UBF1_RAT
ID UBF1_RAT Reviewed; 764 AA.
AC P25977; P25978;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 166.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (UBF1 AND UBF2).
RX PubMed=2014238; DOI=10.1073/pnas.88.8.3180;
RA O'Mahony D.J., Rothblum L.I.;
RT "Identification of two forms of the RNA polymerase I transcription factor
RT UBF.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3180-3184(1991).
RN [2]
RP SUBUNIT.
RX PubMed=10099786; DOI=10.1139/o98-035;
RA Ridsdale R.A., Semotok J.L., Larson D.E., Rothblum L.I., Harauz G.;
RT "Topology of recombinant rat upstream binding factor.";
RL Biochem. Cell Biol. 76:649-655(1998).
RN [3]
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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P25976}.
CC -!- SUBUNIT: Homodimer (PubMed:10099786). Interacts with TBP (By
CC similarity). Interacts with TAF1A (By similarity). Interacts with PHF6
CC (By similarity). Interacts with CEBPA (isoform 1 and isoform 4)
CC (PubMed:20075868). Interacts with DDX11 (By similarity). Interacts with
CC NOP53 (By similarity). Interacts with RASL11A (By similarity).
CC Interacts with DHX33 (By similarity). Binds to IRS1 and PIK3CA (By
CC similarity). Interacts with ALKBH2. {ECO:0000250|UniProtKB:P17480,
CC ECO:0000250|UniProtKB:P25976, ECO:0000269|PubMed:10099786,
CC ECO:0000269|PubMed:20075868}.
CC -!- INTERACTION:
CC P25977; Q9Z2J9: Runx2; NbExp=2; IntAct=EBI-15620127, EBI-6119952;
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=P25977-1; Sequence=Displayed;
CC Name=UBF2; Synonyms=Short;
CC IsoId=P25977-2; Sequence=VSP_002195;
CC -!- PTM: Phosphorylated and activated by PIK3CA.
CC {ECO:0000250|UniProtKB:P25976}.
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DR EMBL; M61726; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M61725; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A40439; A40439.
DR PIR; B40439; B40439.
DR RefSeq; NP_001099193.2; NM_001105723.3. [P25977-2]
DR RefSeq; NP_001121162.1; NM_001127690.2. [P25977-1]
DR RefSeq; XP_006247324.1; XM_006247262.3. [P25977-1]
DR RefSeq; XP_006247325.1; XM_006247263.3. [P25977-1]
DR RefSeq; XP_006247326.1; XM_006247264.3. [P25977-1]
DR RefSeq; XP_008766174.1; XM_008767952.2. [P25977-2]
DR AlphaFoldDB; P25977; -.
DR BMRB; P25977; -.
DR SMR; P25977; -.
DR DIP; DIP-60265N; -.
DR IntAct; P25977; 2.
DR STRING; 10116.ENSRNOP00000063740; -.
DR iPTMnet; P25977; -.
DR PhosphoSitePlus; P25977; -.
DR jPOST; P25977; -.
DR PaxDb; P25977; -.
DR PRIDE; P25977; -.
DR Ensembl; ENSRNOT00000048418; ENSRNOP00000044305; ENSRNOG00000020937. [P25977-2]
DR Ensembl; ENSRNOT00000064283; ENSRNOP00000063740; ENSRNOG00000020937. [P25977-1]
DR GeneID; 25574; -.
DR KEGG; rno:25574; -.
DR UCSC; RGD:3927; rat. [P25977-1]
DR CTD; 7343; -.
DR RGD; 3927; Ubtf.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000161141; -.
DR HOGENOM; CLU_021068_1_0_1; -.
DR InParanoid; P25977; -.
DR OMA; DKARFHT; -.
DR OrthoDB; 1237679at2759; -.
DR PhylomeDB; P25977; -.
DR TreeFam; TF328989; -.
DR Reactome; R-RNO-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR PRO; PR:P25977; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000020937; Expressed in thymus and 20 other tissues.
DR Genevisible; P25977; RN.
DR GO; GO:0001650; C:fibrillar center; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:RGD.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; ISO:RGD.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; ISO:RGD.
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 Acetylation; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..764
FT /note="Nucleolar transcription factor 1"
FT /id="PRO_0000048627"
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..488
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 381..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..487
FT /note="Basic and acidic 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..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:0000250|UniProtKB:P17480"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25976"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25976"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25976"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17480"
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:0000250|UniProtKB:P17480"
FT VAR_SEQ 221..257
FT /note="Missing (in isoform UBF2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002195"
SQ SEQUENCE 764 AA; 89437 MW; E9D3371615DB0534 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 NINKKQTTSP ASKKPSQEGG KGGSEKPKRP VSAMFIFSEE
KRRQLQEERP ELSESELTRL LARMWNDLSE KKKAKYKARE AALKAQSERK PGGEREDRGK
LPESPKRAEE IWQQSVIGDY LARFKNDRVK ALKAMEMTWN NMEKKEKLMW IKKAAEDQKR
YERELSEMRA PPAATNSSKK MKFQGEPKKP PMNGYQKFSQ ELLSNGELNH LPLKERMVEI
GSRWQRISQS QKEHYKKLAE EQQRQYKVHL DLWVKSLSPQ DRAAYKEYIS NKRKNMTKLR
GPNPKSSRTT LQSKSESEED DDEEDDDDDD EEEEEDDENG DSSEDGGDSS ESSSEDESED
GDENEDDDDD EDDDEDDDED EDNESEGSSS SSSSSGDSSD SDSN
