TOD6_YEAST - dbPTM
TOD6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOD6_YEAST
UniProt AC P34219
Protein Name Transcriptional regulatory protein TOD6
Gene Name TOD6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 525
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the RPD3 histone deacetylase complex RPD3C(L) 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. TOD6 binds to sequences containing the core CGATG, which resembles the PAC (Polymerase A and C) motif..
Protein Sequence MTLPKLSSVSVSSGHVSANSHGFSILSKHPHPNNLVHSHSLSHTNAKSHLPISSTSTKENSTNKEEAESLKKNNPSSWDPSDDIKLRHLKEIKNLGWKEIAHHFPNRTPNACQFRWRRLKSGNLKSNKTAVIDINKLFGVYATGDATPSAGTPSAEEAVKEEAVEDEDITAGSSAIEDSPPDFKPLVKPKYMDRKLITQRSTSTFSDHEPQHTKPRKLFVKPRSFSHSITTNTPNVKTAQQTNLSLYNTTSAKTNKAVNSNDYENIGLVPKIIIRSRRNSFIPSTQIPHSTTKTRKNSHSVISSRRSSFNMMHSRRSSFNSHAPTEPISRRASLVVSPYMSPRRLSTSQSVHYHPQHQYYLNPIASPNCKTDHANDKITHTRTFLDMQKFANKHPWSREDDEVLLNNTKDKQNHLSPLEISIVLPNNRSELEIQQRMDYLKRKGRVSGFHTNEGCKDEEEEDDIDPLHKENGINTPSQQSQNYGMLEAKHDNPKSSELSSMTSANDIRNEQDELPGINSIFKNIF
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 Orthologous
Protein Cluster
17PhosphorylationSVSSGHVSANSHGFS
EEECCCEECCCCCEE		18.9628132839
71AcetylationKEEAESLKKNNPSSW
HHHHHHHHHCCCCCC		63.8425381059
72UbiquitinationEEAESLKKNNPSSWD
HHHHHHHHCCCCCCC		68.2215699485
85UbiquitinationWDPSDDIKLRHLKEI
CCCCHHHHHHHHHHH		46.6015699485
85AcetylationWDPSDDIKLRHLKEI
CCCCHHHHHHHHHHH		46.6024489116
125AcetylationRLKSGNLKSNKTAVI
ECCCCCCCCCCEEEE		56.8525381059
141PhosphorylationINKLFGVYATGDATP
HHHHHEEEECCCCCC		9.9928889911
147PhosphorylationVYATGDATPSAGTPS
EEECCCCCCCCCCCC		23.6328889911
149PhosphorylationATGDATPSAGTPSAE
ECCCCCCCCCCCCHH		34.6728889911
152PhosphorylationDATPSAGTPSAEEAV
CCCCCCCCCCHHHHH		17.4928132839
173PhosphorylationDEDITAGSSAIEDSP
CCCCCCCCHHHCCCC		17.7121551504
179PhosphorylationGSSAIEDSPPDFKPL
CCHHHCCCCCCCCCC		26.0728889911
201PhosphorylationRKLITQRSTSTFSDH
CEEECCCCCCCCCCC		19.5228132839
203PhosphorylationLITQRSTSTFSDHEP
EECCCCCCCCCCCCC		28.8028889911
206PhosphorylationQRSTSTFSDHEPQHT
CCCCCCCCCCCCCCC		37.8421440633
224PhosphorylationKLFVKPRSFSHSITT
EEEECCCCCCCCCCC		39.3621082442
226PhosphorylationFVKPRSFSHSITTNT
EECCCCCCCCCCCCC		19.9925533186
228PhosphorylationKPRSFSHSITTNTPN
CCCCCCCCCCCCCCC		22.0419684113
230PhosphorylationRSFSHSITTNTPNVK
CCCCCCCCCCCCCCC		19.6027717283
231PhosphorylationSFSHSITTNTPNVKT
CCCCCCCCCCCCCCC		35.1127717283
237UbiquitinationTTNTPNVKTAQQTNL
CCCCCCCCCCCCCCC		44.7915699485
245PhosphorylationTAQQTNLSLYNTTSA
CCCCCCCCCEECCCC		30.7721551504
256UbiquitinationTTSAKTNKAVNSNDY
CCCCCCCCCCCCCCC		59.9715699485
271UbiquitinationENIGLVPKIIIRSRR
CCCCCCCEEEEECCC		38.7715699485
276PhosphorylationVPKIIIRSRRNSFIP
CCEEEEECCCCCCCC		25.7819684113
280PhosphorylationIIRSRRNSFIPSTQI
EEECCCCCCCCCCCC		23.8125533186
284PhosphorylationRRNSFIPSTQIPHST
CCCCCCCCCCCCCCC		28.2924961812
298PhosphorylationTTKTRKNSHSVISSR
CCCCCCCCCCHHHCC		21.8528889911
300PhosphorylationKTRKNSHSVISSRRS
CCCCCCCCHHHCCCH		22.4419684113
303PhosphorylationKNSHSVISSRRSSFN
CCCCCHHHCCCHHHH		18.6819684113
304PhosphorylationNSHSVISSRRSSFNM
CCCCHHHCCCHHHHH		22.1619684113
307PhosphorylationSVISSRRSSFNMMHS
CHHHCCCHHHHHHHC		37.8728889911
308PhosphorylationVISSRRSSFNMMHSR
HHHCCCHHHHHHHCC		20.8728889911
314PhosphorylationSSFNMMHSRRSSFNS
HHHHHHHCCHHHCCC		16.1128889911
317PhosphorylationNMMHSRRSSFNSHAP
HHHHCCHHHCCCCCC		37.8729136822
318PhosphorylationMMHSRRSSFNSHAPT
HHHCCHHHCCCCCCC		27.0025533186
321PhosphorylationSRRSSFNSHAPTEPI
CCHHHCCCCCCCCCC		21.0024909858
325PhosphorylationSFNSHAPTEPISRRA
HCCCCCCCCCCCCHH		56.0028889911
329PhosphorylationHAPTEPISRRASLVV
CCCCCCCCCHHHEEE		26.8225533186
333PhosphorylationEPISRRASLVVSPYM
CCCCCHHHEEECCCC		21.6419684113
337PhosphorylationRRASLVVSPYMSPRR
CHHHEEECCCCCCCC		11.6625752575
339PhosphorylationASLVVSPYMSPRRLS
HHEEECCCCCCCCCC		11.6119684113
341PhosphorylationLVVSPYMSPRRLSTS
EEECCCCCCCCCCCC		14.9325533186
366PhosphorylationYYLNPIASPNCKTDH
EECCCCCCCCCCCCC		19.8417330950
377AcetylationKTDHANDKITHTRTF
CCCCCCCCCCCCHHH		49.6825381059
383PhosphorylationDKITHTRTFLDMQKF
CCCCCCHHHHHHHHH		29.7021440633
389AcetylationRTFLDMQKFANKHPW
HHHHHHHHHHHCCCC		39.5425381059
393AcetylationDMQKFANKHPWSRED
HHHHHHHCCCCCCCC		47.8425381059
475PhosphorylationHKENGINTPSQQSQN
HHHCCCCCHHHHHHH		23.5421440633
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 TOD6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOD6_YEAST !!
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 TOD6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOT6_YEASTDOT6genetic
19158363
HAP3_YEASTHAP3genetic
20959818
UBP3_YEASTUBP3genetic
20959818
CCS1_YEASTCCS1genetic
20959818
SDS3_YEASTSDS3genetic
21730963
RPD3_YEASTRPD3genetic
21730963
SDS3_YEASTSDS3physical
21730963
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOD6_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-224, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASSSPECTROMETRY.

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