TAF6_RAT
ID TAF6_RAT Reviewed; 678 AA.
AC Q63801;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Transcription initiation factor TFIID subunit 6;
DE AltName: Full=Transcription initiation factor TFIID 70 kDa subunit;
DE Short=TAF(II)70;
DE Short=TAFII70;
DE AltName: Full=Transcription initiation factor TFIID 80 kDa subunit;
DE Short=TAF(II)80;
DE Short=TAFII-80;
DE Short=TAFII80;
DE AltName: Full=p80;
GN Name=Taf6; Synonyms=Taf2e;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7665101; DOI=10.1016/0378-1119(95)00296-i;
RA Kida S., Umehara T., Horikoshi M.;
RT "Three distinct regions in a rat TFIID subunit containing histone H4
RT homology.";
RL Gene 161:303-304(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; TYR-253 AND SER-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. The TFIID complex structure can be divided into 3 modules TFIID-
CC A, TFIID-B, and TFIID-C. TAF6 homodimer connects TFIID modules, forming
CC a rigid core. {ECO:0000250|UniProtKB:P49848}.
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. Interacts
CC directly with TBP, TAF1/TAFII250, TAF9/TAFII31 AND TAF12/TAFII20. The
CC TAF6/TAFII70-TAF9/TAFII31 heterodimer forms an octamer complex with the
CC TAF4B/TFII105-TAF12/TFIID20 heterodimer. Component of some MLL1/MLL
CC complex, at least composed of the core components KMT2A/MLL1, ASH2L,
CC HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
CC BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA,
CC MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Also interacts with the
CC GTFs, TFIIEalpha/GTF2E1 and TFIIFalpha/GTF2F1. Component of the TBP-
CC free TAFII-histone acetylase complex (TFTC-HAT) (By similarity).
CC Interacts with TP53/p53 (By similarity).
CC {ECO:0000250|UniProtKB:P49848}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
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DR EMBL; D49446; BAA08435.1; -; mRNA.
DR RefSeq; XP_008767283.1; XM_008769061.2.
DR RefSeq; XP_008767284.1; XM_008769062.2.
DR RefSeq; XP_017453783.1; XM_017598294.1.
DR AlphaFoldDB; Q63801; -.
DR SMR; Q63801; -.
DR BioGRID; 252593; 1.
DR STRING; 10116.ENSRNOP00000001829; -.
DR iPTMnet; Q63801; -.
DR PhosphoSitePlus; Q63801; -.
DR PaxDb; Q63801; -.
DR PRIDE; Q63801; -.
DR GeneID; 288533; -.
DR UCSC; RGD:1311608; rat.
DR CTD; 6878; -.
DR RGD; 1311608; Taf6.
DR eggNOG; KOG2549; Eukaryota.
DR HOGENOM; CLU_021711_2_0_1; -.
DR InParanoid; Q63801; -.
DR OrthoDB; 384329at2759; -.
DR PhylomeDB; Q63801; -.
DR TreeFam; TF313632; -.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR PRO; PR:Q63801; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q63801; RN.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:RGD.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:RGD.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:RGD.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:RGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:RGD.
DR CDD; cd08050; TAF6C; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.25.40.770; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037796; TAF6.
DR InterPro; IPR011442; TAF6_C.
DR InterPro; IPR046344; TAF6_C_sf.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR PANTHER; PTHR10221; PTHR10221; 1.
DR Pfam; PF02969; TAF; 1.
DR Pfam; PF07571; TAF6_C; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..678
FT /note="Transcription initiation factor TFIID subunit 6"
FT /id="PRO_0000118875"
FT REGION 142..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49848"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 524
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P49848"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62311"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49848"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49848"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 660
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49848"
SQ SEQUENCE 678 AA; 72713 MW; 92D7225E3B7CC171 CRC64;
MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM
GKRQKLTTSD IDYALKLKNV EPLYGFHAQE FIPFRFASGG GRELYFYEEK EVDLSDIINT
PLPRVPLDVC LKAHWLSIEG CQPAIPENPP PAPKEQQKAE ATEPLKSAKP GQEEDGPLKG
KGQGAAAADG KGKEKKAPPL LEGAPFRLKP RSIHELSVEQ QLYYKEITEA CVGSCEAKRA
EALQSIATDP GLYQMLPRFS TFISEGVRVN VVQNNLALLI YLMRMVKALM DNPTLYLEKY
VHELIPAVMT CIVSRQLCLR PDVDNHWALR DFAARLVAQI CKHFSTTTNN IQSRITKTFT
KSWVDEKTPW TTRYGSIAGL AELGHDVIKT LILPRLQQEG ERIRSVLDGP VLSNIDRIGA
DHVQSLLLKH CAPVLAKLRP PPDNQDAYRG EFGSLGPLLC SHVVKARAQA ALQAQQVNRT
TLTITQPRPT LTLSQAPQPG PRTPGLLKVP GSIALPVQTL VSARAAAPPQ PSPPPTKFIV
MSSSSSASST QQVLSLSTSA PGSGSTTTSP VTTTVPSVQP IVKLVSTATT APPSTAPAGP
GSVQKYIVVS LPPTGEGKGG PPSHPSPVPP SSSSPSPLGG SALCGGKQET GDSPPPAPGT
PKANGSQPTG PSSPQPAL
