWDYRMGTLLDRFDGHDGPVRGIAFHPTQPLFVSGGDDYKVNVWNYKSRKLLFSLCGHMDYVRVCTFHHEYPWILSCSDDQTIRIWNWQSRNCIAILTGHSHYVMCAAFHPSEDLIVSASLDQTVRVWDISGLRMKNAAPVSMSLEDQLAQAHNSISNDLFGSTDAIVKFVLEGHDRGVNWCAFHPTLPLILSAGDDRLVKLWRMTASKAWEVDTCRGHFNNVSCCLFHPHQELILSASEDKTIRVWDLNRRTAVQTFRRDNDRFWFITVHPKLNLFAAAHDSGVMVFKLERERPAHALNINTLLYVNKEKSIVSYDLLRAQSTTVASVKHLGSAWLPPRSLSYNPAEKVALLTSSADNGVYELVNVSSRSNSLPLKDNIKGPGDDAIFVARNRFAVFSRSDQTIEIKDLSNKVTKTIQLPEKTRDIFFAGMGHVLLSTATQVHLFDLQQKKIVSSFNANRVKYVVWSNDNSQAALLGKHYVYIVKKNLELITSIHETIRIKSAVWVENNVLLYATLDHLKYALMSGDTGVIKTLESTLYLVKAKGNMVFALNRAAEPVSFEIDPTEYLFKLALLRKDYEQVLHLIQNSNLVGQAIIAYLQKKGYPEIALQFVEDPSTRFELALECGNLETALELARTIDRPEVWSRLASDAMSYGNHKIAEITFQKLRYFEKLSFLYLITGNAEKLQKMAIIAEKRNDTLSLFQNSLYLNEVESRINILEQAGMYPIAYLTAKSNGLEEKAQQILSHCNKTEEEIKLPSLGSAFTTPVPVNETYTHNWPLLDTSHSTFEKSLQERMEQLAIERQEEQESEEEYEEVEQSLMDVVDEMSDLAESVPEEEVDGWEVEDLAPEEAVNDVVDDASAFVGADEIFLWKRNSPLAADHIAAGDFESAMKILNKQVGAINFSPLKTRFLEIYTASRVYLPTISGLDPLVSYVRRNAETAERSQALPFITRNLASIKSHELHEAYRLVKANKILEAQICFRSIIYLALTTVANSEEEADEISALIDECCRYIVALSCELERRRLGEEDTKRALELSYYFASADLQPMHSIIALRLAINASHKLKNYKSASFLGNKLLQLAESGPAAEAANRAITLGDRNPHDAFEIEYDPHVEMRICPKTLTPVYSGDDFDVCSVCGAVYHKGYVNEVCTVCDVGGIGQKGTGRRFFA

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
191	Phosphorylation	QLAQAHNSISNDLFG HHHHHHHHHCCCCCC	19.95	21712547
407	Phosphorylation	LVNVSSRSNSLPLKD EEECCCCCCCCCCCC	32.49	25720772
409	Phosphorylation	NVSSRSNSLPLKDNI ECCCCCCCCCCCCCC	32.39	28889911
913	Phosphorylation	IFLWKRNSPLAADHI EEEEECCCCCCCCHH	25.89	28889911
942	Phosphorylation	QVGAINFSPLKTRFL CCCCEECCCCCHHHH	25.49	28889911
982	Phosphorylation	NAETAERSQALPFIT CHHHHHHHHHHHHHH	16.00	25720772

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of COPA_SCHPO !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-409 AND SER-942, ANDMASS SPECTROMETRY.
PubMed: 18257517