TAF1B_RAT
ID TAF1B_RAT Reviewed; 586 AA.
AC D3ZYB7;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit B;
DE AltName: Full=RNA polymerase I-specific TBP-associated factor 63 kDa;
DE Short=TAFI63;
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 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FLNA (via N-terminus) (By similarity).
CC Component of the transcription factor SL1/TIF-IB complex, composed of
CC TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex
CC interacts directly with TBP, TAF1A and TAF1C. Interaction of the
CC SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with TBP and RRN3
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; NP_001178036.1; NM_001191107.1.
DR AlphaFoldDB; D3ZYB7; -.
DR STRING; 10116.ENSRNOP00000006187; -.
DR PaxDb; D3ZYB7; -.
DR PRIDE; D3ZYB7; -.
DR Ensembl; ENSRNOT00000086798; ENSRNOP00000069237; ENSRNOG00000061415.
DR GeneID; 690450; -.
DR KEGG; rno:690450; -.
DR CTD; 9014; -.
DR RGD; 1596058; Taf1b.
DR eggNOG; ENOG502QVGU; Eukaryota.
DR GeneTree; ENSGT00440000033827; -.
DR HOGENOM; CLU_032815_0_0_1; -.
DR InParanoid; D3ZYB7; -.
DR OMA; PRSFVWL; -.
DR OrthoDB; 329399at2759; -.
DR PhylomeDB; D3ZYB7; -.
DR TreeFam; TF324353; -.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR PRO; PR:D3ZYB7; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000061415; Expressed in thymus and 19 other tissues.
DR Genevisible; D3ZYB7; RN.
DR GO; GO:0070860; C:RNA polymerase I core factor complex; ISO:RGD.
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 InterPro; IPR033599; TAF1B/Rrn7.
DR InterPro; IPR021752; TF_Rrn7_Zf.
DR PANTHER; PTHR31576; PTHR31576; 1.
DR Pfam; PF11781; zf-RRN7; 1.
PE 3: Inferred from homology;
KW Acetylation; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..586
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit B"
FT /id="PRO_0000416869"
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 158..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 586 AA; 68022 MW; 12D8B55FB785329C CRC64;
MDVEQMKAFT DRCSQCAAVS WGLTDEGKYY CTSCHNVTDR SEEVVSTAVI PNTKINSISR
GLRQRSKHEK GWDWYVCEGF QCILYHQAEA LETLGVSPEL KNEVLHSFWK RYLQKSKQAY
CKNPVRTSGR KAKVLEDNLQ SSDWGSDFEL LSDTTCPPES GAEFQSDSQT PKPFPATKRS
SKSASVCSGS VDGVEYSERK EKGLLKMTVP RTLALCYLSL LWQRETITLS DLLRFVEEDR
IPYINAFKVF PEEMKVYGRD KGIFAVESWP DYEDIYKNMI EVAVFLDLPR FPDITEDCYL
HPNTLCMKYL LEVNLPEEMY TLTCQVVKLT GIGEVDFLTF DPIAKMTRTV KHDVQAVAVI
VLVLKLLFLL DDKLEWSYSD LAEAYNEGHK EETPQFDFRK WYQVMKKTFD EKRRKWEEAR
AKYVWKTKRP LYRSHIDKSV AYKRREMVEN LQKQFSALIG SAPEVERQAP SSFQLNWTGE
DTGSPCFHGH SLQGLLISKG QALITKNSLY WLSTHKFCKS YCKHVTTYEE SNFSLSYQFI
LNIFSFLLRI KTSALHEEVS LLEKKLFEKK YNESKRSSRS KKVRRH
