Skip Header

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

UniProtKB - Q00403 (TF2B_HUMAN)

Entry version 219 (02 Dec 2020)
Sequence version 1 (01 Dec 1992)
Previous versions | rss
Add a publicationFeedback
Protein

Transcription initiation factor IIB

Gene

GTF2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

General transcription factor that plays a role in transcription initiation by RNA polymerase II (Pol II). Involved in the pre-initiation complex (PIC) formation and Pol II recruitment at promoter DNA (PubMed:1876184, PubMed:1946368, PubMed:1517211, PubMed:3818643, PubMed:3029109, PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:7601352, PubMed:9420329, PubMed:12931194, PubMed:27193682). Together with the TATA box-bound TBP forms the core initiation complex and provides a bridge between TBP and the Pol II-TFIIF complex (PubMed:8504927, PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312). Released from the PIC early following the onset of transcription during the initiation and elongation transition and reassociates with TBP during the next transcription cycle (PubMed:7601352). Associates with chromatin to core promoter-specific regions (PubMed:12931194, PubMed:24441171). Binds to two distinct DNA core promoter consensus sequence elements in a TBP-independent manner; these IIB-recognition elements (BREs) are localized immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element (PubMed:9420329, PubMed:16230532, PubMed:7675079, PubMed:10619841). Modulates transcription start site selection (PubMed:10318856). Exhibits also autoacetyltransferase activity that contributes to the activated transcription (PubMed:12931194).19 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.117 mM for acetyl-CoA1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi15ZincCombined sources2 Publications1
    Metal bindingi18Zinc; via tele nitrogenCombined sources2 Publications1
    Metal bindingi34ZincCombined sources2 Publications1
    Metal bindingi37ZincCombined sources2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri11 – 42TFIIB-typePROSITE-ProRule annotationAdd BLAST32

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, DNA-binding, Transferase
    Biological processHost-virus interaction, Transcription, Transcription regulation
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    Pathway Commons web resource for biological pathway data

    More...    PathwayCommonsi    		Q00403

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-167161, HIV Transcription Initiation
    R-HSA-167162, RNA Polymerase II HIV Promoter Escape
    R-HSA-167172, Transcription of the HIV genome
    R-HSA-674695, RNA Polymerase II Pre-transcription Events
    R-HSA-6807505, RNA polymerase II transcribes snRNA genes
    R-HSA-73776, RNA Polymerase II Promoter Escape
    R-HSA-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
    R-HSA-75953, RNA Polymerase II Transcription Initiation
    R-HSA-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		Q00403

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Transcription initiation factor IIB1 Publication (EC:2.3.1.481 Publication)
    Alternative name(s):
    General transcription factor TFIIB1 Publication
    S300-II1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:GTF2B
    Synonyms:TF2B, TFIIB
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Eukaryotic Pathogen and Host Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000137947.11

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:4648, GTF2B

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		189963, gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q00403

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chromosome, Nucleus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi37C → S: Does not inhibit interaction with TBP. Inhibits the recruitment of RNA polymerase II into the initiation complex. 1 Publication1
    Mutagenesisi51 – 56EWRTFS → AWRTFA: Partial loss of HIV-1 Vpr binding. 1 Publication6
    Mutagenesisi51E → R, A or D: Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type. 1 Publication1
    Mutagenesisi52W → A: Partial loss of HIV-1 Vpr binding. 1 Publication1
    Mutagenesisi53 – 54RT → AA: Partial loss of HIV-1 Vpr binding. 1 Publication2
    Mutagenesisi55F → A: Partial loss of HIV-1 Vpr binding. 1 Publication1
    Mutagenesisi66R → A, E or K: Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type. 1 Publication1
    Mutagenesisi153G → Q: Decreases BREd-dependent pre-initiation complex formation. 1 Publication1
    Mutagenesisi185R → E: Reduces interaction with SSU72; when associated with E-193 or E-200. Inhibits interaction with VP16; when associated with E-193. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-193. 2 Publications1
    Mutagenesisi185R → L: Reduces interaction with VP16; when associated with L-189. 1 Publication1
    Mutagenesisi189K → E: Inhibits interaction with SSU72; when associated with E-193. Reduces interaction with SSU72; when associated with E-200. Inhibits interaction with VP16; when associated with E-200. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-200. 2 Publications1
    Mutagenesisi189K → L: Reduces interaction with VP16; when associated with L-185. 1 Publication1
    Mutagenesisi193R → E: Inhibits interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-185. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-185. 2 Publications1
    Mutagenesisi196K → L: Reduces interaction with VP16; when associated with L-200. 1 Publication1
    Mutagenesisi200 – 208KALETSVDL → GSGS: Reduces the formation of the TATA box-bound TBP ternary complex. 1 Publication9
    Mutagenesisi200K → E: Reduces interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-189. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-189. 2 Publications1
    Mutagenesisi200K → KGSGS: Reduces the formation of the TATA box-bound TBP ternary complex. 1 Publication1
    Mutagenesisi200K → L: Reduces interaction with VP16; when associated with L-196. 1 Publication1
    Mutagenesisi208L → LGSGS: Does not inhibit the formation of the TATA box-bound TBP ternary complex. 1 Publication1
    Mutagenesisi238K → A: Abolishes autoacetylation, represses transcription activity, does not inhibit its association with chromatin to promoter-specific regions and decreases the association of GTF2F1 with chromatin to promoter-specific regions. 1 Publication1
    Mutagenesisi247G → V: Inhibits interaction with TBP. 1 Publication1
    Mutagenesisi283V → A: Reduces DNA-binding. 1 Publication1
    Mutagenesisi286R → A: Reduces DNA-binding. 1 Publication1
    Mutagenesisi286R → E: Inhibits interaction with RNA polymerase II; when associated with E-290 and E-295. 1 Publication1
    Mutagenesisi290R → E: Inhibits interaction with RNA polymerase II; when associated with E-286 and E-295. 1 Publication1
    Mutagenesisi295R → E: Inhibits interaction with RNA polymerase II; when associated with E-286 and E-290. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		2959

    Open Targets

    More...    OpenTargetsi    		ENSG00000137947

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA29035

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		Q00403, Tbio

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		GTF2B

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		135629

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001192931 – 316Transcription initiation factor IIBAdd BLAST316

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei70PhosphoserineCombined sources1
    Modified residuei76PhosphoserineCombined sources1
    Modified residuei92PhosphoserineCombined sources1
    Modified residuei238N6-acetyllysine; by autocatalysis1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Acetylated (PubMed:24441171). Autoacetylated; autoacetylation at Lys-238 stimulates transcription activation (PubMed:12931194).2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		Q00403

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		Q00403

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		Q00403

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		Q00403

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		Q00403

    PeptideAtlas

    More...    PeptideAtlasi    		Q00403

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q00403

    ProteomicsDB: a multi-organism proteome resource

    More...    ProteomicsDBi    		57846

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q00403

    MetOSite database of methionine sulfoxide sites

    More...    MetOSitei    		Q00403

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		Q00403

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in the inner cell mass forming the embryoblast (PubMed:24441171). Not detected in cells from the outer thin layer trophoblast (at protein level) (PubMed:24441171).1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000137947, Expressed in oocyte and 237 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		Q00403, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q00403, HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		ENSG00000137947, Low tissue specificity

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Found in a ternary complex with TATA box-bound TBP (PubMed:8413225, PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:10619841, PubMed:29158257).

    Part of a TFIID-containing RNA polymerase II pre-initiation complex (PIC) that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27193682). Associates with TFIID-TFIIA (DA complex) to form TFIID-TFIIA-TFIIB (DAB complex), which is then recognized by RNA polymerase II (Pol II) (PubMed:1876184, PubMed:2247058).

    Found in a RNA polymerase II initiation complex (PubMed:3818643, PubMed:3029109, PubMed:8413225, PubMed:8516312, PubMed:7601352).

    Interacts (via C-terminus) with TBP; this interaction with TATA box-bound TBP guides Pol II into the PIC (PubMed:8504927, PubMed:10619841).

    Interacts (via N-terminus) with Pol II (PubMed:8504927, PubMed:8413225).

    Interacts (via C-terminus) with SSU72; this interaction is inhibited by SYMPK (PubMed:29158257).

    Interacts with NR2F1; this interaction is direct (PubMed:1517211).

    Interacts with PGR (PubMed:1517211).

    Interacts with ESR1 (PubMed:1517211).

    Interacts with GTF2F1 (via C-terminus and preferentially via acetylated form); this interaction prevents binding of GTF2B to GTF2F2 (PubMed:8662660, PubMed:12931194).

    Interacts with GTF2F2 (via N-terminus); this interaction is inhibited in presence of GTF2F1 (PubMed:8504927, PubMed:8662660).

    Interacts with the transcription elongation factor TCEA2 (PubMed:8566795).

    Interacts with HSF1 (via transactivation domain) (PubMed:11005381).

    Interacts with GPBP1 (By similarity).

    By similarity18 Publications

    (Microbial infection) Interacts with HIV-1 Vpr.

    1 Publication

    (Microbial infection) Interacts with Epstein-Barr virus EBNA2.

    1 Publication

    (Microbial infection) Interacts with Herpes simplex virus 1 protein ICP4.

    1 Publication

    (Microbial infection) Interacts (via C-terminus) with the Herpes simplex virus activator VP16; this interaction stimulates RNA Pol II transcription by increasing the extent of pre-initiation complex assembly.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		109214, 96 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		Q00403

    Database of interacting proteins

    More...    DIPi    		DIP-1077N

    Protein interaction database and analysis system

    More...    IntActi    		Q00403, 55 interactors

    Molecular INTeraction database

    More...    MINTi    		Q00403

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000359531

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		Q00403, protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1316
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		Q00403

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		Q00403

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati124 – 2001Add BLAST77
    Repeati218 – 2942Add BLAST77

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni189 – 193Core promoter DNA-binding1 Publication5
    Regioni244 – 316Necessary for TATA box-bound TBP complex formation2 PublicationsAdd BLAST73
    Regioni249 – 252Core promoter DNA-binding1 Publication4
    Regioni283 – 286Core promoter DNA-binding2 Publications4

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The TFIIB-type zinc-binding domain is necessary for the interaction and recruitment of RNA polymerase II to the core promoter, the formation of a fully competent pre-initiation complex (PIC) assembly and basal transcription initiation (PubMed:8515820, PubMed:8516311, PubMed:8516312, PubMed:8413225). The C-terminus is necessary and sufficient for interaction with the TATA box-bound TBP complex and for the formation of PIC (PubMed:8515820, PubMed:8516311, PubMed:8413225).4 Publications

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the TFIIB family.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri11 – 42TFIIB-typePROSITE-ProRule annotationAdd BLAST32

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG1597, Eukaryota

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00390000006671

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q00403

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		DQRMKRS

    Database of Orthologous Groups

    More...    OrthoDBi    		729732at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q00403

    TreeFam database of animal gene trees

    More...    TreeFami    		TF105953

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00043, CYCLIN, 2 hits

    Intrinsically Disordered proteins with Extensive Annotations and Literature

    More...    IDEALi    		IID00314

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR013763, Cyclin-like
    IPR036915, Cyclin-like_sf
    IPR000812, TFIIB
    IPR023486, TFIIB_CS
    IPR013150, TFIIB_cyclin
    IPR013137, Znf_TFIIB

    The PANTHER Classification System

    More...    PANTHERi    		PTHR11618, PTHR11618, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF08271, TF_Zn_Ribbon, 1 hit
    PF00382, TFIIB, 2 hits

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00685, TIFACTORIIB

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00385, CYCLIN, 2 hits

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF47954, SSF47954, 2 hits

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00782, TFIIB, 2 hits
    PS51134, ZF_TFIIB, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    Q00403-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS 
            60         70         80         90        100
    EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK 
           110        120        130        140        150
    YQNRRTMSSS DRAMMNAFKE ITTMADRINL PRNIVDRTNN LFKQVYEQKS 
           160        170        180        190        200
    LKGRANDAIA SACLYIACRQ EGVPRTFKEI CAVSRISKKE IGRCFKLILK 
           210        220        230        240        250
    ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV ELDLVPGRSP 
           260        270        280        290        300
    ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF 
           310 
    PTDFKFDTPV DKLPQL
    Length:316
    Mass (Da):34,833
    Last modified:December 1, 1992 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9CC7E102526C2722
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    B1APE2B1APE2_HUMAN
    General transcription factor TFIIB
    GTF2B
    		231Annotation score:

    Annotation score:3 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    B1APE1B1APE1_HUMAN
    General transcription factor TFIIB
    GTF2B
    		224Annotation score:

    Annotation score:3 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01197719P → S. Corresponds to variant dbSNP:rs1804499Ensembl.1
    Natural variantiVAR_035722132R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs144944840Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		X59268 mRNA Translation: CAA41958.1
    M76766 mRNA Translation: AAA61149.1
    AK289822 mRNA Translation: BAF82511.1
    AB451296 mRNA Translation: BAG70110.1
    AL445991 Genomic DNA No translation available.
    BC020597 mRNA Translation: AAH20597.1
    S44184 mRNA Translation: AAB23144.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS715.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S17654, TWHU2B

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001505.1, NM_001514.5

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000370500; ENSP00000359531; ENSG00000137947

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		2959

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:2959

    UCSC genome browser

    More...    UCSCi    		uc001dmo.5, human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		X59268 mRNA Translation: CAA41958.1
    M76766 mRNA Translation: AAA61149.1
    AK289822 mRNA Translation: BAF82511.1
    AB451296 mRNA Translation: BAG70110.1
    AL445991 Genomic DNA No translation available.
    BC020597 mRNA Translation: AAH20597.1
    S44184 mRNA Translation: AAB23144.1
    CCDSiCCDS715.1
    PIRiS17654, TWHU2B
    RefSeqiNP_001505.1, NM_001514.5

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1C9BX-ray2.65A/E/I/M/Q110-316[»]
    1DL6NMR-A2-59[»]
    1RLYNMR-A1-60[»]
    1RO4NMR-A1-60[»]
    1TFBNMR-A112-316[»]
    1VOLX-ray2.70A113-316[»]
    2PHGNMR-A112-316[»]
    5IY6electron microscopy7.20M1-316[»]
    5IY7electron microscopy8.60M1-316[»]
    5IY8electron microscopy7.90M1-316[»]
    5IY9electron microscopy6.30M1-316[»]
    5IYAelectron microscopy5.40M1-316[»]
    5IYBelectron microscopy3.90M1-316[»]
    5IYCelectron microscopy3.90M1-316[»]
    5IYDelectron microscopy3.90M1-316[»]
    5WH1X-ray3.39A/B/C/D107-316[»]
    6O9Lelectron microscopy7.20M1-316[»]
    SMRiQ00403
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi109214, 96 interactors
    CORUMiQ00403
    DIPiDIP-1077N
    IntActiQ00403, 55 interactors
    MINTiQ00403
    STRINGi9606.ENSP00000359531

    PTM databases

    iPTMnetiQ00403
    MetOSiteiQ00403
    PhosphoSitePlusiQ00403

    Polymorphism and mutation databases

    BioMutaiGTF2B
    DMDMi135629

    Proteomic databases

    EPDiQ00403
    jPOSTiQ00403
    MassIVEiQ00403
    MaxQBiQ00403
    PaxDbiQ00403
    PeptideAtlasiQ00403
    PRIDEiQ00403
    ProteomicsDBi57846

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...    Antibodypediai    		19819, 417 antibodies

    The DNASU plasmid repository

    More...    DNASUi    		2959

    Genome annotation databases

    EnsembliENST00000370500; ENSP00000359531; ENSG00000137947
    GeneIDi2959
    KEGGihsa:2959
    UCSCiuc001dmo.5, human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		2959
    DisGeNETi2959
    EuPathDBiHostDB:ENSG00000137947.11

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		GTF2B
    HGNCiHGNC:4648, GTF2B
    HPAiENSG00000137947, Low tissue specificity
    MIMi189963, gene
    neXtProtiNX_Q00403
    OpenTargetsiENSG00000137947
    PharmGKBiPA29035

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG1597, Eukaryota
    GeneTreeiENSGT00390000006671
    InParanoidiQ00403
    OMAiDQRMKRS
    OrthoDBi729732at2759
    PhylomeDBiQ00403
    TreeFamiTF105953

    Enzyme and pathway databases

    PathwayCommonsiQ00403
    ReactomeiR-HSA-167161, HIV Transcription Initiation
    R-HSA-167162, RNA Polymerase II HIV Promoter Escape
    R-HSA-167172, Transcription of the HIV genome
    R-HSA-674695, RNA Polymerase II Pre-transcription Events
    R-HSA-6807505, RNA polymerase II transcribes snRNA genes
    R-HSA-73776, RNA Polymerase II Promoter Escape
    R-HSA-73779, RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
    R-HSA-75953, RNA Polymerase II Transcription Initiation
    R-HSA-76042, RNA Polymerase II Transcription Initiation And Promoter Clearance
    SIGNORiQ00403

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...    BioGRID-ORCSi    		2959, 762 hits in 850 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		GTF2B, human
    EvolutionaryTraceiQ00403

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		Transcription_factor_II_B

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		2959
    PharosiQ00403, Tbio

    Protein Ontology

    More...    PROi    		PR:Q00403
    RNActiQ00403, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000137947, Expressed in oocyte and 237 other tissues
    ExpressionAtlasiQ00403, baseline and differential
    GenevisibleiQ00403, HS

    Family and domain databases

    CDDicd00043, CYCLIN, 2 hits
    IDEALiIID00314
    InterProiView protein in InterPro
    IPR013763, Cyclin-like
    IPR036915, Cyclin-like_sf
    IPR000812, TFIIB
    IPR023486, TFIIB_CS
    IPR013150, TFIIB_cyclin
    IPR013137, Znf_TFIIB
    PANTHERiPTHR11618, PTHR11618, 1 hit
    PfamiView protein in Pfam
    PF08271, TF_Zn_Ribbon, 1 hit
    PF00382, TFIIB, 2 hits
    PRINTSiPR00685, TIFACTORIIB
    SMARTiView protein in SMART
    SM00385, CYCLIN, 2 hits
    SUPFAMiSSF47954, SSF47954, 2 hits
    PROSITEiView protein in PROSITE
    PS00782, TFIIB, 2 hits
    PS51134, ZF_TFIIB, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTF2B_HUMAN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q00403
    Secondary accession number(s): A8K1A7, Q5JS30
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: December 2, 2020
    This is version 219 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    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
    5. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again