Transcription initiation factor IIF subunit alpha

<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

Miscellaneous

<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

• DNA binding Source: UniProtKB-KW
• protein phosphatase activator activity Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1."
    Kops O., Zhou X.Z., Lu K.P.
    FEBS Lett 513:305-311(2002) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II general transcription initiation factor activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• TFIIF-class transcription factor complex binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• dephosphorylation of RNA polymerase II C-terminal domain Source: SGDInferred from direct assayⁱ
  • "Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1."
    Kops O., Zhou X.Z., Lu K.P.
    FEBS Lett 513:305-311(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription elongation from RNA polymerase II promoter Source: InterPro
• promoter clearance from RNA polymerase II promoter Source: SGD <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • Ref.1

    "TFIIF-TAF-RNA polymerase II connection."
    Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.
    Genes Dev. 8:2868-2878(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 125-142 AND 143-161.
• regulation of protein serine/threonine phosphatase activity Source: SGDInferred from direct assayⁱ
  • "Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1."
    Kops O., Zhou X.Z., Lu K.P.
    FEBS Lett 513:305-311(2002) [PubMed] [Europe PMC] [Abstract]
• RNA polymerase II preinitiation complex assembly Source: SGDInferred by curatorⁱ
  • Ref.1

    "TFIIF-TAF-RNA polymerase II connection."
    Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.
    Genes Dev. 8:2868-2878(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 125-142 AND 143-161.
• transcriptional start site selection at RNA polymerase II promoter Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Amino acid substitutions in yeast TFIIF confer upstream shifts in transcription initiation and altered interaction with RNA polymerase II."
    Ghazy M.A., Brodie S.A., Ammerman M.L., Ziegler L.M., Ponticelli A.S.
    Mol Cell Biol 24:10975-10985(2004) [PubMed] [Europe PMC] [Abstract]
  • "A functional role for the switch 2 region of yeast RNA polymerase II in transcription start site utilization and abortive initiation."
    Majovski R.C., Khaperskyy D.A., Ghazy M.A., Ponticelli A.S.
    J Biol Chem 280:34917-34923(2005) [PubMed] [Europe PMC] [Abstract]
  • "Functions of Saccharomyces cerevisiae TFIIF during transcription start site utilization."
    Khaperskyy D.A., Ammerman M.L., Majovski R.C., Ponticelli A.S.
    Mol Cell Biol 28:3757-3766(2008) [PubMed] [Europe PMC] [Abstract]
• transcription elongation from RNA polymerase II promoter Source: SGDInferred from direct assayⁱ
  • "Functions of Saccharomyces cerevisiae TFIIF during transcription start site utilization."
    Khaperskyy D.A., Ammerman M.L., Majovski R.C., Ponticelli A.S.
    Mol Cell Biol 28:3757-3766(2008) [PubMed] [Europe PMC] [Abstract]
• transcription initiation from RNA polymerase II promoter Source: SGDInferred from direct assayⁱ
  • "Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae."
    Sayre M.H., Tschochner H., Kornberg R.D.
    J Biol Chem 267:23376-23382(1992) [PubMed] [Europe PMC] [Abstract]
  • "Functions of Saccharomyces cerevisiae TFIIF during transcription start site utilization."
    Khaperskyy D.A., Ammerman M.L., Majovski R.C., Ponticelli A.S.
    Mol Cell Biol 28:3757-3766(2008) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Keywords - Cellular componentⁱ

<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

Amino acid modifications

<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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

GO - Molecular functionⁱ

• TFIIF-class transcription factor complex binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

<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

Compositional bias

<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

Phylogenomic databases

Family and domain databases

<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.

        10         20         30         40         50
MSRRNPPGSR NGGGPTNASP FIKRDRMRRN FLRMRMGQNG SNSSSPGVPN 
        60         70         80         90        100
GDNSRGSLVK KDDPEYAEER EKMLLQIGVE ADAGRSNVKV KDEDPNEYNE 
       110        120        130        140        150
FPLRAIPKED LENMRTHLLK FQSKKKINPV TDFHLPVRLH RKDTRNLQFQ 
       160        170        180        190        200
LTRAEIVQRQ KEISEYKKKA EQERSTPNSG GMNKSGTVSL NNTVKDGSQT 
       210        220        230        240        250
PTVDSVTKDN TANGVNSSIP TVTGSSVPPA SPTTVSAVES NGLSNGSTSA 
       260        270        280        290        300
ANGLDGNAST ANLANGRPLV TKLEDAGPAE DPTKVGMVKY DGKEVTNEPE 
       310        320        330        340        350
FEEGTMDPLA DVAPDGGGRA KRGNLRRKTR QLKVLDENAK KLRFEEFYPW 
       360        370        380        390        400
VMEDFDGYNT WVGSYEAGNS DSYVLLSVED DGSFTMIPAD KVYKFTARNK 
       410        420        430        440        450
YATLTIDEAE KRMDKKSGEV PRWLMKHLDN IGTTTTRYDR TRRKLKAVAD 
       460        470        480        490        500
QQAMDEDDRD DNSEVELDYD EEFADDEEAP IIDGNEQENK ESEQRIKKEM 
       510        520        530        540        550
LQANAMGLRD EEAPSENEED ELFGEKKIDE DGERIKKALQ KTELAALYSS 
       560        570        580        590        600
DENEINPYLS ESDIENKENE SPVKKEEDSD TLSKSKRSSP KKQQKKATNA 
       610        620        630        640        650
HVHKEPTLRV KSIKNCVIIL KGDKKILKSF PEGEWNPQTT KAVDSSNNAS 
       660        670        680        690        700
NTVPSPIKQE EGLNSTVAER EETPAPTITE KDIIEAIGDG KVNIKEFGKF 
       710        720        730 
IRRKYPGAEN KKLMFAIVKK LCRKVGNDHM ELKKE                 

Experimental Info

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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