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Q16594 (TAF9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 9
Alternative name(s):
RNA polymerase II TBP-associated factor subunit G
STAF31/32
Transcription initiation factor TFIID 31 kDa subunit
Short name=TAFII-31
Short name=TAFII31
Transcription initiation factor TFIID 32 kDa subunit
Short name=TAFII-32
Short name=TAFII32
Gene names
Name:TAF9
Synonyms:TAF2G, TAFII31
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. Ref.14

Subunit structure

Component of TFIID, the TATA-binding protein-free TAF complex (TFTC), the PCAF complex and the STAGA transcription coactivator-HAT complex. The PCAF complex consists at least of TADA2L/ADA2, SUPT3H/SPT3, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. The STAGA transcription coactivator-HAT complex consists at least of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Binds N-terminal domain of p53/TP53 which is essential for transcription. 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. Binds TFIIB and the Herpes simplex virus activator VP16. Forms a heterodimer with TAF6/TAFII80 in a complex with the TAF4B/TAFII105-TAF12/TAFII20 heterodimer. Also interacts with TAF5. Binds directly DNA. Increased DNA binding when complexed with TAF6/TAFII80. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Subcellular location

Nucleus Ref.8 Ref.9.

Induction

6 to 8-fold by apoptotic signals. Ref.14

Sequence similarities

Belongs to the TAF9 family.

Caution

Together with AK6, were initially considered as products of the same gene since they are sharing exons. However, they are translated from different initiation codons and reading frames and encode unrelated proteins. This arrangement is conserved in mammals but these proteins are produced by separate genes in non-mammalian species.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred by curator PubMed 11278372. Source: BHF-UCL

chromatin organization

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay Ref.9Ref.8. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.14. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred by curator Ref.14. Source: BHF-UCL

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 11278372. Source: BHF-UCL

positive regulation of cell growth

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of response to cytokine stimulus

Inferred from mutant phenotype PubMed 15489227. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11278372. Source: BHF-UCL

protein stabilization

Inferred from direct assay Ref.14. Source: BHF-UCL

response to interleukin-1

Inferred from mutant phenotype PubMed 15489227. Source: BHF-UCL

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

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.11. Source: UniProtKB

PCAF complex

Inferred from direct assay Ref.8. Source: UniProtKB

STAGA complex

Inferred from direct assay Ref.9. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

pre-snoRNP complex

Inferred from direct assay PubMed 17636026. Source: BHF-UCL

transcription factor TFIID complex

Inferred from direct assay Ref.14. Source: UniProtKB

transcription factor TFTC complex

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionC2H2 zinc finger domain binding

Inferred from physical interaction PubMed 19251649. Source: BHF-UCL

DNA binding

Inferred from direct assay Ref.13. Source: UniProtKB

activating transcription factor binding

Inferred from physical interaction PubMed 19251649PubMed 9171108. Source: BHF-UCL

p53 binding

Inferred from physical interaction PubMed 11278372. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay Ref.9. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19251649. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Transcription initiation factor TFIID subunit 9
PRO_0000118888

Regions

DNA binding120 – 13718 Ref.13
Compositional bias250 – 26213Poly-Asp

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17
Modified residue51N6-acetyllysine Ref.17
Modified residue1491Phosphoserine Ref.16 Ref.18
Modified residue1581Phosphoserine Ref.16
Modified residue1591Phosphothreonine Ref.16
Modified residue1611Phosphothreonine Ref.15
Modified residue1781Phosphothreonine Ref.15 Ref.18
Modified residue1811Phosphoserine Ref.15

Natural variations

Natural variant61T → M. Ref.5
Corresponds to variant rs4252233 [ dbSNP | Ensembl ].
VAR_016279
Natural variant2101Q → H.
Corresponds to variant rs11542580 [ dbSNP | Ensembl ].
VAR_052260

Experimental info

Sequence conflict461Y → V AA sequence Ref.8
Sequence conflict2251L → F in AAH03400. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q16594 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 1925AEC65D6C84C7

FASTA26428,974
        10         20         30         40         50         60 
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH 

        70         80         90        100        110        120 
AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN QTPLPLIKPY SGPRLPPDRY 

       130        140        150        160        170        180 
CLTAPNYRLK SLQKKASTSA GRITVPRLSV GSVTSRPSTP TLGTPTPQTM SVSTKVGTPM 

       190        200        210        220        230        240 
SLTGQRFTVQ MPTSQSPAVK ASIPATSAVQ NVLINPSLIG SKNILITTNM MSSQNTANES 

       250        260 
SNALKRKRED DDDDDDDDDD YDNL 

« Hide

References

« Hide 'large scale' references
[1]"Human TAFII31 protein is a transcriptional coactivator of the p53 protein."
Lu H., Levine A.J.
Proc. Natl. Acad. Sci. U.S.A. 92:5154-5158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VP16 AND TFIIB.
[2]"Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation."
Klemm R.D., Goodrich J.A., Zhou S., Tjian R.
Proc. Natl. Acad. Sci. U.S.A. 92:5788-5792(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAF6.
[3]"Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors."
Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-6.
[6]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].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Testis.
[8]"Histone-like TAFs within the PCAF histone acetylase complex."
Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J., Howard B.H., Qin J., Nakatani Y.
Cell 94:35-44(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-55; 79-89; 176-200 AND 223-246, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 AND TAF12, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily."
Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J., Nakatani Y.
Mol. Cell 2:869-875(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H; TAF6L; TAF10; TAF12 AND TRRAP.
[11]"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.
[12]"Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locus."
Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.
J. Biol. Chem. 280:36429-36441(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[13]"Core promoter binding by histone-like TAF complexes."
Shao H., Revach M., Moshonov S., Tzuman Y., Gazit K., Albeck S., Unger T., Dikstein R.
Mol. Cell. Biol. 25:206-219(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF6 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B, DNA-BINDING.
[14]"TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9."
Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B., Scheer E., Tora L.
Mol. Cell. Biol. 25:4638-4649(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INDUCTION, INTERACTION WITH TAF5 AND TAF6.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; THR-178 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-158 AND THR-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25112 mRNA. Translation: AAA91318.1.
U21858 mRNA. Translation: AAC50153.1.
U30504 mRNA. Translation: AAA84389.1.
BT019652 mRNA. Translation: AAV38458.1.
AY189986 Genomic DNA. Translation: AAN84793.1.
CH471137 Genomic DNA. Translation: EAW51295.1.
CH471137 Genomic DNA. Translation: EAW51296.1.
BC003400 mRNA. Translation: AAH03400.1.
BC033320 mRNA. Translation: AAH33320.1.
PIRI39141.
RefSeqNP_001015892.1. NM_001015892.1.
NP_003178.1. NM_003187.4.
UniGeneHs.653163.

3D structure databases

ProteinModelPortalQ16594.
SMRQ16594. Positions 13-76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112743. 70 interactions.
DIPDIP-435N.
IntActQ16594. 42 interactions.
MINTMINT-2860193.
STRING9606.ENSP00000217893.

PTM databases

PhosphoSiteQ16594.

Polymorphism databases

DMDM2498981.

Proteomic databases

PaxDbQ16594.
PRIDEQ16594.

Protocols and materials databases

DNASU6880.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217893; ENSP00000217893; ENSG00000085231.
ENST00000328663; ENSP00000370193; ENSG00000085231.
ENST00000506736; ENSP00000421873; ENSG00000085231.
ENST00000571444; ENSP00000459034; ENSG00000263302.
ENST00000577094; ENSP00000460768; ENSG00000263302.
GeneID6880.
KEGGhsa:6880.
UCSCuc003jwc.1. human.

Organism-specific databases

CTD6880.
GeneCardsGC05M068646.
GC05M068647.
HGNCHGNC:11542. TAF9.
HPACAB005361.
MIM600822. gene.
neXtProtNX_Q16594.
PharmGKBPA36317.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5094.
HOGENOMHOG000231730.
HOVERGENHBG002304.
InParanoidQ16594.
KOK14535.
PhylomeDBQ16594.
TreeFamTF351417.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_172623. Chromatin organization.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ16594.
BgeeQ16594.
CleanExHS_TAF9.
GenevestigatorQ16594.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view]
PANTHERPTHR12075. PTHR12075. 1 hit.
PfamPF02291. TFIID-31kDa. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTAF9. human.
GeneWikiTAF9.
GenomeRNAi6880.
NextBio26873.
PROQ16594.
SOURCESearch...

Entry information

Entry nameTAF9_HUMAN
AccessionPrimary (citable) accession number: Q16594
Secondary accession number(s): D3DWA3, Q5U0D1, Q9BTS1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 143 of the entry and version 1 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

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 5

Human chromosome 5: entries, gene names and cross-references to MIM