ID NOP58_RAT Reviewed; 534 AA. AC Q9QZ86; O88525; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=Nucleolar protein 58; DE AltName: Full=Nopp140-associated protein of 65 kDa; DE AltName: Full=Nucleolar protein 5; GN Name=Nop58; Synonyms=Nap65, Nol5, Nop5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-22, AND INTERACTION WITH RP NOLC1. RX PubMed=10679015; DOI=10.1091/mbc.11.2.567; RA Yang Y., Isaac C., Wang C., Dragon F., Pogacic V., Meier U.T.; RT "Conserved composition of mammalian box H/ACA and box C/D small nucleolar RT ribonucleoprotein particles and their interaction with the common factor RT Nopp140."; RL Mol. Biol. Cell 11:567-577(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-461. RA Hatton D., Gray J.C.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND SER-519, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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). Part of CC the small subunit (SSU) processome, first precursor of the small CC eukaryotic ribosomal subunit. During the assembly of the SSU processome CC in the nucleolus, many ribosome biogenesis factors, an RNA chaperone CC and ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (By similarity). {ECO:0000250|UniProtKB:Q9Y2X3}. 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 (By similarity). Interacts with CC NOLC1/Nopp140 (PubMed:10679015). Interacts with NUFIP1, RUVBL1 and CC RUVBL2; RUVBL1:RUVBL2 seem to bridge the association of NOP58 with CC NUFIP1. Interacts with PIH1D1 (By similarity). CC {ECO:0000250|UniProtKB:Q9Y2X3, ECO:0000269|PubMed:10679015}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:Q9Y2X3}. Nucleus, nucleoplasm CC {ECO:0000250|UniProtKB:Q9Y2X3}. Note=Localizes to the nucleolus with a CC minor part present in the nucleoplasm. {ECO:0000250|UniProtKB:Q9Y2X3}. CC -!- PTM: Sumoylation is essential for high-affinity binding to snoRNAs. CC {ECO:0000250|UniProtKB:Q9Y2X3}. CC -!- SIMILARITY: Belongs to the NOP5/NOP56 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; AF194371; AAF05769.1; -; mRNA. DR EMBL; AF069782; AAC23535.1; -; mRNA. DR RefSeq; NP_068522.1; NM_021754.1. DR AlphaFoldDB; Q9QZ86; -. DR SMR; Q9QZ86; -. DR BioGRID; 248802; 1. DR IntAct; Q9QZ86; 2. DR STRING; 10116.ENSRNOP00000022676; -. DR iPTMnet; Q9QZ86; -. DR PhosphoSitePlus; Q9QZ86; -. DR jPOST; Q9QZ86; -. DR PaxDb; 10116-ENSRNOP00000022676; -. DR Ensembl; ENSRNOT00000022676.7; ENSRNOP00000022676.3; ENSRNOG00000016486.7. DR Ensembl; ENSRNOT00055041011; ENSRNOP00055033341; ENSRNOG00055023889. DR Ensembl; ENSRNOT00060033227; ENSRNOP00060027195; ENSRNOG00060019139. DR Ensembl; ENSRNOT00065047088; ENSRNOP00065038627; ENSRNOG00065027245. DR GeneID; 60373; -. DR KEGG; rno:60373; -. DR UCSC; RGD:620484; rat. DR AGR; RGD:620484; -. DR CTD; 51602; -. DR RGD; 620484; Nop58. DR eggNOG; KOG2572; Eukaryota. DR GeneTree; ENSGT00940000153534; -. DR InParanoid; Q9QZ86; -. DR OMA; KGKMARI; -. DR OrthoDB; 5489581at2759; -. DR PhylomeDB; Q9QZ86; -. DR TreeFam; TF105688; -. DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR PRO; PR:Q9QZ86; -. DR Proteomes; UP000002494; Chromosome 9. DR Bgee; ENSRNOG00000016486; Expressed in ovary and 20 other cell types or tissues. DR ExpressionAtlas; Q9QZ86; baseline and differential. DR GO; GO:0031428; C:box C/D RNP complex; ISO:RGD. DR GO; GO:0015030; C:Cajal body; ISO:RGD. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; ISO:RGD. DR GO; GO:0070761; C:pre-snoRNP complex; ISO:RGD. DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB. DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISO:RGD. DR GO; GO:0051117; F:ATPase binding; ISO:RGD. DR GO; GO:0030515; F:snoRNA binding; ISO:RGD. DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; ISO:RGD. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB. DR GO; GO:0048254; P:snoRNA localization; ISO:RGD. DR Gene3D; 1.10.287.4070; -; 1. DR Gene3D; 1.10.246.90; Nop domain; 1. DR InterPro; IPR045056; Nop56/Nop58. DR InterPro; IPR012974; NOP58/56_N. DR InterPro; IPR042239; Nop_C. DR InterPro; IPR002687; Nop_dom. DR InterPro; IPR036070; Nop_dom_sf. DR InterPro; IPR012976; NOSIC. DR PANTHER; PTHR10894; NUCLEOLAR PROTEIN 5 NUCLEOLAR PROTEIN NOP5 NOP58; 1. DR PANTHER; PTHR10894:SF1; NUCLEOLAR PROTEIN 58; 1. DR Pfam; PF01798; Nop; 1. DR Pfam; PF08156; NOP5NT; 1. DR SMART; SM00931; NOSIC; 1. DR SUPFAM; SSF89124; Nop domain; 1. DR PROSITE; PS51358; NOP; 1. DR Genevisible; Q9QZ86; RN. PE 1: Evidence at protein level; KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosome biogenesis; KW Ubl conjugation. FT CHAIN 1..534 FT /note="Nucleolar protein 58" FT /id="PRO_0000219024" FT DOMAIN 282..400 FT /note="Nop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690" FT REGION 470..534 FT /note="Disordered" 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 507 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 519 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" 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 490 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3" FT CROSSLNK 502 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250" FT CROSSLNK 502 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3" FT CONFLICT 396 FT /note="R -> K (in Ref. 2; AAC23535)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="A -> K (in Ref. 2; AAC23535)" FT /evidence="ECO:0000305" SQ SEQUENCE 534 AA; 60071 MW; 4B9585FA14E67799 CRC64; MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA TLSEFLSEEV EAEVKAAAEI SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT SPKHKGKISR MLAAKTVLAI RYDAFGEDSS SAMGAENRAK LEARLRILED RGIRKISGTG KALAKAEKYE HKSEVKTYDP SGDSTLPTCS KKRKIEEVDK EDEITEKKAK KAKIKIKAEV EEEMEEAEEE QVVEEEPTVK KKKKKDKKKH IKEEPLSEEE PCTSTAVPSP EKKKKKKKKK DAED //