Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor IIIB 50 kDa subunit

Gene

BRF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites (PubMed:11040218, PubMed:11121026, PubMed:11564744, PubMed:26638071). Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress (PubMed:26638071). Down-regulates expression of target genes in response to oxidative stress (PubMed:26638071). Overexpression protects cells against apoptosis in response to oxidative stress (PubMed:26638071).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi7ZincBy similarity1
Metal bindingi10ZincBy similarity1
Metal bindingi28ZincBy similarity1
Metal bindingi31ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2 – 36TFIIB-typePROSITE-ProRule annotationAdd BLAST35

GO - Molecular functioni

  • RNA polymerase III type 3 promoter DNA binding Source: UniProtKB
  • transcription factor activity, RNA polymerase III transcription factor binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to oxidative stress Source: UniProtKB
  • DNA-templated transcription, initiation Source: InterPro
  • regulation of transcription from RNA polymerase III promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104221-MONOMER.
ReactomeiR-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor IIIB 50 kDa subunit
Short name:
TFIIIB501 Publication
Short name:
hTFIIIB501 Publication
Alternative name(s):
B-related factor 2
Short name:
BRF-2
hBRFU
Gene namesi
Name:BRF2
Synonyms:BRFU1 Publication
ORF Names:PRO1470
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:17298. BRF2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi110R → A: Decreases affinity for DNA. 1 Publication1
Mutagenesisi361C → A: Abolishes response to oxidative stress. Abolishes the decrease in the formation of a ternary complex with DNA and TBP in response to oxidative stress. 1 Publication1
Mutagenesisi361C → D: Impairs formation of a ternary complex with DNA and TBP. 1 Publication1

Organism-specific databases

DisGeNETi55290.
OpenTargetsiENSG00000104221.
PharmGKBiPA164741329.

Polymorphism and mutation databases

BioMutaiBRF2.
DMDMi74734246.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003371871 – 419Transcription factor IIIB 50 kDa subunitAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei353PhosphoserineCombined sources1
Modified residuei361Cysteine sulfenic acid (-SOH)1 Publication1

Post-translational modificationi

In response to oxidative stress, Cys-361 is reversibly oxidized to cysteine sulfenic acid. Oxidation of Cys-361 impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress.1 Publication

Keywords - PTMi

Oxidation, Phosphoprotein

Proteomic databases

MaxQBiQ9HAW0.
PaxDbiQ9HAW0.
PeptideAtlasiQ9HAW0.
PRIDEiQ9HAW0.

PTM databases

iPTMnetiQ9HAW0.
PhosphoSitePlusiQ9HAW0.

Expressioni

Inductioni

Down-regulated by epigallocatechin gallate (EGCG) treatment.1 Publication

Gene expression databases

BgeeiENSG00000104221.
CleanExiHS_BRF2.
ExpressionAtlasiQ9HAW0. baseline and differential.
GenevisibleiQ9HAW0. HS.

Organism-specific databases

HPAiCAB019269.
HPA023378.

Interactioni

Subunit structurei

Component of TFIIIB complexes. The TFIIIB complex has two activities, alpha and beta. The TFIIIB-alpha activity complex is composed of TBP, BDP1, and a complex containing both BRF2 and at least four stably associated proteins; this complex inhibits the transcription by pol III via its phosphorylation by CK2; YY1 facilitates the TFIIIB-alpha complex formation. Interacts with TBP; this interaction promotes recruitment of BRF2 to TATA box-containing promoters (PubMed:26638071). Interacts with TBP and the BURE sequence (GC-rich sequence downstream from the TATA box) to form a strong ternary complex which is joined by BDP1; this ternary complex stimulates pol III transcription. Forms a trimeric complex composed of TBP, BRF2 and mini-SNAPc complex (SNAP43, SNAP50, and the N-terminal third of SNAP190) on the promoter. Assembly of the TBP-BRF2 complex is stimulated by SNAP190. Interacts with MAF1 and SNAPC4.9 Publications

Protein-protein interaction databases

BioGridi120578. 30 interactors.
STRINGi9606.ENSP00000220659.

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi67 – 82Combined sources16
Helixi87 – 101Combined sources15
Helixi104 – 107Combined sources4
Helixi111 – 128Combined sources18
Helixi135 – 142Combined sources8
Helixi146 – 159Combined sources14
Helixi169 – 178Combined sources10
Helixi191 – 193Combined sources3
Helixi197 – 213Combined sources17
Helixi223 – 237Combined sources15
Helixi239 – 242Combined sources4
Helixi247 – 253Combined sources7
Helixi262 – 277Combined sources16
Helixi281 – 284Combined sources4
Turni285 – 287Combined sources3
Turni290 – 293Combined sources4
Helixi294 – 296Combined sources3
Helixi297 – 302Combined sources6
Helixi304 – 313Combined sources10
Turni360 – 362Combined sources3
Helixi386 – 390Combined sources5
Helixi396 – 406Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ROCX-ray1.90A62-419[»]
4RODX-ray2.70A62-419[»]
4ROEX-ray2.20A62-419[»]
ProteinModelPortaliQ9HAW0.
SMRiQ9HAW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati72 – 1571Add BLAST86
Repeati173 – 2492Add BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 114Interaction with target DNACombined sources1 Publication7
Regioni357 – 363Required for the formation of a ternary complex with DNA and TBP; not required for interaction with TBP in the absence of DNA1 Publication7
Regioni365 – 419Required for interaction with TBP and formation of a ternary complex with DNA and TBP1 PublicationAdd BLAST55

Sequence similaritiesi

Belongs to the TFIIB family.Curated
Contains 1 TFIIB-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2 – 36TFIIB-typePROSITE-ProRule annotationAdd BLAST35

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1598. Eukaryota.
COG1405. LUCA.
GeneTreeiENSGT00390000002288.
HOGENOMiHOG000095260.
HOVERGENiHBG107537.
InParanoidiQ9HAW0.
KOiK15197.
OMAiCMLKPPK.
OrthoDBiEOG091G0ADG.
PhylomeDBiQ9HAW0.
TreeFamiTF331596.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR000812. TFIIB.
IPR013137. Znf_TFIIB.
[Graphical view]
PANTHERiPTHR11618. PTHR11618. 1 hit.
PfamiPF08271. TF_Zn_Ribbon. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
PROSITEiPS51134. ZF_TFIIB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HAW0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPGRGRCPDC GSTELVEDSH YSQSQLVCSD CGCVVTEGVL TTTFSDEGNL
60 70 80 90 100
REVTYSRSTG ENEQVSRSQQ RGLRRVRDLC RVLQLPPTFE DTAVAYYQQA
110 120 130 140 150
YRHSGIRAAR LQKKEVLVGC CVLITCRQHN WPLTMGAICT LLYADLDVFS
160 170 180 190 200
STYMQIVKLL GLDVPSLCLA ELVKTYCSSF KLFQASPSVP AKYVEDKEKM
210 220 230 240 250
LSRTMQLVEL ANETWLVTGR HPLPVITAAT FLAWQSLQPA DRLSCSLARF
260 270 280 290 300
CKLANVDLPY PASSRLQELL AVLLRMAEQL AWLRVLRLDK RSVVKHIGDL
310 320 330 340 350
LQHRQSLVRS AFRDGTAEVE TREKEPPGWG QGQGEGEVGN NSLGLPQGKR
360 370 380 390 400
PASPALLLPP CMLKSPKRIC PVPPVSTVTG DENISDSEIE QYLRTPQEVR
410
DFQRAQAARQ AATSVPNPP
Length:419
Mass (Da):46,533
Last modified:March 1, 2001 - v1
Checksum:i90A39F72DBA14888
GO
Isoform 2 (identifier: Q9HAW0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-32: Missing.

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):44,104
Checksum:iBBD3AA1989495531
GO

Sequence cautioni

The sequence AAG35486 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti153Y → C in BAA91975 (PubMed:14702039).Curated1
Sequence conflicti376S → F in AAG35669 (PubMed:11121026).Curated1
Sequence conflicti379T → I in BAG57607 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05683410 – 32Missing in isoform 2. 1 PublicationAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298153 mRNA. Translation: AAG30222.1.
AF206673 mRNA. Translation: AAG35669.2.
AK001914 mRNA. Translation: BAA91975.1.
AK294337 mRNA. Translation: BAG57607.1.
AK315420 mRNA. Translation: BAG37809.1.
CH471080 Genomic DNA. Translation: EAW63351.1.
CH471080 Genomic DNA. Translation: EAW63352.1.
CH471080 Genomic DNA. Translation: EAW63353.1.
BC010648 mRNA. Translation: AAH10648.1.
AF130058 mRNA. Translation: AAG35486.1. Different initiation.
CCDSiCCDS6098.1. [Q9HAW0-1]
RefSeqiNP_060780.2. NM_018310.3. [Q9HAW0-1]
UniGeneiHs.709301.

Genome annotation databases

EnsembliENST00000220659; ENSP00000220659; ENSG00000104221. [Q9HAW0-1]
GeneIDi55290.
KEGGihsa:55290.
UCSCiuc003xkk.4. human. [Q9HAW0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298153 mRNA. Translation: AAG30222.1.
AF206673 mRNA. Translation: AAG35669.2.
AK001914 mRNA. Translation: BAA91975.1.
AK294337 mRNA. Translation: BAG57607.1.
AK315420 mRNA. Translation: BAG37809.1.
CH471080 Genomic DNA. Translation: EAW63351.1.
CH471080 Genomic DNA. Translation: EAW63352.1.
CH471080 Genomic DNA. Translation: EAW63353.1.
BC010648 mRNA. Translation: AAH10648.1.
AF130058 mRNA. Translation: AAG35486.1. Different initiation.
CCDSiCCDS6098.1. [Q9HAW0-1]
RefSeqiNP_060780.2. NM_018310.3. [Q9HAW0-1]
UniGeneiHs.709301.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ROCX-ray1.90A62-419[»]
4RODX-ray2.70A62-419[»]
4ROEX-ray2.20A62-419[»]
ProteinModelPortaliQ9HAW0.
SMRiQ9HAW0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120578. 30 interactors.
STRINGi9606.ENSP00000220659.

PTM databases

iPTMnetiQ9HAW0.
PhosphoSitePlusiQ9HAW0.

Polymorphism and mutation databases

BioMutaiBRF2.
DMDMi74734246.

Proteomic databases

MaxQBiQ9HAW0.
PaxDbiQ9HAW0.
PeptideAtlasiQ9HAW0.
PRIDEiQ9HAW0.

Protocols and materials databases

DNASUi55290.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220659; ENSP00000220659; ENSG00000104221. [Q9HAW0-1]
GeneIDi55290.
KEGGihsa:55290.
UCSCiuc003xkk.4. human. [Q9HAW0-1]

Organism-specific databases

CTDi55290.
DisGeNETi55290.
GeneCardsiBRF2.
HGNCiHGNC:17298. BRF2.
HPAiCAB019269.
HPA023378.
MIMi607013. gene.
neXtProtiNX_Q9HAW0.
OpenTargetsiENSG00000104221.
PharmGKBiPA164741329.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1598. Eukaryota.
COG1405. LUCA.
GeneTreeiENSGT00390000002288.
HOGENOMiHOG000095260.
HOVERGENiHBG107537.
InParanoidiQ9HAW0.
KOiK15197.
OMAiCMLKPPK.
OrthoDBiEOG091G0ADG.
PhylomeDBiQ9HAW0.
TreeFamiTF331596.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104221-MONOMER.
ReactomeiR-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Miscellaneous databases

ChiTaRSiBRF2. human.
GeneWikiiBRF2_(gene).
GenomeRNAii55290.
PROiQ9HAW0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104221.
CleanExiHS_BRF2.
ExpressionAtlasiQ9HAW0. baseline and differential.
GenevisibleiQ9HAW0. HS.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR013763. Cyclin-like.
IPR000812. TFIIB.
IPR013137. Znf_TFIIB.
[Graphical view]
PANTHERiPTHR11618. PTHR11618. 1 hit.
PfamiPF08271. TF_Zn_Ribbon. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
PROSITEiPS51134. ZF_TFIIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBRF2_HUMAN
AccessioniPrimary (citable) accession number: Q9HAW0
Secondary accession number(s): B2RD62
, B4DFZ6, D3DSW6, Q9H2Y3, Q9H3B3, Q9NUY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.