ID   NOP56_MACFA             Reviewed;         594 AA.
AC   Q95K50;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Nucleolar protein 56;
DE   AltName: Full=Nucleolar protein 5A;
GN   Name=NOP56; Synonyms=NOL5A; ORFNames=QtrA-10084;
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=Temporal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the early to middle stages of 60S ribosomal
CC       subunit biogenesis. {ECO:0000250}.
CC   -!- SUBUNIT: Part of a large pre-ribosomal ribonucleoprotein (RNP) complex,
CC       that consists of at least 62 ribosomal proteins, 45 nonribosomal
CC       proteins and both pre-rRNA and mature rRNA species. Within this complex
CC       directly interacts with TCOF1 in an RNA-independent manner. Interacts
CC       with NOP1 and NOP58 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
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DR   EMBL; AB066543; BAB62217.1; -; mRNA.
DR   RefSeq; NP_001271483.1; NM_001284554.1.
DR   AlphaFoldDB; Q95K50; -.
DR   SMR; Q95K50; -.
DR   STRING; 9541.XP_005568574.1; -.
DR   GeneID; 102131987; -.
DR   CTD; 10528; -.
DR   VEuPathDB; HostDB:ENSMFAG00000041293; -.
DR   eggNOG; KOG2573; Eukaryota.
DR   OMA; DNYMFAK; -.
DR   OrthoDB; 632707at2759; -.
DR   Proteomes; UP000233100; Chromosome 10.
DR   GO; GO:0031428; C:box C/D RNP complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; 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   Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT   CHAIN           1..594
FT                   /note="Nucleolar protein 56"
FT                   /id="PRO_0000219026"
FT   DOMAIN          292..410
FT                   /note="Nop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT   REGION          457..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         359
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         468
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         561
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        87
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        230
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        540
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        564
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
SQ   SEQUENCE   594 AA;  66029 MW;  A29D005D218DAB92 CRC64;
     MVLLHVLFEH AVGYALLALK EVEEISLLQP QVEESVLNLG KFHNIVRLVA FCPFASSQVA
     LENANAVSEG VVHEDLRLLL ETHLPSKKKK VLLGVGDPKI GAAIQEELGY NCQTGGVIAE
     ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK
     DINTFSMRVR EWYGYHFPEL VKIINDNATY CRLAQFIGNR RELNEEKLEK LEELTMDGAK
     AKAILDASRS SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI
     GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL IFHSTFIGRA
     AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ VEERLSFYET GEIPRKNLDV
     MKEAMVQAEE AAAEITRKLE KQEKKRLKKE KKRLAALALA SSENSSSTPE ECEETSEKPK
     KKKKQKPQEV PQENGMEDPS IPFSKPKKKK SFSKEELMSS DLEETAGSTS LPKRKKSSPK
     EETVNDPEEA GHRSGSKKKR KFSKEEPVSS GPEEAAGKSS SKKKKKFHKA SQED