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P34111 (TFC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor tau 138 kDa subunit
Alternative name(s):
TFIIIC 138 kDa subunit
Transcription factor C subunit 3
Gene names
Name:TFC3
Synonyms:TSV115
Ordered Locus Names:YAL001C
ORF Names:FUN24
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. TFC3 is essential for cell viability. Cooperates with TFC6 in DNA binding. Ref.1 Ref.6 Ref.9

Subunit structure

Component of the TFIIIC complex composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are organized in two globular domains, tauA and tauB, connected by a proteolysis-sensitive and flexible linker. Interacts with TFC1, TFC4 and TFC6. Ref.1 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus. Mitochondrion Ref.11 Ref.13 Ref.14.

Miscellaneous

Present with 125 molecules/cell in log phase SD medium.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11601160Transcription factor tau 138 kDa subunit
PRO_0000072497

Amino acid modifications

Modified residue5461Phosphoserine Ref.15

Experimental info

Mutagenesis3491G → E in TSV115; thermosensitive. Level of TFIIIC and its affinity for tDNA reduced. tDNA binding activity very sensitive to mild heat treatments, and TFIIIC-DNA interaction inhibited at moderate salt concentrations. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P34111 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 3ACB7893ED536581

FASTA1,160132,108
        10         20         30         40         50         60 
MVLTIYPDEL VQIVSDKIAS NKGKITLNQL WDISGKYFDL SDKKVKQFVL SCVILKKDIE 

        70         80         90        100        110        120 
VYCDGAITTK NVTDIIGDAN HSYSVGITED SLWTLLTGYT KKESTIGNSA FELLLEVAKS 

       130        140        150        160        170        180 
GEKGINTMDL AQVTGQDPRS VTGRIKKINH LLTSSQLIYK GHVVKQLKLK KFSHDGVDSN 

       190        200        210        220        230        240 
PYINIRDHLA TIVEVVKRSK NGIRQIIDLK RELKFDKEKR LSKAFIAAIA WLDEKEYLKK 

       250        260        270        280        290        300 
VLVVSPKNPA IKIRCVKYVK DIPDSKGSPS FEYDSNSADE DSVSDSKAAF EDEDLVEGLD 

       310        320        330        340        350        360 
NFNATDLLQN QGLVMEEKED AVKNEVLLNR FYPLQNQTYD IADKSGLKGI STMDVVNRIT 

       370        380        390        400        410        420 
GKEFQRAFTK SSEYYLESVD KQKENTGGYR LFRIYDFEGK KKFFRLFTAQ NFQKLTNAED 

       430        440        450        460        470        480 
EISVPKGFDE LGKSRTDLKT LNEDNFVALN NTVRFTTDSD GQDIFFWHGE LKIPPNSKKT 

       490        500        510        520        530        540 
PNKNKRKRQV KNSTNASVAG NISNPKRIKL EQHVSTAQEP KSAEDSPSSN GGTVVKGKVV 

       550        560        570        580        590        600 
NFGGFSARSL RSLQRQRAIL KVMNTIGGVA YLREQFYESV SKYMGSTTTL DKKTVRGDVD 

       610        620        630        640        650        660 
LMVESEKLGA RTEPVSGRKI IFLPTVGEDA IQRYILKEKD SKKATFTDVI HDTEIYFFDQ 

       670        680        690        700        710        720 
TEKNRFHRGK KSVERIRKFQ NRQKNAKIKA SDDAISKKST SVNVSDGKIK RRDKKVSAGR 

       730        740        750        760        770        780 
TTVVVENTKE DKTVYHAGTK DGVQALIRAV VVTKSIKNEI MWDKITKLFP NNSLDNLKKK 

       790        800        810        820        830        840 
WTARRVRMGH SGWRAYVDKW KKMLVLAIKS EKISLRDVEE LDLIKLLDIW TSFDEKEIKR 

       850        860        870        880        890        900 
PLFLYKNYEE NRKKFTLVRD DTLTHSGNDL AMSSMIQREI SSLKKTYTRK ISASTKDLSK 

       910        920        930        940        950        960 
SQSDDYIRTV IRSILIESPS TTRNEIEALK NVGNESIDNV IMDMAKEKQI YLHGSKLECT 

       970        980        990       1000       1010       1020 
DTLPDILENR GNYKDFGVAF QYRCKVNELL EAGNAIVINQ EPSDISSWVL IDLISGELLN 

      1030       1040       1050       1060       1070       1080 
MDVIPMVRNV RPLTYTSRRF EIRTLTPPLI IYANSQTKLN TARKSAVKVP LGKPFSRLWV 

      1090       1100       1110       1120       1130       1140 
NGSGSIRPNI WKQVVTMVVN EIIFHPGITL SRLQSRCREV LSLHEISEIC KWLLERQVLI 

      1150       1160 
TTDFDGYWVN HNWYSIYEST 

« Hide

References

« Hide 'large scale' references
[1]"TFC3: gene encoding the B-block binding subunit of the yeast transcription factor IIIC."
Lefebvre O., Carles C., Conesa C., Swanson R.N., Bouet F., Riva M., Sentenac A.
Proc. Natl. Acad. Sci. U.S.A. 89:10512-10516(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 124-143; 331-347; 440-453; 508-520 AND 539-547, FUNCTION, IDENTIFICATION IN TFIIIC.
Strain: ATCC 204508 / S288c.
[2]"A mutation in the largest subunit of yeast TFIIIC affects tRNA and 5 S RNA synthesis. Identification of two classes of suppressors."
Lefebvre O., Rueth J., Sentenac A.
J. Biol. Chem. 269:23374-23381(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-349.
[3]"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Two polypeptide chains in yeast transcription factor tau interact with DNA."
Gabrielsen O.S., Marzouki N., Ruet A., Sentenac A., Fromageot P.
J. Biol. Chem. 264:7505-7511(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Purification and characterization of Saccharomyces cerevisiae transcription factor TFIIIC. Polypeptide composition defined with polyclonal antibodies."
Parsons M.C., Weil P.A.
J. Biol. Chem. 265:5095-5103(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN TFIIIC.
[8]"On the subunit composition, stoichiometry, and phosphorylation of the yeast transcription factor TFIIIC/tau."
Conesa C., Swanson R.N., Schultz P., Oudet P., Sentenac A.
J. Biol. Chem. 268:18047-18052(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TFC1; TFC4 AND TFC6, PHOSPHORYLATION.
[9]"Tau91, an essential subunit of yeast transcription factor IIIC, cooperates with tau138 in DNA binding."
Arrebola R., Manaud N., Rozenfeld S., Marsolier M.C., Lefebvre O., Carles C., Thuriaux P., Conesa C., Sentenac A.
Mol. Cell. Biol. 18:1-9(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The tau95 subunit of yeast TFIIIC influences upstream and downstream functions of TFIIIC.DNA complexes."
Jourdain S., Acker J., Ducrot C., Sentenac A., Lefebvre O.
J. Biol. Chem. 278:10450-10457(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TFC1 AND TFC6.
[11]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[14]"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[15]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M98261 Genomic DNA. Translation: AAA34378.1.
L22015 Genomic DNA. Translation: AAC04956.1.
BK006935 Genomic DNA. Translation: DAA06985.1.
PIRA46423.
RefSeqNP_009400.1. NM_001178148.1.

3D structure databases

ProteinModelPortalP34111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31789. 38 interactions.
DIPDIP-6739N.
IntActP34111. 3 interactions.
MINTMINT-636763.
STRING4932.YAL001C.

Proteomic databases

PaxDbP34111.
PeptideAtlasP34111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL001C; YAL001C; YAL001C.
GeneID851262.
KEGGsce:YAL001C.

Organism-specific databases

CYGDYAL001c.
SGDS000000001. TFC3.

Phylogenomic databases

eggNOGNOG72796.
HOGENOMHOG000142056.
KOK15204.
OMAMSSMIQR.
OrthoDBEOG7RRFGW.

Enzyme and pathway databases

BioCycYEAST:G3O-28816-MONOMER.
ReactomeREACT_87991. Transcription.
REACT_98256. Gene Expression.

Gene expression databases

GenevestigatorP34111.

Family and domain databases

InterProIPR007309. TFIIIC_Bblock-bd.
[Graphical view]
PfamPF04182. B-block_TFIIIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968222.

Entry information

Entry nameTFC3_YEAST
AccessionPrimary (citable) accession number: P34111
Secondary accession number(s): D6VPL5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD