dbPTM

DOA10_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DOA10_SCHPO
UniProt AC	O60103
Protein Name	ERAD-associated E3 ubiquitin-protein ligase doa10
Gene Name	doa10
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	1242
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the doa10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron)..
Protein Sequence	MNADDEICRVCRCEGAPDSPLFHPCKCTGSIRYVHQECLVEWLGHSKKTHCELCKAKFEFTKVYSESMPRTIPFTILCRKLASTLKQRVIFFTRVLLTFFCWTVLLPLIFKHVWNLNFKIGDTYTIHARNKTFTAPQKPGYFESISQITSSPRLNTLIANTAEGQVLTFVVTFILITAFLVREWVLQNAVQVADELQGQQFENVNQNNQAQAAAAAAQNLREVREARQRLAMVMEHLRERQEQRNLELQRNGSFEEIERARQRFALLGDNIREPQEEENDVDVDEIFNRQQLNQPALDLNDANSSNSVPVEFNSLHSQNVDYRDEVDSLRPQFNVDEQSSISHSSNASENIVDGAVTQANGIESDFTRVDHEPIIVNNDDENGNNESENEEVIEEDNLNRNVIAEAQNQVVADEERNAVARAAQIAEADDADDFDGILEFLGLRGPITGFLQNCLVIAFVVSVFLTTAVGIPYMSGRLMVEWILFIIHRPTFILRFILSFVNILFDWTVGGAFNIVKILTKLPLLSTVFVKLKLQGIFSSSFQQVSNNMYSWIYDHVFSSSDHAYESLIYYMKTGHKQVVQSFSIFPVFRVCQMFAVILKDFVENYSNRPVDRVFTTLIGYCMFTFLGISYLNRKQFLFNDPQIRNVELAFREVLRQCGSIAKFGIIFSIELVVFPIFCGILLSMCLIGTFKKLAAENLLNVMTVYPAQSIFLAWFIGITFMFEFAVFISMVRKIVRPGVLYFLRDPNDPQFHPIREILEKPMLFQLKKIGFSAILYFAFIIGCVGSVIHLLKSTGIIFPIEFTTKPAVFEAPIDLLALEILIFLSIKLFKPLELTRSFWRTLVSTFCRCLRLSSYVMGQRYSDEEGYYPKQYFSFLRRIISKPSDTENQDDGDKQKAKKDFVQDGFFLWCPSKDVVPVRQGAMLIPVTENGYEIFGEKKKVEENADYTITYAPSNFYKRLIALLLFCWICSTLVTVLLVFVPLSLGRAIYAWCFPNVVKHDFYAYAIGFYSISFPMYAIHASVKFLKLDYLRSLMNKLNLKIVMRSLVMALKYLLLAFLGIFILPLLLGAIWELYVAIPFRTIFNRGTLALDAFQNWVIGLFMLRMIYFTVTSNEERFVSRLFQDAFRDRWTNPQILPLLKNVLIPFTSALIAAVVLPSVFTYVTYPFLSSIFPSASKTLMYRLMHPIFLALLGLALLGRRFVETSSKWSQGIRDDLYLVGTRLHNFGESAPPAISESAEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
253	Phosphorylation	LELQRNGSFEEIERA HHHHHCCCHHHHHHH	32.79	28889911
387	Phosphorylation	DENGNNESENEEVIE CCCCCCCCCCCHHHC	48.09	29996109

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 DOA10_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DOA10_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 DOA10_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DOA10_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of DOA10_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-253, AND MASSSPECTROMETRY.	18257517 [Abstract]