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Protein

General transcription and DNA repair factor IIH subunit TFB1

Gene

TFB1

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

Functioni

Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.3 Publications

Miscellaneous

Present with 5150 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • phosphatidylinositol-3-phosphate binding Source: SGD
  • phosphatidylinositol-5-phosphate binding Source: SGD

GO - Biological processi

  • nucleotide-excision repair Source: SGD
  • phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  • transcription from RNA polymerase II promoter Source: SGD
  • transcription from RNA polymerase I promoter Source: SGD

Keywordsi

Biological processDNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29870-MONOMER.
ReactomeiR-SCE-113418. Formation of the Early Elongation Complex.
R-SCE-5696395. Formation of Incision Complex in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-SCE-72086. mRNA Capping.
R-SCE-73776. RNA Polymerase II Promoter Escape.
R-SCE-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SCE-75953. RNA Polymerase II Transcription Initiation.
R-SCE-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription and DNA repair factor IIH subunit TFB1
Short name:
TFIIH subunit TFB1
Alternative name(s):
RNA polymerase II transcription factor B 73 kDa subunit
RNA polymerase II transcription factor B p73 subunit
RNA polymerase II transcription factor B subunit 1
Gene namesi
Name:TFB1
Ordered Locus Names:YDR311W
ORF Names:D9740.3
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR311W.
SGDiS000002719. TFB1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001192611 – 642General transcription and DNA repair factor IIH subunit TFB1Add BLAST642

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei150PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32776.
PaxDbiP32776.
PRIDEiP32776.

PTM databases

iPTMnetiP32776.

Interactioni

Subunit structurei

Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription (PubMed:7961739, PubMed:7813015, PubMed:14500720). Interacts with XPC/RAD4. XPC/RAD4 recruits TFIIH to the NER machinery (PubMed:23295669). Interacts with the NER 3'-endonuclease XPG/RAD2. XPG/RAD2 displaces XPC/RAD4 from the repair complex (PubMed:22373916, PubMed:23295669).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KLF1Q133513EBI-19146,EBI-8284732From Homo sapiens.

Protein-protein interaction databases

BioGridi32364. 660 interactors.
DIPiDIP-1702N.
IntActiP32776. 45 interactors.
MINTiMINT-387816.
STRINGi4932.YDR311W.

Structurei

Secondary structure

1642
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi13 – 19Combined sources7
Beta strandi21 – 24Combined sources4
Beta strandi26 – 35Combined sources10
Beta strandi37 – 42Combined sources6
Beta strandi48 – 50Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi56 – 64Combined sources9
Beta strandi69 – 71Combined sources3
Beta strandi75 – 77Combined sources3
Beta strandi85 – 92Combined sources8
Helixi94 – 114Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y5ONMR-A1-115[»]
2GS0NMR-A1-115[»]
2K2UNMR-A1-115[»]
2L2INMR-A2-115[»]
2LOXNMR-A2-115[»]
2M14NMR-A2-115[»]
2MKRNMR-A1-115[»]
2N0YNMR-A1-115[»]
2N23NMR-A2-115[»]
5URNNMR-A2-115[»]
ProteinModelPortaliP32776.
SMRiP32776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32776.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini165 – 221BSD 1PROSITE-ProRule annotationAdd BLAST57
Domaini243 – 295BSD 2PROSITE-ProRule annotationAdd BLAST53

Sequence similaritiesi

Belongs to the TFB1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000015066.
HOGENOMiHOG000248691.
InParanoidiP32776.
KOiK03141.
OMAiEFWSRFF.
OrthoDBiEOG092C337H.

Family and domain databases

Gene3Di1.10.3970.10. 1 hit.
2.30.29.30. 1 hit.
InterProiView protein in InterPro
IPR005607. BSD_dom.
IPR035925. BSD_dom_sf.
IPR011993. PH-like_dom_sf.
IPR027079. Tfb1/p62.
IPR013876. TFIIH_BTF_p62_N.
PANTHERiPTHR12856. PTHR12856. 1 hit.
PfamiView protein in Pfam
PF03909. BSD. 2 hits.
PF08567. PH_TFIIH. 1 hit.
SMARTiView protein in SMART
SM00751. BSD. 2 hits.
SUPFAMiSSF140383. SSF140383. 2 hits.
SSF50729. SSF50729. 1 hit.
PROSITEiView protein in PROSITE
PS50858. BSD. 2 hits.

Sequencei

Sequence statusi: Complete.

P32776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA
60 70 80 90 100
TPASSEKMML RLIGKVDESK KRKDNEGNEV VPKPQRHMFS FNNRTVMDNI
110 120 130 140 150
KMTLQQIISR YKDADIYEEK RRREESAQHT ETPMSSSSVT AGTPTPHLDT
160 170 180 190 200
PQLNNGAPLI NTAKLDDSLS KEKLLTNLKL QQSLLKGNKV LMKVFQETVI
210 220 230 240 250
NAGLPPSEFW STRIPLLRAF ALSTSQKVGP YNVLSTIKPV ASSENKVNVN
260 270 280 290 300
LSREKILNIF ENYPIVKKAY TDNVPKNFKE PEFWARFFSS KLFRKLRGEK
310 320 330 340 350
IMQNDRGDVI IDRYLTLDQE FDRKDDDMLL HPVKKIIDLD GNIQDDPVVR
360 370 380 390 400
GNRPDFTMQP GVDINGNSDG TVDILKGMNR LSEKMIMALK NEYSRTNLQN
410 420 430 440 450
KSNITNDEED EDNDERNELK IDDLNESYKT NYAIIHLKRN AHEKTTDNDA
460 470 480 490 500
KSSADSIKNA DLKVSNQQML QQLSLVMDNL INKLDLNQVV PNNEVSNKIN
510 520 530 540 550
KRVITAIKIN AKQAKHNNVN SALGSFVDNT SQANELEVKS TLPIDLLESC
560 570 580 590 600
RMLHTTCCEF LKHFYIHFQS GEQKQASTVK KLYNHLKDCI EKLNELFQDV
610 620 630 640
LNGDGESMSN TCTAYLKPVL NSITLATHKY DEYFNEYNNN SN
Length:642
Mass (Da):72,894
Last modified:October 1, 1993 - v1
Checksum:iDAE369FE90A224F8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209F → L in AAU09707 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95750 Genomic DNA. Translation: AAA35143.1.
U28374 Genomic DNA. Translation: AAB64747.1.
AY723790 Genomic DNA. Translation: AAU09707.1.
BK006938 Genomic DNA. Translation: DAA12150.1.
PIRiS31285.
RefSeqiNP_010597.3. NM_001180619.3.

Genome annotation databases

EnsemblFungiiYDR311W; YDR311W; YDR311W.
GeneIDi851906.
KEGGisce:YDR311W.

Similar proteinsi

Entry informationi

Entry nameiTFB1_YEAST
AccessioniPrimary (citable) accession number: P32776
Secondary accession number(s): D6VSU0, E9P948
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 31, 2018
This is version 163 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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