ID   RL24_MACFA              Reviewed;         157 AA.
AC   P61122;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=60S ribosomal protein L24;
GN   Name=RPL24; ORFNames=QccE-19346;
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=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA   Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC       large ribonucleoprotein complex responsible for the synthesis of
CC       proteins in the cell. {ECO:0000250|UniProtKB:P83731}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P83731}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P83731}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC       {ECO:0000305}.
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DR   EMBL; AB093678; BAC21652.1; -; mRNA.
DR   RefSeq; XP_005548319.1; XM_005548262.2.
DR   AlphaFoldDB; P61122; -.
DR   SMR; P61122; -.
DR   STRING; 9541.XP_005548319.1; -.
DR   Ensembl; ENSMFAT00000013188; ENSMFAP00000038929; ENSMFAG00000038803.
DR   GeneID; 101866107; -.
DR   KEGG; mcf:101866107; -.
DR   CTD; 6152; -.
DR   VEuPathDB; HostDB:ENSMFAG00000038803; -.
DR   eggNOG; KOG1722; Eukaryota.
DR   GeneTree; ENSGT00950000183105; -.
DR   OMA; PGKGKIY; -.
DR   OrthoDB; 1502432at2759; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000038803; Expressed in lymph node and 13 other tissues.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   CDD; cd00472; Ribosomal_L24e_L24; 1.
DR   Gene3D; 2.30.170.20; -; 1.
DR   InterPro; IPR038630; L24e/L24_sf.
DR   InterPro; IPR000988; Ribosomal_L24e-rel.
DR   InterPro; IPR023442; Ribosomal_L24e_CS.
DR   InterPro; IPR011017; TRASH_dom.
DR   PANTHER; PTHR10792; PTHR10792; 1.
DR   Pfam; PF01246; Ribosomal_L24e; 1.
DR   SMART; SM00746; TRASH; 1.
DR   PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..157
FT                   /note="60S ribosomal protein L24"
FT                   /id="PRO_0000136868"
FT   REGION          106..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   MOD_RES         77
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   MOD_RES         83
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   MOD_RES         93
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   MOD_RES         131
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BP67"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   CROSSLNK        2
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   CROSSLNK        35
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
FT   CROSSLNK        147
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P83731"
SQ   SEQUENCE   157 AA;  17779 MW;  1D48EEB7C0652574 CRC64;
     MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK
     KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ
     ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR