P32776 (TFB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase II transcription factor B subunit 1

Alternative name(s):
General transcription and DNA repair factor IIH subunit TFB1
Short name=TFIIH subunit TFB1
RNA polymerase II transcription factor B 73 kDa subunit
RNA polymerase II transcription factor B p73 subunit

Gene names

Name:	TFB1
Ordered Locus Names:	YDR311W
ORF Names:	D9740.3

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, 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. Ref.5 Ref.6
Subunit structure	Component of the TFIIH core complex, which is composed of RAD3, SSL1, SSL2, TFB1, TFB2, TFB4 and TFB5. Ref.5 Ref.7
Subcellular location	Nucleus.
Miscellaneous	Present with 5150 molecules/cell in log phase SD medium.
Sequence similarities	Contains 2 BSD domains.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide-excision repair Inferred from mutant phenotype PubMed 7891722. Source: SGD phosphorylation of RNA polymerase II C-terminal domain Inferred from direct assay PubMed 19450536PubMed 19679665. Source: SGD transcription from RNA polymerase I promoter Inferred from mutant phenotype PubMed 12015980. Source: SGD transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19818408. Source: SGD
Cellular_component	core TFIIH complex Inferred from direct assay Ref.7PubMed 19818408. Source: SGD holo TFIIH complex Inferred from direct assay PubMed 19818408. Source: SGD nucleotide-excision repair factor 3 complex Inferred from direct assay PubMed 8855246. Source: SGD
Molecular_function	phosphatidylinositol-3-phosphate binding Inferred from direct assay PubMed 15909982. Source: SGD phosphatidylinositol-5-phosphate binding Inferred from direct assay PubMed 15909982. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TFA1	P36100	3	EBI-19146,EBI-18903

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 642

642

RNA polymerase II transcription factor B subunit 1

PRO_0000119261

Regions

Domain

165 – 221

57

BSD 1

Domain

243 – 295

53

BSD 2

Amino acid modifications

Modified residue

150

1

Phosphothreonine Ref.9

Modified residue

521

1

Phosphoserine Ref.9

Experimental info

Sequence conflict

209

1

F → L in AAU09707. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

642

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

13 – 19

7

Beta strand

21 – 24

4

Beta strand

26 – 35

10

Beta strand

37 – 42

6

Beta strand

48 – 50

3

Beta strand

53 – 55

3

Beta strand

56 – 64

9

Beta strand

69 – 71

3

Beta strand

75 – 77

3

Beta strand

85 – 92

8

Helix

94 – 114

21

Sequences

	Sequence		Length	Mass (Da)
	P32776 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: DAE369FE90A224F8	FASTA	642	72,894
	10 20 30 40 50 60 MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA TPASSEKMML 70 80 90 100 110 120 RLIGKVDESK KRKDNEGNEV VPKPQRHMFS FNNRTVMDNI KMTLQQIISR YKDADIYEEK 130 140 150 160 170 180 RRREESAQHT ETPMSSSSVT AGTPTPHLDT PQLNNGAPLI NTAKLDDSLS KEKLLTNLKL 190 200 210 220 230 240 QQSLLKGNKV LMKVFQETVI NAGLPPSEFW STRIPLLRAF ALSTSQKVGP YNVLSTIKPV 250 260 270 280 290 300 ASSENKVNVN LSREKILNIF ENYPIVKKAY TDNVPKNFKE PEFWARFFSS KLFRKLRGEK 310 320 330 340 350 360 IMQNDRGDVI IDRYLTLDQE FDRKDDDMLL HPVKKIIDLD GNIQDDPVVR GNRPDFTMQP 370 380 390 400 410 420 GVDINGNSDG TVDILKGMNR LSEKMIMALK NEYSRTNLQN KSNITNDEED EDNDERNELK 430 440 450 460 470 480 IDDLNESYKT NYAIIHLKRN AHEKTTDNDA KSSADSIKNA DLKVSNQQML QQLSLVMDNL 490 500 510 520 530 540 INKLDLNQVV PNNEVSNKIN KRVITAIKIN AKQAKHNNVN SALGSFVDNT SQANELEVKS 550 560 570 580 590 600 TLPIDLLESC RMLHTTCCEF LKHFYIHFQS GEQKQASTVK KLYNHLKDCI EKLNELFQDV 610 620 630 640 LNGDGESMSN TCTAYLKPVL NSITLATHKY DEYFNEYNNN SN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a subunit of yeast RNA polymerase II transcription factor b and CTD kinase." Gileadi O., Feaver W.J., Kornberg R.D. Science 257:1389-1392(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 314-322 AND 630-639.
[2]	"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 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"RNA polymerase transcription factor IIH holoenzyme from yeast." Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D. J. Biol. Chem. 269:28044-28048(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION, IDENTIFICATION IN THE TFIIH COMPLEX.
[6]	"Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair." Sung P., Guzder S.N., Prakash L., Prakash S. J. Biol. Chem. 271:10821-10826(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
[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: IDENTIFICATION IN THE TFIIH CORE COMPLEX.
[8]	"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].
[9]	"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 THR-150 AND SER-521, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M95750 Genomic DNA. Translation: AAA35143.1.
U28374 Genomic DNA. Translation: AAB64747.1.
AY723790 Genomic DNA. Translation: AAU09707.1.
BK006938 Genomic DNA. Translation: DAA12150.1.

PIR

S31285.

RefSeq

NP_010597.3. NM_001180619.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y5O	NMR	-	A	2-115	[»]
2GS0	NMR	-	A	2-115	[»]
2K2U	NMR	-	A	2-115	[»]
2L2I	NMR	-	A	2-115	[»]
2LOX	NMR	-	A	2-115	[»]
2M14	NMR	-	A	2-115	[»]

ProteinModelPortal

P32776.

SMR

P32776. Positions 2-115.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1702N.

IntAct

P32776. 20 interactions.

MINT

MINT-387816.

STRING

4932.YDR311W.

Proteomic databases

PaxDb

P32776.

PeptideAtlas

P32776.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR311W; YDR311W; YDR311W.

GeneID

851906.

KEGG

sce:YDR311W.
sce:YDR315C.

Organism-specific databases

CYGD

YDR311w.

SGD

S000002719. TFB1.

Phylogenomic databases

eggNOG

NOG315835.

GeneTree

ENSGT00390000015066.

HOGENOM

HOG000248691.

KO

K03141.

OMA

EFWARFF.

OrthoDB

EOG47H8ZG.

Gene expression databases

Genevestigator

P32776.

GermOnline

YDR311W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR005607. BSD.
IPR011993. PH_like_dom.
IPR027079. Tfb1/p62.
IPR013876. TFIIH_BTF_p62_N.
[Graphical view]

PANTHER

PTHR12856. PTHR12856. 1 hit.

Pfam

PF03909. BSD. 2 hits.
PF08567. TFIIH_BTF_p62_N. 1 hit.
[Graphical view]

SMART

SM00751. BSD. 2 hits.
[Graphical view]

PROSITE

PS50858. BSD. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32776.

NextBio

969921.

Entry information

Entry name

TFB1_YEAST

Accession

Primary (citable) accession number: P32776
Secondary accession number(s): D6VSU0, E9P948

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program