Full text data of UBTF
UBTF
(UBF, UBF1)
[Confidence: low (only semi-automatic identification from reviews)]
Nucleolar transcription factor 1 (Autoantigen NOR-90; Upstream-binding factor 1; UBF-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nucleolar transcription factor 1 (Autoantigen NOR-90; Upstream-binding factor 1; UBF-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P17480
ID UBF1_HUMAN Reviewed; 764 AA.
AC P17480; A8K6R8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1990, sequence version 1.
DT 22-JAN-2014, entry version 152.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT and 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH TBP.
RX PubMed=7982918;
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
RT TAFs.";
RL Science 270:1506-1509(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-412 AND
RP SER-638, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-484 AND
RP SER-495, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
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
RT growth.";
RL Mol. Cell. Biol. 31:4676-4691(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
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 [15]
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
RT binding factor.";
RL Biochemistry 41:5415-5420(2002).
RN [16]
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
RT domain in comparison with the first HMG box domain in human upstream
RT binding 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
CC binds specifically to the upstream control element.
CC -!- SUBUNIT: Homodimer. Interacts with TBP. Interacts with RASL11A,
CC TAF1A and TAF1D. Binds to IRS1 and PIK3CA (By similarity).
CC Interacts with DHX33. Interacts with PHF6.
CC -!- INTERACTION:
CC P01106:MYC; NbExp=2; IntAct=EBI-396235, EBI-447544;
CC Q01105:SET; NbExp=4; IntAct=EBI-396235, EBI-1053182;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
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 (By similarity).
CC -!- SIMILARITY: Contains 6 HMG box DNA-binding domains.
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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 PIR; S09318; S09318.
DR PIR; S18193; S18193.
DR RefSeq; NP_001070151.1; NM_001076683.1.
DR RefSeq; NP_001070152.1; NM_001076684.2.
DR RefSeq; NP_055048.1; NM_014233.3.
DR UniGene; Hs.89781; -.
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 ProteinModelPortal; P17480; -.
DR SMR; P17480; 103-192, 288-383, 394-472, 481-546, 567-655.
DR DIP; DIP-640N; -.
DR IntAct; P17480; 10.
DR MINT; MINT-1348764; -.
DR STRING; 9606.ENSP00000302640; -.
DR PhosphoSite; P17480; -.
DR DMDM; 136652; -.
DR PaxDb; P17480; -.
DR PRIDE; P17480; -.
DR Ensembl; ENST00000302904; ENSP00000302640; ENSG00000108312.
DR Ensembl; ENST00000343638; ENSP00000345297; ENSG00000108312.
DR Ensembl; ENST00000393606; ENSP00000377231; ENSG00000108312.
DR Ensembl; ENST00000436088; ENSP00000390669; ENSG00000108312.
DR Ensembl; ENST00000526094; ENSP00000432925; ENSG00000108312.
DR Ensembl; ENST00000529383; ENSP00000435708; ENSG00000108312.
DR Ensembl; ENST00000533177; ENSP00000437180; ENSG00000108312.
DR GeneID; 7343; -.
DR KEGG; hsa:7343; -.
DR UCSC; uc010czs.3; human.
DR CTD; 7343; -.
DR GeneCards; GC17M042282; -.
DR HGNC; HGNC:12511; UBTF.
DR HPA; CAB004611; -.
DR HPA; HPA006385; -.
DR MIM; 600673; gene.
DR neXtProt; NX_P17480; -.
DR PharmGKB; PA37158; -.
DR eggNOG; NOG327891; -.
DR HOGENOM; HOG000232068; -.
DR HOVERGEN; HBG008708; -.
DR InParanoid; P17480; -.
DR KO; K09273; -.
DR OMA; CSQRWKL; -.
DR OrthoDB; EOG7P2XTJ; -.
DR PhylomeDB; P17480; -.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; UBTF; human.
DR EvolutionaryTrace; P17480; -.
DR GeneWiki; UBTF; -.
DR GenomeRNAi; 7343; -.
DR NextBio; 28746; -.
DR PRO; PR:P17480; -.
DR ArrayExpress; P17480; -.
DR Bgee; P17480; -.
DR CleanEx; HS_UBTF; -.
DR Genevestigator; P17480; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; ISS:UniProtKB.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR Gene3D; 1.10.30.10; -; 6.
DR InterPro; IPR009071; HMG_box_dom.
DR Pfam; PF00505; HMG_box; 3.
DR Pfam; PF09011; HMG_box_2; 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 Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1 764 Nucleolar transcription factor 1.
FT /FTId=PRO_0000048625.
FT DNA_BIND 112 180 HMG box 1.
FT DNA_BIND 196 264 HMG box 2.
FT DNA_BIND 298 362 HMG box 3.
FT DNA_BIND 407 475 HMG box 4.
FT DNA_BIND 482 549 HMG box 5.
FT DNA_BIND 568 634 HMG box 6.
FT COMPBIAS 675 764 Asp/Glu/Ser-rich (acidic).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 201 201 Phosphothreonine.
FT MOD_RES 273 273 Phosphoserine (By similarity).
FT MOD_RES 336 336 Phosphoserine (By similarity).
FT MOD_RES 364 364 Phosphoserine (By similarity).
FT MOD_RES 389 389 Phosphoserine (By similarity).
FT MOD_RES 412 412 Phosphoserine.
FT MOD_RES 433 433 Phosphoserine (By similarity).
FT MOD_RES 484 484 Phosphoserine.
FT MOD_RES 495 495 Phosphoserine.
FT MOD_RES 546 546 Phosphoserine (By similarity).
FT MOD_RES 584 584 Phosphoserine (By similarity).
FT MOD_RES 638 638 Phosphoserine.
FT VAR_SEQ 221 257 Missing (in isoform UBF2).
FT /FTId=VSP_002193.
FT STRAND 107 111
FT HELIX 118 131
FT HELIX 140 152
FT HELIX 158 176
FT HELIX 177 181
FT HELIX 488 503
FT TURN 504 506
FT HELIX 508 521
FT HELIX 524 545
FT HELIX 551 553
FT STRAND 554 558
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
//
ID UBF1_HUMAN Reviewed; 764 AA.
AC P17480; A8K6R8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1990, sequence version 1.
DT 22-JAN-2014, entry version 152.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT and 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH TBP.
RX PubMed=7982918;
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
RT TAFs.";
RL Science 270:1506-1509(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-412 AND
RP SER-638, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-484 AND
RP SER-495, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
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
RT growth.";
RL Mol. Cell. Biol. 31:4676-4691(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
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 [15]
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
RT binding factor.";
RL Biochemistry 41:5415-5420(2002).
RN [16]
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
RT domain in comparison with the first HMG box domain in human upstream
RT binding 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
CC binds specifically to the upstream control element.
CC -!- SUBUNIT: Homodimer. Interacts with TBP. Interacts with RASL11A,
CC TAF1A and TAF1D. Binds to IRS1 and PIK3CA (By similarity).
CC Interacts with DHX33. Interacts with PHF6.
CC -!- INTERACTION:
CC P01106:MYC; NbExp=2; IntAct=EBI-396235, EBI-447544;
CC Q01105:SET; NbExp=4; IntAct=EBI-396235, EBI-1053182;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
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 (By similarity).
CC -!- SIMILARITY: Contains 6 HMG box DNA-binding domains.
CC -----------------------------------------------------------------------
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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 PIR; S09318; S09318.
DR PIR; S18193; S18193.
DR RefSeq; NP_001070151.1; NM_001076683.1.
DR RefSeq; NP_001070152.1; NM_001076684.2.
DR RefSeq; NP_055048.1; NM_014233.3.
DR UniGene; Hs.89781; -.
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 ProteinModelPortal; P17480; -.
DR SMR; P17480; 103-192, 288-383, 394-472, 481-546, 567-655.
DR DIP; DIP-640N; -.
DR IntAct; P17480; 10.
DR MINT; MINT-1348764; -.
DR STRING; 9606.ENSP00000302640; -.
DR PhosphoSite; P17480; -.
DR DMDM; 136652; -.
DR PaxDb; P17480; -.
DR PRIDE; P17480; -.
DR Ensembl; ENST00000302904; ENSP00000302640; ENSG00000108312.
DR Ensembl; ENST00000343638; ENSP00000345297; ENSG00000108312.
DR Ensembl; ENST00000393606; ENSP00000377231; ENSG00000108312.
DR Ensembl; ENST00000436088; ENSP00000390669; ENSG00000108312.
DR Ensembl; ENST00000526094; ENSP00000432925; ENSG00000108312.
DR Ensembl; ENST00000529383; ENSP00000435708; ENSG00000108312.
DR Ensembl; ENST00000533177; ENSP00000437180; ENSG00000108312.
DR GeneID; 7343; -.
DR KEGG; hsa:7343; -.
DR UCSC; uc010czs.3; human.
DR CTD; 7343; -.
DR GeneCards; GC17M042282; -.
DR HGNC; HGNC:12511; UBTF.
DR HPA; CAB004611; -.
DR HPA; HPA006385; -.
DR MIM; 600673; gene.
DR neXtProt; NX_P17480; -.
DR PharmGKB; PA37158; -.
DR eggNOG; NOG327891; -.
DR HOGENOM; HOG000232068; -.
DR HOVERGEN; HBG008708; -.
DR InParanoid; P17480; -.
DR KO; K09273; -.
DR OMA; CSQRWKL; -.
DR OrthoDB; EOG7P2XTJ; -.
DR PhylomeDB; P17480; -.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; UBTF; human.
DR EvolutionaryTrace; P17480; -.
DR GeneWiki; UBTF; -.
DR GenomeRNAi; 7343; -.
DR NextBio; 28746; -.
DR PRO; PR:P17480; -.
DR ArrayExpress; P17480; -.
DR Bgee; P17480; -.
DR CleanEx; HS_UBTF; -.
DR Genevestigator; P17480; -.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; ISS:UniProtKB.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR Gene3D; 1.10.30.10; -; 6.
DR InterPro; IPR009071; HMG_box_dom.
DR Pfam; PF00505; HMG_box; 3.
DR Pfam; PF09011; HMG_box_2; 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 Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1 764 Nucleolar transcription factor 1.
FT /FTId=PRO_0000048625.
FT DNA_BIND 112 180 HMG box 1.
FT DNA_BIND 196 264 HMG box 2.
FT DNA_BIND 298 362 HMG box 3.
FT DNA_BIND 407 475 HMG box 4.
FT DNA_BIND 482 549 HMG box 5.
FT DNA_BIND 568 634 HMG box 6.
FT COMPBIAS 675 764 Asp/Glu/Ser-rich (acidic).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 201 201 Phosphothreonine.
FT MOD_RES 273 273 Phosphoserine (By similarity).
FT MOD_RES 336 336 Phosphoserine (By similarity).
FT MOD_RES 364 364 Phosphoserine (By similarity).
FT MOD_RES 389 389 Phosphoserine (By similarity).
FT MOD_RES 412 412 Phosphoserine.
FT MOD_RES 433 433 Phosphoserine (By similarity).
FT MOD_RES 484 484 Phosphoserine.
FT MOD_RES 495 495 Phosphoserine.
FT MOD_RES 546 546 Phosphoserine (By similarity).
FT MOD_RES 584 584 Phosphoserine (By similarity).
FT MOD_RES 638 638 Phosphoserine.
FT VAR_SEQ 221 257 Missing (in isoform UBF2).
FT /FTId=VSP_002193.
FT STRAND 107 111
FT HELIX 118 131
FT HELIX 140 152
FT HELIX 158 176
FT HELIX 177 181
FT HELIX 488 503
FT TURN 504 506
FT HELIX 508 521
FT HELIX 524 545
FT HELIX 551 553
FT STRAND 554 558
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
//
MIM
600673
*RECORD*
*FIELD* NO
600673
*FIELD* TI
*600673 UPSTREAM BINDING TRANSCRIPTION FACTOR (RNA POLYMERASE I); UBTF
;;UPSTREAM BINDING FACTOR; UBF
read more*FIELD* TX
DESCRIPTION
Upstream binding factor (UBF) is a transcription factor required for
expression of the 18S, 5.8S, and 28S ribosomal RNAs, along with SL1 (a
complex of TBP (600075) and multiple TBP-associated factors or 'TAFs').
Two UBF polypeptides, of 94 and 97 kD, exist in the human (Bell et al.,
1988). UBF is a nucleolar phosphoprotein with both DNA binding and
transactivation domains. Sequence-specific DNA binding to the core and
upstream control elements of the human rRNA promoter is mediated through
several HMG boxes (Jantzen et al., 1990).
CLONING
The mouse Ubf cDNA and gene were cloned by Hisatake et al. (1991).
Alternative use of exon 8 produces cDNAs encoding either a 765- or
728-amino acid protein. O'Mahony and Rothblum (1991) identified 2 forms
of the Ubtf mRNA in the rat.
Jantzen et al. (1990) cloned human UBF by screening a HeLa cell cDNA
library with DNA probes based on tryptic peptides of the protein. They
found an open reading frame encoding the 764-amino acid UBF. The authors
also characterized DNA binding characteristics of UBF. Chan et al.
(1991) cloned the human cDNA by screening an expression library with a
specific autoantibody that recognizes nucleolar organizing regions.
Matera et al. (1997) reported that the 2 observed isoforms of UBTF,
which differ by 37 amino acids, are generated by alternative splicing.
GENE FUNCTION
Cell size is strongly dependent on ribosome biogenesis, which is
controlled by RNA polymerase I (see 602000). The activity of this
polymerase is modulated by a complex of proteins, including UBTF. From
experiments with mouse embryonic fibroblasts, Drakas et al. (2004)
presented evidence that a nuclear complex forms between IRS1 (147545),
UBTF, and PI3K (see 171834), leading to the serine phosphorylation of
UBF1 and regulation of rRNA synthesis.
By immunoprecipitation analysis, Shimono et al. (2005) found that MCRS1
(609504) interacted with MI2-beta (CHD4; 603277), RFP (TRIM27; 602165),
and UBF. Confocal microscopy demonstrated colocalization of MCRS1,
MI2-beta, RFP, and UBF in nucleoli. Chromatin immunoprecipitation assays
showed that MCRS1, MI2-beta, and RFP associated with rDNA and were
involved in transactivation of ribosomal gene transcription, which could
be downregulated by small interfering RNA-mediated downregulation of
MCRS1, MI2-beta, and RFP.
GENE STRUCTURE
Hisatake et al. (1991) showed that the mouse Ubf gene contains 13 exons
and spans more than 13 kb.
MAPPING
Jones et al. (1995) mapped the UBTF gene to the BRCA1 region of 17q21 by
analyzing genomic clones from that region. They found the gene order to
be cen--PPY(167780)--UBTF--EPB3(109270)--GP2B(607759)--tel. Using
fluorescence in situ hybridization and radiation hybrid mapping, Matera
et al. (1997) mapped the UBTF gene to 17q21.3.
*FIELD* RF
1. Bell, S. P.; Learned, R. M.; Jantzen, H.-M.; Tjian, R.: Functional
cooperativity between transcription factors UBF1 and SL1 mediates
human ribosomal RNA synthesis. Science 241: 1192-1197, 1988.
2. Chan, E. K. L.; Imai, H.; Hamel, J. C.; Tan, E. M.: Human autoantibody
to RNA polymerase I transcription factor hUBF: molecular identity
of nucleolus organizer region autoantigen NOR-90 and ribosomal RNA
transcription upstream binding factor. J. Exp. Med. 174: 1239-1244,
1991.
3. Drakas, R.; Tu, X.; Baserga, R.: Control of cell size through
phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol
3-kinase. Proc. Nat. Acad. Sci. 101: 9272-9276, 2004.
4. Hisatake, K.; Nishimura, T.; Maeda, Y.; Hanada, K.; Song, C.-Z.;
Muramatsu, M.: Cloning and structural analysis of cDNA and the gene
for mouse transcription factor UBF. Nucleic Acids Res. 19: 4631-4637,
1991.
5. Jantzen, H.-M.; Admon, A.; Bell, S. P.; Tjian, R.: Nucleolar transcription
factor hUBF contains a DNA-binding motif with homology to HMG proteins. Nature 344:
830-836, 1990.
6. Jones, K. A.; Black, D. M.; Griffiths, B. L.; Solomon, E.: Localization
of the human RNA polymerase I transcription factor gene (UBTF) to
the S17S183 locus on chromosome 17q21 and construction of a long-range
restriction map of the region. Genomics 30: 602-604, 1995.
7. Matera, A. G.; Wu, W.; Imai, H.; O'Keefe, C. L.; Chan, E. K. L.
: Molecular cloning of the RNA polymerase I transcription factor hUBF/NOR-90
(UBTF) gene and localization to 17q21.3 by fluorescence in situ hybridization
and radiation hybrid mapping. Genomics 41: 135-138, 1997.
8. O'Mahony, D. J.; Rothblum, L. I.: Identification of two forms
of the RNA polymerase I transcription factor UBF. Proc. Nat. Acad.
Sci. 88: 3180-3184, 1991.
9. Shimono, K.; Shimono, Y.; Shimokata, K.; Ishiguro, N.; Takahashi,
M.: Microspherule protein 1, Mi-2-beta, and RET finger protein associate
in the nucleolus and up-regulate ribosomal gene transcription. J.
Biol. Chem. 280: 39436-39447, 2005.
*FIELD* CN
Paul J. Converse - updated: 11/6/2006
Patricia A. Hartz - updated: 8/26/2004
Rebekah S. Rasooly - updated: 5/15/1998
*FIELD* CD
Alan F. Scott: 2/28/1996
*FIELD* ED
terry: 04/20/2011
mgross: 11/6/2006
mgross: 8/31/2004
terry: 8/26/2004
ckniffin: 5/15/2003
psherman: 5/15/1998
terry: 3/19/1996
mark: 3/18/1996
terry: 3/11/1996
mark: 3/11/1996
mark: 2/27/1996
*RECORD*
*FIELD* NO
600673
*FIELD* TI
*600673 UPSTREAM BINDING TRANSCRIPTION FACTOR (RNA POLYMERASE I); UBTF
;;UPSTREAM BINDING FACTOR; UBF
read more*FIELD* TX
DESCRIPTION
Upstream binding factor (UBF) is a transcription factor required for
expression of the 18S, 5.8S, and 28S ribosomal RNAs, along with SL1 (a
complex of TBP (600075) and multiple TBP-associated factors or 'TAFs').
Two UBF polypeptides, of 94 and 97 kD, exist in the human (Bell et al.,
1988). UBF is a nucleolar phosphoprotein with both DNA binding and
transactivation domains. Sequence-specific DNA binding to the core and
upstream control elements of the human rRNA promoter is mediated through
several HMG boxes (Jantzen et al., 1990).
CLONING
The mouse Ubf cDNA and gene were cloned by Hisatake et al. (1991).
Alternative use of exon 8 produces cDNAs encoding either a 765- or
728-amino acid protein. O'Mahony and Rothblum (1991) identified 2 forms
of the Ubtf mRNA in the rat.
Jantzen et al. (1990) cloned human UBF by screening a HeLa cell cDNA
library with DNA probes based on tryptic peptides of the protein. They
found an open reading frame encoding the 764-amino acid UBF. The authors
also characterized DNA binding characteristics of UBF. Chan et al.
(1991) cloned the human cDNA by screening an expression library with a
specific autoantibody that recognizes nucleolar organizing regions.
Matera et al. (1997) reported that the 2 observed isoforms of UBTF,
which differ by 37 amino acids, are generated by alternative splicing.
GENE FUNCTION
Cell size is strongly dependent on ribosome biogenesis, which is
controlled by RNA polymerase I (see 602000). The activity of this
polymerase is modulated by a complex of proteins, including UBTF. From
experiments with mouse embryonic fibroblasts, Drakas et al. (2004)
presented evidence that a nuclear complex forms between IRS1 (147545),
UBTF, and PI3K (see 171834), leading to the serine phosphorylation of
UBF1 and regulation of rRNA synthesis.
By immunoprecipitation analysis, Shimono et al. (2005) found that MCRS1
(609504) interacted with MI2-beta (CHD4; 603277), RFP (TRIM27; 602165),
and UBF. Confocal microscopy demonstrated colocalization of MCRS1,
MI2-beta, RFP, and UBF in nucleoli. Chromatin immunoprecipitation assays
showed that MCRS1, MI2-beta, and RFP associated with rDNA and were
involved in transactivation of ribosomal gene transcription, which could
be downregulated by small interfering RNA-mediated downregulation of
MCRS1, MI2-beta, and RFP.
GENE STRUCTURE
Hisatake et al. (1991) showed that the mouse Ubf gene contains 13 exons
and spans more than 13 kb.
MAPPING
Jones et al. (1995) mapped the UBTF gene to the BRCA1 region of 17q21 by
analyzing genomic clones from that region. They found the gene order to
be cen--PPY(167780)--UBTF--EPB3(109270)--GP2B(607759)--tel. Using
fluorescence in situ hybridization and radiation hybrid mapping, Matera
et al. (1997) mapped the UBTF gene to 17q21.3.
*FIELD* RF
1. Bell, S. P.; Learned, R. M.; Jantzen, H.-M.; Tjian, R.: Functional
cooperativity between transcription factors UBF1 and SL1 mediates
human ribosomal RNA synthesis. Science 241: 1192-1197, 1988.
2. Chan, E. K. L.; Imai, H.; Hamel, J. C.; Tan, E. M.: Human autoantibody
to RNA polymerase I transcription factor hUBF: molecular identity
of nucleolus organizer region autoantigen NOR-90 and ribosomal RNA
transcription upstream binding factor. J. Exp. Med. 174: 1239-1244,
1991.
3. Drakas, R.; Tu, X.; Baserga, R.: Control of cell size through
phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol
3-kinase. Proc. Nat. Acad. Sci. 101: 9272-9276, 2004.
4. Hisatake, K.; Nishimura, T.; Maeda, Y.; Hanada, K.; Song, C.-Z.;
Muramatsu, M.: Cloning and structural analysis of cDNA and the gene
for mouse transcription factor UBF. Nucleic Acids Res. 19: 4631-4637,
1991.
5. Jantzen, H.-M.; Admon, A.; Bell, S. P.; Tjian, R.: Nucleolar transcription
factor hUBF contains a DNA-binding motif with homology to HMG proteins. Nature 344:
830-836, 1990.
6. Jones, K. A.; Black, D. M.; Griffiths, B. L.; Solomon, E.: Localization
of the human RNA polymerase I transcription factor gene (UBTF) to
the S17S183 locus on chromosome 17q21 and construction of a long-range
restriction map of the region. Genomics 30: 602-604, 1995.
7. Matera, A. G.; Wu, W.; Imai, H.; O'Keefe, C. L.; Chan, E. K. L.
: Molecular cloning of the RNA polymerase I transcription factor hUBF/NOR-90
(UBTF) gene and localization to 17q21.3 by fluorescence in situ hybridization
and radiation hybrid mapping. Genomics 41: 135-138, 1997.
8. O'Mahony, D. J.; Rothblum, L. I.: Identification of two forms
of the RNA polymerase I transcription factor UBF. Proc. Nat. Acad.
Sci. 88: 3180-3184, 1991.
9. Shimono, K.; Shimono, Y.; Shimokata, K.; Ishiguro, N.; Takahashi,
M.: Microspherule protein 1, Mi-2-beta, and RET finger protein associate
in the nucleolus and up-regulate ribosomal gene transcription. J.
Biol. Chem. 280: 39436-39447, 2005.
*FIELD* CN
Paul J. Converse - updated: 11/6/2006
Patricia A. Hartz - updated: 8/26/2004
Rebekah S. Rasooly - updated: 5/15/1998
*FIELD* CD
Alan F. Scott: 2/28/1996
*FIELD* ED
terry: 04/20/2011
mgross: 11/6/2006
mgross: 8/31/2004
terry: 8/26/2004
ckniffin: 5/15/2003
psherman: 5/15/1998
terry: 3/19/1996
mark: 3/18/1996
terry: 3/11/1996
mark: 3/11/1996
mark: 2/27/1996