UBF1_MOUSE
ID UBF1_MOUSE Reviewed; 765 AA.
AC P25976;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 169.
DE RecName: Full=Nucleolar transcription factor 1;
DE AltName: Full=Upstream-binding factor 1;
DE Short=UBF-1;
GN Name=Ubtf; Synonyms=Tcfubf, Ubf-1, Ubf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS UBF1 AND UBF2).
RC STRAIN=C3H/He;
RX PubMed=1891354; DOI=10.1093/nar/19.17.4631;
RA Hisatake K., Nishimura T., Maeda Y., Hanada K., Song C.Z., Muramatsu M.;
RT "Cloning and structural analysis of cDNA and the gene for mouse
RT transcription factor UBF.";
RL Nucleic Acids Res. 19:4631-4637(1991).
RN [2]
RP INTERACTION WITH IRS1 AND PIK3CA.
RX PubMed=15197263; DOI=10.1073/pnas.0403328101;
RA Drakas R., Tu X., Baserga R.;
RT "Control of cell size through phosphorylation of upstream binding factor 1
RT by nuclear phosphatidylinositol 3-kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004).
RN [3]
RP PHOSPHORYLATION AT SER-273; SER-336; SER-364; SER-389; SER-412; SER-433;
RP SER-484; SER-546; SER-584 AND SER-638.
RX PubMed=17182730; DOI=10.1152/ajpcell.00176.2006;
RA Lin C.H., Platt M.D., Ficarro S.B., Hoofnagle M.H., Shabanowitz J.,
RA Comai L., Hunt D.F., Owens G.K.;
RT "Mass spectrometric identification of phosphorylation sites of rRNA
RT transcription factor upstream binding factor.";
RL Am. J. Physiol. 292:C1617-C1624(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201 AND SER-484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RASL11A.
RX PubMed=20168301; DOI=10.1038/emboj.2010.16;
RA Pistoni M., Verrecchia A., Doni M., Guccione E., Amati B.;
RT "Chromatin association and regulation of rDNA transcription by the Ras-
RT family protein RasL11a.";
RL EMBO J. 29:1215-1224(2010).
RN [6]
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 [7]
RP STRUCTURE BY NMR OF 288-654.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 3rd, 4th and 6th HMG-box of mouse UBF1.";
RL Submitted (NOV-2004) to the PDB data bank.
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:20168301}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with TBP (By similarity).
CC Interacts with TAF1A (By similarity). Interacts with RASL11A
CC (PubMed:20168301). Binds to IRS1 and PIK3CA (PubMed:15197263).
CC Interacts with DHX33 (PubMed:21930779). Interacts with PHF6 (By
CC similarity). Interacts with CEBPA (isoform 1 and isoform 4) (By
CC similarity). Interacts with DDX11 (By similarity). Interacts with NOP53
CC (By similarity). Interacts with ALKBH2. {ECO:0000250|UniProtKB:P17480,
CC ECO:0000250|UniProtKB:P25977, ECO:0000269|PubMed:15197263,
CC ECO:0000269|PubMed:20168301, ECO:0000269|PubMed:21930779}.
CC -!- INTERACTION:
CC P25976; Q08775: Runx2; NbExp=4; IntAct=EBI-7364139, EBI-903354;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20168301}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=UBF1; Synonyms=Long;
CC IsoId=P25976-1; Sequence=Displayed;
CC Name=UBF2; Synonyms=Short;
CC IsoId=P25976-2; Sequence=VSP_002194;
CC -!- PTM: Phosphorylated and activated by PIK3CA.
CC {ECO:0000269|PubMed:17182730}.
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DR EMBL; X60831; CAA43222.1; -; mRNA.
DR PIR; S22314; S22314.
DR PDB; 1V63; NMR; -; A=567-654.
DR PDB; 1V64; NMR; -; A=288-382.
DR PDB; 1WGF; NMR; -; A=394-470.
DR PDBsum; 1V63; -.
DR PDBsum; 1V64; -.
DR PDBsum; 1WGF; -.
DR AlphaFoldDB; P25976; -.
DR BMRB; P25976; -.
DR SMR; P25976; -.
DR DIP; DIP-29977N; -.
DR ELM; P25976; -.
DR IntAct; P25976; 10.
DR MINT; P25976; -.
DR STRING; 10090.ENSMUSP00000133844; -.
DR iPTMnet; P25976; -.
DR PhosphoSitePlus; P25976; -.
DR EPD; P25976; -.
DR jPOST; P25976; -.
DR MaxQB; P25976; -.
DR PaxDb; P25976; -.
DR PeptideAtlas; P25976; -.
DR PRIDE; P25976; -.
DR ProteomicsDB; 298449; -. [P25976-1]
DR ProteomicsDB; 298450; -. [P25976-2]
DR MGI; MGI:98512; Ubtf.
DR eggNOG; KOG0381; Eukaryota.
DR InParanoid; P25976; -.
DR PhylomeDB; P25976; -.
DR Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR ChiTaRS; Ubtf; mouse.
DR EvolutionaryTrace; P25976; -.
DR PRO; PR:P25976; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P25976; protein.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001165; F:RNA polymerase I cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006360; P:transcription by RNA polymerase I; ISO:MGI.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:MGI.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; ISO:MGI.
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; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..765
FT /note="Nucleolar transcription factor 1"
FT /id="PRO_0000048626"
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 370..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..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 649..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Polar residues"
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..747
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17182730"
FT VAR_SEQ 221..257
FT /note="Missing (in isoform UBF2)"
FT /evidence="ECO:0000303|PubMed:1891354"
FT /id="VSP_002194"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1V64"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:1V64"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:1V64"
FT HELIX 337..364
FT /evidence="ECO:0007829|PDB:1V64"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:1V64"
FT TURN 375..379
FT /evidence="ECO:0007829|PDB:1V64"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:1WGF"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:1WGF"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:1WGF"
FT HELIX 450..463
FT /evidence="ECO:0007829|PDB:1WGF"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:1WGF"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:1V63"
FT HELIX 575..585
FT /evidence="ECO:0007829|PDB:1V63"
FT TURN 587..590
FT /evidence="ECO:0007829|PDB:1V63"
FT HELIX 593..604
FT /evidence="ECO:0007829|PDB:1V63"
FT HELIX 609..636
FT /evidence="ECO:0007829|PDB:1V63"
FT HELIX 641..651
FT /evidence="ECO:0007829|PDB:1V63"
SQ SEQUENCE 765 AA; 89509 MW; 006A20A7F968DB6A 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
KTLKWIHKAL EQRKEYEEIM RDYIQKHPEL NISEEGITKS TLTKAERQLK DKFDGRPTKP
PPNSYSLYCA ELMANMKDVP STERMVLCSQ QWKLLSQKEK DAYHKKCDQK KKDYEVELLR
FLESLPEEEQ QRVLGEEKML NINKKQTTSP ASKKPSQEGG KGGSEKPKRP VSAMFIFSEE
KRRQLQEERP ELSESELTRL LARMWNDLTE KKKAKYKARE AALKAQSERK PGGEREDRGK
LPESPKRAEE IWQQSVIGDY LARFKNDRVK ALKAMEMTWN NMEKKEKLMW IKKAAEDQKR
YERELSEMRA PPAATNSSKK MKFQGEPKKP PMNGYQKFSQ ELLSNGELNH LPLKERMVEI
GSRWQRISQS QKEHYKKLAE EQQRQYKVHL DLWVKSLSPQ DRAAYKEYIS NKRKNMTKLR
GPNPKSSRTT LQSKSESEED DDEEEEDDEE EEEEEEDDEN GDSSEDGGDS SESSSEDESE
DGDENDDDDD DEDDEDDDDE DEDNESEGSS SSSSSSGDSS DSGSN
