UniProt ID | HOS3_YEAST | |
---|---|---|
UniProt AC | Q02959 | |
Protein Name | Histone deacetylase HOS3 | |
Gene Name | HOS3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 697 | |
Subcellular Localization | Nucleus. | |
Protein Description | Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).. | |
Protein Sequence | MSSKHSDPLERFYKQFQAFVQNNPNVISAARAAAQIPESAKAVVVLSPYSLQHVFPREWVTKSYRKTIVERPERLLASSMGISAAITMYPSLFTLKSSHQRKGSLMAPHVLKVHGSSWPAELIELCQMADAKLLKGEIEVPDTWNSGDIYLSSKTIKALQGTIGAIETGVDSIFKGPSAEHISNRAFVAIRPPGHHCHYGTPSGFCLLNNAHVAIEYAYDTYNVTHVVVLDFDLHHGDGTQDICWKRAGFKPEEEPEDSSYDDFGKKFAEFPKVGYFSMHDINSFPTESGFATKENIKNASTCIMNSHDLNIWNIHLSKWTTEEEFNVLYRTKYRTLFAKADEFFRSAKLEMNQQGRPFKGLVVISAGFDASEFEQTSMQRHSVNVPTSFYTTFTKDALKLAQMHCHGKVLSLMEGGYSDKAICSGVFAHLIGLQNQDWVKEWGSEQVVKEIVRGCKPAWKPYKTKRAKDVIRIWAEEVIRLGRAMIPEFDDIIFKDAVNSAPSNSLLKATVEPASTSTIAQRIIRSHRSNASPEKELHENKPRSTEKQEQREIRSDTKVKQLSSNNRAAETQIPFLQQEFSSEDEDEEYVYDEELNKTFNRTVEDITIDDISRHLETLEIEKKGDEDSDHELKEKNWKNSHQRRLQGNGMYKIPSNTKPHRIRQPQNANTPTYDDSDISMISHVSRKHTTRSGGRW | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
259 | Phosphorylation | PEEEPEDSSYDDFGK CCCCCCCCCCCCHHH | 29.18 | 20377248 | |
260 | Phosphorylation | EEEPEDSSYDDFGKK CCCCCCCCCCCHHHH | 44.92 | 29136822 | |
261 | Phosphorylation | EEPEDSSYDDFGKKF CCCCCCCCCCHHHHH | 24.39 | 20377248 | |
276 | Phosphorylation | AEFPKVGYFSMHDIN HHCCCEEEEEHHCCC | 8.75 | 20377248 | |
284 | Phosphorylation | FSMHDINSFPTESGF EEHHCCCCCCCCCCC | 32.70 | 20377248 | |
293 | Phosphorylation | PTESGFATKENIKNA CCCCCCCCHHHHCCC | 36.31 | 20377248 | |
332 | Phosphorylation | EFNVLYRTKYRTLFA HHHHHHHHCHHHHHH | 20.90 | 19779198 | |
336 | Phosphorylation | LYRTKYRTLFAKADE HHHHCHHHHHHHHHH | 24.12 | 19779198 | |
412 | Phosphorylation | HCHGKVLSLMEGGYS HHCCHHHHHHCCCCC | 28.76 | 19684113 | |
501 | Phosphorylation | IFKDAVNSAPSNSLL EHHHHHHCCCCCCCC | 34.65 | 27214570 | |
504 | Phosphorylation | DAVNSAPSNSLLKAT HHHHCCCCCCCCEEE | 38.47 | 27214570 | |
506 | Phosphorylation | VNSAPSNSLLKATVE HHCCCCCCCCEEECC | 39.14 | 21551504 | |
516 | Phosphorylation | KATVEPASTSTIAQR EEECCCCCHHHHHHH | 33.34 | 27214570 | |
517 | Phosphorylation | ATVEPASTSTIAQRI EECCCCCHHHHHHHH | 31.81 | 28889911 | |
518 | Phosphorylation | TVEPASTSTIAQRII ECCCCCHHHHHHHHH | 18.47 | 21440633 | |
533 | Phosphorylation | RSHRSNASPEKELHE HHHHCCCCHHHHHHC | 37.53 | 21082442 | |
536 | Acetylation | RSNASPEKELHENKP HCCCCHHHHHHCCCC | 69.80 | 25381059 | |
542 | Acetylation | EKELHENKPRSTEKQ HHHHHCCCCCCHHHH | 38.53 | 25381059 | |
548 | Acetylation | NKPRSTEKQEQREIR CCCCCHHHHHHHHHH | 60.26 | 25381059 | |
558 | Phosphorylation | QREIRSDTKVKQLSS HHHHHHHHHHHHHHH | 38.70 | 21551504 | |
582 | Phosphorylation | PFLQQEFSSEDEDEE CHHHHHCCCCCCCCC | 31.87 | 21440633 | |
583 | Phosphorylation | FLQQEFSSEDEDEEY HHHHHCCCCCCCCCE | 55.15 | 28152593 | |
590 | Phosphorylation | SEDEDEEYVYDEELN CCCCCCCEECHHHHH | 11.40 | 19795423 | |
592 | Phosphorylation | DEDEEYVYDEELNKT CCCCCEECHHHHHHH | 19.41 | 19779198 | |
599 | Phosphorylation | YDEELNKTFNRTVED CHHHHHHHCCCCHHH | 25.68 | 21440633 | |
603 | Phosphorylation | LNKTFNRTVEDITID HHHHCCCCHHHCCHH | 29.38 | 22369663 | |
608 | Phosphorylation | NRTVEDITIDDISRH CCCHHHCCHHHHHHH | 30.58 | 22369663 | |
613 | Phosphorylation | DITIDDISRHLETLE HCCHHHHHHHHHHEE | 22.20 | 28889911 | |
623 | Acetylation | LETLEIEKKGDEDSD HHHEEHHHCCCCCCH | 68.65 | 22865919 | |
629 | Phosphorylation | EKKGDEDSDHELKEK HHCCCCCCHHHHHHH | 38.53 | 25521595 | |
656 | Phosphorylation | NGMYKIPSNTKPHRI CCCCCCCCCCCCCCC | 61.68 | 27017623 |
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 HOS3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HOS3_YEAST !! |
* 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 HOS3_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"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-533 AND SER-629, ANDMASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND MASSSPECTROMETRY. |