dbPTM

ESF1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ESF1_SCHPO
UniProt AC	O74828
Protein Name	Pre-rRNA-processing protein esf1
Gene Name	esf1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	682
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Involved in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2 (By similarity)..
Protein Sequence	MGKKQTKPINAKSRSESNVVADPRFQSVHSDPRFSRLKRGNFKVKVDERFKSLKEDKDFKTTASVDRYGRPLNQDKATKEIDRLYELENEGSSSSSESSEITDNEEVASASSKSTKSEELTDEESEDEEVYDPARGEGIISTSESSDESDAESETEAQPEISELAGIEPEENIPRGSETNRLAVVNMDWDNLQAVDLFVALSSFCPPGGKLLKVSIYPSEFGKSRMAAEHVQGPPRDIFTPADNQPSSAELHEAQKFGFDNNESDQDEEDALIEEDLGNEFDMVKLRQYQLERLRYYYAVVECDSVRTAKVIYETCDGAEYETSANIYDLRFIPDDVTFDDDESREVCTKAPEKYEPRDFVTDALQHSKVKLSWDAEDPHRKDLIKKAFTSQDIEDLDFSAYIASSESEDEDVDVIRSRYQKLLSGDADDFQANSNPFEDDDKLEGANGEMEVTFTSGFDVDNNANSSEKDETTIEKYKRKAAERKQRRKELRQLKKTKDDEGEGSDVDLGFDDPFFKDKDASRNNKKNKKGKHTQIEDPTAASKEELENLVREDENDSEQLDHFDMKSILKAEKFKKNRKLKKKASNLEGLQEGFEADVSDPRFAALYTNHNFALDPTNPHFKRTKTVEKIMDESRKRRSNQLEQTQDGKPELKIKKRKAEKGDQRQELDRIVKSIKRSGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
114	Phosphorylation	VASASSKSTKSEELT HHHHCCCCCCCCCCC	42.91	25720772
115	Phosphorylation	ASASSKSTKSEELTD HHHCCCCCCCCCCCC	42.18	25720772
117	Phosphorylation	ASSKSTKSEELTDEE HCCCCCCCCCCCCCC	36.07	28889911
121	Phosphorylation	STKSEELTDEESEDE CCCCCCCCCCCCCCC	44.65	28889911
125	Phosphorylation	EELTDEESEDEEVYD CCCCCCCCCCCCCCC	48.58	28889911
247	Phosphorylation	TPADNQPSSAELHEA CCCCCCCCHHHHHHH	32.20	29996109
248	Phosphorylation	PADNQPSSAELHEAQ CCCCCCCHHHHHHHH	32.23	28889911
264	Phosphorylation	FGFDNNESDQDEEDA HCCCCCCCCCCHHHH	42.57	24763107
498	Phosphorylation	ELRQLKKTKDDEGEG HHHHHHHCCCCCCCC	37.81	21712547
506	Phosphorylation	KDDEGEGSDVDLGFD CCCCCCCCCCCCCCC	30.11	28889911
559	Phosphorylation	VREDENDSEQLDHFD HHCCCCCHHHCCCCC	38.53	21712547
641	Phosphorylation	DESRKRRSNQLEQTQ HHHHHHHHHHHHHCC	32.72	24763107

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 ESF1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ESF1_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 ESF1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ESF1_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of ESF1_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-117; THR-121; SER-125AND SER-506, AND MASS SPECTROMETRY.	18257517 [Abstract]