BTAF1_HUMAN
ID BTAF1_HUMAN Reviewed; 1849 AA.
AC O14981; B4E0W6; O43578;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=TATA-binding protein-associated factor 172;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase BTAF1;
DE AltName: Full=B-TFIID transcription factor-associated 170 kDa subunit;
DE AltName: Full=TAF(II)170;
DE AltName: Full=TBP-associated factor 172;
DE Short=TAF-172;
GN Name=BTAF1; Synonyms=TAF172;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9342322; DOI=10.1073/pnas.94.22.11827;
RA van der Knaap J.A., Borst J.W., van der Vliet P.C., Gentz R.,
RA Timmers H.T.M.;
RT "Cloning of the cDNA for the TATA-binding protein-associated factorII170
RT subunit of transcription factor B-TFIID reveals homology to global
RT transcription regulators in yeast and Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11827-11832(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9488487; DOI=10.1128/mcb.18.3.1701;
RA Chicca J.J. II, Auble D.T., Pugh B.F.;
RT "Cloning and biochemical characterization of TAF-172, a human homolog of
RT yeast Mot1.";
RL Mol. Cell. Biol. 18:1701-1710(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-330.
RX PubMed=10642510; DOI=10.1042/0264-6021:3450521;
RA Van Der Knaap J.A., Van Den Boom V., Kuipers J., Van Eijk M.J.T.,
RA Van Der Vliet P.C., Timmers H.T.M.;
RT "The gene for human TATA-binding-protein-associated factor (TAFII) 170:
RT structure, promoter and chromosomal localization.";
RL Biochem. J. 345:521-527(2000).
RN [6]
RP INTERACTION WITH DRAP1.
RX PubMed=15509807; DOI=10.1128/mcb.24.22.10072-10082.2004;
RA Klejman M.P., Pereira L.A., van Zeeburg H.J.T., Gilfillan S.,
RA Meisterernst M., Timmers H.T.M.;
RT "NC2alpha interacts with BTAF1 and stimulates its ATP-dependent association
RT with TATA-binding protein.";
RL Mol. Cell. Biol. 24:10072-10082(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulates transcription in association with TATA binding
CC protein (TBP). Removes TBP from the TATA box in an ATP-dependent
CC manner.
CC -!- SUBUNIT: Associates with TBP to form B-TFIID. Binds DRAP1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14981-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14981-2; Sequence=VSP_056510;
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AJ001017; CAA04475.1; -; mRNA.
DR EMBL; AF038362; AAC04573.1; -; mRNA.
DR EMBL; AK303554; BAG64578.1; -; mRNA.
DR EMBL; AL359198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF166118; AAF37803.1; -; Genomic_DNA.
DR CCDS; CCDS7419.1; -. [O14981-1]
DR RefSeq; NP_003963.1; NM_003972.2. [O14981-1]
DR AlphaFoldDB; O14981; -.
DR SMR; O14981; -.
DR BioGRID; 114506; 137.
DR IntAct; O14981; 42.
DR MINT; O14981; -.
DR STRING; 9606.ENSP00000265990; -.
DR GlyGen; O14981; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14981; -.
DR MetOSite; O14981; -.
DR PhosphoSitePlus; O14981; -.
DR BioMuta; BTAF1; -.
DR EPD; O14981; -.
DR jPOST; O14981; -.
DR MassIVE; O14981; -.
DR MaxQB; O14981; -.
DR PaxDb; O14981; -.
DR PeptideAtlas; O14981; -.
DR PRIDE; O14981; -.
DR ProteomicsDB; 48357; -. [O14981-1]
DR ProteomicsDB; 5702; -.
DR Antibodypedia; 16397; 168 antibodies from 22 providers.
DR DNASU; 9044; -.
DR Ensembl; ENST00000265990.12; ENSP00000265990.6; ENSG00000095564.15. [O14981-1]
DR GeneID; 9044; -.
DR KEGG; hsa:9044; -.
DR MANE-Select; ENST00000265990.12; ENSP00000265990.6; NM_003972.3; NP_003963.1.
DR CTD; 9044; -.
DR DisGeNET; 9044; -.
DR GeneCards; BTAF1; -.
DR HGNC; HGNC:17307; BTAF1.
DR HPA; ENSG00000095564; Low tissue specificity.
DR MIM; 605191; gene.
DR neXtProt; NX_O14981; -.
DR OpenTargets; ENSG00000095564; -.
DR PharmGKB; PA25437; -.
DR VEuPathDB; HostDB:ENSG00000095564; -.
DR eggNOG; KOG0392; Eukaryota.
DR GeneTree; ENSGT00940000157500; -.
DR HOGENOM; CLU_000315_1_1_1; -.
DR InParanoid; O14981; -.
DR OMA; SYDICRN; -.
DR PhylomeDB; O14981; -.
DR TreeFam; TF300546; -.
DR PathwayCommons; O14981; -.
DR SignaLink; O14981; -.
DR SIGNOR; O14981; -.
DR BioGRID-ORCS; 9044; 320 hits in 1082 CRISPR screens.
DR ChiTaRS; BTAF1; human.
DR GeneWiki; BTAF1; -.
DR GenomeRNAi; 9044; -.
DR Pharos; O14981; Tbio.
DR PRO; PR:O14981; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O14981; protein.
DR Bgee; ENSG00000095564; Expressed in endothelial cell and 207 other tissues.
DR ExpressionAtlas; O14981; baseline and differential.
DR Genevisible; O14981; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0035562; P:negative regulation of chromatin binding; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR36498; PTHR36498; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Direct protein sequencing; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1849
FT /note="TATA-binding protein-associated factor 172"
FT /id="PRO_0000074311"
FT REPEAT 385..422
FT /note="HEAT 1"
FT REPEAT 426..463
FT /note="HEAT 2"
FT REPEAT 513..550
FT /note="HEAT 3"
FT REPEAT 554..596
FT /note="HEAT 4"
FT REPEAT 818..855
FT /note="HEAT 5"
FT REPEAT 872..910
FT /note="HEAT 6"
FT REPEAT 1102..1139
FT /note="HEAT 7"
FT REPEAT 1182..1219
FT /note="HEAT 8"
FT DOMAIN 1278..1453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1636..1790
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 77..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 191..207
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1404..1407
FT /note="DEGH box"
FT COMPBIAS 81..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1291..1298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056510"
SQ SEQUENCE 1849 AA; 206887 MW; FE3675B75A44F113 CRC64;
MAVSRLDRLF ILLDTGTTPV TRKAAAQQLG EVVKLHPHEL NNLLSKVLIY LRSANWDTRI
AAGQAVEAIV KNVPEWNPVP RTRQEPTSES SMEDSPTTER LNFDRFDICR LLQHGASLLG
SAGAEFEVQD EKSGEVDPKE RIARQRKLLQ KKLGLNMGEA IGMSTEELFN DEDLDYTPTS
ASFVNKQPTL QAAELIDSEF RAGMSNRQKN KAKRMAKLFA KQRSRDAVET NEKSNDSTDG
EPEEKRRKIA NVVINQSAND SKVLIDNIPD SSSLIEETNE WPLESFCEEL CNDLFNPSWE
VRHGAGTGLR EILKAHGKSG GKMGDSTLEE MIQQHQEWLE DLVIRLLCVF ALDRFGDFVS
DEVVAPVRET CAQTLGVVLK HMNETGVHKT VDVLLKLLTQ EQWEVRHGGL LGIKYALAVR
QDVINTLLPK VLTRIIEGLQ DLDDDVRAVA AASLVPVVES LVYLQTQKVP FIINTLWDAL
LELDDLTAST NSIMTLLSSL LTYPQVQQCS IQQSLTVLVP RVWPFLHHTI SSVRRAALET
LFTLLSTQDQ NSSSWLIPIL PDMLRHIFQF CVLESSQEIL DLIHKVWMEL LSKASVQYVV
AAACPWMGAW LCLMMQPSHL PIDLNMLLEV KARAKEKTGG KVRQGQSQNK EVLQEYIAGA
DTIMEDPATR DFVVMRARMM AAKLLGALCC CICDPGVNVV TQEIKPAESL GQLLLFHLNS
KSALQRISVA LVICEWAALQ KECKAVTLAV QPRLLDILSE HLYYDEIAVP FTRMQNECKQ
LISSLADVHI EVGNRVNNNV LTIDQASDLV TTVFNEATSS FDLNPQVLQQ LDSKRQQVQM
TVTETNQEWQ VLQLRVHTFA ACAVVSLQQL PEKLNPIIKP LMETIKKEEN TLVQNYAAQC
IAKLLQQCTT RTPCPNSKII KNLCSSLCVD PYLTPCVTCP VPTQSGQENS KGSTSEKDGM
HHTVTKHRGI ITLYRHQKAA FAITSRRGPT PKAVKAQIAD LPAGSSGNIL VELDEAQKPY
LVQRRGAEFA LTTIVKHFGG EMAVKLPHLW DAMVGPLRNT IDINNFDGKS LLDKGDSPAQ
ELVNSLQVFE TAAASMDSEL HPLLVQHLPH LYMCLQYPST AVRHMAARCV GVMSKIATME
TMNIFLEKVL PWLGAIDDSV KQEGAIEALA CVMEQLDVGI VPYIVLLVVP VLGRMSDQTD
SVRFMATQCF ATLIRLMPLE AGIPDPPNMS AELIQLKAKE RHFLEQLLDG KKLENYKIPV
PINAELRKYQ QDGVNWLAFL NKYKLHGILC DDMGLGKTLQ SICILAGDHC HRAQEYARSK
LAECMPLPSL VVCPPTLTGH WVDEVGKFCS REYLNPLHYT GPPTERIRLQ HQVKRHNLIV
ASYDVVRNDI DFFRNIKFNY CILDEGHVIK NGKTKLSKAV KQLTANYRII LSGTPIQNNV
LELWSLFDFL MPGFLGTERQ FAARYGKPIL ASRDARSSSR EQEAGVLAMD ALHRQVLPFL
LRRMKEDVLQ DLPPKIIQDY YCTLSPLQVQ LYEDFAKSRA KCDVDETVSS ATLSEETEKP
KLKATGHVFQ ALQYLRKLCN HPALVLTPQH PEFKTTAEKL AVQNSSLHDI QHAPKLSALK
QLLLDCGLGN GSTSESGTES VVAQHRILIF CQLKSMLDIV EHDLLKPHLP SVTYLRLDGS
IPPGQRHSIV SRFNNDPSID VLLLTTHVGG LGLNLTGADT VVFVEHDWNP MRDLQAMDRA
HRIGQKRVVN VYRLITRGTL EEKIMGLQKF KMNIANTVIS QENSSLQSMG TDQLLDLFTL
DKDGKAEKAD TSTSGKASMK SILENLSDLW DQEQYDSEYS LENFMHSLK
