UBF1B_XENLA
ID UBF1B_XENLA Reviewed; 701 AA.
AC P25980;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nucleolar transcription factor 1-B;
DE AltName: Full=Upstream-binding factor 1-B;
DE Short=UBF-1-B;
DE Short=xUBF-2;
GN Name=ubtf-b; Synonyms=ubf2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2065665; DOI=10.1002/j.1460-2075.1991.tb07766.x;
RA McStay B., Hu C.H., Pikaard C.S., Reeder R.H.;
RT "xUBF and Rib 1 are both required for formation of a stable polymerase I
RT promoter complex in X. laevis.";
RL EMBO J. 10:2297-2303(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1879565; DOI=10.1016/0014-5793(91)81002-p;
RA Bachvarov D., Normandeau M., Moss T.;
RT "Heterogeneity in the Xenopus ribosomal transcription factor xUBF has a
RT molecular basis distinct from that in mammals.";
RL FEBS Lett. 288:55-59(1991).
RN [3]
RP DOMAINS.
RX PubMed=1936987; DOI=10.1101/gad.5.11.1957;
RA McStay B., Frazier M.W., Reeder R.H.;
RT "xUBF contains a novel dimerization domain essential for RNA polymerase I
RT transcription.";
RL Genes Dev. 5:1957-1968(1991).
CC -!- FUNCTION: UBF recognizes the ribosomal RNA gene promotor and activates
CC transcription mediated by RNA polymerase I through cooperative
CC interactions with the species-specific factor SL1. It binds
CC specifically to the upstream control element.
CC -!- SUBUNIT: XUBF consists of 2 polypeptides of 82 and 85 kDa, encoded by
CC the same or closely related genes.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; X57561; CAA40794.1; -; mRNA.
DR EMBL; X59863; CAA42523.1; -; mRNA.
DR PIR; S17196; S17196.
DR PIR; S78454; S78454.
DR RefSeq; NP_001079429.1; NM_001085960.1.
DR AlphaFoldDB; P25980; -.
DR SMR; P25980; -.
DR BioGRID; 97359; 1.
DR PRIDE; P25980; -.
DR GeneID; 379116; -.
DR KEGG; xla:379116; -.
DR CTD; 379116; -.
DR Xenbase; XB-GENE-966569; ubtf.S.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 379116; Expressed in brain and 19 other tissues.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 5.
DR InterPro; IPR029215; HMG_box_5.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 2.
DR Pfam; PF09011; HMG_box_2; 1.
DR Pfam; PF14887; HMG_box_5; 1.
DR SMART; SM00398; HMG; 5.
DR SUPFAM; SSF47095; SSF47095; 5.
DR PROSITE; PS50118; HMG_BOX_2; 5.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..701
FT /note="Nucleolar transcription factor 1-B"
FT /id="PRO_0000048629"
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 422..489
FT /note="HMG box 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 508..574
FT /note="HMG box 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..683
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 32
FT /note="Q -> H (in Ref. 2; CAA42523)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="V -> A (in Ref. 2; CAA42523)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="D -> E (in Ref. 2; CAA42523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 82015 MW; 7795B29BFE8545E2 CRC64;
MNGAAGGDTQ GKMTAPKDQD QWSQEDMLTL LQTMKTLLPG QDNSKFKTTE SHLDWNKLAF
KHYSGSMCRQ KWMEISNEVR KFRTLTELIL DADEHVRHPY KGKKLKKHPE FPKKPLTPYF
RFFMEKRAKY AKLHPEMSNL DLTKILSKKY KELPEKKKMK YIQDFQREKQ DFERNMAKFR
EEHPDLMQNP KKSDVPEKPK TPQQLWYNHE RKVYLKLHAD ASTKDIKDAL GKQWSQLPDK
KRLKWIHKAL EQRKQYEGVM REYMQKHPEL NITEEGITRS TLTKAERQLK DKFDGRPTKP
PPNSYSMYCA ELMANMKDVP STERMVLCSQ RWKLLSQKEK DAYHKKCEQR KKDYEVELMR
FLENLPEEEQ QRVLAEEKMV GMKRKRTNTP ASKMATEDAA KVKSRSGQAD KKKAAEERAK
LPETPKTAEE IWQQSVIGDY LARFKNDRAK ALKVMEATWL NMEKKEKIMW IKKAAEDQKR
YERELSDMRS TPAPTTAGKK VKFLGEPKKA PMNGYQKFSQ ELLSNGELNH LPLKERMVEI
GSRWHRISPT QKDYYKKLAE DQQRLYRTQF DTWMKGLSTQ DRAAYKEQNT NKRKSTTKIQ
APSSKSKLVI QSKSDDDEDD EDDEDEEDDD DDDDEDKEDS SEDGDSSDSS SDEDSEEGEE
NEDEEDEEDD DEDNEEDDDD NESGSSSSSS SSADSSDSDS N
