TAF7_CRIGR
ID TAF7_CRIGR Reviewed; 341 AA.
AC Q6R1L1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Transcription initiation factor TFIID subunit 7;
GN Name=TAF7;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=15078871; DOI=10.1074/jbc.m401078200;
RA Fukuchi J., Hiipakka R.A., Kokontis J.M., Nishimura K., Igarashi K.,
RA Liao S.;
RT "TATA-binding protein-associated factor 7 regulates polyamine transport
RT activity and polyamine analog-induced apoptosis.";
RL J. Biol. Chem. 279:29921-29929(2004).
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-256 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; AY518896; AAS13444.1; -; mRNA.
DR RefSeq; NP_001233653.1; NM_001246724.1.
DR AlphaFoldDB; Q6R1L1; -.
DR SMR; Q6R1L1; -.
DR STRING; 10029.NP_001233653.1; -.
DR GeneID; 100689466; -.
DR KEGG; cge:100689466; -.
DR CTD; 6879; -.
DR eggNOG; KOG4011; Eukaryota.
DR OrthoDB; 1348389at2759; -.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
DR GO; GO:0000296; P:spermine transport; IDA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
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 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Transcription;
KW Transcription regulation.
FT CHAIN 1..341
FT /note="Transcription initiation factor TFIID subunit 7"
FT /id="PRO_0000293544"
FT REGION 105..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..341
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 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
SQ SEQUENCE 341 AA; 39156 MW; A4651C8FD4B1D008 CRC64;
MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD GRHGIVRVDR
VPLAAKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD GDLYPPVEEP VAPADPKASK
KKDKDKEKKF VWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR
WEIIAEDETK ETENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEEDVNVID
TEEDLERQLQ DKLNESDEQH QENEGTNQLV MGIQKQIDNM KGKLQETQDR AKRQEDLIMK
VENLALKNRF QAVLDELKQK EDREKEQLSS LQEGLESLLE K
