dbPTM

CHO2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHO2_SCHPO
UniProt AC	O74787
Protein Name	Phosphatidylethanolamine N-methyltransferase {ECO:0000255\|HAMAP-Rule:MF_03217, ECO:0000303\|Ref.2}
Gene Name	cho2 {ECO:0000303\|Ref.2}
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	905
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME)..
Protein Sequence	MTNQIPSASSAADFGSSKSTSVDAVPNMDKSSSVRRKNIDSNGLQQTNQIEQAESSLNAEADHSEPERYGCTPSGKVFLLPKEQENRRSILETVDPRFSKTPWDWIVISSILAQVLLFFMTTGAVRRYSMMLCFFFWRISYDAGIGFLLHMQSNHRKVVTWISDFGFFDKENHPKLYDLTKKQLISKMDSSYNYDTSPLEFNSWLVFRHFVDLILMCDFCSYILMGLAWTCWPKVNIILQFLRIFGGIALIVFNYWVKMDAHRVVRDYAWYWGDFFFLLRSSLVFNGVFELAPHPMYSVGYAGYYGMSLLTGSYAVLFASILAHAAQFGFLLFVENPHIERTYGTDINHARLSPRGEDNEFELPPEHDLVGFVNFDFTRISDVALLIIALYSIFIILLSSNSHYSQFWAIFQAFVWRFLHSIIHAFILFYQSKSKAWTKHFIRNGESAAYAWSQWKGLYNLTLNMSYISFVMAAWKLYHLPSNWTYGLVSLRHALGFGLIALHIYTSVSIYEDLGQYGWFYGDFFLPSRSPKLVYQGIYRYVNNPERFLGCSAYWGLALISSSAWIFLIAILAQLSNLAIIRLVEQPHMQKVYGNTLRKEAGISKLIKQATSEKGNILPKTVETHMKALTTSVDKVLDQTAEALEEFVNTAPPKVQELLKGTESNLRKNAQLAILKLFAPQLSSSTHFDYKLEIKGIDNNQVLLGHPITVCWTASPNHEINDWIGLYKLSDNASDLYTQTSSEGRWSAIDANGYTSHCSSIKSLSNDKNSGEVEFSGDLLFWETGTFEFRYHYGGKHLVMAKTEPFVITATSMNTTDVDEVSAYLLKSIKFCDPNITPHDGDASLCDISEGSARKLTSIIKYSFGIDLSYRVVQVDGSCSALSRRIVNSLKILQSFDGPSGAKDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	TNQIPSASSAADFGS CCCCCCCCCCHHCCC	25.50	24763107
10	Phosphorylation	NQIPSASSAADFGSS CCCCCCCCCHHCCCC	27.48	29996109
19	Phosphorylation	ADFGSSKSTSVDAVP HHCCCCCCCCCCCCC	28.06	29996109
20	Phosphorylation	DFGSSKSTSVDAVPN HCCCCCCCCCCCCCC	36.18	25720772
21	Phosphorylation	FGSSKSTSVDAVPNM CCCCCCCCCCCCCCC	25.70	24763107
31	Phosphorylation	AVPNMDKSSSVRRKN CCCCCCCCCCHHHCC	24.47	25720772
33	Phosphorylation	PNMDKSSSVRRKNID CCCCCCCCHHHCCCC	27.08	25720772
89	Phosphorylation	KEQENRRSILETVDP HHHHCHHHHHHHCCC	28.43	25720772
345	Phosphorylation	HIERTYGTDINHARL CCCHHCCCCCCCCCC	24.24	29996109
353	Phosphorylation	DINHARLSPRGEDNE CCCCCCCCCCCCCCC	13.65	28889911
664	Phosphorylation	ELLKGTESNLRKNAQ HHHHCCCCHHHHHHH	40.79	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 CHO2_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CHO2_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 CHO2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CHO2_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of CHO2_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-353, AND MASSSPECTROMETRY.	18257517 [Abstract]