RRP36_MOUSE
ID RRP36_MOUSE Reviewed; 244 AA.
AC Q3UFY0; Q91X71;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Ribosomal RNA processing protein 36 homolog;
GN Name=Rrp36;
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;
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] OF 12-244.
RC STRAIN=FVB/N; TISSUE=Salivary 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: Involved in the early processing steps of the pre-rRNA in the
CC maturation pathway leading to the 18S rRNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRP36 family. {ECO:0000305}.
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DR EMBL; AK148237; BAE28429.1; -; mRNA.
DR EMBL; BC011248; AAH11248.1; -; mRNA.
DR CCDS; CCDS37639.2; -.
DR RefSeq; NP_659106.1; NM_144857.1.
DR AlphaFoldDB; Q3UFY0; -.
DR SMR; Q3UFY0; -.
DR iPTMnet; Q3UFY0; -.
DR PhosphoSitePlus; Q3UFY0; -.
DR EPD; Q3UFY0; -.
DR jPOST; Q3UFY0; -.
DR MaxQB; Q3UFY0; -.
DR PaxDb; Q3UFY0; -.
DR PeptideAtlas; Q3UFY0; -.
DR PRIDE; Q3UFY0; -.
DR ProteomicsDB; 299816; -.
DR DNASU; 224823; -.
DR GeneID; 224823; -.
DR KEGG; mmu:224823; -.
DR UCSC; uc008ctu.2; mouse.
DR CTD; 88745; -.
DR MGI; MGI:2385053; Rrp36.
DR eggNOG; KOG3190; Eukaryota.
DR InParanoid; Q3UFY0; -.
DR OrthoDB; 1471490at2759; -.
DR PhylomeDB; Q3UFY0; -.
DR TreeFam; TF315154; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 224823; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Rrp36; mouse.
DR PRO; PR:Q3UFY0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UFY0; protein.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IEA:InterPro.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR InterPro; IPR009292; RRP36.
DR PANTHER; PTHR21738; PTHR21738; 1.
DR Pfam; PF06102; RRP36; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..244
FT /note="Ribosomal RNA processing protein 36 homolog"
FT /id="PRO_0000252158"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..190
FT /evidence="ECO:0000255"
FT MOTIF 226..229
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EU6"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 34..36
FT /note="PDV -> SDM (in Ref. 2; AAH11248)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="R -> K (in Ref. 2; AAH11248)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="R -> H (in Ref. 2; AAH11248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 28589 MW; FC33A6B03B399704 CRC64;
MRKAGSRARA EAEGPHRAME GGEVTGDRLK ADTPDVSFEE LLRLQGQGRP KAHKQLVAGN
STRTRSPQQP VCVADKHRPL EMSAKVRVPF LRQVVPISKK VARDPRFDDL SGDYNPEVFD
KTYQFLNDIR AKEKQLVKKQ LKRHRSGEER DKLQQLLQRM EQQEMAQQER KQQQELRLAL
KQERRAQAQQ GHRPYFLKKS EQRQLALAEK FKELRRSKKL ESFLSRKRRR NAGKDRRHLP
LSKE
