RRP15_MOUSE
ID RRP15_MOUSE Reviewed; 281 AA.
AC Q9CYX7; Q8BU28; Q922T8; Q9CWJ2; Q9D8W8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=RRP15-like protein;
DE AltName: Full=Ribosomal RNA-processing protein 15;
GN Name=Rrp15;
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=Liver, Pancreas, and Thymus;
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=Czech II; TISSUE=Mammary tumor;
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-265, AND IDENTIFICATION BY
RP 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-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and 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).
RN [5]
RP CITRULLINATION AT ARG-9.
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 -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the RRP15 family. {ECO:0000305}.
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DR EMBL; AK007616; BAB25137.2; -; mRNA.
DR EMBL; AK010658; BAB27096.1; -; mRNA.
DR EMBL; AK013217; BAB28719.2; -; mRNA.
DR EMBL; AK087997; BAC40083.1; -; mRNA.
DR EMBL; AK169088; BAE40872.1; -; mRNA.
DR EMBL; BC006787; AAH06787.1; -; mRNA.
DR CCDS; CCDS15602.1; -.
DR RefSeq; NP_080317.3; NM_026041.2.
DR AlphaFoldDB; Q9CYX7; -.
DR SMR; Q9CYX7; -.
DR BioGRID; 212028; 3.
DR IntAct; Q9CYX7; 1.
DR MINT; Q9CYX7; -.
DR STRING; 10090.ENSMUSP00000001339; -.
DR iPTMnet; Q9CYX7; -.
DR PhosphoSitePlus; Q9CYX7; -.
DR EPD; Q9CYX7; -.
DR jPOST; Q9CYX7; -.
DR MaxQB; Q9CYX7; -.
DR PaxDb; Q9CYX7; -.
DR PeptideAtlas; Q9CYX7; -.
DR PRIDE; Q9CYX7; -.
DR ProteomicsDB; 260844; -.
DR Antibodypedia; 20731; 79 antibodies from 15 providers.
DR DNASU; 67223; -.
DR Ensembl; ENSMUST00000001339; ENSMUSP00000001339; ENSMUSG00000001305.
DR GeneID; 67223; -.
DR KEGG; mmu:67223; -.
DR UCSC; uc007dzq.2; mouse.
DR CTD; 51018; -.
DR MGI; MGI:1914473; Rrp15.
DR VEuPathDB; HostDB:ENSMUSG00000001305; -.
DR eggNOG; KOG2974; Eukaryota.
DR GeneTree; ENSGT00390000001960; -.
DR HOGENOM; CLU_079732_0_0_1; -.
DR InParanoid; Q9CYX7; -.
DR OMA; EDEPAWA; -.
DR OrthoDB; 1522334at2759; -.
DR PhylomeDB; Q9CYX7; -.
DR TreeFam; TF106119; -.
DR BioGRID-ORCS; 67223; 21 hits in 72 CRISPR screens.
DR PRO; PR:Q9CYX7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CYX7; protein.
DR Bgee; ENSMUSG00000001305; Expressed in dorsal pancreas and 250 other tissues.
DR Genevisible; Q9CYX7; MM.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR InterPro; IPR012459; Rrp15.
DR PANTHER; PTHR13245; PTHR13245; 1.
DR Pfam; PF07890; Rrp15p; 1.
PE 1: Evidence at protein level;
KW Acetylation; Citrullination; Coiled coil; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CHAIN 2..281
FT /note="RRP15-like protein"
FT /id="PRO_0000273214"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..144
FT /evidence="ECO:0000255"
FT COMPBIAS 31..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 9
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3B9"
FT CONFLICT 2
FT /note="A -> G (in Ref. 1; BAB25137)"
FT /evidence="ECO:0000305"
FT CONFLICT 3
FT /note="A -> G (in Ref. 1; BAB25137)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="D -> G (in Ref. 1; BAB25137)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="I -> M (in Ref. 2; AAH06787)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="E -> D (in Ref. 2; AAH06787)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> V (in Ref. 1; BAC40083)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="A -> D (in Ref. 1; BAB25137)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> Q (in Ref. 1; BAC40083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 31058 MW; 9694E4D2B89E52B3 CRC64;
MAAAVQDSRV SPGEILKRSP KKKKKMKMVA KAAASKLEDE VKDSSDGEGS CDSEMDHSDD
GAAEADSEDN VESCEEDNED AAESSAGTNS GWADAMAKIL NKKTPKSKAT ILTKNKELEK
EKEKLKQERL EKRKQLDKKR EWEMLCRVKP DVVKDKEAER NLQRIATRGV VQLFNAVQKH
QRNVGEKVKE AGGSVRKRAK LMSTVSKKDF ISVLRGMDGT SRNSPAGKSP KARQTEVKSE
ESPGWKILRD DFMMGASMKD WDKESEGEEP AGGRAEAAAS R
