NOP58_MOUSE
ID NOP58_MOUSE Reviewed; 536 AA.
AC Q6DFW4; O70396; Q3UYX9; Q3UZA3; Q8C8Y7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Nucleolar protein 58;
DE AltName: Full=MSSP;
DE AltName: Full=Nucleolar protein 5;
DE AltName: Full=SIK-similar protein;
GN Name=Nop58; Synonyms=Nol5;
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 [MRNA].
RC STRAIN=C3H/HeJ;
RA Zierke M., Martin M.U.;
RT "cDNA for mouse SIK similar protein (MSSP).";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Forelimb, and Retina;
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=Brain;
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 ASSOCIATION WITH U14 BOX C/D SNORNPA.
RX PubMed=10864044; DOI=10.1017/s1355838200992446;
RA Newman D.R., Kuhn J.F., Shanab G.M., Maxwell E.S.;
RT "Box C/D snoRNA-associated proteins: two pairs of evolutionarily ancient
RT proteins and possible links to replication and transcription.";
RL RNA 6:861-879(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-521, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 60S ribosomal subunit biogenesis (By
CC similarity). Core component of box C/D small nucleolar
CC ribonucleoprotein (snoRNP) particles. Required for the biogenesis of
CC box C/D snoRNAs such as U3, U8 and U14 snoRNAs (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Core component of box C/D small nucleolar ribonucleoprotein
CC (snoRNP) particles; the core proteins SNU13, NOP56, NOP58 and FBL
CC assemble stepwise onto the snoRNA (PubMed:10864044). Interacts with
CC NOLC1/Nopp140. Interacts with NOPCHAP1, NUFIP1, RUVBL1 and RUVBL2;
CC NOPCHAP1 bridges the association of NOP58 with RUVBL1:RUVBL2 and
CC NUFIP1. Interacts with PIH1D1. {ECO:0000250|UniProtKB:Q9Y2X3,
CC ECO:0000269|PubMed:10864044}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}.
CC -!- PTM: Sumoylation is essential for high-affinity binding to snoRNAs.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08435.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF053232; AAC08435.1; ALT_FRAME; mRNA.
DR EMBL; AK044216; BAC31822.1; -; mRNA.
DR EMBL; AK133959; BAE21954.1; -; mRNA.
DR EMBL; AK134286; BAE22082.1; -; mRNA.
DR EMBL; BC076604; AAH76604.1; -; mRNA.
DR EMBL; BC085135; AAH85135.1; -; mRNA.
DR CCDS; CCDS35587.1; -.
DR RefSeq; NP_061356.2; NM_018868.2.
DR AlphaFoldDB; Q6DFW4; -.
DR SMR; Q6DFW4; -.
DR BioGRID; 207760; 30.
DR CORUM; Q6DFW4; -.
DR IntAct; Q6DFW4; 11.
DR MINT; Q6DFW4; -.
DR STRING; 10090.ENSMUSP00000140250; -.
DR iPTMnet; Q6DFW4; -.
DR PhosphoSitePlus; Q6DFW4; -.
DR SwissPalm; Q6DFW4; -.
DR EPD; Q6DFW4; -.
DR jPOST; Q6DFW4; -.
DR MaxQB; Q6DFW4; -.
DR PaxDb; Q6DFW4; -.
DR PeptideAtlas; Q6DFW4; -.
DR PRIDE; Q6DFW4; -.
DR ProteomicsDB; 252922; -.
DR Antibodypedia; 19944; 162 antibodies from 26 providers.
DR DNASU; 55989; -.
DR Ensembl; ENSMUST00000191142; ENSMUSP00000140250; ENSMUSG00000026020.
DR GeneID; 55989; -.
DR KEGG; mmu:55989; -.
DR UCSC; uc007bdy.1; mouse.
DR CTD; 51602; -.
DR MGI; MGI:1933184; Nop58.
DR VEuPathDB; HostDB:ENSMUSG00000026020; -.
DR eggNOG; KOG2572; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR InParanoid; Q6DFW4; -.
DR OMA; MGMRSNW; -.
DR OrthoDB; 632707at2759; -.
DR PhylomeDB; Q6DFW4; -.
DR TreeFam; TF105688; -.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 55989; 31 hits in 74 CRISPR screens.
DR ChiTaRS; Nop58; mouse.
DR PRO; PR:Q6DFW4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6DFW4; protein.
DR Bgee; ENSMUSG00000026020; Expressed in embryonic post-anal tail and 133 other tissues.
DR ExpressionAtlas; Q6DFW4; baseline and differential.
DR Genevisible; Q6DFW4; MM.
DR GO; GO:0031428; C:box C/D RNP complex; ISS:UniProtKB.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0030515; F:snoRNA binding; ISO:MGI.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; ISO:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048254; P:snoRNA localization; ISO:MGI.
DR Gene3D; 1.10.246.90; -; 1.
DR InterPro; IPR045056; Nop56/Nop58.
DR InterPro; IPR012974; NOP5_N.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR PANTHER; PTHR10894; PTHR10894; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF08156; NOP5NT; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 1.
DR PROSITE; PS51358; NOP; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..536
FT /note="Nucleolar protein 58"
FT /id="PRO_0000287350"
FT DOMAIN 282..400
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 414..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 426
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CONFLICT 78
FT /note="K -> R (in Ref. 1; AAC08435)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> V (in Ref. 2; BAC31822)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="K -> P (in Ref. 2; BAE22082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 60343 MW; D5FE1819F092D701 CRC64;
MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF
TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR
SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI
MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA SLSEFLSEEV EAEVKAAAEI
SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA
HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQS SPKHKGKISR
MLAAKTVLAI RYDAFGEDSS SAMGIENRAK LEARLRILED RGIRKISGTG KALAKAEKYE
HKSEVKTYDP SGDSTLPTCS KKRKIEEVDK EDEITEKKAK KAKIKIKAEV EEEMEEEEAE
EEQVVEEEPT VKKKKKKDKK KHIKEEPLSE EEPCTSTAVP SPEKKKKKKK KKDAED
