TAF12_BOVIN
ID TAF12_BOVIN Reviewed; 161 AA.
AC Q3T174;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transcription initiation factor TFIID subunit 12;
DE AltName: Full=Transcription initiation factor TFIID 20/15 kDa subunits;
DE Short=TAFII-20/TAFII-15;
DE Short=TAFII20/TAFII15;
GN Name=TAF12;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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. Component of the TATA-binding protein-free TAF complex (TFTC),
CC the PCAF histone acetylase complex and the STAGA transcription
CC coactivator-HAT complex. {ECO:0000250|UniProtKB:Q16514}.
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. Component of the
CC TATA-binding protein-free TAF complex (TFTC), the PCAF histone
CC acetylase complex and the STAGA transcription coactivator-HAT complex.
CC Component of the PCAF complex, at least composed of TADA2L/ADA2,
CC TADA3L/ADA3, TAF5L/PAF65-beta, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and
CC TRRAP. Component of the STAGA transcription coactivator-HAT complex, at
CC least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, STAF65-gamma/SUPT7L,
CC TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Interacts with ATF7 (via
CC the transactivation domain); the interaction is prevented by
CC sumoylation of ATF7. {ECO:0000250|UniProtKB:Q16514}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=TAFII20;
CC IsoId=Q3T174-1; Sequence=Displayed;
CC Name=TAFII15;
CC IsoId=Q3T174-2; Sequence=VSP_021966;
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
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DR EMBL; BC102082; AAI02083.1; -; mRNA.
DR RefSeq; NP_001029926.1; NM_001034754.1. [Q3T174-1]
DR RefSeq; XP_005203291.1; XM_005203234.3. [Q3T174-1]
DR RefSeq; XP_005203292.1; XM_005203235.3. [Q3T174-1]
DR AlphaFoldDB; Q3T174; -.
DR SMR; Q3T174; -.
DR STRING; 9913.ENSBTAP00000037817; -.
DR PaxDb; Q3T174; -.
DR PRIDE; Q3T174; -.
DR Ensembl; ENSBTAT00000037998; ENSBTAP00000037817; ENSBTAG00000026660. [Q3T174-1]
DR Ensembl; ENSBTAT00000067990; ENSBTAP00000068815; ENSBTAG00000026660. [Q3T174-1]
DR GeneID; 614227; -.
DR KEGG; bta:614227; -.
DR CTD; 6883; -.
DR VEuPathDB; HostDB:ENSBTAG00000026660; -.
DR eggNOG; KOG1142; Eukaryota.
DR GeneTree; ENSGT00390000002144; -.
DR HOGENOM; CLU_093619_3_1_1; -.
DR InParanoid; Q3T174; -.
DR OMA; HRRDTTV; -.
DR OrthoDB; 1569957at2759; -.
DR TreeFam; TF323652; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000026660; Expressed in oocyte and 106 other tissues.
DR GO; GO:0000124; C:SAGA complex; IEA:Ensembl.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0033276; C:transcription factor TFTC complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:Ensembl.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0043966; P:histone H3 acetylation; 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:0051091; P:positive regulation of DNA-binding transcription factor activity; 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; IBA:GO_Central.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..161
FT /note="Transcription initiation factor TFIID subunit 12"
FT /id="PRO_0000268197"
FT DOMAIN 56..128
FT /note="Histone-fold"
FT /evidence="ECO:0000305"
FT REGION 15..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform TAFII15)"
FT /evidence="ECO:0000305"
FT /id="VSP_021966"
SQ SEQUENCE 161 AA; 17955 MW; 055E01737D0F99CE CRC64;
MNQFGPSALI NLSNFSSIKP EPASTPPQGS MANSTAVVKI PGTPGTGGRL SPENNQVLTK
KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC QLARHRKSST LEVKDVQLHL
ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ RMALIRKTTK K
