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RL11_CHILA
ID   RL11_CHILA              Reviewed;         178 AA.
AC   Q6QMZ8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=60S ribosomal protein L11;
GN   Name=RPL11;
OS   Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC   Chinchillidae; Chinchilla.
OX   NCBI_TaxID=34839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Middle ear mucosa;
RA   Erdos G., Hu F.Z., Donfack J., Ahmed A.I., Preston R.A., Hayes J.D.,
RA   Post J.C., Ehrlich G.D.;
RT   "Gene expression in normal chinchilla middle ear mucosa.";
RL   Submitted (JAN-2004) 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 5S RNP/5S ribonucleoprotein particle it is an
CC       essential component of the LSU, required for its formation and the
CC       maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53
CC       activation. As part of the 5S RNP it accumulates in the nucleoplasm and
CC       inhibits MDM2, when ribosome biogenesis is perturbed, mediating the
CC       stabilization and the activation of TP53. Promotes nucleolar location
CC       of PML. {ECO:0000250|UniProtKB:P62913}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Part of a LSU
CC       subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11.
CC       Interacts with PML. Interacts with MDM2; negatively regulates MDM2-
CC       mediated TP53 ubiquitination and degradation. Interacts with NOP53;
CC       retains RPL11 into the nucleolus. {ECO:0000250|UniProtKB:P62913}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9CXW4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9CXW4}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000305}.
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DR   EMBL; AY533222; AAS59424.1; -; mRNA.
DR   RefSeq; NP_001269300.1; NM_001282371.1.
DR   AlphaFoldDB; Q6QMZ8; -.
DR   SMR; Q6QMZ8; -.
DR   IntAct; Q6QMZ8; 1.
DR   MINT; Q6QMZ8; -.
DR   Ensembl; ENSCLAT00000018333; ENSCLAP00000018154; ENSCLAG00000012453.
DR   GeneID; 102017736; -.
DR   CTD; 6135; -.
DR   GeneTree; ENSGT00910000144211; -.
DR   OMA; QTETIKW; -.
DR   OrthoDB; 1340833at2759; -.
DR   Proteomes; UP000694398; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR020929; Ribosomal_L5_CS.
DR   InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_L5_N.
DR   PANTHER; PTHR11994; PTHR11994; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; SSF55282; 1.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CHAIN           2..178
FT                   /note="60S ribosomal protein L11"
FT                   /id="PRO_0000125081"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         44
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         47
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         52
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CROSSLNK        38
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CROSSLNK        52
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
FT   CROSSLNK        154
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62913"
SQ   SEQUENCE   178 AA;  20252 MW;  26EC965C9239774E CRC64;
     MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF
     GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD
     PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKY DGIILPGK
 
 
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