RRS1_MOUSE
ID RRS1_MOUSE Reviewed; 365 AA.
AC Q9CYH6; Q3UQW6; Q9CS27; Q9D2B2; Q9D6M6; Q9JJC1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ribosome biogenesis regulatory protein homolog;
GN Name=Rrs1; Synonyms=Rrr; ORFNames=MNCb-2643;
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;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Eye, Pituitary, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Mammary gland;
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 [4]
RP CITRULLINATION AT ARG-273.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Involved in ribosomal large subunit assembly. May regulate
CC the localization of the 5S RNP/5S ribonucleoprotein particle to the
CC nucleolus. {ECO:0000250|UniProtKB:Q15050}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q15050}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the RRS1 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; AB041589; BAA95072.1; -; mRNA.
DR EMBL; AK010178; BAB26750.1; -; mRNA.
DR EMBL; AK017683; BAB30871.1; -; mRNA.
DR EMBL; AK019257; BAB31631.1; -; mRNA.
DR EMBL; AK019913; BAB31912.1; -; mRNA.
DR EMBL; AK142041; BAE24922.1; -; mRNA.
DR EMBL; BC003481; AAH03481.1; -; mRNA.
DR EMBL; BC055925; AAH55925.1; -; mRNA.
DR CCDS; CCDS14811.1; -.
DR RefSeq; NP_067486.2; NM_021511.2.
DR AlphaFoldDB; Q9CYH6; -.
DR SMR; Q9CYH6; -.
DR BioGRID; 208485; 5.
DR CORUM; Q9CYH6; -.
DR STRING; 10090.ENSMUSP00000071955; -.
DR iPTMnet; Q9CYH6; -.
DR PhosphoSitePlus; Q9CYH6; -.
DR SwissPalm; Q9CYH6; -.
DR EPD; Q9CYH6; -.
DR jPOST; Q9CYH6; -.
DR MaxQB; Q9CYH6; -.
DR PaxDb; Q9CYH6; -.
DR PeptideAtlas; Q9CYH6; -.
DR PRIDE; Q9CYH6; -.
DR ProteomicsDB; 299935; -.
DR TopDownProteomics; Q9CYH6; -.
DR Antibodypedia; 24827; 197 antibodies from 27 providers.
DR DNASU; 59014; -.
DR Ensembl; ENSMUST00000072079; ENSMUSP00000071955; ENSMUSG00000061024.
DR GeneID; 59014; -.
DR KEGG; mmu:59014; -.
DR UCSC; uc007agk.2; mouse.
DR CTD; 23212; -.
DR MGI; MGI:1929721; Rrs1.
DR VEuPathDB; HostDB:ENSMUSG00000061024; -.
DR eggNOG; KOG1765; Eukaryota.
DR GeneTree; ENSGT00390000005213; -.
DR HOGENOM; CLU_065163_1_0_1; -.
DR InParanoid; Q9CYH6; -.
DR OMA; LLINEIW; -.
DR OrthoDB; 1264304at2759; -.
DR PhylomeDB; Q9CYH6; -.
DR TreeFam; TF313067; -.
DR BioGRID-ORCS; 59014; 23 hits in 70 CRISPR screens.
DR ChiTaRS; Rrs1; mouse.
DR PRO; PR:Q9CYH6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CYH6; protein.
DR Bgee; ENSMUSG00000061024; Expressed in epiblast (generic) and 134 other tissues.
DR Genevisible; Q9CYH6; MM.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:1902570; P:protein localization to nucleolus; ISS:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISS:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR InterPro; IPR007023; Ribosom_reg.
DR PANTHER; PTHR17602; PTHR17602; 1.
DR Pfam; PF04939; RRS1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Citrullination; Isopeptide bond; Nucleus; Reference proteome;
KW Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..365
FT /note="Ribosome biogenesis regulatory protein homolog"
FT /id="PRO_0000185375"
FT REGION 200..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15050"
FT MOD_RES 273
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15050"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15050"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15050"
FT CONFLICT 135
FT /note="E -> V (in Ref. 2; BAB26750)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="N -> G (in Ref. 2; BAB31912)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="K -> R (in Ref. 1; BAA95072)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 41552 MW; A99BDE7321652E66 CRC64;
MEGQRVEELL AKAEQEEAEK LQRITVHKEL ELEFDLGNLL ASDRNPPTVL RQAGPSPEAE
LRALARDNTQ LLINQLWRLP TERVEEAVVA RLPEPATRLP REKPLPRPRP LTRWQQFARL
KGIRPKKKTN LVWDEASGQW RRRWGYKRAR DDTKEWLIEV PGSADPMEDQ FAKRTQAKKE
RVAKNELNRL RNLARAHKMQ MPSSAGLHPT GHQSKEELGR AMQVAKVSTA SVGRFQERLP
KEKAPRGSGK KRKFQPLFGD FAAEKKNQLE LLRVMNSKKP RLDVTRATNK QMREEDQEEA
AKRRKMSQKG KRKGGRQGPS GKRKGGPPGQ GEKRKGGLGS KKHSWPSALA GKKKGVPPQG
GKRRK
