ID TAF1B_HUMAN Reviewed; 588 AA. AC Q53T94; B4DI42; F8WD72; Q15574; Q8WVC3; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 160. 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 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], PROTEIN SEQUENCE OF 11-20; 42-56; 93-110; RP 123-135; 264-276; 281-289; 311-321; 331-340; 396-407; 429-444; 448-466 AND RP 471-480, FUNCTION, INTERACTION WITH TBP; TAF1A AND TAF1C, AND VARIANTS RP SER-6; ILE-282; ALA-351 AND ASP-462. RX PubMed=7801123; DOI=10.1126/science.7801123; RA Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.; RT "Reconstitution of transcription factor SL1: exclusive binding of TBP by RT SL1 or TFIID subunits."; RL Science 266:1966-1972(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ILE-282; RP ALA-351 AND ASP-462. RC TISSUE=Corpus callosum; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-6; ILE-282; RP ALA-351 AND ASP-462. RC TISSUE=Colon; 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 FUNCTION. RX PubMed=7801130; DOI=10.1126/science.7801130; RA Zomerdijk J.C., Beckmann H., Comai L., Tjian R.; RT "Assembly of transcriptionally active RNA polymerase I initiation factor RT SL1 from recombinant subunits."; RL Science 266:2015-2018(1994). RN [6] RP FUNCTION, AND DNA-BINDING. RX PubMed=7491500; DOI=10.1126/science.270.5241.1506; RA Beckmann H., Chen J.L., O'Brien T., Tjian R.; RT "Coactivator and promoter-selective properties of RNA polymerase I TAFs."; RL Science 270:1506-1509(1995). RN [7] RP IDENTIFICATION. RX PubMed=10894955; DOI=10.1159/000015592; RA Di Pietro C., Rapisarda A., Amico V., Bonaiuto C., Viola A., Scalia M., RA Motta S., Amato A., Engel H., Messina A., Sichel G., Grzeschik K., RA Purrello M.; RT "Genomic localization of the human genes TAF1A, TAF1B and TAF1C, encoding RT TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I general transcription RT initiation factor SL1."; RL Cytogenet. Cell Genet. 89:133-136(2000). RN [8] RP FUNCTION OF THE SL1/TIF-IB COMPLEX, SUBUNIT, INTERACTION WITH RRN3, AND RP SUBCELLULAR LOCATION. RX PubMed=11250903; DOI=10.1093/emboj/20.6.1373; RA Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I., RA Zomerdijk J.C.B.M.; RT "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to RT rRNA gene promoters."; RL EMBO J. 20:1373-1382(2001). RN [9] RP FUNCTION OF THE SL1/TIF-IB COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11283244; DOI=10.1128/mcb.21.8.2641-2649.2001; RA Panov K.I., Friedrich J.K., Zomerdijk J.C.; RT "A step subsequent to preinitiation complex assembly at the ribosomal RNA RT gene promoter is rate limiting for human RNA polymerase I-dependent RT transcription."; RL Mol. Cell. Biol. 21:2641-2649(2001). RN [10] RP FUNCTION OF THE SL1/TIF-IB COMPLEX. RX PubMed=15970593; DOI=10.1074/jbc.m501595200; RA Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.; RT "TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex RT formation and stabilizes upstream binding factor at the rDNA promoter."; RL J. Biol. Chem. 280:29551-29558(2005). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP FUNCTION. RX PubMed=21921198; DOI=10.1126/science.1207699; RA Knutson B.A., Hahn S.; RT "Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I general RT transcription factors."; RL Science 333:1637-1640(2011). RN [13] RP FUNCTION, AND MUTAGENESIS OF CYS-13; CYS-31 AND CYS-34. RX PubMed=21921199; DOI=10.1126/science.1207656; RA Naidu S., Friedrich J.K., Russell J., Zomerdijk J.C.; RT "TAF1B is a TFIIB-like component of the basal transcription machinery for RT RNA polymerase I."; RL Science 333:1640-1642(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). 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:11250903, ECO:0000269|PubMed:11283244, CC ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:21921198, CC ECO:0000269|PubMed:21921199, ECO:0000269|PubMed:7491500, CC ECO:0000269|PubMed:7801123, ECO:0000269|PubMed:7801130}. 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 Part of Pol I pre-initiation complex (PIC), in which Pol I core CC assembles with RRN3 and promoter-bound UTBF and SL1/TIF-IB complex. CC {ECO:0000250, ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11283244, CC ECO:0000269|PubMed:7801123}. CC -!- INTERACTION: CC Q53T94; P49748: ACADVL; NbExp=3; IntAct=EBI-1560239, EBI-727618; CC Q53T94; P27797: CALR; NbExp=3; IntAct=EBI-1560239, EBI-1049597; CC Q53T94; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1560239, EBI-16439278; CC Q53T94; Q01105: SET; NbExp=3; IntAct=EBI-1560239, EBI-1053182; CC Q53T94; P20226: TBP; NbExp=4; IntAct=EBI-1560239, EBI-355371; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305|PubMed:11250903, CC ECO:0000305|PubMed:11283244}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q53T94-1; Sequence=Displayed; CC Name=2; CC IsoId=Q53T94-2; Sequence=VSP_021677; CC Name=3; CC IsoId=Q53T94-3; Sequence=VSP_042954; 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 (PubMed:21921198, CC PubMed:21921199). CC -!- SIMILARITY: Belongs to the RRN7/TAF1B family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA62863.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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 EMBL; L39061; AAA62863.1; ALT_INIT; mRNA. DR EMBL; AK295402; BAG58354.1; -; mRNA. DR EMBL; AC010969; AAX93272.1; -; Genomic_DNA. DR EMBL; BC018137; AAH18137.1; -; mRNA. DR CCDS; CCDS33143.1; -. [Q53T94-1] DR PIR; I61581; I61581. DR RefSeq; NP_001305905.1; NM_001318976.1. DR RefSeq; NP_005671.2; NM_005680.2. [Q53T94-1] DR AlphaFoldDB; Q53T94; -. DR BioGRID; 114483; 96. DR ComplexPortal; CPX-7978; RNA polymerase I selectivity factor 1 compex. DR CORUM; Q53T94; -. DR IntAct; Q53T94; 23. DR MINT; Q53T94; -. DR STRING; 9606.ENSP00000263663; -. DR iPTMnet; Q53T94; -. DR PhosphoSitePlus; Q53T94; -. DR BioMuta; TAF1B; -. DR DMDM; 74726856; -. DR EPD; Q53T94; -. DR jPOST; Q53T94; -. DR MassIVE; Q53T94; -. DR MaxQB; Q53T94; -. DR PaxDb; 9606-ENSP00000263663; -. DR PeptideAtlas; Q53T94; -. DR ProteomicsDB; 62543; -. [Q53T94-1] DR ProteomicsDB; 62544; -. [Q53T94-2] DR ProteomicsDB; 62545; -. [Q53T94-3] DR Pumba; Q53T94; -. DR Antibodypedia; 26617; 184 antibodies from 22 providers. DR DNASU; 9014; -. DR Ensembl; ENST00000263663.10; ENSP00000263663.4; ENSG00000115750.17. [Q53T94-1] DR GeneID; 9014; -. DR KEGG; hsa:9014; -. DR MANE-Select; ENST00000263663.10; ENSP00000263663.4; NM_005680.3; NP_005671.3. DR UCSC; uc002qzz.4; human. [Q53T94-1] DR AGR; HGNC:11533; -. DR CTD; 9014; -. DR DisGeNET; 9014; -. DR GeneCards; TAF1B; -. DR HGNC; HGNC:11533; TAF1B. DR HPA; ENSG00000115750; Low tissue specificity. DR MIM; 604904; gene. DR neXtProt; NX_Q53T94; -. DR OpenTargets; ENSG00000115750; -. DR PharmGKB; PA36308; -. DR VEuPathDB; HostDB:ENSG00000115750; -. DR eggNOG; ENOG502QVGU; Eukaryota. DR GeneTree; ENSGT00440000033827; -. DR HOGENOM; CLU_032815_0_0_1; -. DR InParanoid; Q53T94; -. DR OMA; SFRFCWG; -. DR OrthoDB; 5319728at2759; -. DR PhylomeDB; Q53T94; -. DR TreeFam; TF324353; -. DR PathwayCommons; Q53T94; -. DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination. DR SignaLink; Q53T94; -. DR SIGNOR; Q53T94; -. DR BioGRID-ORCS; 9014; 671 hits in 1165 CRISPR screens. DR ChiTaRS; TAF1B; human. DR GeneWiki; TAF1B; -. DR GenomeRNAi; 9014; -. DR Pharos; Q53T94; Tbio. DR PRO; PR:Q53T94; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q53T94; Protein. DR Bgee; ENSG00000115750; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 176 other cell types or tissues. DR ExpressionAtlas; Q53T94; baseline and differential. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0070860; C:RNA polymerase I core factor complex; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; TAS:UniProtKB. DR GO; GO:0006351; P:DNA-templated transcription; NAS: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; IDA:UniProtKB. 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; Q53T94; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Direct protein sequencing; DNA-binding; KW Metal-binding; Nucleus; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..588 FT /note="TATA box-binding protein-associated factor RNA FT polymerase I subunit B" FT /id="PRO_0000261392" FT ZN_FING 4..39 FT /note="RRN7-type" FT REGION 40..68 FT /note="B-reader" FT REGION 69..73 FT /note="B-linker" FT REGION 74..261 FT /note="N-terminal cyclin fold" FT REGION 262..372 FT /note="C-terminal cyclin fold" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000305" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 440 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..255 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042954" FT VAR_SEQ 523..588 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_021677" FT VARIANT 6 FT /note="A -> S (in dbSNP:rs2303914)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:7801123" FT /id="VAR_029378" FT VARIANT 282 FT /note="V -> I (in dbSNP:rs396190)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123" FT /id="VAR_029379" FT VARIANT 292 FT /note="R -> H (in dbSNP:rs16867223)" FT /id="VAR_057260" FT VARIANT 351 FT /note="T -> A (in dbSNP:rs1054565)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123" FT /id="VAR_029380" FT VARIANT 462 FT /note="E -> D (in dbSNP:rs1820965)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7801123" FT /id="VAR_029381" FT VARIANT 487 FT /note="T -> M (in dbSNP:rs16867245)" FT /id="VAR_029382" FT MUTAGEN 13 FT /note="C->A: Abolishes Pol I transcription but not FT recruitment of SL1/TIF-IB complex to rDNA promoters." FT /evidence="ECO:0000269|PubMed:21921199" FT MUTAGEN 31 FT /note="C->A: Abolishes Pol I transcription but not FT recruitment of SL1/TIF-IB complex to rDNA promoters." FT /evidence="ECO:0000269|PubMed:21921199" FT MUTAGEN 34 FT /note="C->A: Abolishes Pol I transcription but not FT recruitment of SL1/TIF-IB complex to rDNA promoters." FT /evidence="ECO:0000269|PubMed:21921199" FT CONFLICT 1 FT /note="M -> L (in Ref. 1; AAA62863)" FT /evidence="ECO:0000305" FT CONFLICT 372 FT /note="L -> M (in Ref. 1; AAA62863)" FT /evidence="ECO:0000305" FT CONFLICT 522 FT /note="C -> W (in Ref. 1; AAA62863)" FT /evidence="ECO:0000305" SQ SEQUENCE 588 AA; 68832 MW; CE45DE622E28FD6E CRC64; MDLEEAEEFK ERCTQCAAVS WGLTDEGKYY CTSCHNVTER YQEVTNTDLI PNTQIKALNR GLKKKNNTEK GWDWYVCEGF QYILYQQAEA LKNLGVGPEL KNDVLHNFWK RYLQKSKQAY CKNPVYTTGR KPTVLEDNLS HSDWASEPEL LSDVSCPPFL ESGAESQSDI HTRKPFPVSK ASQSETSVCS GSLDGVEYSQ RKEKGIVKMT MPQTLAFCYL SLLWQREAIT LSDLLRFVEE DHIPYINAFQ HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TVEVGTFLDL PRFPDITEDC YLHPNILCMK YLMEVNLPDE MHSLTCHVVK MTGMGEVDFL TFDPIAKMAK TVKYDVQAVA IIVVVLKLLF LLDDSFEWSL SNLAEKHNEK NKKDKPWFDF RKWYQIMKKA FDEKKQKWEE ARAKYLWKSE KPLYYSFVDK PVAYKKREMV VNLQKQFSTL VESTATAGKK SPSSFQFNWT EEDTDRTCFH GHSLQGVLKE KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ FILNLFSFLL RIKTSLLHEE VSLVEKKLFE KKYSVKRKKS RSKKVRRH //