ID   TAF1B_MOUSE             Reviewed;         586 AA.
AC   P97358; E9QJY7; Q08AT7; Q3V292; Q6NSS9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE   AltName: Full=RNA polymerase I-specific TBP-associated factor 68 kDa;
DE            Short=TAFI68;
DE   AltName: Full=TATA box-binding protein-associated factor 1B;
DE            Short=TBP-associated factor 1B;
DE   AltName: Full=Transcription initiation factor SL1/TIF-IB subunit B;
GN   Name=Taf1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH TBP;
RP   TAF1A AND TAF1C.
RX   PubMed=9050847; DOI=10.1073/pnas.94.5.1733;
RA   Heix J., Zomerdijk J.C.B.M., Ravanpay A., Tjian R., Grummt I.;
RT   "Cloning of murine RNA polymerase I-specific TAF factors: conserved
RT   interactions between the subunits of the species-specific transcription
RT   initiation factor TIF-IB/SL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1733-1738(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C3H/HeJ, C57BL/6J, and NOD;
RC   TISSUE=Brain, Dendritic cell, and Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH RRN3.
RX   PubMed=12015311; DOI=10.1074/jbc.m201232200;
RA   Cavanaugh A.H., Hirschler-Laszkiewicz I., Hu Q., Dundr M., Smink T.,
RA   Misteli T., Rothblum L.I.;
RT   "Rrn3 phosphorylation is a regulatory checkpoint for ribosome biogenesis.";
RL   J. Biol. Chem. 277:27423-27432(2002).
RN   [6]
RP   INTERACTION WITH FLNA.
RX   PubMed=21228480; DOI=10.1271/bbb.100567;
RA   Qiu H., Nomiyama R., Moriguchi K., Fukada T., Sugimoto K.;
RT   "Identification of novel nuclear protein interactions with the N-terminal
RT   part of filamin A.";
RL   Biosci. Biotechnol. Biochem. 75:145-147(2011).
CC   -!- FUNCTION: Component of RNA polymerase I core factor complex that acts
CC       as a GTF2B/TFIIB-like factor and plays a key role in multiple steps
CC       during transcription initiation such as pre-initiation complex (PIC)
CC       assembly and postpolymerase recruitment events in polymerase I (Pol I)
CC       transcription. Binds rDNA promoters and plays a role in Pol I
CC       recruitment as a component of the SL1/TIF-IB complex and, possibly,
CC       directly through its interaction with RRN3.
CC       {ECO:0000269|PubMed:9050847}.
CC   -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC       composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the
CC       complex interacts directly with TBP, TAF1A and TAF1C. Interaction of
CC       the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC       transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3.
CC       Interacts with FLNA (via N-terminus). Part of Pol I pre-initiation
CC       complex (PIC), in which Pol I core assembles with RRN3 and promoter-
CC       bound UTBF and SL1/TIF-IB complex. {ECO:0000250|UniProtKB:Q53T94,
CC       ECO:0000269|PubMed:12015311, ECO:0000269|PubMed:21228480,
CC       ECO:0000269|PubMed:9050847}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q53T94}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P97358-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97358-2; Sequence=VSP_028024, VSP_028025;
CC   -!- DOMAIN: Although it shares weak sequence similarity with GTF2B/TFIIB,
CC       displays a similar subdomain organization as GTF2B/TFIIB, with a N-
CC       terminal zinc finger, a connecting region (composed of B-reader and B-
CC       linker regions), followed by 2 cyclin folds. The RRN7-type zinc finger
CC       plays an essential postrecruitment role in Pol I transcription at a
CC       step preceding synthesis of the first 40 nucleotides (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}.
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DR   EMBL; Y09973; CAA71092.1; -; Genomic_DNA.
DR   EMBL; AK131963; BAE20906.1; -; mRNA.
DR   EMBL; AK165580; BAE38271.1; -; mRNA.
DR   EMBL; AK170313; BAE41709.1; -; mRNA.
DR   EMBL; AC125067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC057167; AAH57167.1; -; mRNA.
DR   EMBL; BC069907; AAH69907.1; -; mRNA.
DR   EMBL; BC094035; AAH94035.1; -; mRNA.
DR   EMBL; BC125027; AAI25028.1; -; mRNA.
DR   EMBL; BC125028; AAI25029.1; -; mRNA.
DR   CCDS; CCDS36419.1; -. [P97358-1]
DR   RefSeq; NP_065639.2; NM_020614.2. [P97358-1]
DR   AlphaFoldDB; P97358; -.
DR   BioGRID; 203957; 13.
DR   CORUM; P97358; -.
DR   IntAct; P97358; 3.
DR   MINT; P97358; -.
DR   STRING; 10090.ENSMUSP00000075339; -.
DR   iPTMnet; P97358; -.
DR   PhosphoSitePlus; P97358; -.
DR   EPD; P97358; -.
DR   MaxQB; P97358; -.
DR   PaxDb; 10090-ENSMUSP00000075339; -.
DR   PeptideAtlas; P97358; -.
DR   ProteomicsDB; 263063; -. [P97358-1]
DR   ProteomicsDB; 263064; -. [P97358-2]
DR   Pumba; P97358; -.
DR   Antibodypedia; 26617; 184 antibodies from 22 providers.
DR   DNASU; 21340; -.
DR   Ensembl; ENSMUST00000075954.9; ENSMUSP00000075339.8; ENSMUSG00000059669.9. [P97358-1]
DR   GeneID; 21340; -.
DR   KEGG; mmu:21340; -.
DR   UCSC; uc007nej.2; mouse. [P97358-1]
DR   UCSC; uc007nel.2; mouse. [P97358-2]
DR   AGR; MGI:109577; -.
DR   CTD; 9014; -.
DR   MGI; MGI:109577; Taf1b.
DR   VEuPathDB; HostDB:ENSMUSG00000059669; -.
DR   eggNOG; ENOG502QVGU; Eukaryota.
DR   GeneTree; ENSGT00440000033827; -.
DR   HOGENOM; CLU_032815_0_0_1; -.
DR   InParanoid; P97358; -.
DR   OMA; SFRFCWG; -.
DR   OrthoDB; 5319728at2759; -.
DR   PhylomeDB; P97358; -.
DR   TreeFam; TF324353; -.
DR   Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   BioGRID-ORCS; 21340; 24 hits in 81 CRISPR screens.
DR   ChiTaRS; Taf1b; mouse.
DR   PRO; PR:P97358; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P97358; Protein.
DR   Bgee; ENSMUSG00000059669; Expressed in spermatocyte and 244 other cell types or tissues.
DR   ExpressionAtlas; P97358; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0070860; C:RNA polymerase I core factor complex; ISO:MGI.
DR   GO; GO:0000120; C:RNA polymerase I transcription regulator complex; TAS:MGI.
DR   GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; ISS:UniProtKB.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; TAS:MGI.
DR   InterPro; IPR048538; Rrn7_cyclin_C.
DR   InterPro; IPR048540; Rrn7_cyclin_N.
DR   InterPro; IPR033599; TAF1B/Rrn7.
DR   InterPro; IPR021752; TF_Rrn7_Zf.
DR   PANTHER; PTHR31576; TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR RNA POLYMERASE I SUBUNIT B; 1.
DR   PANTHER; PTHR31576:SF2; TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR RNA POLYMERASE I SUBUNIT B; 1.
DR   Pfam; PF20645; Rrn7_cyclin_C; 1.
DR   Pfam; PF20644; Rrn7_cyclin_N; 1.
DR   Pfam; PF11781; zf-RRN7; 1.
DR   Genevisible; P97358; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..586
FT                   /note="TATA box-binding protein-associated factor RNA
FT                   polymerase I subunit B"
FT                   /id="PRO_0000304406"
FT   ZN_FING         5..39
FT                   /note="RRN7-type"
FT   REGION          40..68
FT                   /note="B-reader"
FT                   /evidence="ECO:0000250"
FT   REGION          69..73
FT                   /note="B-linker"
FT                   /evidence="ECO:0000250"
FT   REGION          74..259
FT                   /note="N-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   REGION          260..370
FT                   /note="C-terminal cyclin fold"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T94"
FT   MOD_RES         438
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53T94"
FT   VAR_SEQ         1..100
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028024"
FT   VAR_SEQ         101
FT                   /note="K -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028025"
FT   CONFLICT        2
FT                   /note="D -> N (in Ref. 1; CAA71092, 2; BAE38271/BAE41709
FT                   and 4; AAH57167/AAI25028/AAI25029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="K -> T (in Ref. 4; AAI25029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="D -> G (in Ref. 2; BAE20906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   586 AA;  67954 MW;  85E0EBB8C742EE71 CRC64;
     MDVEEVKAFR DRCSQCAAVS WGLTDEGKYY CTSCHNVTDR SEEVVSAADI PNTKINSINR
     GLRQRSKHEK GWDWYVCEGF QCILYHQAKA LETLGVSPEL KNEVLHNFWK RYLQKSKQAY
     CKNPVRTSGR KAKVLEDSVQ SSDLGSDLEL LSDTTCPLES EAEFQSDPQI PKPFPVTKGS
     PKSASVCSGS VDGVEYSERK EKGLVKMTVP RTLALCSLSL LWQRETITVS DLLRFVEEDH
     IPYINAFKLF PEEMKVYGRD KGIFAIESWP DYEDIYKNMI ELAIFLDLPR FPDITEDCYL
     HPNTLCMKYL LEVNLPDEMH TLTCQVVKLT GIGEVDFLTF DPIAKTKRTV KYDVQAMAVI
     VVVLKLLFLL DDKLEWSYSD LAEAYNEQHR EDTPQFDFRK WYQVMKKTFD EKRRKWEEAR
     ARYAWKTKRP LYRSHIDKSV AYKRRKMVEN LQKQFSALVG SSPVVEKQAP SSFQFNWTEE
     GTDSPCFHGH SLQGLLIMKG QSMITKNSLY WLSTQKFCKS YCKHVTTYEE SNFSLSYQFI
     LNIFSFLLRI KTSALHEEVS LLEKKLFEKK YNESKKSSGS KKGRRH
//