RL11_PIG
ID RL11_PIG Reviewed; 178 AA.
AC Q29205; Q6QAS7; Q6QDB2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=60S ribosomal protein L11;
GN Name=RPL11;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee H.Y., Cui X.S., Shin M.L., Hwang K.C., Kim N.H.;
RT "Identification of differentially expressed genes in porcine embryos.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-166.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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; AY547313; AAS55632.1; -; mRNA.
DR EMBL; AY550042; AAS55900.1; -; mRNA.
DR EMBL; F14532; CAA23111.1; -; mRNA.
DR RefSeq; NP_001001638.1; NM_001001638.1.
DR PDB; 3J7O; EM; 3.40 A; J=1-178.
DR PDB; 3J7P; EM; 3.50 A; J=1-178.
DR PDB; 3J7Q; EM; 3.40 A; J=1-178.
DR PDB; 3J7R; EM; 3.90 A; J=1-178.
DR PDBsum; 3J7O; -.
DR PDBsum; 3J7P; -.
DR PDBsum; 3J7Q; -.
DR PDBsum; 3J7R; -.
DR AlphaFoldDB; Q29205; -.
DR SMR; Q29205; -.
DR IntAct; Q29205; 1.
DR STRING; 9823.ENSSSCP00000022003; -.
DR PaxDb; Q29205; -.
DR PeptideAtlas; Q29205; -.
DR PRIDE; Q29205; -.
DR GeneID; 414422; -.
DR KEGG; ssc:414422; -.
DR CTD; 6135; -.
DR eggNOG; KOG0397; Eukaryota.
DR InParanoid; Q29205; -.
DR OrthoDB; 1340833at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0015934; C:large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; 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_0000125084"
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"
FT CONFLICT 143
FT /note="D -> G (in Ref. 2; CAA23111)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="C -> F (in Ref. 2; CAA23111)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="H -> Y (in Ref. 1; AAS55900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20212 MW; 3489965C9239774E CRC64;
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF
GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD
PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKH DGIILPGN
