dbPTM

LEUC_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LEUC_SCHPO
UniProt AC	O14289
Protein Name	3-isopropylmalate dehydratase
Gene Name	leu2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	758
Subcellular Localization
Protein Description	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate..
Protein Sequence	MSPSVASPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASFIHQPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNVRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKDAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFGDVSNGSPSIITNKNYDPSHDVEGDIGLSVDDATDAVTDADGIATNVAGSVSSGSAGIPKFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADGKEIPDFVLNREPYRHATVLVAHDNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQVKFSVDLVNQTITYGDKQVKFDVEPFRKHCLVNGLDDIGLTLQKETMIDAFEAAREENFPWMNIKRSRARLSPVKSNKQSSSRNDW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MSPSVASPKTL ----CCCCCCCCCCH	24.02	19547744
84	Phosphorylation	KDMKDIASFIHQPDS CCHHHHHHHHCCCCC	25.68	25720772
230	Phosphorylation	LSMEARMSMCNMSIE CCHHHHHHHHCCCHH	18.03	25720772
358	Phosphorylation	IDKVFIGSCTNSRIE CCEEEEECCCCCCHH	16.98	28889911
360	Phosphorylation	KVFIGSCTNSRIEDL EEEEECCCCCCHHHH	37.62	25720772
362	Phosphorylation	FIGSCTNSRIEDLRL EEECCCCCCHHHHHH	19.24	25720772
483	Phosphorylation	REFFGDVSNGSPSII HHHHCCCCCCCCCEE	39.97	29996109
486	Phosphorylation	FGDVSNGSPSIITNK HCCCCCCCCCEEECC	21.52	28889911
488	Phosphorylation	DVSNGSPSIITNKNY CCCCCCCCEEECCCC	28.46	28889911
572	Phosphorylation	FLKTIKRTGLGQFAF HHHHHHHHCCCEEEE	31.58	25720772
744	Phosphorylation	KRSRARLSPVKSNKQ CCCHHCCCCCCCCCC	23.30	29996109
748	Phosphorylation	ARLSPVKSNKQSSSR HCCCCCCCCCCCCCC	49.87	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 LEUC_SCHPO !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
YOFG_SCHPO	SPBP4H10.16c	physical	26771498

Drug and Disease Associations

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

Regulatory Network of LEUC_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-486 AND SER-488, ANDMASS SPECTROMETRY.	18257517 [Abstract]