RRP8_MOUSE
ID RRP8_MOUSE Reviewed; 457 AA.
AC Q9DB85; Q3T9X9; Q3TDD7; Q3U3A5; Q8BHW3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ribosomal RNA-processing protein 8;
DE EC=2.1.1.-;
DE AltName: Full=Cerebral protein 1 homolog;
GN Name=Rrp8;
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, and NOD;
RC TISSUE=Cerebellum, Corpora quadrigemina, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-64 AND SER-177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, 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: Essential component of the eNoSC (energy-dependent nucleolar
CC silencing) complex, a complex that mediates silencing of rDNA in
CC response to intracellular energy status and acts by recruiting histone-
CC modifying enzymes. The eNoSC complex is able to sense the energy status
CC of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio
CC activates SIRT1, leading to histone H3 deacetylation followed by
CC dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation
CC of silent chromatin in the rDNA locus. In the complex, RRP8 binds to
CC H3K9me2 and probably acts as a methyltransferase. Its substrates are
CC however unknown (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the eNoSC complex, composed of SIRT1, SUV39H1 and
CC RRP8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Localizes
CC at rDNA locus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37008.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005138; BAB23836.1; -; mRNA.
DR EMBL; AK045361; BAC32326.1; -; mRNA.
DR EMBL; AK077786; BAC37008.1; ALT_FRAME; mRNA.
DR EMBL; AK154858; BAE32883.1; -; mRNA.
DR EMBL; AK170257; BAE41665.1; -; mRNA.
DR EMBL; AK172189; BAE42874.1; -; mRNA.
DR EMBL; AK172224; BAE42891.1; -; mRNA.
DR EMBL; BC022923; AAH22923.1; -; mRNA.
DR EMBL; BC046799; AAH46799.1; -; mRNA.
DR CCDS; CCDS21658.1; -.
DR RefSeq; NP_080173.1; NM_025897.2.
DR AlphaFoldDB; Q9DB85; -.
DR SMR; Q9DB85; -.
DR BioGRID; 221741; 3.
DR ComplexPortal; CPX-468; eNoSc complex.
DR STRING; 10090.ENSMUSP00000033179; -.
DR iPTMnet; Q9DB85; -.
DR PhosphoSitePlus; Q9DB85; -.
DR EPD; Q9DB85; -.
DR jPOST; Q9DB85; -.
DR MaxQB; Q9DB85; -.
DR PaxDb; Q9DB85; -.
DR PeptideAtlas; Q9DB85; -.
DR PRIDE; Q9DB85; -.
DR ProteomicsDB; 299934; -.
DR Antibodypedia; 23905; 154 antibodies from 28 providers.
DR DNASU; 101867; -.
DR Ensembl; ENSMUST00000033179; ENSMUSP00000033179; ENSMUSG00000030888.
DR GeneID; 101867; -.
DR KEGG; mmu:101867; -.
DR UCSC; uc009iyz.2; mouse.
DR CTD; 23378; -.
DR MGI; MGI:1914251; Rrp8.
DR VEuPathDB; HostDB:ENSMUSG00000030888; -.
DR eggNOG; KOG3045; Eukaryota.
DR GeneTree; ENSGT00390000006189; -.
DR HOGENOM; CLU_027694_2_3_1; -.
DR InParanoid; Q9DB85; -.
DR OMA; QNQVKKW; -.
DR PhylomeDB; Q9DB85; -.
DR TreeFam; TF313749; -.
DR Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
DR BioGRID-ORCS; 101867; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Rrp8; mouse.
DR PRO; PR:Q9DB85; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DB85; protein.
DR Bgee; ENSMUSG00000030888; Expressed in animal zygote and 216 other tissues.
DR ExpressionAtlas; Q9DB85; baseline and differential.
DR Genevisible; Q9DB85; MM.
DR GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0061773; C:eNoSc complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR GO; GO:0097009; P:energy homeostasis; ISO:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:MGI.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; ISO:MGI.
DR GO; GO:0046015; P:regulation of transcription by glucose; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.2150; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR007823; RRP8.
DR InterPro; IPR042036; RRP8_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12787; PTHR12787; 1.
DR Pfam; PF05148; Methyltransf_8; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; rRNA processing; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..457
FT /note="Ribosomal RNA-processing protein 8"
FT /id="PRO_0000084091"
FT REGION 47..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 348
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT BINDING 364
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43159"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 30
FT /note="P -> R (in Ref. 1; BAE41665/BAE42891/BAE42874)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="S -> N (in Ref. 1; BAE41665/BAE42891/BAE42874)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="P -> H (in Ref. 1; BAE32883)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="R -> Q (in Ref. 1; BAE41665/BAE42891/BAE42874)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="T -> N (in Ref. 1; BAE32883)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="T -> P (in Ref. 1; BAE41665/BAE42891/BAE42874)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="V -> A (in Ref. 1; BAE41665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 51066 MW; A9DB8CB932E1DB3C CRC64;
MFEEPEWVEA APAIVGLGAA TAQVRPATAP PVKGRKRRHL LATLRALEAA SLSQQTPSLP
GSDSEEEEEV GRKKRHLQRP SLASVSKEVG KKRKGKCQKQ APSISDSEGK EIRRKCHRQA
PPLGGVSAGE EKGKRKCQEY SSLHLTQPLD SVDQTVHNSR TSTATIDPSK PSPESMSPNS
SHTLSRKQWR NRQKNKRRHK NKFRPLQTPE QAPPKASIEE TEVPPVPKSD SQESRAGALR
ARMTQRLDGA RFRYLNEQLY SGPSSAARRL FQEDPEAFLL YHRGFQRQVK KWPLHPVDRI
AKDLRQKPAS LVVADFGCGD CRLASSVRNP VHCFDLASLD PRVTVCDMAQ VPLEDESVDV
AVFCLSLMGT NIRDFLEEAN RVLKTGGLLK VAEVSSRFED IRTFLGAVTK LGFKIIYKDL
TNSHFFLFDF EKTGPPRVGP KAQLSGLKLQ PCLYKRR
