RRN3_MOUSE
ID RRN3_MOUSE Reviewed; 656 AA.
AC B2RS91; Q7TNE7; Q8K052;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=RNA polymerase I-specific transcription initiation factor RRN3;
GN Name=Rrn3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Lung;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP TAF1B.
RX PubMed=12015311; DOI=10.1074/jbc.m201232200;
RA Cavanaugh A.H., Hirschler-Laszkiewicz I., Hu Q., Dundr M., Smink T.,
RA Misteli T., Rothblum L.I.;
RT "Rrn3 phosphorylation is a regulatory checkpoint for ribosome biogenesis.";
RL J. Biol. Chem. 277:27423-27432(2002).
RN [3]
RP FUNCTION.
RX PubMed=12646563; DOI=10.1074/jbc.m301093200;
RA Hirschler-Laszkiewicz I., Cavanaugh A.H., Mirza A., Lun M., Hu Q.,
RA Smink T., Rothblum L.I.;
RT "Rrn3 becomes inactivated in the process of ribosomal DNA transcription.";
RL J. Biol. Chem. 278:18953-18959(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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).
CC -!- FUNCTION: Required for efficient transcription initiation by RNA
CC polymerase I. Required for the formation of the competent preinitiation
CC complex (PIC). Dissociates from pol I as a consequence of
CC transcription. In vitro, cannot activate transcription in a subsequent
CC transcription reaction. {ECO:0000269|PubMed:12015311,
CC ECO:0000269|PubMed:12646563}.
CC -!- SUBUNIT: Interacts with TAF1B. Interacts with POLR1F, EIF3L and TAF1C
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12015311}.
CC -!- PTM: Phosphorylated at Thr-198 by MAPK9/JNK2, which abrogates
CC initiation complex formation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRN3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC055781; AAH55781.1; -; mRNA.
DR EMBL; BC034110; AAH34110.1; -; mRNA.
DR EMBL; BC138774; AAI38775.1; -; mRNA.
DR EMBL; BC138776; AAI38777.1; -; mRNA.
DR CCDS; CCDS27968.1; -.
DR RefSeq; NP_001034610.1; NM_001039521.1.
DR AlphaFoldDB; B2RS91; -.
DR SMR; B2RS91; -.
DR BioGRID; 223022; 3.
DR CORUM; B2RS91; -.
DR STRING; 10090.ENSMUSP00000023363; -.
DR iPTMnet; B2RS91; -.
DR PhosphoSitePlus; B2RS91; -.
DR EPD; B2RS91; -.
DR jPOST; B2RS91; -.
DR MaxQB; B2RS91; -.
DR PaxDb; B2RS91; -.
DR PeptideAtlas; B2RS91; -.
DR PRIDE; B2RS91; -.
DR ProteomicsDB; 299815; -.
DR Antibodypedia; 11691; 230 antibodies from 31 providers.
DR DNASU; 106298; -.
DR Ensembl; ENSMUST00000023363; ENSMUSP00000023363; ENSMUSG00000022682.
DR GeneID; 106298; -.
DR KEGG; mmu:106298; -.
DR UCSC; uc007ygj.1; mouse.
DR CTD; 54700; -.
DR MGI; MGI:1925255; Rrn3.
DR VEuPathDB; HostDB:ENSMUSG00000022682; -.
DR eggNOG; KOG2434; Eukaryota.
DR GeneTree; ENSGT00390000001488; -.
DR HOGENOM; CLU_010579_3_1_1; -.
DR InParanoid; B2RS91; -.
DR OMA; VCSPAIV; -.
DR OrthoDB; 855834at2759; -.
DR PhylomeDB; B2RS91; -.
DR TreeFam; TF312979; -.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR BioGRID-ORCS; 106298; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Rrn3; mouse.
DR PRO; PR:B2RS91; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; B2RS91; protein.
DR Bgee; ENSMUSG00000022682; Expressed in cleaving embryo and 261 other tissues.
DR Genevisible; B2RS91; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070063; F:RNA polymerase binding; IDA:MGI.
DR GO; GO:0001042; F:RNA polymerase I core binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007028; P:cytoplasm organization; IMP:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR GO; GO:0007000; P:nucleolus organization; IMP:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:MGI.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IMP:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007991; RNA_pol_I_trans_ini_fac_RRN3.
DR PANTHER; PTHR12790; PTHR12790; 1.
DR Pfam; PF05327; RRN3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..656
FT /note="RNA polymerase I-specific transcription initiation
FT factor RRN3"
FT /id="PRO_0000384905"
FT REGION 265..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..650
FT /note="Interaction with POLR1F"
FT /evidence="ECO:0000250"
FT REGION 555..650
FT /note="Interaction with EIF3L"
FT /evidence="ECO:0000250"
FT REGION 608..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Phosphothreonine; by MAPK9"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV6"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYV6"
FT CONFLICT 597
FT /note="E -> Q (in Ref. 1; AAH55781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 74518 MW; 8C83C4893E2C2257 CRC64;
MAAPLLHTRL SGDVTAAASA TLSASRTGLS DMLALESDFF NSPPKKTVRF GGTVTEVLLK
YKKGETNDLE LLKNQLSDPD IKDDQIINWL LEFRSSVMYL TKDFEQLINI ILRLPWLNRS
QRVVEEYLAF LGNLVSAQTV FLRPCLSMIA SHFVPPRVIV KEGGIDVSDS DDEDDNLPAI
FDTCHRALQI ITRYVPSTPW FLMPILVEKF PFVRKSERTL ECYVHNLLRI SLYFPTLRRE
ILELVIEKLL KLDVSVSRQD IEDAEEKAAQ TCGGTDTTEG LFNMDEDEDT DPEKKADQEQ
PNQMAHPTAE RLDVLLCLLL SYIEDVCRVH GKIDNNKTKD LYRDLISIFD KLLLPTHASC
HVQFFMFFLC SFKLGFAEAF LEHLWKKLQD PNNPAIIRQA AANYIGSFLA RAKFIPLITV
KTCLDLLVNW LHMYLTNQDS GTKAFCDVAL HGPFYSACQA VFYTVVFRHK QLLSGNLKQG
LQYLQSLNFE RIVLSQLNPL KICLPQVVNF FAAITNKYQL VFCYTIMERN SRQMLPVIRS
TAGGDSVQTC TNPLDTFFPF DPCVLKRSKK FIDPIYQIWE DGSAEELQEF KKSTKKEVVE
DEDDDFLKGE VPQSDTVTGL TPSSFDTHFQ SPSSSVGSPP VLYIPGQSPL LTRIYD
