TAF7_PONAB
ID TAF7_PONAB Reviewed; 349 AA.
AC Q5R7L9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Transcription initiation factor TFIID subunit 7;
GN Name=TAF7;
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=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription. TFIID recognizes and binds promoters with or without a
CC TATA box via its subunit TBP, a TATA-box-binding protein, and promotes
CC assembly of the pre-initiation complex (PIC). The TFIID complex
CC consists of TBP and TBP-associated factors (TAFs), including TAF1,
CC TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and
CC TAF13. TAF7 forms a promoter DNA binding subcomplex of TFIID, together
CC with TAF1 and TAF2. Part of a TFIID complex containing TAF10 (TFIID
CC alpha) and a TFIID complex lacking TAF10 (TFIID beta).
CC {ECO:0000250|UniProtKB:Q15545}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Part of a TFIID-
CC containing RNA polymerase II pre-initiation complex that is composed of
CC TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2,
CC GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3,
CC TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13.
CC Interacts with TAF1; the interaction is direct. Interacts with TAF1,
CC TAF5, TAF11, TAF12, and TAF13, but not with TAF10 or TBP. Component of
CC some MLL1/MLL complex, at least composed of the core components
CC KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the
CC facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L,
CC MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A,
CC RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts
CC with CIITA and TAF1 and inhibits their acetyltransferase activity, and
CC behaving as a repressor of CIITA- and TAF1-regulated promoters.
CC {ECO:0000250|UniProtKB:Q15545}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9R1C0}.
CC -!- PTM: Phosphorylated by CIITA. Phosphorylation at Ser-264 by TAF1 in
CC early G1 phase disrupts binding to TAF1.
CC {ECO:0000250|UniProtKB:Q15545}.
CC -!- SIMILARITY: Belongs to the TAF7 family. {ECO:0000305}.
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DR EMBL; CR860095; CAH92241.1; -; mRNA.
DR RefSeq; NP_001126311.1; NM_001132839.1.
DR AlphaFoldDB; Q5R7L9; -.
DR SMR; Q5R7L9; -.
DR STRING; 9601.ENSPPYP00000017766; -.
DR Ensembl; ENSPPYT00000018481; ENSPPYP00000017766; ENSPPYG00000015885.
DR GeneID; 100173290; -.
DR KEGG; pon:100173290; -.
DR CTD; 6879; -.
DR eggNOG; KOG4011; Eukaryota.
DR GeneTree; ENSGT00940000160861; -.
DR HOGENOM; CLU_037860_0_1_1; -.
DR InParanoid; Q5R7L9; -.
DR OMA; KTLQYPH; -.
DR OrthoDB; 1348389at2759; -.
DR TreeFam; TF313044; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IEA:Ensembl.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; IEA:Ensembl.
DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IEA:Ensembl.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IEA:Ensembl.
DR GO; GO:0106140; F:P-TEFb complex binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:Ensembl.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; IEA:Ensembl.
DR GO; GO:0045344; P:negative regulation of MHC class I biosynthetic process; IEA:Ensembl.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IEA:Ensembl.
DR CDD; cd08047; TAF7; 1.
DR InterPro; IPR037817; TAF7.
DR InterPro; IPR006751; TAFII55_prot_cons_reg.
DR PANTHER; PTHR12228; PTHR12228; 1.
DR Pfam; PF04658; TAFII55_N; 1.
DR SMART; SM01370; TAFII55_N; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..349
FT /note="Transcription initiation factor TFIID subunit 7"
FT /id="PRO_0000293546"
FT REGION 105..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 236..341
FT /evidence="ECO:0000255"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
SQ SEQUENCE 349 AA; 40259 MW; 0AAFD3E33E3CCD6E CRC64;
MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD GRHGIVRVDR
VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD GDLYPPVEEP VASTDPKASK
KKDKDKEKKF IWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR
WEIIAEDETK EAENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD
EEDINIIDTE EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK
RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK
