ID   TAF9B_PONAB             Reviewed;         251 AA.
AC   Q5R7P7; Q5R9Q2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Transcription initiation factor TFIID subunit 9B;
GN   Name=TAF9B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR859331; CAH91508.1; -; mRNA.
DR   EMBL; CR860065; CAH92213.1; -; mRNA.
DR   RefSeq; NP_001126294.1; NM_001132822.1.
DR   AlphaFoldDB; Q5R7P7; -.
DR   SMR; Q5R7P7; -.
DR   STRING; 9601.ENSPPYP00000022945; -.
DR   Ensembl; ENSPPYT00000023912; ENSPPYP00000022945; ENSPPYG00000020497.
DR   GeneID; 100173271; -.
DR   KEGG; pon:100173271; -.
DR   CTD; 51616; -.
DR   eggNOG; KOG3334; Eukaryota.
DR   GeneTree; ENSGT00940000161697; -.
DR   HOGENOM; CLU_068315_2_0_1; -.
DR   InParanoid; Q5R7P7; -.
DR   OrthoDB; 1429345at2759; -.
DR   Proteomes; UP000001595; Chromosome X.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
DR   GO; GO:0033276; C:transcription factor TFTC complex; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..251
FT                   /note="Transcription initiation factor TFIID subunit 9B"
FT                   /id="PRO_0000293547"
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:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         174
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   CONFLICT        41
FT                   /note="E -> G (in Ref. 1; CAH91508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="D -> G (in Ref. 1; CAH91508)"
FT                   /evidence="ECO:0000305"
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