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Q03290

- TFB3_YEAST

UniProt

Q03290 - TFB3_YEAST

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Protein

RNA polymerase II transcription factor B subunit 3

Gene

TFB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as component of the general transcription and DNA repair factor IIH (TFIIH or factor B), which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 6048RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: InterPro
  2. nucleotide-excision repair Source: SGD
  3. phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  4. transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29988-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase II transcription factor B subunit 3
Alternative name(s):
RNA polymerase II transcription factor B 38 kDa subunit
RNA polymerase II transcription factor B p38 subunit
Gene namesi
Name:TFB3
Synonyms:RIG2
Ordered Locus Names:YDR460W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR460w.
SGDiS000002868. TFB3.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. holo TFIIH complex Source: SGD
  2. TFIIK complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321RNA polymerase II transcription factor B subunit 3PRO_0000055942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571Phosphoserine1 Publication
Modified residuei258 – 2581Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03290.
PaxDbiQ03290.
PeptideAtlasiQ03290.

Expressioni

Gene expression databases

GenevestigatoriQ03290.

Interactioni

Subunit structurei

Component of the transcription factor IIH (TFIIH) holo but not the TFIIH core complex. Component of a complex consisting of KIN28, CCL1 and TFB3; the KIN28-CCL1 dimer is known as the TFIIK complex.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCL1P373664EBI-31406,EBI-4385

Protein-protein interaction databases

BioGridi32514. 25 interactions.
DIPiDIP-2398N.
IntActiQ03290. 11 interactions.
MINTiMINT-528793.

Structurei

3D structure databases

ProteinModelPortaliQ03290.
SMRiQ03290. Positions 13-75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 6048RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5220.
GeneTreeiENSGT00390000002319.
HOGENOMiHOG000189680.
InParanoidiQ03290.
KOiK10842.
OMAiRIRQKQA.
OrthoDBiEOG7WMCVV.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR12683. PTHR12683. 1 hit.
PfamiPF06391. MAT1. 1 hit.
[Graphical view]
PIRSFiPIRSF003338. MAT1_metazoa. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00570. cdk7. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03290-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLMDEYEENK DMCPICKTDR YLSPDVKFLV NPECYHRICE SCVDRIFSLG
60 70 80 90 100
PAQCPYKGCD KILRKNKFKT QIFDDVEVEK EVDIRKRVFN VFNKTIDDFN
110 120 130 140 150
GDLVEYNKYL EEVEDIIYKL DHGIDVAKTE EKLRTYEELN KQLIMNNLER
160 170 180 190 200
SRTEIESFEQ RQKFEKEMKL KKRLLERQIE EEERMNKEWT KKEIVNRLST
210 220 230 240 250
TTQDINETIE GVKNTVKLKK SSARRKLEEL NRVLKNNPYF NSNVNVQNSR
260 270 280 290 300
LKDAVPFTPF NGDREAHPRF TLKGSVYNDP FIKDLEHRKE FIASGFNTNY
310 320
AYERVLTEAF MGLGCVISEE L
Length:321
Mass (Da):38,128
Last modified:November 1, 1996 - v1
Checksum:i528D61CF25ADFAF4
GO

Sequence cautioni

The sequence AAB40629.1 differs from that shown. Reason: Frameshift at position 262.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U62805 Genomic DNA. Translation: AAB40629.1. Frameshift.
U33050 Genomic DNA. Translation: AAB64899.1.
BK006938 Genomic DNA. Translation: DAA12294.1.
PIRiS69628.
RefSeqiNP_010748.3. NM_001180768.3.

Genome annotation databases

EnsemblFungiiYDR460W; YDR460W; YDR460W.
GeneIDi852071.
KEGGisce:YDR460W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U62805 Genomic DNA. Translation: AAB40629.1 . Frameshift.
U33050 Genomic DNA. Translation: AAB64899.1 .
BK006938 Genomic DNA. Translation: DAA12294.1 .
PIRi S69628.
RefSeqi NP_010748.3. NM_001180768.3.

3D structure databases

ProteinModelPortali Q03290.
SMRi Q03290. Positions 13-75.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32514. 25 interactions.
DIPi DIP-2398N.
IntActi Q03290. 11 interactions.
MINTi MINT-528793.

Proteomic databases

MaxQBi Q03290.
PaxDbi Q03290.
PeptideAtlasi Q03290.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR460W ; YDR460W ; YDR460W .
GeneIDi 852071.
KEGGi sce:YDR460W.

Organism-specific databases

CYGDi YDR460w.
SGDi S000002868. TFB3.

Phylogenomic databases

eggNOGi COG5220.
GeneTreei ENSGT00390000002319.
HOGENOMi HOG000189680.
InParanoidi Q03290.
KOi K10842.
OMAi RIRQKQA.
OrthoDBi EOG7WMCVV.

Enzyme and pathway databases

BioCyci YEAST:G3O-29988-MONOMER.

Miscellaneous databases

NextBioi 970364.

Gene expression databases

Genevestigatori Q03290.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
PANTHERi PTHR12683. PTHR12683. 1 hit.
Pfami PF06391. MAT1. 1 hit.
[Graphical view ]
PIRSFi PIRSF003338. MAT1_metazoa. 1 hit.
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00570. cdk7. 1 hit.
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair factor IIH. Homology to human cyclin-dependent kinase activating kinase and IIH subunits."
    Feaver W.J., Henry N.L., Wang Z., Wu X., Svejstrup J.Q., Bushnell D.A., Friedberg E.C., Kornberg R.D.
    J. Biol. Chem. 272:19319-19327(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 71-85 AND 236-250, FUNCTION, SUBUNIT, INTERACTION WITH KIN28.
    Strain: DBY2019.
  2. "Rig2, a RING finger protein that interacts with the Kin28/Ccl1 CTD kinase in yeast."
    Faye G., Simon M., Valay J.G., Fesquet D., Facca C.
    Mol. Gen. Genet. 255:460-466(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Sethuraman A., Cherry J.M.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex with differential sensitivities to T-loop phosphorylation."
    Keogh M.-C., Cho E.-J., Podolny V., Buratowski S.
    Mol. Cell. Biol. 22:1288-1297(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH KIN28 AND CCL1.
  7. "Revised subunit structure of yeast transcription factor IIH (TFIIH) and reconciliation with human TFIIH."
    Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H., Tempst P., Kornberg R.D.
    J. Biol. Chem. 278:43897-43900(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-157 AND THR-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTFB3_YEAST
AccessioniPrimary (citable) accession number: Q03290
Secondary accession number(s): D6VT84, P89104
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3050 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3