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O00268 (TAF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 4
Alternative name(s):
RNA polymerase II TBP-associated factor subunit C
TBP-associated factor 4
Transcription initiation factor TFIID 130 kDa subunit
Short name=TAF(II)130
Short name=TAFII-130
Short name=TAFII130
Transcription initiation factor TFIID 135 kDa subunit
Short name=TAF(II)135
Short name=TAFII-135
Short name=TAFII135
Gene names
Name:TAF4
Synonyms:TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1085 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the TFIID complex, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone.

Subunit structure

TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10 and TRRAP. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with ATF7; the interaction inhibits ATF7-mediated tranactivation. Interacts with SV40 Large T antigen. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus.

Sequence similarities

Belongs to the TAF4 family.

Contains 1 TAFH (NHR1) domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, initiation

Inferred from direct assay PubMed 9603525. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12771217. Source: UniProtKB

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 9603525. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.9. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFIID complex

Inferred from direct assay PubMed 14580349. Source: MGI

transcription factor TFTC complex

Inferred from direct assay Ref.7PubMed 9603525. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15601843. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10851085Transcription initiation factor TFIID subunit 4
PRO_0000118869

Regions

Domain590 – 68798TAFH
Compositional bias39 – 424Poly-His
Compositional bias52 – 576Poly-Ala
Compositional bias98 – 1014Poly-Gly
Compositional bias142 – 1487Poly-Ala
Compositional bias270 – 2778Poly-Pro
Compositional bias333 – 3397Poly-Ala
Compositional bias682 – 6854Poly-Pro
Compositional bias810 – 8156Poly-Ala
Compositional bias830 – 8334Poly-Asp

Natural variations

Natural variant6511P → L.
Corresponds to variant rs6089604 [ dbSNP | Ensembl ].
VAR_052258

Experimental info

Sequence conflict105 – 11713PGPPS…PLVPA → GRGLLQQRGGRES in AAC50901. Ref.5
Sequence conflict1361S → A in CAA72189. Ref.1
Sequence conflict1361S → A in AAC50901. Ref.5
Sequence conflict186 – 1872Missing in CAA72189. Ref.1
Sequence conflict186 – 1872Missing in AAC50901. Ref.5
Sequence conflict235 – 26632Missing in AAC50901. Ref.5
Sequence conflict2951P → L in AAC50901. Ref.5

Secondary structure

.................. 1085
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00268 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: BC2F5B5F143DB145

FASTA1,085110,114
        10         20         30         40         50         60 
MAAGSDLLDE VFFNSEVDEK VVSDLVGSLE SQLAASAAHH HHLAPRTPEV RAAAAGALGN 

        70         80         90        100        110        120 
HVVSGSPAGA AGAGPAAPAE GAPGAAPEPP PAGRARPGGG GPQRPGPPSP RRPLVPAGPA 

       130        140        150        160        170        180 
PPAAKLRPPP EGSAGSCAPV PAAAAVAAGP EPAPAGPAKP AGPAALAARA GPGPGPGPGP 

       190        200        210        220        230        240 
GPGPGPGKPA GPGAAQTLNG SAALLNSHHA AAPAVSLVNN GPAALLPLPK PAAPGTVIQT 

       250        260        270        280        290        300 
PPFVGAAAPP APAAPSPPAA PAPAAPAAAP PPPPPAPATL ARPPGHPAGP PTAAPAVPPP 

       310        320        330        340        350        360 
AAAQNGGSAG AAPAPAPAAG GPAGVSGQPG PGAAAAAPAP GVKAESPKRV VQAAPPAAQT 

       370        380        390        400        410        420 
LAASGPASTA ASMVIGPTMQ GALPSPAAVP PPAPGTPTGL PKGAAGAVTQ SLSRTPTATT 

       430        440        450        460        470        480 
SGIRATLTPT VLAPRLPQPP QNPTNIQNFQ LPPGMVLVRS ENGQLLMIPQ QALAQMQAQA 

       490        500        510        520        530        540 
HAQPQTTMAP RPATPTSAPP VQISTVQAPG TPIIARQVTP TTIIKQVSQA QTTVQPSATL 

       550        560        570        580        590        600 
QRSPGVQPQL VLGGAAQTAS LGTATAVQTG TPQRTVPGAT TTSSAATETM ENVKKCKNFL 

       610        620        630        640        650        660 
STLIKLASSG KQSTETAANV KELVQNLLDG KIEAEDFTSR LYRELNSSPQ PYLVPFLKRS 

       670        680        690        700        710        720 
LPALRQLTPD SAAFIQQSQQ QPPPPTSQAT TALTAVVLSS SVQRTAGKTA ATVTSALQPP 

       730        740        750        760        770        780 
VLSLTQPTQV GVGKQGQPTP LVIQQPPKPG ALIRPPQVTL TQTPMVALRQ PHNRIMLTTP 

       790        800        810        820        830        840 
QQIQLNPLQP VPVVKPAVLP GTKALSAVSA QAAAAQKNKL KEPGGGSFRD DDDINDVASM 

       850        860        870        880        890        900 
AGVNLSEESA RILATNSELV GTLTRSCKDE TFLLQAPLQR RILEIGKKHG ITELHPDVVS 

       910        920        930        940        950        960 
YVSHATQQRL QNLVEKISET AQQKNFSYKD DDRYEQASDV RAQLKFFEQL DQIEKQRKDE 

       970        980        990       1000       1010       1020 
QEREILMRAA KSRSRQEDPE QLRLKQKAKE MQQQELAQMR QRDANLTALA AIGPRKKRKV 

      1030       1040       1050       1060       1070       1080 
DCPGPGSGAE GSGPGSVVPG SSGVGTPRQF TRQRITRVNL RDLIFCLENE RETSHSLLLY 


KAFLK 

« Hide

References

« Hide 'large scale' references
[1]"Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells."
Mengus G., May M., Carre L., Chambon P., Davidson I.
Genes Dev. 11:1381-1395(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100."
Tanese N., Saluja D., Vassallo M.F., Chen J.-L., Admon A.
Proc. Natl. Acad. Sci. U.S.A. 93:13611-13616(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-1085, PARTIAL PROTEIN SEQUENCE.
[6]"TAF-like function of SV40 large T antigen."
Damania B., Alwine J.C.
Genes Dev. 10:1369-1381(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[7]"Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."
Brand M., Yamamoto K., Staub A., Tora L.
J. Biol. Chem. 274:18285-18289(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF5; TRRAP; GCN5L2 AND TAF10.
[8]"Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis."
Cavusoglu N., Brand M., Tora L., van Dorsselaer A.
Proteomics 3:217-223(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[10]"A functional interaction between ATF7 and TAF12 that is modulated by TAF4."
Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C., Chatton B.
Oncogene 24:3472-3483(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs."
Gangloff Y.-G., Werten S., Romier C., Carre L., Poch O., Moras D., Davidson I.
Mol. Cell. Biol. 20:340-351(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 872-920 IN COMPLEX WITH TAF12.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11354 mRNA. Translation: CAA72189.1.
AY623115 Genomic DNA. Translation: AAT38111.1.
AL109911, AL137077 Genomic DNA. Translation: CAI19182.1.
AL137077, AL109911 Genomic DNA. Translation: CAI11045.1.
CH471077 Genomic DNA. Translation: EAW75407.1.
U75308 mRNA. Translation: AAC50901.1.
RefSeqNP_003176.2. NM_003185.3.
UniGeneHs.18857.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3OX-ray2.30A/C872-945[»]
2P6VX-ray2.00A575-688[»]
ProteinModelPortalO00268.
SMRO00268. Positions 583-679, 872-919.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112737. 36 interactions.
DIPDIP-35350N.
IntActO00268. 8 interactions.
MINTMINT-236922.
STRING9606.ENSP00000252996.

PTM databases

PhosphoSiteO00268.

Proteomic databases

PaxDbO00268.
PRIDEO00268.

Protocols and materials databases

DNASU6874.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252996; ENSP00000252996; ENSG00000130699.
GeneID6874.
KEGGhsa:6874.
UCSCuc002ybs.3. human.

Organism-specific databases

CTD6874.
GeneCardsGC20M060529.
H-InvDBHIX0015971.
HIX0174705.
HGNCHGNC:11537. TAF4.
HPACAB031484.
HPA008599.
MIM601796. gene.
neXtProtNX_O00268.
PharmGKBPA36312.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237595.
HOGENOMHOG000154502.
HOVERGENHBG058585.
InParanoidO00268.
KOK03129.
OMALDEVFFN.
PhylomeDBO00268.
TreeFamTF316520.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO00268.
BgeeO00268.
CleanExHS_TAF4.
GenevestigatorO00268.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007900. TAF4.
IPR003894. TAFH_NHR1.
[Graphical view]
PfamPF05236. TAF4. 1 hit.
PF07531. TAFH. 1 hit.
[Graphical view]
SMARTSM00549. TAFH. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS51119. TAFH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTAF4. human.
EvolutionaryTraceO00268.
GeneWikiTAF4.
GenomeRNAi6874.
NextBio26837.
PROO00268.
SOURCESearch...

Entry information

Entry nameTAF4_HUMAN
AccessionPrimary (citable) accession number: O00268
Secondary accession number(s): A6NGD9 expand/collapse secondary AC list , Q5TBP6, Q99721, Q9BR40, Q9BX42
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM