ID UBF1_HUMAN Reviewed; 764 AA. AC P17480; A8K6R8; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 27-MAR-2024, entry version 235. DE RecName: Full=Nucleolar transcription factor 1; DE AltName: Full=Autoantigen NOR-90; DE AltName: Full=Upstream-binding factor 1; DE Short=UBF-1; GN Name=UBTF; Synonyms=UBF, UBF1; 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 UBF1). RX PubMed=2330041; DOI=10.1038/344830a0; RA Jantzen H.M., Admon A., Bell S.P., Tjian R.; RT "Nucleolar transcription factor hUBF contains a DNA-binding motif with RT homology to HMG proteins."; RL Nature 344:830-836(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM UBF2). RX PubMed=1940801; DOI=10.1084/jem.174.5.1239; RA Chan E.K.L., Imai H., Hamel J.C., Tan E.M.; RT "Human autoantibody to RNA polymerase I transcription factor hUBF. RT Molecular identity of nucleolus organizer region autoantigen NOR-90 and RT ribosomal RNA transcription upstream binding factor."; RL J. Exp. Med. 174:1239-1244(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM UBF1). RC TISSUE=Placenta, and Testis; 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 MRNA] (ISOFORM UBF2). RC TISSUE=Testis; 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, AND INTERACTION WITH TBP. RX PubMed=7982918; DOI=10.1016/s0021-9258(18)43788-x; RA Kwon H., Green M.R.; RT "The RNA polymerase I transcription factor, upstream binding factor, RT interacts directly with the TATA box-binding protein."; RL J. Biol. Chem. 269:30140-30146(1994). RN [6] RP INTERACTION WITH TAF1A. 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 FUNCTION OF POL I PIC, AND SUBUNIT. 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 [8] RP FUNCTION OF POL I PIC, AND SUBUNIT. 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 [9] RP FUNCTION. RX PubMed=16858408; DOI=10.1038/sj.emboj.7601221; RA Panov K.I., Friedrich J.K., Russell J., Zomerdijk J.C.; RT "UBF activates RNA polymerase I transcription by stimulating promoter RT escape."; RL EMBO J. 25:3310-3322(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-412 AND SER-638, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP INTERACTION WITH CEBPA. RX PubMed=20075868; DOI=10.1038/emboj.2009.404; RA Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.; RT "Nucleolar retention of a translational C/EBPalpha isoform stimulates rDNA RT transcription and cell size."; RL EMBO J. 29:897-909(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-484 AND SER-495, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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 [15] RP INTERACTION WITH DHX33. RX PubMed=21930779; DOI=10.1128/mcb.05832-11; RA Zhang Y., Forys J.T., Miceli A.P., Gwinn A.S., Weber J.D.; RT "Identification of DHX33 as a mediator of rRNA synthesis and cell growth."; RL Mol. Cell. Biol. 31:4676-4691(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP IDENTIFICATION BY MASS 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). RN [18] RP INTERACTION WITH ALKBH2. RX PubMed=23972994; DOI=10.1016/j.celrep.2013.07.027; RA Li P., Gao S., Wang L., Yu F., Li J., Wang C., Li J., Wong J.; RT "ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation RT repair."; RL Cell Rep. 4:817-829(2013). RN [19] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PHF6. RX PubMed=23229552; DOI=10.1074/jbc.m112.414839; RA Wang J., Leung J.W., Gong Z., Feng L., Shi X., Chen J.; RT "PHF6 regulates cell cycle progression by suppressing ribosomal RNA RT synthesis."; RL J. Biol. Chem. 288:3174-3183(2013). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-364 AND SER-435, 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). RN [21] RP INTERACTION WITH DDX11. RX PubMed=26089203; DOI=10.1093/hmg/ddv213; RA Sun X., Chen H., Deng Z., Hu B., Luo H., Zeng X., Han L., Cai G., Ma L.; RT "The Warsaw breakage syndrome-related protein DDX11 is required for RT ribosomal RNA synthesis and embryonic development."; RL Hum. Mol. Genet. 24:4901-4915(2015). RN [22] RP INTERACTION WITH NOP53. RX PubMed=27729611; DOI=10.18632/oncotarget.12288; RA Chen H., Duo Y., Hu B., Wang Z., Zhang F., Tsai H., Zhang J., Zhou L., RA Wang L., Wang X., Huang L.; RT "PICT-1 triggers a pro-death autophagy through inhibiting rRNA RT transcription and AKT/mTOR/p70S6K signaling pathway."; RL Oncotarget 7:78747-78763(2016). RN [23] RP SUBUNIT, AND INTERACTION WITH TOP2A. RX PubMed=36271492; DOI=10.26508/lsa.202201568; RA Daiss J.L., Pilsl M., Straub K., Bleckmann A., Hocherl M., Heiss F.B., RA Abascal-Palacios G., Ramsay E.P., Tluckova K., Mars J.C., Furtges T., RA Bruckmann A., Rudack T., Bernecky C., Lamour V., Panov K., Vannini A., RA Moss T., Engel C.; RT "The human RNA polymerase I structure reveals an HMG-like docking domain RT specific to metazoans."; RL Life. Sci Alliance 5:1-20(2022). RN [24] RP FUNCTION, INVOLVEMENT IN CONDBA, VARIANT CONDBA LYS-210, AND RP CHARACTERIZATION OF VARIANT CONDBA LYS-210. RX PubMed=28777933; DOI=10.1016/j.ajhg.2017.07.002; RA Edvardson S., Nicolae C.M., Agrawal P.B., Mignot C., Payne K., Prasad A.N., RA Prasad C., Sadler L., Nava C., Mullen T.E., Begtrup A., Baskin B., RA Powis Z., Shaag A., Keren B., Moldovan G.L., Elpeleg O.; RT "Heterozygous de novo UBTF gain-of-function variant is associated with RT neurodegeneration in childhood."; RL Am. J. Hum. Genet. 101:267-273(2017). RN [25] RP STRUCTURE BY NMR OF 103-192. RX PubMed=11969401; DOI=10.1021/bi015977a; RA Xu Y., Yang W., Wu J., Shi Y.; RT "Solution structure of the first HMG box domain in human upstream binding RT factor."; RL Biochemistry 41:5415-5420(2002). RN [26] RP STRUCTURE BY NMR OF 479-560. RX PubMed=12590579; DOI=10.1021/bi026372x; RA Yang W., Xu Y., Wu J., Zeng W., Shi Y.; RT "Solution structure and DNA binding property of the fifth HMG box domain in RT comparison with the first HMG box domain in human upstream binding RT factor."; RL Biochemistry 42:1930-1938(2003). CC -!- FUNCTION: Recognizes the ribosomal RNA gene promoter and activates CC transcription mediated by RNA polymerase I (Pol I) through cooperative CC interactions with the transcription factor SL1/TIF-IB complex. It binds CC specifically to the upstream control element and can activate Pol I CC promoter escape. {ECO:0000269|PubMed:11250903, CC ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:16858408, CC ECO:0000269|PubMed:28777933, ECO:0000269|PubMed:7982918}. CC -!- SUBUNIT: Homodimer (By similarity). 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 (PubMed:11250903, PubMed:11283244, CC PubMed:36271492). Interacts with TOP2A in the context of Pol I complex CC (PubMed:36271492). Interacts with TBP (PubMed:7982918). Interacts with CC TAF1A (PubMed:7491500). Interacts with RASL11A (By similarity). Binds CC to IRS1 and PIK3CA (By similarity). Interacts with DHX33 CC (PubMed:21930779). Interacts with PHF6 (PubMed:23229552). Interacts CC with CEBPA (isoform 1 and isoform 4) (PubMed:20075868). Interacts with CC DDX11 (PubMed:26089203). Interacts with NOP53 (PubMed:27729611). CC Interacts with ALKBH2. {ECO:0000250|UniProtKB:P25976, CC ECO:0000250|UniProtKB:P25977, ECO:0000269|PubMed:11250903, CC ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:20075868, CC ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:23229552, CC ECO:0000269|PubMed:23972994, ECO:0000269|PubMed:26089203, CC ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:36271492, CC ECO:0000269|PubMed:7491500, ECO:0000269|PubMed:7982918}. CC -!- INTERACTION: CC P17480; P01106: MYC; NbExp=2; IntAct=EBI-396235, EBI-447544; CC P17480; Q13950: RUNX2; NbExp=4; IntAct=EBI-396235, EBI-976402; CC P17480; Q01105: SET; NbExp=4; IntAct=EBI-396235, EBI-1053182; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P25976}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=UBF1; Synonyms=Long; CC IsoId=P17480-1; Sequence=Displayed; CC Name=UBF2; Synonyms=Short; CC IsoId=P17480-2; Sequence=VSP_002193; CC -!- PTM: Phosphorylated and activated by PIK3CA. CC {ECO:0000250|UniProtKB:P25976}. CC -!- DISEASE: Neurodegeneration, childhood-onset, with brain atrophy CC (CONDBA) [MIM:617672]: An autosomal dominant neurodegenerative disease CC with onset in childhood, characterized by progressive cortical atrophy, CC developmental delay, developmental regression, loss of motor skills and CC ambulation, absence of language, and intellectual disability. CC {ECO:0000269|PubMed:28777933}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; X53390; CAA37469.1; -; mRNA. DR EMBL; X53461; CAA37548.1; -; mRNA. DR EMBL; X56687; CAA40016.1; -; mRNA. DR EMBL; AK291733; BAF84422.1; -; mRNA. DR EMBL; AK292518; BAF85207.1; -; mRNA. DR EMBL; BC042297; AAH42297.1; -; mRNA. DR CCDS; CCDS11480.1; -. [P17480-1] DR CCDS; CCDS42346.1; -. [P17480-2] DR PIR; S09318; S09318. DR PIR; S18193; S18193. DR RefSeq; NP_001070151.1; NM_001076683.1. [P17480-2] DR RefSeq; NP_001070152.1; NM_001076684.2. [P17480-2] DR RefSeq; NP_055048.1; NM_014233.3. [P17480-1] DR RefSeq; XP_006722122.1; XM_006722059.3. DR RefSeq; XP_006722123.1; XM_006722060.2. DR RefSeq; XP_006722124.1; XM_006722061.2. DR RefSeq; XP_016880492.1; XM_017025003.1. DR RefSeq; XP_016880493.1; XM_017025004.1. DR PDB; 1K99; NMR; -; A=103-192. DR PDB; 1L8Y; NMR; -; A=479-560. DR PDB; 1L8Z; NMR; -; A=479-560. DR PDB; 2HDZ; X-ray; 2.00 A; A=479-560. DR PDBsum; 1K99; -. DR PDBsum; 1L8Y; -. DR PDBsum; 1L8Z; -. DR PDBsum; 2HDZ; -. DR AlphaFoldDB; P17480; -. DR BMRB; P17480; -. DR SMR; P17480; -. DR BioGRID; 113190; 241. DR DIP; DIP-640N; -. DR IntAct; P17480; 53. DR MINT; P17480; -. DR STRING; 9606.ENSP00000302640; -. DR GlyCosmos; P17480; 2 sites, 1 glycan. DR GlyGen; P17480; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P17480; -. DR PhosphoSitePlus; P17480; -. DR SwissPalm; P17480; -. DR BioMuta; UBTF; -. DR DMDM; 136652; -. DR EPD; P17480; -. DR jPOST; P17480; -. DR MassIVE; P17480; -. DR MaxQB; P17480; -. DR PaxDb; 9606-ENSP00000302640; -. DR PeptideAtlas; P17480; -. DR ProteomicsDB; 53473; -. [P17480-1] DR ProteomicsDB; 53474; -. [P17480-2] DR Pumba; P17480; -. DR Antibodypedia; 1769; 446 antibodies from 34 providers. DR DNASU; 7343; -. DR Ensembl; ENST00000302904.8; ENSP00000302640.4; ENSG00000108312.16. [P17480-1] DR Ensembl; ENST00000343638.9; ENSP00000345297.5; ENSG00000108312.16. [P17480-2] DR Ensembl; ENST00000393606.7; ENSP00000377231.3; ENSG00000108312.16. [P17480-2] DR Ensembl; ENST00000436088.6; ENSP00000390669.1; ENSG00000108312.16. [P17480-1] DR Ensembl; ENST00000526094.5; ENSP00000432925.1; ENSG00000108312.16. [P17480-2] DR Ensembl; ENST00000529383.5; ENSP00000435708.1; ENSG00000108312.16. [P17480-1] DR Ensembl; ENST00000533177.5; ENSP00000437180.1; ENSG00000108312.16. [P17480-2] DR Ensembl; ENST00000704741.1; ENSP00000516019.1; ENSG00000108312.16. [P17480-1] DR Ensembl; ENST00000704742.1; ENSP00000516020.1; ENSG00000108312.16. [P17480-2] DR Ensembl; ENST00000704746.1; ENSP00000516023.1; ENSG00000108312.16. [P17480-1] DR GeneID; 7343; -. DR KEGG; hsa:7343; -. DR MANE-Select; ENST00000436088.6; ENSP00000390669.1; NM_014233.4; NP_055048.1. DR UCSC; uc002igc.4; human. [P17480-1] DR AGR; HGNC:12511; -. DR CTD; 7343; -. DR DisGeNET; 7343; -. DR GeneCards; UBTF; -. DR HGNC; HGNC:12511; UBTF. DR HPA; ENSG00000108312; Low tissue specificity. DR MalaCards; UBTF; -. DR MIM; 600673; gene. DR MIM; 617672; phenotype. DR neXtProt; NX_P17480; -. DR OpenTargets; ENSG00000108312; -. DR Orphanet; 500180; Childhood-onset motor and cognitive regression syndrome with extrapyramidal movement disorder. DR PharmGKB; PA37158; -. DR VEuPathDB; HostDB:ENSG00000108312; -. DR eggNOG; KOG0381; Eukaryota. DR GeneTree; ENSGT00940000161141; -. DR HOGENOM; CLU_021068_1_0_1; -. DR InParanoid; P17480; -. DR OMA; RTAYKEY; -. DR OrthoDB; 4260911at2759; -. DR PhylomeDB; P17480; -. DR TreeFam; TF328989; -. DR PathwayCommons; P17480; -. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening. 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; P17480; -. DR SIGNOR; P17480; -. DR BioGRID-ORCS; 7343; 827 hits in 1177 CRISPR screens. DR ChiTaRS; UBTF; human. DR EvolutionaryTrace; P17480; -. DR GeneWiki; UBTF; -. DR GenomeRNAi; 7343; -. DR Pharos; P17480; Tbio. DR PRO; PR:P17480; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P17480; Protein. DR Bgee; ENSG00000108312; Expressed in sural nerve and 179 other cell types or tissues. DR ExpressionAtlas; P17480; baseline and differential. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0001165; F:RNA polymerase I cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IDA:ARUK-UCL. DR GO; GO:0097110; F:scaffold protein binding; IPI:CAFA. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB. DR GO; GO:0006360; P:transcription by RNA polymerase I; IMP:UniProtKB. DR GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IDA:UniProtKB. DR CDD; cd21998; HMG-box_UBF1_rpt1-like; 1. DR CDD; cd21999; HMG-box_UBF1_rpt2; 1. DR CDD; cd22000; HMG-box_UBF1_rpt3; 1. DR CDD; cd22001; HMG-box_UBF1_rpt4; 1. DR CDD; cd22002; HMG-box_UBF1_rpt5; 1. DR CDD; cd22003; HMG-box_UBF1_rpt6-like; 1. DR DisProt; DP02468; -. DR Gene3D; 1.10.30.10; High mobility group box domain; 6. DR InterPro; IPR029215; HMG_box_5. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR PANTHER; PTHR46318:SF4; NUCLEOLAR TRANSCRIPTION FACTOR 1; 1. DR PANTHER; PTHR46318; UPSTREAM BINDING TRANSCRIPTION FACTOR; 1. DR Pfam; PF00505; HMG_box; 3. DR Pfam; PF09011; HMG_box_2; 1. DR Pfam; PF14887; HMG_box_5; 1. DR SMART; SM00398; HMG; 6. DR SUPFAM; SSF47095; HMG-box; 6. DR PROSITE; PS50118; HMG_BOX_2; 6. DR Genevisible; P17480; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Disease variant; DNA-binding; Intellectual disability; Neurodegeneration; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1..764 FT /note="Nucleolar transcription factor 1" FT /id="PRO_0000048625" FT DNA_BIND 112..180 FT /note="HMG box 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 196..264 FT /note="HMG box 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 298..362 FT /note="HMG box 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 407..475 FT /note="HMG box 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 482..549 FT /note="HMG box 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 568..634 FT /note="HMG box 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 381..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 459..487 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 546..576 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..764 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 656..671 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 676..746 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 747..764 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 201 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 273 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25976" FT MOD_RES 364 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25976" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25976" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 495 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 546 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25976" FT MOD_RES 584 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25976" FT MOD_RES 638 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 221..257 FT /note="Missing (in isoform UBF2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1940801" FT /id="VSP_002193" FT VARIANT 210 FT /note="E -> K (in CONDBA; increased RNA polymerase I core FT element sequence-specific DNA binding; increased FT transcription from RNA polymerase I promoter; FT dbSNP:rs1555582065)" FT /evidence="ECO:0000269|PubMed:28777933" FT /id="VAR_080139" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:1K99" FT HELIX 118..131 FT /evidence="ECO:0007829|PDB:1K99" FT HELIX 140..152 FT /evidence="ECO:0007829|PDB:1K99" FT HELIX 158..176 FT /evidence="ECO:0007829|PDB:1K99" FT HELIX 177..181 FT /evidence="ECO:0007829|PDB:1K99" FT HELIX 488..503 FT /evidence="ECO:0007829|PDB:2HDZ" FT TURN 504..506 FT /evidence="ECO:0007829|PDB:2HDZ" FT HELIX 508..521 FT /evidence="ECO:0007829|PDB:2HDZ" FT HELIX 524..545 FT /evidence="ECO:0007829|PDB:2HDZ" FT HELIX 551..553 FT /evidence="ECO:0007829|PDB:1L8Y" FT STRAND 554..558 FT /evidence="ECO:0007829|PDB:1L8Y" SQ SEQUENCE 764 AA; 89406 MW; D4F0F8BB180E757D CRC64; MNGEADCPTD LEMAAPKGQD RWSQEDMLTL LECMKNNLPS NDSSKFKTTE SHMDWEKVAF KDFSGDMCKL KWVEISNEVR KFRTLTELIL DAQEHVKNPY KGKKLKKHPD FPKKPLTPYF RFFMEKRAKY AKLHPEMSNL DLTKILSKKY KELPEKKKMK YIQDFQREKQ EFERNLARFR EDHPDLIQNA KKSDIPEKPK TPQQLWYTHE KKVYLKVRPD ATTKEVKDSL GKQWSQLSDK KRLKWIHKAL EQRKEYEEIM RDYIQKHPEL NISEEGITKS TLTKAERQLK DKFDGRPTKP PPNSYSLYCA ELMANMKDVP STERMVLCSQ QWKLLSQKEK DAYHKKCDQK KKDYEVELLR FLESLPEEEQ QRVLGEEKML NINKKQATSP ASKKPAQEGG KGGSEKPKRP VSAMFIFSEE KRRQLQEERP ELSESELTRL LARMWNDLSE KKKAKYKARE AALKAQSERK PGGEREERGK LPESPKRAEE IWQQSVIGDY LARFKNDRVK ALKAMEMTWN NMEKKEKLMW IKKAAEDQKR YERELSEMRA PPAATNSSKK MKFQGEPKKP PMNGYQKFSQ ELLSNGELNH LPLKERMVEI GSRWQRISQS QKEHYKKLAE EQQKQYKVHL DLWVKSLSPQ DRAAYKEYIS NKRKSMTKLR GPNPKSSRTT LQSKSESEED DEEDEDDEDE DEEEEDDENG DSSEDGGDSS ESSSEDESED GDENEEDDED EDDDEDDDED EDNESEGSSS SSSSSGDSSD SDSN //