dbPTM

KSP1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KSP1_SCHPO
UniProt AC	O14328
Protein Name	Serine/threonine-protein kinase ksp1
Gene Name	ksp1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	474
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description
Protein Sequence	MKLLQKKGYKVERPLNKGSYGTVVLAHRLFRTPRCKDLKYAIKCIKKPAYTFLQEVNILRQLSRSRHRNIIHFVESFEDNVYYYVVLEYCPLGDLYECILNNDFPNAKNQPEMIKNIFLQIIDGVAHLHSHGIYHRDLKPENFLLSLSEDGSELVVKISDFGLACRDKISYDFGTGSDRYMAPEQFEEVDGAGYSPRAADIWALGICLLNLIFARNPFTYPHEKDPIFADYMLDAMTLFDVFPTLSQDTYNVLRACLCVSPEKRSLAKTREAVLAVTKWTTDDEELESFVNEEEEFRASDFMPAEDNVRCTQSDREPLRTPSVLTPANTIQRGLLPSKLPALSDVDENISTSSSPRSPASLAPVNNSERSYDSGLGESLNNMHIGKSIATAVPVNTKRSPYSCSAPAIVFPNSIKGNKDHLKFGRSWCDMDEEDEEDIVSFGSNDDFGASDELSSKHIGLADDWNVLSQWNDNS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
320	Phosphorylation	SDREPLRTPSVLTPA CCCCCCCCCCCCCCC	27.83	29996109
322	Phosphorylation	REPLRTPSVLTPANT CCCCCCCCCCCCCHH	29.19	29996109
350	Phosphorylation	SDVDENISTSSSPRS CCCCCCCCCCCCCCC	33.54	25720772
351	Phosphorylation	DVDENISTSSSPRSP CCCCCCCCCCCCCCC	28.91	25720772
352	Phosphorylation	VDENISTSSSPRSPA CCCCCCCCCCCCCCC	23.25	25720772
353	Phosphorylation	DENISTSSSPRSPAS CCCCCCCCCCCCCCC	44.44	28889911
354	Phosphorylation	ENISTSSSPRSPASL CCCCCCCCCCCCCCC	24.89	28889911
357	Phosphorylation	STSSSPRSPASLAPV CCCCCCCCCCCCCCC	28.36	28889911
360	Phosphorylation	SSPRSPASLAPVNNS CCCCCCCCCCCCCCC	28.57	25720772
370	Phosphorylation	PVNNSERSYDSGLGE CCCCCCCCCCCCCCH	29.28	25720772
371	Phosphorylation	VNNSERSYDSGLGES CCCCCCCCCCCCCHH	21.98	25720772
373	Phosphorylation	NSERSYDSGLGESLN CCCCCCCCCCCHHHH	27.90	28889911
378	Phosphorylation	YDSGLGESLNNMHIG CCCCCCHHHHCCCCC	34.30	28889911
399	Phosphorylation	VPVNTKRSPYSCSAP ECCCCCCCCCCCCCC	29.73	25720772
401	Phosphorylation	VNTKRSPYSCSAPAI CCCCCCCCCCCCCEE	24.45	29996109
402	Phosphorylation	NTKRSPYSCSAPAIV CCCCCCCCCCCCEEE	12.65	21712547
404	Phosphorylation	KRSPYSCSAPAIVFP CCCCCCCCCCEEECC	31.20	28889911
413	Phosphorylation	PAIVFPNSIKGNKDH CEEECCCCCCCCHHH	26.39	28889911

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 KSP1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KSP1_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 KSP1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KSP1_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of KSP1_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; SER-354; SER-357;SER-378; SER-404 AND SER-413, AND MASS SPECTROMETRY.	18257517 [Abstract]