NOP58_RAT
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 03-AUG-2022, entry version 144.
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).
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. Interacts with NOLC1/Nopp140.
CC Interacts with NUFIP1, RUVBL1 AND RUVBL2; RUVBL1:RUVBL2 seem to bridge
CC the association of NOP58 with NUFIP1. Interacts with PIH1D1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2X3,
CC ECO:0000269|PubMed:10679015}.
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}.
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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; Q9QZ86; -.
DR PRIDE; Q9QZ86; -.
DR Ensembl; ENSRNOT00000022676; ENSRNOP00000022676; ENSRNOG00000016486.
DR GeneID; 60373; -.
DR KEGG; rno:60373; -.
DR UCSC; RGD:620484; rat.
DR CTD; 51602; -.
DR RGD; 620484; Nop58.
DR eggNOG; KOG2572; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR InParanoid; Q9QZ86; -.
DR OMA; MGMRSNW; -.
DR OrthoDB; 632707at2759; -.
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 tissues.
DR ExpressionAtlas; Q9QZ86; baseline and differential.
DR Genevisible; Q9QZ86; RN.
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:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:RGD.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
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:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048254; P:snoRNA localization; ISO:RGD.
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 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
