YHY2_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YHY2_YEAST
• UniProt AC: P38870
• Protein Name: Uncharacterized protein YHR182W
• Gene Name: YHR182W
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 785
• Protein Sequence: MSVKEHNEEDIIGDELQNSRQLSIDCDSVKISLRNTYWTKDYTTGIKLFIKHMKRENDLLIKDIKFYNDFVNKFWKPTLNNLQKMEATNSMNSRLLEVMSKQFNIISTEQVERDCKIPLQELRDLNESFLREAENDLSSRYSAYIKDLVAAKEALIGCEKRVQSIYKLKKANTPVENSSSVFDNGKDSAPLTRLNFVCEFPYTLDERLKFEDCDQFMSFLQTLKGKVILEKSVFSVPGLSNQSFQGRSLIKELKKLEPRLNLSLFNIDRIGNEFIQLGIIQEYSLSFYSSKVSQFDQEKYYYWNSEVLATQESNGNAGNRKKKSYGELTHSDNEHEEKSNVSSIKTSISDWIRKVSQHDNDDCDAAGSTDMNKNEWKSLKQQLESSQDIFFSKCCQLEYSKVQLEKTIYDYCKNYSKMEDGIKRALESSNMMFQQKCEKFTDSPVCSLQEAQLPQETANADVRGFFLRDNGIPFRRWNILEASDPVDACKEISIKSEKFFCGSEINNELAALDTLGAIKIILRQIEKEPNANKVIQSWHRDIDFVRVSNLKRDLLGEFKGSKTTENTNSIITAHFFENSHSYVTNDLVGLIKLWLLELPDSLIPSNHYDDLIKAEKSLTSLCEQFPTSSLRFLQELANHFQLINSKYSLPPQTIQDLFRDNSDIDIPLAHHFVRRTGLQNPIDIKILSPTLSTFFINERTVETLQTLIANRITTATTATLTEPPTIIIKDTTAPIHSTPKPPPNDKDGHFIPRPFKTSSTPTTPERPKRKSGLFLPINVNDVPST

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVKEHNEE ------CCCCCCCHH	41.73	22814378
23	Phosphorylation	LQNSRQLSIDCDSVK HHHCCEEEECCCEEE	14.19	21440633
173	Phosphorylation	YKLKKANTPVENSSS HHHHHCCCCCCCCCC	33.30	21440633
178	Phosphorylation	ANTPVENSSSVFDNG CCCCCCCCCCCCCCC	15.52	21440633
188	Phosphorylation	VFDNGKDSAPLTRLN CCCCCCCCCCCEEEE	34.96	27017623
329	Phosphorylation	KKSYGELTHSDNEHE CCCCCCCCCCCCCCC	18.28	21440633
331	Phosphorylation	SYGELTHSDNEHEEK CCCCCCCCCCCCCHH	36.57	22369663
346	Phosphorylation	SNVSSIKTSISDWIR CCHHHHHHHHHHHHH	29.62	19779198
349	Phosphorylation	SSIKTSISDWIRKVS HHHHHHHHHHHHHHH	27.02	21440633
356	Phosphorylation	SDWIRKVSQHDNDDC HHHHHHHHHCCCCCC	25.49	28889911
738	Phosphorylation	TTAPIHSTPKPPPND CCCCCCCCCCCCCCC	22.59	21440633
757	Phosphorylation	FIPRPFKTSSTPTTP CCCCCCCCCCCCCCC	28.43	22369663
758	Phosphorylation	IPRPFKTSSTPTTPE CCCCCCCCCCCCCCC	32.57	22369663
759	Phosphorylation	PRPFKTSSTPTTPER CCCCCCCCCCCCCCC	43.57	22369663
760	Phosphorylation	RPFKTSSTPTTPERP CCCCCCCCCCCCCCC	25.15	22369663
762	Phosphorylation	FKTSSTPTTPERPKR CCCCCCCCCCCCCCC	55.88	22369663
763	Phosphorylation	KTSSTPTTPERPKRK CCCCCCCCCCCCCCC	25.10	22369663
771	Phosphorylation	PERPKRKSGLFLPIN CCCCCCCCCCCCCCC	44.77	21440633

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of YHY2_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of YHY2_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of YHY2_YEAST !!

Protein-Protein Interaction

Oops, there are no PPI records of YHY2_YEAST !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-331, AND MASSSPECTROMETRY.
PubMed: 18407956