UBF1_HUMAN
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 03-AUG-2022, entry version 226.
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 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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 through cooperative
CC interactions with the transcription factor SL1/TIF-IB complex. It binds
CC specifically to the upstream control element.
CC {ECO:0000269|PubMed:28777933, ECO:0000269|PubMed:7982918}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with TBP
CC (PubMed:7982918). Interacts with TAF1A (PubMed:7491500). Interacts with
CC RASL11A (By similarity). Binds to IRS1 and PIK3CA (By similarity).
CC Interacts with DHX33 (PubMed:21930779). Interacts with PHF6
CC (PubMed:23229552). Interacts with CEBPA (isoform 1 and isoform 4)
CC (PubMed:20075868). Interacts with DDX11 (PubMed:26089203). Interacts
CC with NOP53 (PubMed:27729611). Interacts with ALKBH2.
CC {ECO:0000250|UniProtKB:P25976, ECO:0000250|UniProtKB:P25977,
CC ECO:0000269|PubMed:20075868, ECO:0000269|PubMed:21930779,
CC ECO:0000269|PubMed:23229552, ECO:0000269|PubMed:23972994,
CC ECO:0000269|PubMed:26089203, ECO:0000269|PubMed:27729611,
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.
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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. [P17480-1]
DR RefSeq; XP_006722123.1; XM_006722060.2. [P17480-1]
DR RefSeq; XP_006722124.1; XM_006722061.2. [P17480-1]
DR RefSeq; XP_016880492.1; XM_017025003.1. [P17480-2]
DR RefSeq; XP_016880493.1; XM_017025004.1. [P17480-2]
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; 214.
DR DIP; DIP-640N; -.
DR IntAct; P17480; 52.
DR MINT; P17480; -.
DR STRING; 9606.ENSP00000302640; -.
DR GlyGen; P17480; 2 sites, 1 O-linked glycan (2 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; P17480; -.
DR PeptideAtlas; P17480; -.
DR PRIDE; P17480; -.
DR ProteomicsDB; 53473; -. [P17480-1]
DR ProteomicsDB; 53474; -. [P17480-2]
DR Antibodypedia; 1769; 405 antibodies from 34 providers.
DR DNASU; 7343; -.
DR Ensembl; ENST00000302904.8; ENSP00000302640.4; ENSG00000108312.15. [P17480-1]
DR Ensembl; ENST00000343638.9; ENSP00000345297.5; ENSG00000108312.15. [P17480-2]
DR Ensembl; ENST00000393606.7; ENSP00000377231.3; ENSG00000108312.15. [P17480-2]
DR Ensembl; ENST00000436088.6; ENSP00000390669.1; ENSG00000108312.15. [P17480-1]
DR Ensembl; ENST00000526094.5; ENSP00000432925.1; ENSG00000108312.15. [P17480-2]
DR Ensembl; ENST00000529383.5; ENSP00000435708.1; ENSG00000108312.15. [P17480-1]
DR Ensembl; ENST00000533177.5; ENSP00000437180.1; ENSG00000108312.15. [P17480-2]
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 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; DKARFHT; -.
DR OrthoDB; 1403160at2759; -.
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; 797 hits in 1100 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 177 other tissues.
DR ExpressionAtlas; P17480; baseline and differential.
DR Genevisible; P17480; HS.
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 from RNA polymerase I promoter; IDA:ParkinsonsUK-UCL.
DR Gene3D; 1.10.30.10; -; 6.
DR InterPro; IPR029215; HMG_box_5.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
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; SSF47095; 6.
DR PROSITE; PS50118; HMG_BOX_2; 6.
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
