dbPTM

PCY1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCY1_SCHPO
UniProt AC	O74975
Protein Name	Probable choline-phosphate cytidylyltransferase
Gene Name	SPCC1827.02c
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	362
Subcellular Localization	Nucleus .
Protein Description
Protein Sequence	MGEEGIKINDTHKRRIDEVEPSEKEDNVERQTKKYNFEIDEPEEQEKKDEKEDDKEESPSKSLEEISQSVSPVEEEPRDVRFKELSTPFSYPINDPPEGRPVRVYADGVFDLFHIGHMRQLEQAKKVFPNVHLIVGLPNDQLTHRLKGLTVMNDKERAEALRHCKWVDEVLENAPWVITPEFLEEHKIDFVAHDDIPYASDDSGDIYLPVKKVGKFIPTKRTEGVSTSDLITRIIRDYDQYVMRNLARGVNRKELNVSLFKKNELDLRHHIKVLRDTLRNHWVSTTRDLKADIKSFLSMATTDYQLQKNPLHGSSEPSSPGPTGFLGGINRWMQRRSSSHYDLPRVGNEIAASSSSATEENH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	RIDEVEPSEKEDNVE CCCCCCCCCCCCCHH	48.04	29996109
58	Phosphorylation	KEDDKEESPSKSLEE CCCCCCCCCCHHHHH	35.25	21712547
60	Phosphorylation	DDKEESPSKSLEEIS CCCCCCCCHHHHHHH	44.12	21712547
62	Phosphorylation	KEESPSKSLEEISQS CCCCCCHHHHHHHHC	45.40	24763107
67	Phosphorylation	SKSLEEISQSVSPVE CHHHHHHHHCCCCCC	21.49	25720772
69	Phosphorylation	SLEEISQSVSPVEEE HHHHHHHCCCCCCCC	20.12	29996109
71	Phosphorylation	EEISQSVSPVEEEPR HHHHHCCCCCCCCCC	28.60	28889911
226	Phosphorylation	TKRTEGVSTSDLITR CCCCCCCCHHHHHHH	32.81	25720772
314	Phosphorylation	QKNPLHGSSEPSSPG HCCCCCCCCCCCCCC	22.30	29996109
315	Phosphorylation	KNPLHGSSEPSSPGP CCCCCCCCCCCCCCC	59.11	28889911
318	Phosphorylation	LHGSSEPSSPGPTGF CCCCCCCCCCCCCCC	45.15	25720772
319	Phosphorylation	HGSSEPSSPGPTGFL CCCCCCCCCCCCCCC	44.59	28889911
323	Phosphorylation	EPSSPGPTGFLGGIN CCCCCCCCCCCCHHH	46.62	28889911
337	Phosphorylation	NRWMQRRSSSHYDLP HHHHHHHCCCCCCCC	38.08	25720772
338	Phosphorylation	RWMQRRSSSHYDLPR HHHHHHCCCCCCCCC	21.23	25720772
339	Phosphorylation	WMQRRSSSHYDLPRV HHHHHCCCCCCCCCC	27.58	25720772
341	Phosphorylation	QRRSSSHYDLPRVGN HHHCCCCCCCCCCCC	22.56	29996109
353	Phosphorylation	VGNEIAASSSSATEE CCCHHHHCCCCCCCC	23.02	25720772
354	Phosphorylation	GNEIAASSSSATEEN CCHHHHCCCCCCCCC	24.48	25720772
355	Phosphorylation	NEIAASSSSATEENH CHHHHCCCCCCCCCC	22.84	28889911
356	Phosphorylation	EIAASSSSATEENH- HHHHCCCCCCCCCC-	40.95	25720772
358	Phosphorylation	AASSSSATEENH--- HHCCCCCCCCCC---	45.86	25720772

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 PCY1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PCY1_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 PCY1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PCY1_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of PCY1_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-315; SER-319; THR-323AND SER-355, AND MASS SPECTROMETRY.	18257517 [Abstract]