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Protein

Transcription initiation factor TFIID subunit 9

Gene

TAF9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi120 – 13718Add
BLAST

GO - Molecular functioni

  • activating transcription factor binding Source: BHF-UCL
  • C2H2 zinc finger domain binding Source: BHF-UCL
  • DNA binding Source: UniProtKB
  • p53 binding Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  • cellular response to DNA damage stimulus Source: BHF-UCL
  • chromatin organization Source: Reactome
  • gene expression Source: Reactome
  • histone H3 acetylation Source: UniProtKB
  • negative regulation of apoptotic process Source: BHF-UCL
  • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of response to cytokine stimulus Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein stabilization Source: BHF-UCL
  • response to interleukin-1 Source: BHF-UCL
  • transcription elongation from RNA polymerase II promoter Source: Reactome
  • transcription from RNA polymerase II promoter Source: Reactome
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_264245. HATs acetylate histones.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TAF9
Synonyms:TAF2G, TAFII31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:11542. TAF9.

Subcellular locationi

GO - Cellular componenti

  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • PCAF complex Source: UniProtKB
  • pre-snoRNP complex Source: BHF-UCL
  • STAGA complex Source: UniProtKB
  • transcription factor TFIID complex Source: UniProtKB
  • transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36317.

Polymorphism and mutation databases

BioMutaiSLC26A3.
DMDMi2498981.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Transcription initiation factor TFIID subunit 9PRO_0000118888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei161 – 1611PhosphothreonineBy similarity
Modified residuei178 – 1781PhosphothreonineBy similarity
Modified residuei181 – 1811PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16594.
PaxDbiQ16594.
PRIDEiQ16594.

PTM databases

PhosphoSiteiQ16594.

Expressioni

Inductioni

6 to 8-fold by apoptotic signals.1 Publication

Gene expression databases

BgeeiQ16594.
CleanExiHS_TAF9.
ExpressionAtlasiQ16594. baseline and differential.
GenevisibleiQ16594. HS.

Organism-specific databases

HPAiCAB005361.
HPA053429.

Interactioni

Subunit structurei

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/TAFII80.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DRAP1Q149196EBI-712521,EBI-712941
KAT2BQ928313EBI-712521,EBI-477430
KPNA1P522944EBI-712521,EBI-358383
TAF6LQ9Y6J96EBI-712521,EBI-743984

Protein-protein interaction databases

BioGridi112743. 73 interactions.
DIPiDIP-435N.
IntActiQ16594. 42 interactions.
MINTiMINT-2860193.
STRINGi9606.ENSP00000217893.

Structurei

3D structure databases

ProteinModelPortaliQ16594.
SMRiQ16594. Positions 13-76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi250 – 26213Poly-AspAdd
BLAST

Sequence similaritiesi

Belongs to the TAF9 family.Curated

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000231730.
HOVERGENiHBG002304.
InParanoidiQ16594.
KOiK14535.
OMAiTTEYEPR.
PhylomeDBiQ16594.
TreeFamiTF351417.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view]
PANTHERiPTHR12075. PTHR12075. 1 hit.
PfamiPF02291. TFIID-31kDa. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Q16594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI
60 70 80 90 100
LDDAKIYSSH AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN
110 120 130 140 150
QTPLPLIKPY SGPRLPPDRY CLTAPNYRLK SLQKKASTSA GRITVPRLSV
160 170 180 190 200
GSVTSRPSTP TLGTPTPQTM SVSTKVGTPM SLTGQRFTVQ MPTSQSPAVK
210 220 230 240 250
ASIPATSAVQ NVLINPSLIG SKNILITTNM MSSQNTANES SNALKRKRED
260
DDDDDDDDDD YDNL
Length:264
Mass (Da):28,974
Last modified:November 1, 1997 - v1
Checksum:i1925AEC65D6C84C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461Y → V AA sequence (PubMed:9674425).Curated
Sequence conflicti225 – 2251L → F in AAH03400 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61T → M.1 Publication
Corresponds to variant rs4252233 [ dbSNP | Ensembl ].
VAR_016279
Natural varianti210 – 2101Q → H.
Corresponds to variant rs11542580 [ dbSNP | Ensembl ].
VAR_052260

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4002.1.
PIRiI39141.
RefSeqiNP_001015892.1. NM_001015892.1.
NP_003178.1. NM_003187.4.
UniGeneiHs.653163.

Genome annotation databases

EnsembliENST00000615325; ENSP00000484214; ENSG00000085231.
ENST00000615404; ENSP00000478935; ENSG00000276463.
ENST00000616867; ENSP00000477750; ENSG00000276463.
ENST00000617893; ENSP00000477611; ENSG00000276463.
GeneIDi6880.
KEGGihsa:6880.
UCSCiuc003jwc.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4002.1.
PIRiI39141.
RefSeqiNP_001015892.1. NM_001015892.1.
NP_003178.1. NM_003187.4.
UniGeneiHs.653163.

3D structure databases

ProteinModelPortaliQ16594.
SMRiQ16594. Positions 13-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112743. 73 interactions.
DIPiDIP-435N.
IntActiQ16594. 42 interactions.
MINTiMINT-2860193.
STRINGi9606.ENSP00000217893.

PTM databases

PhosphoSiteiQ16594.

Polymorphism and mutation databases

BioMutaiSLC26A3.
DMDMi2498981.

Proteomic databases

MaxQBiQ16594.
PaxDbiQ16594.
PRIDEiQ16594.

Protocols and materials databases

DNASUi6880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000615325; ENSP00000484214; ENSG00000085231.
ENST00000615404; ENSP00000478935; ENSG00000276463.
ENST00000616867; ENSP00000477750; ENSG00000276463.
ENST00000617893; ENSP00000477611; ENSG00000276463.
GeneIDi6880.
KEGGihsa:6880.
UCSCiuc003jwc.1. human.

Organism-specific databases

CTDi6880.
GeneCardsiGC05M068646.
HGNCiHGNC:11542. TAF9.
HPAiCAB005361.
HPA053429.
MIMi600822. gene.
neXtProtiNX_Q16594.
PharmGKBiPA36317.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000231730.
HOVERGENiHBG002304.
InParanoidiQ16594.
KOiK14535.
OMAiTTEYEPR.
PhylomeDBiQ16594.
TreeFamiTF351417.

Enzyme and pathway databases

ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_264245. HATs acetylate histones.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

GeneWikiiTAF9.
GenomeRNAii6880.
NextBioi26873.
PROiQ16594.
SOURCEiSearch...

Gene expression databases

BgeeiQ16594.
CleanExiHS_TAF9.
ExpressionAtlasiQ16594. baseline and differential.
GenevisibleiQ16594. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view]
PANTHERiPTHR12075. PTHR12075. 1 hit.
PfamiPF02291. TFIID-31kDa. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiTAF9_HUMAN
AccessioniPrimary (citable) accession number: Q16594
Secondary accession number(s): D3DWA3, Q5U0D1, Q9BTS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 158 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Caution

AK6 and TAF9 were initially considered as products of the same gene since they share two exons. However, they are translated from different initiation codons and reading frames and encode unrelated proteins. This arrangement is conserved in some mammalian species.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.