ID   RL13_CRIGR              Reviewed;         211 AA.
AC   Q9Z313;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=60S ribosomal protein L13;
GN   Name=RPL13;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sasaki Y., Itoh F., Suzuki H., Hinoda Y., Imai K.;
RT   "Identification of genes highly expressed in association with G2 arrest
RT   induced by DNA damage of Chinese hamster overy cells by differential
RT   display.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. As part of the LSU, it is probably required for its formation
CC       and the maturation of rRNAs. Plays a role in bone development.
CC       {ECO:0000250|UniProtKB:P26373}.
CC   -!- SUBUNIT: Component of the 60S large ribosomal subunit (LSU).
CC       {ECO:0000250|UniProtKB:P26373}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26373}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC       {ECO:0000305}.
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DR   EMBL; AB014876; BAA34291.1; -; mRNA.
DR   RefSeq; NP_001233732.1; NM_001246803.2.
DR   AlphaFoldDB; Q9Z313; -.
DR   SMR; Q9Z313; -.
DR   IntAct; Q9Z313; 1.
DR   MINT; Q9Z313; -.
DR   STRING; 10029.NP_001233732.1; -.
DR   Ensembl; ENSCGRT00001029001; ENSCGRP00001024755; ENSCGRG00001022563.
DR   GeneID; 100689376; -.
DR   KEGG; cge:100689376; -.
DR   CTD; 6137; -.
DR   eggNOG; KOG3295; Eukaryota.
DR   GeneTree; ENSGT00390000007818; -.
DR   OrthoDB; 1239434at2759; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:Ensembl.
DR   GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR   GO; GO:0060348; P:bone development; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_00499; Ribosomal_L13e; 1.
DR   InterPro; IPR001380; Ribosomal_L13e.
DR   InterPro; IPR018256; Ribosomal_L13e_CS.
DR   PANTHER; PTHR11722; PTHR11722; 1.
DR   Pfam; PF01294; Ribosomal_L13e; 1.
DR   PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..211
FT                   /note="60S ribosomal protein L13"
FT                   /id="PRO_0000192918"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   MOD_RES         177
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   CROSSLNK        123
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   CROSSLNK        145
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   CROSSLNK        174
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   CROSSLNK        174
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
FT   CROSSLNK        177
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26373"
SQ   SEQUENCE   211 AA;  24393 MW;  5860CA75674A19A6 CRC64;
     MAPSRNGMIL KPHFHKDWQR RVDTWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR
     CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY
     RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMRIRNV YKKEKARVIT EEEKNFKAFA
     SLRMARANAR LFGIRAKRAK EAAEQDVEKK K