SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9HBM6

- TAF9B_HUMAN

UniProt

Q9HBM6 - TAF9B_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Transcription initiation factor TFIID subunit 9B
Gene
TAF9B, TAF9L
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. protein binding Source: UniProtKB
  2. transcription corepressor activity Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. DNA-templated transcription, initiation Source: InterPro
  2. negative regulation of apoptotic process Source: BHF-UCL
  3. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  4. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  5. positive regulation of cell growth Source: UniProtKB
  6. programmed cell death Source: Ensembl
  7. protein stabilization Source: BHF-UCL
  8. response to organic cyclic compound Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

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: Chromosome X

Organism-specific databases

HGNCiHGNC:17306. TAF9B.

Subcellular locationi

Nucleus By similarity By similarity

GO - Cellular componenti

  1. transcription factor TFIID complex Source: UniProtKB
  2. transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38225.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Transcription initiation factor TFIID subunit 9B
PRO_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.
GenevestigatoriQ9HBM6.

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

Protein-protein interaction databases

BioGridi119639. 21 interactions.
IntActiQ9HBM6. 2 interactions.
MINTiMINT-1441128.
STRINGi9606.ENSP00000339917.

Structurei

3D structure databases

ProteinModelPortaliQ9HBM6.
SMRiQ9HBM6. Positions 13-76.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the TAF9 family.

Phylogenomic databases

eggNOGiCOG5094.
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

MESGKMAPPK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI    50
LDDAKIYSSH AKKPNVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN 100
QTPLPLIKPY AGPRLPPDRY CLTAPNYRLK SLIKKGPNQG RLVPRLSVGA 150
VSSKPTTPTI ATPQTVSVPN KVATPMSVTS QRFTVQIPPS QSTPVKPVPA 200
TTAVQNVLIN PSMIGPKNIL ITTNMVSSQN TANEANPLKR KHEDDDDNDI 250
M 251
Length:251
Mass (Da):27,622
Last modified:March 1, 2001 - v1
Checksum:iEB3A1116F7E8BCA0
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000598686; ENSP00000472882; ENSG00000269257.
GeneIDi51616.
KEGGihsa:51616.
UCSCiuc004eda.3. human.

Polymorphism databases

DMDMi74752778.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS35340.1.
RefSeqi NP_057059.2. NM_015975.4.
UniGenei Hs.592248.

3D structure databases

ProteinModelPortali Q9HBM6.
SMRi Q9HBM6. Positions 13-76.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119639. 21 interactions.
IntActi Q9HBM6. 2 interactions.
MINTi MINT-1441128.
STRINGi 9606.ENSP00000339917.

PTM databases

PhosphoSitei Q9HBM6.

Polymorphism databases

DMDMi 74752778.

Proteomic databases

MaxQBi Q9HBM6.
PaxDbi Q9HBM6.
PRIDEi Q9HBM6.

Protocols and materials databases

DNASUi 51616.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341864 ; ENSP00000339917 ; ENSG00000187325 .
ENST00000598686 ; ENSP00000472882 ; ENSG00000269257 .
GeneIDi 51616.
KEGGi hsa:51616.
UCSCi uc004eda.3. human.

Organism-specific databases

CTDi 51616.
GeneCardsi GC0XM077385.
H-InvDBi HIX0176727.
HGNCi HGNC:17306. TAF9B.
HPAi HPA045275.
MIMi 300754. gene.
neXtProti NX_Q9HBM6.
PharmGKBi PA38225.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5094.
HOGENOMi HOG000231730.
HOVERGENi HBG002304.
InParanoidi Q9HBM6.
KOi K03133.
OMAi NMANESN.
OrthoDBi EOG7HF1KM.
PhylomeDBi Q9HBM6.
TreeFami TF351417.

Miscellaneous databases

GeneWikii TAF9B.
GenomeRNAii 51616.
NextBioi 55524.
PROi Q9HBM6.
SOURCEi Search...

Gene expression databases

Bgeei Q9HBM6.
CleanExi HS_TAF9B.
Genevestigatori Q9HBM6.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view ]
PANTHERi PTHR12075. PTHR12075. 1 hit.
Pfami PF02291. TFIID-31kDa. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
ProtoNeti Search...

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: Pituitary.
  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: Brain and Urinary bladder.
  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: July 9, 2014
This is version 124 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