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Protein

Transcription initiation factor TFIID subunit 9B

Gene

Taf9b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Biological processi

  1. DNA-templated transcription, initiation Source: InterPro
  2. negative regulation of apoptotic process Source: MGI
  3. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  4. positive regulation of cell growth Source: MGI
  5. protein stabilization Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 9B
Alternative name(s):
Transcription initiation factor TFIID subunit 9-like
Transcription-associated factor TAFII31L
Gene namesi
Name:Taf9b
Synonyms:Taf9l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:3039562. Taf9b.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Transcription initiation factor TFIID subunit 9BPRO_0000118892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei172 – 1721PhosphothreonineBy similarity
Modified residuei175 – 1751PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6NZA9.
PaxDbiQ6NZA9.
PRIDEiQ6NZA9.

PTM databases

PhosphoSiteiQ6NZA9.

Expressioni

Gene expression databases

BgeeiQ6NZA9.
ExpressionAtlasiQ6NZA9. baseline and differential.
GenevestigatoriQ6NZA9.

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6NZA9.
SMRiQ6NZA9. Positions 13-76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi241 – 2477Poly-AspSequence Analysis

Sequence similaritiesi

Belongs to the TAF9 family.Sequence Analysis

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000231730.
HOVERGENiHBG002304.
InParanoidiQ6NZA9.
KOiK03133.
OrthoDBiEOG7HF1KM.
PhylomeDBiQ6NZA9.

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.

Q6NZA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAKMAPIK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI
60 70 80 90 100
LDDAKIYSSH AKKPTVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN
110 120 130 140 150
QTPLPLIKPY AGPRLPPDRY CLTAPNYRLK SLVKKGPNQG RLVPRLSAVS
160 170 180 190 200
SRPTTPPVAP PQAVSGPNKA ATPVSVTSQR FAVQIPPSQS TPAKPAPAAT
210 220 230 240
AVQNVLINPS MIGPKNILIT TSMVSSQNTA TDSNPLKRKH DDDDDNDTM
Length:249
Mass (Da):27,172
Last modified:January 24, 2006 - v2
Checksum:i5615C356885322FD
GO

Sequence cautioni

The sequence AAH51635.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE20773.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281I → T in AAH66223 (PubMed:15489334).Curated
Sequence conflicti193 – 1931A → T in BAE22420 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK131710 mRNA. Translation: BAE20773.1. Different initiation.
AK135097 mRNA. Translation: BAE22420.1.
AL833778 Genomic DNA. Translation: CAM23480.1.
BC051635 mRNA. Translation: AAH51635.1. Different initiation.
BC066223 mRNA. Translation: AAH66223.1.
CCDSiCCDS30340.1.
RefSeqiNP_001001176.2. NM_001001176.2.
NP_001161460.1. NM_001167988.1.
UniGeneiMm.19440.

Genome annotation databases

EnsembliENSMUST00000055497; ENSMUSP00000059751; ENSMUSG00000047242.
GeneIDi407786.
KEGGimmu:407786.
UCSCiuc009ubq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK131710 mRNA. Translation: BAE20773.1. Different initiation.
AK135097 mRNA. Translation: BAE22420.1.
AL833778 Genomic DNA. Translation: CAM23480.1.
BC051635 mRNA. Translation: AAH51635.1. Different initiation.
BC066223 mRNA. Translation: AAH66223.1.
CCDSiCCDS30340.1.
RefSeqiNP_001001176.2. NM_001001176.2.
NP_001161460.1. NM_001167988.1.
UniGeneiMm.19440.

3D structure databases

ProteinModelPortaliQ6NZA9.
SMRiQ6NZA9. Positions 13-76.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ6NZA9.

Proteomic databases

MaxQBiQ6NZA9.
PaxDbiQ6NZA9.
PRIDEiQ6NZA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055497; ENSMUSP00000059751; ENSMUSG00000047242.
GeneIDi407786.
KEGGimmu:407786.
UCSCiuc009ubq.2. mouse.

Organism-specific databases

CTDi51616.
MGIiMGI:3039562. Taf9b.

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000231730.
HOVERGENiHBG002304.
InParanoidiQ6NZA9.
KOiK03133.
OrthoDBiEOG7HF1KM.
PhylomeDBiQ6NZA9.

Enzyme and pathway databases

ReactomeiREACT_230204. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_232708. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_244380. RNA Polymerase II Transcription Initiation.
REACT_255009. RNA Polymerase II Pre-transcription Events.
REACT_255334. RNA Polymerase II Promoter Escape.

Miscellaneous databases

NextBioi407183.
PROiQ6NZA9.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NZA9.
ExpressionAtlasiQ6NZA9. baseline and differential.
GenevestigatoriQ6NZA9.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: Olfactory bulbImported and TestisImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6Imported and C57BL/6JImported.
    Tissue: EmbryoImported and KidneyImported.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTAF9B_MOUSE
AccessioniPrimary (citable) accession number: Q6NZA9
Secondary accession number(s): A2AP80
, Q3UXZ3, Q3V2M4, Q80WW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: March 4, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.