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Entry version 180 (17 Jun 2020)
Sequence version 1 (01 Feb 1994)
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Protein

Transcription initiation factor TFIID subunit 14

Gene

TAF14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Functions as a component of the DNA-binding general transcription factor complex TFIID, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIIF is essential for the initiation of transcription by RNA polymerase II (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation (PubMed:10788514, PubMed:12138208, PubMed:12516863, PubMed:9618449, PubMed:30385749). TAF14 acts as a chromatin reader that specifically recognizes and binds histones that are acylated (PubMed:26341557, PubMed:27089029). Recognizes and binds histone H3 acetylated or crotonylated at 'Lys-9' (H3K9ac and H3K9cr, respectively), with some preference for crotonylated lysine (PubMed:26341557, PubMed:27089029, PubMed:30385749). Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes (PubMed:12672490). It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors (PubMed:12672490). Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3 (PubMed:17157260). In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation (PubMed:17157260). Does not bind DNA (PubMed:30385749).9 Publications

Miscellaneous

TAF14 is the only non-essential TAF.
Present with 3100 molecules/cell in log phase SD medium.1 Publication
There is no homolog of TAF14 present in the TFIIF complexes of higher eukaryotes.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei104Acylated histoneCombined sources1 Publication1

<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

GO - Biological processi

<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

Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-34028-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-674695 RNA Polymerase II Pre-transcription Events
R-SCE-75955 RNA Polymerase II Transcription Elongation

<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 TFIID subunit 14
Alternative name(s):
Actin non-complementing mutant 1
Chromosome stability protein 10
SWI/SNF chromatin-remodeling complex subunit TAF14
SWI/SNF complex 29 kDa subunit
SWI/SNF complex subunit TAF14
TBP-associated factor 14
TBP-associated factor 30 kDa
Transcription factor G 30 kDa subunit
Transcription initiation factor TFIIF 30 kDa subunit
<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:TAF14
Synonyms:ANC1, CST10, SWP29, TAF30, TFG3
Ordered Locus Names:YPL129W
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 XVI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YPL129W

Saccharomyces Genome Database

More...
SGDi
S000006050 TAF14

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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>Mutagenesisi24V → A: Does not affect binding to acylated histone H3. 1 Publication1
Mutagenesisi80G → A: Abolished binding to acylated histone H3. 1 Publication1
Mutagenesisi81W → A: Abolished binding to acetylated histone H3. 1 Publication1
Mutagenesisi82G → A: Does not affect ability to bind crotonylated lysines, while abolishing binding to acetylated lysines. 1 Publication1

<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_00002112411 – 244Transcription initiation factor TFIID subunit 14Add BLAST244

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P35189

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

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PaxDbi
P35189

PRoteomics IDEntifications database

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PRIDEi
P35189

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35189

<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

The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. TFIIF is composed of three different subunits: TFG1/RAP74, TFG2/RAP30 and TAF14.

Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.

Component of the chromatin-remodeling INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80.

Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
36052, 298 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1149 Transcription factor TFIIF complex
CPX-1150 SWI/SNF chromatin remodelling complex
CPX-1642 General transcription factor complex TFIID
CPX-1810 NuA3 histone acetyltransferase complex
CPX-863 INO80 chromatin remodeling complex

Database of interacting proteins

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DIPi
DIP-1147N

Protein interaction database and analysis system

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IntActi
P35189, 53 interactors

Molecular INTeraction database

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MINTi
P35189

STRING: functional protein association networks

More...
STRINGi
4932.YPL129W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P35189 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

1244
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

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SMRi
P35189

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P35189

<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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 115YEATSPROSITE-ProRule annotationAdd BLAST108

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>Regioni59 – 61Acylated histone bindingCombined sources1 Publication3
Regioni81 – 83Acylated histone bindingCombined sources1 Publication3

<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 YEATS domain specifically recognizes and binds acylated histones (acetylated and crotonylated) (PubMed:26341557, PubMed:27089029, PubMed:30385749). Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism (PubMed:27089029, PubMed:30385749).3 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 TAF14 family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176465

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_078004_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35189

KEGG Orthology (KO)

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KOi
K03140

Identification of Orthologs from Complete Genome Data

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OMAi
YNLHPTF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.1970, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

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IDEALi
IID50207

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027353 NET_dom
IPR016665 Sas5/TAF14
IPR038704 YEAST_sf
IPR005033 YEATS

The PANTHER Classification System

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PANTHERi
PTHR23195 PTHR23195, 1 hit
PTHR23195:SF2 PTHR23195:SF2, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF17035 BET, 1 hit
PF03366 YEATS, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF016551 SAS5/TFIID_14, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51037 YEATS, 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>Sequencei

<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.

P35189-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVATVKRTIR IKTQQHILPE VPPVENFPVR QWSIEIVLLD DEGKEIPATI
60 70 80 90 100
FDKVIYHLHP TFANPNRTFT DPPFRIEEQG WGGFPLDISV FLLEKAGERK
110 120 130 140 150
IPHDLNFLQE SYEVEHVIQI PLNKPLLTEE LAKSGSTEET TANTGTIGKR
160 170 180 190 200
RTTTNTTAEP KAKRAKTGSA STVKGSVDLE KLAFGLTKLN EDDLVGVVQM
210 220 230 240
VTDNKTPEMN VTNNVEEGEF IIDLYSLPEG LLKSLWDYVK KNTE
Length:244
Mass (Da):27,440
Last modified:February 1, 1994 - 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:i60EA5EC2474B1B9C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti116H → Q in CAA49192 (PubMed:8423796).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U13017 Genomic DNA Translation: AAA61644.1
Z26040 Genomic DNA Translation: CAA81125.1
U43703 Genomic DNA Translation: AAB68235.1
X69394 Genomic DNA Translation: CAA49192.1
BK006949 Genomic DNA Translation: DAA11304.1

Protein sequence database of the Protein Information Resource

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PIRi
S38568

NCBI Reference Sequences

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RefSeqi
NP_015196.1, NM_001183943.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YPL129W_mRNA; YPL129W; YPL129W

Database of genes from NCBI RefSeq genomes

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GeneIDi
855974

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YPL129W

<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
U13017 Genomic DNA Translation: AAA61644.1
Z26040 Genomic DNA Translation: CAA81125.1
U43703 Genomic DNA Translation: AAB68235.1
X69394 Genomic DNA Translation: CAA49192.1
BK006949 Genomic DNA Translation: DAA11304.1
PIRiS38568
RefSeqiNP_015196.1, NM_001183943.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L7ENMR-A1-123[»]
3QRLX-ray1.70A1-137[»]
5D7EX-ray1.90A1-137[»]
5IOKX-ray2.22A1-137[»]
5SVAelectron microscopy15.30n1-244[»]
6MINX-ray1.90A1-137[»]
6MIOX-ray1.85A1-137[»]
6MIPX-ray2.00A1-137[»]
6MIQX-ray1.75A1-137[»]
SMRiP35189
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36052, 298 interactors
ComplexPortaliCPX-1149 Transcription factor TFIIF complex
CPX-1150 SWI/SNF chromatin remodelling complex
CPX-1642 General transcription factor complex TFIID
CPX-1810 NuA3 histone acetyltransferase complex
CPX-863 INO80 chromatin remodeling complex
DIPiDIP-1147N
IntActiP35189, 53 interactors
MINTiP35189
STRINGi4932.YPL129W

PTM databases

iPTMnetiP35189

Proteomic databases

MaxQBiP35189
PaxDbiP35189
PRIDEiP35189

Genome annotation databases

EnsemblFungiiYPL129W_mRNA; YPL129W; YPL129W
GeneIDi855974
KEGGisce:YPL129W

Organism-specific databases

EuPathDBiFungiDB:YPL129W
SGDiS000006050 TAF14

Phylogenomic databases

GeneTreeiENSGT00940000176465
HOGENOMiCLU_078004_0_0_1
InParanoidiP35189
KOiK03140
OMAiYNLHPTF

Enzyme and pathway databases

BioCyciYEAST:G3O-34028-MONOMER
ReactomeiR-SCE-674695 RNA Polymerase II Pre-transcription Events
R-SCE-75955 RNA Polymerase II Transcription Elongation

Miscellaneous databases

EvolutionaryTraceiP35189

Protein Ontology

More...
PROi
PR:P35189
RNActiP35189 protein

Family and domain databases

Gene3Di2.60.40.1970, 1 hit
IDEALiIID50207
InterProiView protein in InterPro
IPR027353 NET_dom
IPR016665 Sas5/TAF14
IPR038704 YEAST_sf
IPR005033 YEATS
PANTHERiPTHR23195 PTHR23195, 1 hit
PTHR23195:SF2 PTHR23195:SF2, 1 hit
PfamiView protein in Pfam
PF17035 BET, 1 hit
PF03366 YEATS, 1 hit
PIRSFiPIRSF016551 SAS5/TFIID_14, 1 hit
PROSITEiView protein in PROSITE
PS51037 YEATS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiTAF14_YEAST
<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: P35189
Secondary accession number(s): D6W3N8, Q02460
<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: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 17, 2020
This is version 180 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 programFungal Protein Annotation Program

<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, 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
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