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Protein

Transcription initiation factor TFIID subunit 9B

Gene

TAF9B

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

GO - Molecular functioni

  • transcription corepressor activity Source: BHF-UCL

GO - Biological processi

  • gene expression Source: Reactome
  • 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 transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of cell growth Source: UniProtKB
  • protein stabilization 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

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_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 9B
Alternative name(s):
Neuronal cell death-related protein 7
Short name:
DN-7
Transcription initiation factor TFIID subunit 9-like
Transcription-associated factor TAFII31L
Gene namesi
Name:TAF9B
Synonyms:TAF9L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17306. TAF9B.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • transcription factor TFIID complex Source: UniProtKB
  • transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38225.

Polymorphism and mutation databases

BioMutaiTAF9B.
DMDMi74752778.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Transcription initiation factor TFIID subunit 9BPRO_0000118891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei159 – 1591Phosphothreonine1 Publication
Modified residuei174 – 1741Phosphothreonine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HBM6.
PaxDbiQ9HBM6.
PRIDEiQ9HBM6.

PTM databases

PhosphoSiteiQ9HBM6.

Expressioni

Gene expression databases

BgeeiQ9HBM6.
CleanExiHS_TAF9B.
GenevisibleiQ9HBM6. HS.

Organism-specific databases

HPAiHPA045275.

Interactioni

Subunit structurei

Binds TAF5 and TAF6. Component of TFIID and the TATA-binding protein-free TAF complex (TFTC). TFIID is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Binds N-terminal domain of p53/TP53 which is essential for transcription.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DRAP1Q149194EBI-751601,EBI-712941
TAF6LQ9Y6J93EBI-751601,EBI-743984

Protein-protein interaction databases

BioGridi119639. 31 interactions.
IntActiQ9HBM6. 3 interactions.
MINTiMINT-1441128.

Structurei

3D structure databases

ProteinModelPortaliQ9HBM6.
SMRiQ9HBM6. Positions 13-76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi244 – 2496Poly-AspSequence Analysis

Sequence similaritiesi

Belongs to the TAF9 family.Sequence Analysis

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000231730.
HOVERGENiHBG002304.
InParanoidiQ9HBM6.
KOiK03133.
OMAiNMANESN.
OrthoDBiEOG7HF1KM.
PhylomeDBiQ9HBM6.
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.

Q9HBM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESGKMAPPK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI
60 70 80 90 100
LDDAKIYSSH AKKPNVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN
110 120 130 140 150
QTPLPLIKPY AGPRLPPDRY CLTAPNYRLK SLIKKGPNQG RLVPRLSVGA
160 170 180 190 200
VSSKPTTPTI ATPQTVSVPN KVATPMSVTS QRFTVQIPPS QSTPVKPVPA
210 220 230 240 250
TTAVQNVLIN PSMIGPKNIL ITTNMVSSQN TANEANPLKR KHEDDDDNDI

M
Length:251
Mass (Da):27,622
Last modified:March 1, 2001 - v1
Checksum:iEB3A1116F7E8BCA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → L in AAD27786 (Ref. 1) Curated
Sequence conflicti209 – 2091I → D in AAD27786 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077053 mRNA. Translation: AAD27786.1.
AF220509 mRNA. Translation: AAG09711.1.
AL049589 Genomic DNA. Translation: CAI42952.1.
CH471104 Genomic DNA. Translation: EAW98601.1.
BC009566 mRNA. Translation: AAH09566.1.
BC010350 mRNA. Translation: AAH10350.1.
BC071649 mRNA. Translation: AAH71649.1.
BC146952 mRNA. Translation: AAI46953.1.
BC146960 mRNA. Translation: AAI46961.1.
CCDSiCCDS35340.1.
RefSeqiNP_057059.2. NM_015975.4.
UniGeneiHs.592248.

Genome annotation databases

EnsembliENST00000341864; ENSP00000339917; ENSG00000187325.
GeneIDi51616.
KEGGihsa:51616.
UCSCiuc004eda.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077053 mRNA. Translation: AAD27786.1.
AF220509 mRNA. Translation: AAG09711.1.
AL049589 Genomic DNA. Translation: CAI42952.1.
CH471104 Genomic DNA. Translation: EAW98601.1.
BC009566 mRNA. Translation: AAH09566.1.
BC010350 mRNA. Translation: AAH10350.1.
BC071649 mRNA. Translation: AAH71649.1.
BC146952 mRNA. Translation: AAI46953.1.
BC146960 mRNA. Translation: AAI46961.1.
CCDSiCCDS35340.1.
RefSeqiNP_057059.2. NM_015975.4.
UniGeneiHs.592248.

3D structure databases

ProteinModelPortaliQ9HBM6.
SMRiQ9HBM6. Positions 13-76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119639. 31 interactions.
IntActiQ9HBM6. 3 interactions.
MINTiMINT-1441128.

PTM databases

PhosphoSiteiQ9HBM6.

Polymorphism and mutation databases

BioMutaiTAF9B.
DMDMi74752778.

Proteomic databases

MaxQBiQ9HBM6.
PaxDbiQ9HBM6.
PRIDEiQ9HBM6.

Protocols and materials databases

DNASUi51616.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341864; ENSP00000339917; ENSG00000187325.
GeneIDi51616.
KEGGihsa:51616.
UCSCiuc004eda.3. human.

Organism-specific databases

CTDi51616.
GeneCardsiGC0XM077385.
H-InvDBHIX0176727.
HGNCiHGNC:17306. TAF9B.
HPAiHPA045275.
MIMi300754. gene.
neXtProtiNX_Q9HBM6.
PharmGKBiPA38225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000231730.
HOVERGENiHBG002304.
InParanoidiQ9HBM6.
KOiK03133.
OMAiNMANESN.
OrthoDBiEOG7HF1KM.
PhylomeDBiQ9HBM6.
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_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

GeneWikiiTAF9B.
GenomeRNAii51616.
NextBioi55524.
PROiQ9HBM6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBM6.
CleanExiHS_TAF9B.
GenevisibleiQ9HBM6. 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 neuronal cell death related gene in neuron-7 (DN-7)."
    Peng Y., Song H., Zhou J., Huang Q., Dai M., Mao Y., Yu Y., Xu X., Luo B., Chen J., Hu R.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: PituitaryImported.
  2. "Characterization of a new TAFII31 gene located in Xq13.3."
    Villard L.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: BrainImported and Urinary bladderImported.
  6. "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, IDENTIFICATION IN THE TFTC-HAT COMPLEX, INTERACTION WITH TAF5 AND TAF6.
  7. "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 THR-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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 THR-174 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTAF9B_HUMAN
AccessioniPrimary (citable) accession number: Q9HBM6
Secondary accession number(s): B2RUZ9, Q9Y2S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 132 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.