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Q9HBM6 (TAF9B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TAF9B
Synonyms:TAF9L
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length251 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.6

Subunit structure

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. Ref.6

Subcellular location

Nucleus By similarity UniProtKB Q16594.

Sequence similarities

Belongs to the TAF9 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Transcription initiation factor TFIID subunit 9B
PRO_0000118891

Regions

Compositional bias244 – 2496Poly-Asp

Amino acid modifications

Modified residue1561Phosphothreonine By similarity
Modified residue1571Phosphothreonine Ref.7
Modified residue1591Phosphothreonine Ref.8

Experimental info

Sequence conflict31S → L in AAD27786. Ref.1
Sequence conflict2091I → D in AAD27786. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9HBM6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EB3A1116F7E8BCA0

FASTA25127,622
        10         20         30         40         50         60 
MESGKMAPPK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH 

        70         80         90        100        110        120 
AKKPNVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN QTPLPLIKPY AGPRLPPDRY 

       130        140        150        160        170        180 
CLTAPNYRLK SLIKKGPNQG RLVPRLSVGA VSSKPTTPTI ATPQTVSVPN KVATPMSVTS 

       190        200        210        220        230        240 
QRFTVQIPPS QSTPVKPVPA TTAVQNVLIN PSMIGPKNIL ITTNMVSSQN TANEANPLKR 

       250 
KHEDDDDNDI M 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 15772651] [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]"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: 15489334] [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: 15899866] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE TFTC-HAT COMPLEX, INTERACTION WITH TAF5 AND TAF6.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00642105.
RefSeqNP_057059.2. NM_015975.4.
UniGeneHs.592248.
Hs.714006.

3D structure databases

ProteinModelPortalQ9HBM6.
SMRQ9HBM6. Positions 13-76.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HBM6. 2 interactions.
MINTMINT-1441128.
STRINGQ9HBM6.

PTM databases

PhosphoSiteQ9HBM6.

Polymorphism databases

DMDM74752778.

Proteomic databases

PRIDEQ9HBM6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341864; ENSP00000339917; ENSG00000187325.
GeneID51616.
KEGGhsa:51616.
UCSCuc004eda.1. human.

Organism-specific databases

CTD51616.
GeneCardsGC0XM077385.
HGNCHGNC:17306. TAF9B.
HPAHPA045275.
MIM300754. gene.
neXtProtNX_Q9HBM6.
PharmGKBPA38225.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12217.
GeneTreeENSGT00390000001626.
HOGENOMHBG320253.
HOVERGENHBG002304.
InParanoidQ9HBM6.
OMANMANESN.
OrthoDBEOG45757B.
PhylomeDBQ9HBM6.

Gene expression databases

ArrayExpressQ9HBM6.
BgeeQ9HBM6.
CleanExHS_TAF9B.
GenevestigatorQ9HBM6.
GermOnlineENSG00000187325. Homo sapiens.

Family and domain databases

InterProIPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view]
Gene3DG3DSA:1.10.20.10. Histone-fold. 1 hit.
KOK03133.
PANTHERPTHR12075. TFIID-31. 1 hit.
PfamPF02291. TFIID-31kDa. 1 hit.
[Graphical view]
SUPFAMSSF47113. Histone-fold. 1 hit.
ProtoNetSearch...

Other

NextBio55524.
SOURCESearch...

Entry information

Entry nameTAF9B_HUMAN
AccessionPrimary (citable) accession number: Q9HBM6
Secondary accession number(s): B2RUZ9, Q9Y2S3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 101 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

Human chromosome X

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families