TAF9B_HUMAN
ID TAF9B_HUMAN Reviewed; 251 AA.
AC Q9HBM6; B2RUZ9; Q9Y2S3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcription initiation factor TFIID subunit 9B;
DE AltName: Full=Neuronal cell death-related protein 7;
DE Short=DN-7;
DE AltName: Full=Transcription initiation factor TFIID subunit 9-like;
DE AltName: Full=Transcription-associated factor TAFII31L;
GN Name=TAF9B; Synonyms=TAF9L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:AAD27786.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary {ECO:0000312|EMBL:AAD27786.1};
RA Peng Y., Song H., Zhou J., Huang Q., Dai M., Mao Y., Yu Y., Xu X., Luo B.,
RA Chen J., Hu R.;
RT "Human neuronal cell death related gene in neuron-7 (DN-7).";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAD27786.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Villard L.;
RT "Characterization of a new TAFII31 gene located in Xq13.3.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AL049589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4] {ECO:0000312|EMBL:AAD27786.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH09566.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH10350.1}, and
RC Urinary bladder {ECO:0000312|EMBL:AAH09566.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND INTERACTION WITH TAF5
RP AND TAF6.
RX PubMed=15899866; DOI=10.1128/mcb.25.11.4638-4649.2005;
RA Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B.,
RA Scheer E., Tora L.;
RT "TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping
RT roles with TAF9.";
RL Mol. Cell. Biol. 25:4638-4649(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-174, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in
CC transcriptional activation as well as repression of distinct but
CC overlapping sets of genes. May have a role in gene regulation
CC associated with apoptosis. TAFs are components of the transcription
CC factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF
CC histone acetylase complex and the STAGA transcription coactivator-HAT
CC complex. TFIID or TFTC are essential for the regulation of RNA
CC polymerase II-mediated transcription. {ECO:0000269|PubMed:15899866}.
CC -!- SUBUNIT: Binds TAF5 and TAF6. Component of TFIID and the TATA-binding
CC protein-free TAF complex (TFTC). TFIID is composed of TATA binding
CC protein (TBP) and a number of TBP-associated factors (TAFs). Binds N-
CC terminal domain of p53/TP53 which is essential for transcription.
CC {ECO:0000269|PubMed:15899866}.
CC -!- INTERACTION:
CC Q9HBM6; Q14919: DRAP1; NbExp=7; IntAct=EBI-751601, EBI-712941;
CC Q9HBM6; Q9Y6J9: TAF6L; NbExp=10; IntAct=EBI-751601, EBI-743984;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000255}.
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DR EMBL; AF077053; AAD27786.1; -; mRNA.
DR EMBL; AF220509; AAG09711.1; -; mRNA.
DR EMBL; AL049589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98601.1; -; Genomic_DNA.
DR EMBL; BC009566; AAH09566.1; -; mRNA.
DR EMBL; BC010350; AAH10350.1; -; mRNA.
DR EMBL; BC071649; AAH71649.1; -; mRNA.
DR EMBL; BC146952; AAI46953.1; -; mRNA.
DR EMBL; BC146960; AAI46961.1; -; mRNA.
DR CCDS; CCDS35340.1; -.
DR RefSeq; NP_057059.2; NM_015975.4.
DR PDB; 7KTR; EM; 2.93 A; E=1-251.
DR PDB; 7KTS; EM; 19.09 A; E=1-251.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; Q9HBM6; -.
DR SMR; Q9HBM6; -.
DR BioGRID; 119639; 103.
DR CORUM; Q9HBM6; -.
DR IntAct; Q9HBM6; 32.
DR MINT; Q9HBM6; -.
DR STRING; 9606.ENSP00000339917; -.
DR GlyGen; Q9HBM6; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q9HBM6; -.
DR PhosphoSitePlus; Q9HBM6; -.
DR BioMuta; TAF9B; -.
DR DMDM; 74752778; -.
DR EPD; Q9HBM6; -.
DR jPOST; Q9HBM6; -.
DR MassIVE; Q9HBM6; -.
DR MaxQB; Q9HBM6; -.
DR PaxDb; Q9HBM6; -.
DR PeptideAtlas; Q9HBM6; -.
DR PRIDE; Q9HBM6; -.
DR ProteomicsDB; 81578; -.
DR Antibodypedia; 28250; 135 antibodies from 23 providers.
DR DNASU; 51616; -.
DR Ensembl; ENST00000341864.6; ENSP00000339917.5; ENSG00000187325.5.
DR GeneID; 51616; -.
DR KEGG; hsa:51616; -.
DR MANE-Select; ENST00000341864.6; ENSP00000339917.5; NM_015975.5; NP_057059.2.
DR UCSC; uc004eda.4; human.
DR CTD; 51616; -.
DR GeneCards; TAF9B; -.
DR HGNC; HGNC:17306; TAF9B.
DR HPA; ENSG00000187325; Low tissue specificity.
DR MIM; 300754; gene.
DR neXtProt; NX_Q9HBM6; -.
DR OpenTargets; ENSG00000187325; -.
DR PharmGKB; PA38225; -.
DR VEuPathDB; HostDB:ENSG00000187325; -.
DR eggNOG; KOG3334; Eukaryota.
DR GeneTree; ENSGT00940000161697; -.
DR HOGENOM; CLU_068315_2_0_1; -.
DR InParanoid; Q9HBM6; -.
DR OMA; PNYRLKP; -.
DR OrthoDB; 1429345at2759; -.
DR PhylomeDB; Q9HBM6; -.
DR TreeFam; TF351417; -.
DR PathwayCommons; Q9HBM6; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; Q9HBM6; -.
DR BioGRID-ORCS; 51616; 14 hits in 707 CRISPR screens.
DR ChiTaRS; TAF9B; human.
DR GeneWiki; TAF9B; -.
DR GenomeRNAi; 51616; -.
DR Pharos; Q9HBM6; Tbio.
DR PRO; PR:Q9HBM6; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9HBM6; protein.
DR Bgee; ENSG00000187325; Expressed in saphenous vein and 189 other tissues.
DR Genevisible; Q9HBM6; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IC:BHF-UCL.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IC:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR CDD; cd07979; TAF9; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003162; TFIID-31.
DR Pfam; PF02291; TFIID-31kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..251
FT /note="Transcription initiation factor TFIID subunit 9B"
FT /id="PRO_0000118891"
FT REGION 229..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CONFLICT 3
FT /note="S -> L (in Ref. 1; AAD27786)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="I -> D (in Ref. 1; AAD27786)"
FT /evidence="ECO:0000305"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 35..60
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 251 AA; 27622 MW; EB3A1116F7E8BCA0 CRC64;
MESGKMAPPK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
AKKPNVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN QTPLPLIKPY AGPRLPPDRY
CLTAPNYRLK SLIKKGPNQG RLVPRLSVGA VSSKPTTPTI ATPQTVSVPN KVATPMSVTS
QRFTVQIPPS QSTPVKPVPA TTAVQNVLIN PSMIGPKNIL ITTNMVSSQN TANEANPLKR
KHEDDDDNDI M
