NOP58_MACFA
ID NOP58_MACFA Reviewed; 530 AA.
AC Q4R779;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Nucleolar protein 58;
DE AltName: Full=Nucleolar protein 5;
GN Name=NOP58; Synonyms=NOL5; ORFNames=QtsA-15965;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 NOPCHAP1, NUFIP1,
CC RUVBL1 and RUVBL2; NOPCHAP1 bridges the association of NOP58 with
CC RUVBL1:RUVBL2 and NUFIP1. Interacts with PIH1D1.
CC {ECO:0000250|UniProtKB:Q9Y2X3}.
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; AB168942; BAE01043.1; -; mRNA.
DR RefSeq; NP_001274590.1; NM_001287661.1.
DR AlphaFoldDB; Q4R779; -.
DR SMR; Q4R779; -.
DR STRING; 9541.XP_005574020.1; -.
DR PRIDE; Q4R779; -.
DR Ensembl; ENSMFAT00000006019; ENSMFAP00000031799; ENSMFAG00000036935.
DR GeneID; 102131118; -.
DR CTD; 51602; -.
DR VEuPathDB; HostDB:ENSMFAG00000036935; -.
DR eggNOG; KOG2572; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR OMA; MGMRSNW; -.
DR OrthoDB; 632707at2759; -.
DR Proteomes; UP000233100; Chromosome 12.
DR Bgee; ENSMFAG00000036935; Expressed in lymph node and 13 other tissues.
DR GO; GO:0031428; C:box C/D RNP complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032040; C:small-subunit processome; IEA:InterPro.
DR GO; GO:0030515; F:snoRNA binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..530
FT /note="Nucleolar protein 58"
FT /id="PRO_0000287349"
FT DOMAIN 282..400
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 409..530
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 439..472
FT /note="Basic and 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 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
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 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X3"
SQ SEQUENCE 530 AA; 59665 MW; 4839D4DE3B564C9C CRC64;
MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF
TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR
SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI
MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA KLSELLPEEV EAEVKAAAEI
SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA
HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT SPKHKGKISR
MLAAKTVLAI RYDAFGEDSS SAMGVENRAK LEARLRTLED RGIRKISGTG KALAKTEKYE
HKSEVKTYDP SGDSTLPTCS KKRKIEQVDK EDEITEKKAK KAKIKVKVEE EEEEEKVAEE
EETSVKKKKK KGKKKHIKEE PLSEEEPCTS TAIASPEKKK KKKKKRDNED
