TF3B_YEAST - dbPTM
TF3B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TF3B_YEAST
UniProt AC P29056
Protein Name Transcription factor IIIB 70 kDa subunit
Gene Name BRF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 596
Subcellular Localization Nucleus.
Protein Description General activator of RNA polymerase III transcription. Interacts with TBP. Binds to Pol III subunit C34 and to the TAU135 component of TFIIIC..
Protein Sequence MPVCKNCHGTEFERDLSNANNDLVCKACGVVSEDNPIVSEVTFGETSAGAAVVQGSFIGAGQSHAAFGGSSALESREATLNNARRKLRAVSYALHIPEYITDAAFQWYKLALANNFVQGRRSQNVIASCLYVACRKEKTHHMLIDFSSRLQVSVYSIGATFLKMVKKLHITELPLADPSLFIQHFAEKLDLADKKIKVVKDAVKLAQRMSKDWMFEGRRPAGIAGACILLACRMNNLRRTHTEIVAVSHVAEETLQQRLNEFKNTKAAKLSVQKFRENDVEDGEARPPSFVKNRKKERKIKDSLDKEEMFQTSEEALNKNPILTQVLGEQELSSKEVLFYLKQFSERRARVVERIKATNGIDGENIYHEGSENETRKRKLSEVSIQNEHVEGEDKETEGTEEKVKKVKTKTSEEKKENESGHFQDAIDGYSLETDPYCPRNLHLLPTTDTYLSKVSDDPDNLEDVDDEELNAHLLNEEASKLKERIWIGLNADFLLEQESKRLKQEADIATGNTSVKKKRTRRRNNTRSDEPTKTVDAAAAIGLMSDLQDKSGLHAALKAAEESGDFTTADSVKNMLQKASFSKKINYDAIDGLFR
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
128PhosphorylationRSQNVIASCLYVACR
CCHHHHHHHHHHHHC		8.1125704821
274AcetylationAAKLSVQKFRENDVE
HHHHHHHHHHHCCCC		44.2125381059
358PhosphorylationVVERIKATNGIDGEN
HHHHHHHHCCCCCCC		29.0419823750
367PhosphorylationGIDGENIYHEGSENE
CCCCCCCCCCCCCCH		12.8521440633
371PhosphorylationENIYHEGSENETRKR
CCCCCCCCCCHHHHH		33.9721440633
375PhosphorylationHEGSENETRKRKLSE
CCCCCCHHHHHHHHH		53.7419823750
381PhosphorylationETRKRKLSEVSIQNE
HHHHHHHHHHCCCCC		38.7019823750
384PhosphorylationKRKLSEVSIQNEHVE
HHHHHHHCCCCCCCC		17.8819823750
546PhosphorylationAAAIGLMSDLQDKSG
HHHHHHHHHHCCHHH		39.9630377154
564PhosphorylationALKAAEESGDFTTAD
HHHHHHHHCCCCCHH		34.8627214570
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 TF3B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TF3B_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 TF3B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_YEASTSPT15physical
10788514
TFC4_YEASTTFC4physical
12930823
RPC6_YEASTRPC34physical
10329159
TFC4_YEASTTFC4physical
10329159
MAF1_YEASTMAF1physical
15590667
RPC9_YEASTRPC17physical
10611227
TFC4_YEASTTFC4physical
10393904
RPC6_YEASTRPC34physical
8407894
TFC1_YEASTTFC1physical
7797524
TFC5_YEASTBDP1physical
7568218
TFC5_YEASTBDP1genetic
10329159
TBP_YEASTSPT15genetic
10329159
RPC6_YEASTRPC34genetic
10329159
SLX5_YEASTSLX5genetic
17314980
BUD27_YEASTBUD27genetic
17314980
GCN20_YEASTGCN20genetic
17314980
HST4_YEASTHST4genetic
17314980
AIM4_YEASTAIM4genetic
17314980
SLX8_YEASTSLX8genetic
17314980
SMC2_YEASTSMC2physical
18708579
RPC1_YEASTRPO31physical
24277937
RPC2_YEASTRET1physical
24277937
RPC9_YEASTRPC17physical
24277937
TBP_YEASTSPT15physical
24277937
RPC6_YEASTRPC34physical
24277937
TFC5_YEASTBDP1physical
24277937
MOD5_YEASTMOD5physical
23898186
TFC5_YEASTBDP1physical
26055328
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TF3B_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-384, AND MASSSPECTROMETRY.
"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-381 AND SER-384, ANDMASS SPECTROMETRY.

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