TAF1_MESAU
ID TAF1_MESAU Reviewed; 1865 AA.
AC Q60544;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Transcription initiation factor TFIID subunit 1;
DE EC=2.3.1.48;
DE EC=2.7.11.1;
DE AltName: Full=Cell cycle gene 1 protein;
DE AltName: Full=TBP-associated factor 250 kDa;
DE Short=p250;
DE AltName: Full=Transcription initiation factor TFIID 250 kDa subunit;
DE Short=TAF(II)250;
DE Short=TAFII-250;
DE Short=TAFII250 {ECO:0000303|PubMed:8163200};
GN Name=TAF1; Synonyms=CCG1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8163200; DOI=10.1016/0378-1119(94)90583-5;
RA Hayashida T., Sekiguchi T., Noguchi E., Sunamoto H., Ohba T., Nishimoto T.;
RT "The CCG1/TAFII250 gene is mutated in thermosensitive G1 mutants of the
RT BHK21 cell line derived from golden hamster.";
RL Gene 141:267-270(1994).
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. TAF1 is the largest component and core scaffold of the TFIID
CC complex, involved in nucleating complex assembly. TAF1 forms a promoter
CC DNA binding subcomplex of TFIID, together with TAF7 and TAF2. Contains
CC novel N- and C-terminal Ser/Thr kinase domains which can
CC autophosphorylate or transphosphorylate other transcription factors.
CC Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated
CC degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues.
CC Possesses DNA-binding activity (By similarity). Essential for
CC progression of the G1 phase of the cell cycle (PubMed:8163200).
CC {ECO:0000250|UniProtKB:P21675, ECO:0000269|PubMed:8163200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Autophosphorylates on Ser residues. Inhibited by
CC retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA
CC inhibits the histone acetyltransferase activity.
CC {ECO:0000250|UniProtKB:P21675}.
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 with
CC TAF7; the interaction is direct. TAF1, when part of the TFIID complex,
CC interacts with C-terminus of TP53. Part of a TFIID-containing RNA
CC polymerase II pre-initiation complex that is composed of TBP and at
CC least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4,
CC GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6,
CC TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. RB1 interacts with the
CC N-terminal domain of TAF1. Interacts with ASF1A and ASF1B. Interacts
CC (via bromo domains) with acetylated lysine residues on the N-terminus
CC of histone H1.4, H2A, H2B, H3 and H4 (in vitro).
CC {ECO:0000250|UniProtKB:P21675}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21675}.
CC -!- DOMAIN: The Bromo domain mediates interaction with histones that have
CC acetylated lysine residues at specific positions. The second domain
CC also recognizes and binds histones that are butyrylated and
CC crotonylated. {ECO:0000250|UniProtKB:P21675}.
CC -!- PTM: Phosphorylated by casein kinase II in vitro.
CC {ECO:0000250|UniProtKB:P21675}.
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
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DR EMBL; D26114; BAA05110.1; -; mRNA.
DR PIR; I48155; I48155.
DR RefSeq; NP_001268498.1; NM_001281569.1.
DR AlphaFoldDB; Q60544; -.
DR SMR; Q60544; -.
DR STRING; 10036.XP_005081284.1; -.
DR GeneID; 101838159; -.
DR CTD; 6872; -.
DR OrthoDB; 103411at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IGI:ParkinsonsUK-UCL.
DR Gene3D; 1.10.1100.10; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR011177; TAF1_animal.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR InterPro; IPR009067; TAF_II_230-bd.
DR InterPro; IPR036741; TAFII-230_TBP-bd_sf.
DR InterPro; IPR041670; Znf-CCHC_6.
DR PANTHER; PTHR13900; PTHR13900; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF09247; TBP-binding; 1.
DR Pfam; PF15288; zf-CCHC_6; 1.
DR PIRSF; PIRSF003047; TAF1_animal; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47055; SSF47055; 1.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; ATP-binding; Bromodomain; Cell cycle;
KW DNA-binding; Isopeptide bond; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..1865
FT /note="Transcription initiation factor TFIID subunit 1"
FT /id="PRO_0000278523"
FT DOMAIN 1..409
FT /note="Protein kinase 1"
FT DOMAIN 1392..1462
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1420..1865
FT /note="Protein kinase 2"
FT DOMAIN 1515..1585
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DNA_BIND 1190..1268
FT /note="HMG box"
FT /evidence="ECO:0000250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..971
FT /note="Histone acetyltransferase (HAT)"
FT /evidence="ECO:0000250"
FT REGION 964..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1624
FT /note="Interaction with ASF1A and ASF1B"
FT /evidence="ECO:0000250"
FT REGION 1625..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1346..1353
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1728
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT MOD_RES 302
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT MOD_RES 539
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT CROSSLNK 557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P21675"
SQ SEQUENCE 1865 AA; 211868 MW; A81614946C0C0F24 CRC64;
MLLPATGASR SAAIMSDTDS DEDSSGGGPF SLTGFLFGNI NGAGQLEGES VLDDECKKHL
AGLGALGLGS LITELTANEE LAGTDGALVN DEGWIRSRED AVDYSDINEV AEDESRRYQQ
TMGSLQPLCH SADYDEDDYD ADCEDIDCKL MPPPPPPPGP VKKEKDQDGL TGEKVDFSSS
SDSESEMGPQ EAAQAESKDG KLTLPLAGIM QHDATKLLPS VTELFPEFRP GKVLRFLRLF
GPGKNVPSVW RSARRKRKKK HREPIQEEQI QEEECSVELE VNQKSLWNYD YAPPPPPEQC
LSDDEITMMA PVESKFSQST GDTDKVMDTK PRVAEWRYGP ARLWYDMLGV PEDGSGFDYG
FKMRKTEHEP AIKCKMMTKL RKLEESNGID LLADENFLMV TQLHWEDDII WDGEDVKHKG
TKPQRASLAG WLPSSMTRNA MAYNVQQGFA ATLDDDKPWY SIFPIDNEDL VYGRWEDNII
WDAQAMPRIL EPPVLTLDPN DENLILEIPD EKEEATSNSP SKENKKESSL KKSRILLGKT
GVIKEEPQQN MSQPEVKDPW NLSNDEYYYP KQQGLRGTFG GNIIQHSIPA VELRQPFFPT
HMGPIKLRQF HRPPLKKYSF GALSQPGPHS VQPLLKHIKK KAKMREQERQ ASGGGEMFFM
RTPQDLTGKD GDLILAEYSE ENGPLMMQVG MATKIKNYYK RKPGKDPGAP DCKYGETVYC
HTSPFLGSLH PGQLLQAFEN NLFRAPIYLH KMPETDFLII RTRQGYYIRE LVDIFVVGQQ
CPLFEVPGPN SKRANTHIRD FLQVFIYRLF WKSKDRPRRI RMEDIKKAFP SHSESSIRKR
LKLCADFKRT GMDSNWWVLK SDFRLPTEEE IRAMVSPEQC CAYYSMIAAE QRLKDAGYGE
KSFFAPEEEN EEDFQMKIDD EVRTAPWNTT RAFIAAMKGK CLLEVTGVAD PTGCGEGFSY
VKIPNKPTQQ KDDKEPQPVK KTVTGTDADL RRLSLKNAKQ LLRKFGVPEE EIKKLSRWEV
IDVVRTMSTE QARSGEGPMS KFARGSRFSV AEHQERYKEE CQRIFDLQNK VLSSTEVLST
DTDSSSAEDS DFEEMGKNIE NMLQNKKTSS QLSREREEQE RKELQRMLLA AGSASAGNNH
RDDDTASVTS LNSSATGRCL KIYRTFRDEE GKEYVRCETV RKPAVIDAYV RIRTTKDEEF
IRKFALFDEQ HREEMRKERR RIQEQLRRLK RNQEKEKLKG PPEKKPKKMK ERPDLKLKCG
ACGAIGHMRT NKFCPLYYQT NAPPSNPVAM TEEQEEELEK TVIHNDNEEL IKVEGTKIVL
GKQLIESADE VRRKSLVLKF PKQQLPPKKK RRVGTTVHCD YLNRPHKSIH RRRTDPMVTL
SSILESIIND MRDLPNTYPF HTPVNAKVVK DYYKIITRPM DLQTLRENVR KRLYPSREEF
REHLELIVKN SATYNGPKHS LTQISQSMLD LCDEKLKEKE DKLARLEKAI NPLLDDDDQV
AFSFILDNIV TQKMMAVPDS WPFHHPVNKK FVPDYYKVIV SPMDLETIRK NISKHKYQSR
ESFLDDVNLI LANSVKYNGS ESQYTKTAQE IVNVCYQTLT EYDEHLTQLE KDICTAKEAA
LEEAELESLD PMTPGPYTPQ PPDLYDNSTS LSVSRDASVY QDESNMSVLD IPSATSEKQL
TQEGEDGDGD LADEEEGTVQ QPQASVLYED LLMSEGEDDE EDAGSDEEGD NPFSAIQLSE
SGSDSDVGSG SIRPKQPRVL QENTRMGMEN EESMMSYEGD GGEVSRGLED SNISYGSYEE
PDPKSNTQDT SFSSIGGYEV SEEEEDEEEQ RSGPSVLSQV HLSEDEEDSE DFHSIAGDSD
MDSDE
