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NOP56_PONAB
ID   NOP56_PONAB             Reviewed;         594 AA.
AC   Q5RA29;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Nucleolar protein 56;
DE   AltName: Full=Nucleolar protein 5A;
GN   Name=NOP56; Synonyms=NOL5A;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the early to middle stages of 60S ribosomal
CC       subunit biogenesis. Core component of box C/D small nucleolar
CC       ribonucleoprotein (snoRNP) particles. Required for the biogenesis of
CC       box C/D snoRNAs such U3, U8 and U14 snoRNAs (By similarity).
CC       {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. Core
CC       component of box C/D small nucleolar ribonucleoprotein (snoRNP)
CC       particles; the core proteins SNU13, NOP56, NOP58 and FBL assemble
CC       stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with
CC       NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association
CC       of NOP56 with NUFIP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
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DR   EMBL; CR859194; CAH91381.1; -; mRNA.
DR   RefSeq; NP_001125816.1; NM_001132344.2.
DR   AlphaFoldDB; Q5RA29; -.
DR   SMR; Q5RA29; -.
DR   STRING; 9601.ENSPPYP00000012104; -.
DR   PRIDE; Q5RA29; -.
DR   GeneID; 100172744; -.
DR   KEGG; pon:100172744; -.
DR   CTD; 10528; -.
DR   eggNOG; KOG2573; Eukaryota.
DR   InParanoid; Q5RA29; -.
DR   OrthoDB; 632707at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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: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   Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW   Ubl conjugation.
FT   CHAIN           1..594
FT                   /note="Nucleolar protein 56"
FT                   /id="PRO_0000219028"
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        535..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;  65947 MW;  682C8AE02A168764 CRC64;
     MVLLHVLFEH AVGYALLALK EVEEISLLQP QVEESVLNLG KFHNIVRLVA FCPFASSQVA
     LENANAVSEG VVHEDLRLLL ETHLPSKKKR VLLGVGDPKI GAAIQEELGY NCQTGGVIAE
     ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRTKVKFN VNRVDNMIIQ SISLLDQLDK
     DINTFSMRVR EWYGYHFPEL VKIINDNATY CRLAQFIGNR RELNEDKLEK 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 ISFSKPKKKK SFSKEELMSS DPEETAGSTS IPKKKKSSPK
     GETVNDPEEA GHRSGSKKKR KFSKEEPVSS GPEEAAGKSS SKKKKKFHKA SQED
 
 
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