RL29_MOUSE
ID RL29_MOUSE Reviewed; 160 AA.
AC P47915;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=60S ribosomal protein L29;
GN Name=Rpl29; Synonyms=Rpl43;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8224911; DOI=10.1016/0378-1119(93)90647-l;
RA Rudert F., Garnier J.-M., Schuhbaur B.;
RT "Cloning a pseudogene and cDNA encoding a 17-kDa ribosomal protein from
RT mouse: structure and regulation of expression.";
RL Gene 133:249-254(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N-3;
RC TISSUE=Brain, Kidney, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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:P47914}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P47914}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47914}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family.
CC {ECO:0000305}.
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DR EMBL; L08651; AAA16857.1; -; mRNA.
DR EMBL; BC002062; AAH02062.1; -; mRNA.
DR EMBL; BC081467; AAH81467.1; -; mRNA.
DR EMBL; BC082292; AAH82292.1; -; mRNA.
DR EMBL; BC086897; AAH86897.1; -; mRNA.
DR EMBL; BC086898; AAH86898.1; -; mRNA.
DR CCDS; CCDS23476.1; -.
DR PIR; JC2012; JC2012.
DR RefSeq; NP_001311462.1; NM_001324533.1.
DR RefSeq; NP_001311463.1; NM_001324534.1.
DR RefSeq; NP_033108.1; NM_009082.3.
DR RefSeq; XP_006511723.1; XM_006511660.3.
DR RefSeq; XP_990228.1; XM_985134.6.
DR PDB; 6SWA; EM; 3.10 A; Z=1-160.
DR PDB; 7LS1; EM; 3.30 A; V2=1-160.
DR PDB; 7LS2; EM; 3.10 A; V2=1-160.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P47915; -.
DR SMR; P47915; -.
DR BioGRID; 202976; 23.
DR BioGRID; 578473; 3.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; P47915; 2.
DR STRING; 10090.ENSMUSP00000080203; -.
DR iPTMnet; P47915; -.
DR PhosphoSitePlus; P47915; -.
DR SwissPalm; P47915; -.
DR EPD; P47915; -.
DR jPOST; P47915; -.
DR PaxDb; P47915; -.
DR PeptideAtlas; P47915; -.
DR PRIDE; P47915; -.
DR DNASU; 19944; -.
DR Ensembl; ENSMUST00000059802; ENSMUSP00000080203; ENSMUSG00000048758.
DR Ensembl; ENSMUST00000098994; ENSMUSP00000096592; ENSMUSG00000048758.
DR Ensembl; ENSMUST00000150576; ENSMUSP00000117834; ENSMUSG00000048758.
DR GeneID; 19944; -.
DR KEGG; mmu:19944; -.
DR UCSC; uc007avm.2; mouse.
DR CTD; 6159; -.
DR MGI; MGI:99687; Rpl29.
DR VEuPathDB; HostDB:ENSMUSG00000048758; -.
DR eggNOG; KOG3504; Eukaryota.
DR GeneTree; ENSGT00390000007084; -.
DR HOGENOM; CLU_139508_0_0_1; -.
DR InParanoid; P47915; -.
DR OMA; RTHIAKG; -.
DR OrthoDB; 1608986at2759; -.
DR PhylomeDB; P47915; -.
DR TreeFam; TF313858; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 19944; 15 hits in 103 CRISPR screens.
DR ChiTaRS; Rpl29; mouse.
DR PRO; PR:P47915; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P47915; protein.
DR Bgee; ENSMUSG00000048758; Expressed in urinary bladder and 63 other tissues.
DR ExpressionAtlas; P47915; baseline and differential.
DR Genevisible; P47915; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:MGI.
DR GO; GO:0042788; C:polysomal ribosome; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR InterPro; IPR002673; Ribosomal_L29e.
DR PANTHER; PTHR12884; PTHR12884; 1.
DR Pfam; PF01779; Ribosomal_L29e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..160
FT /note="60S ribosomal protein L29"
FT /id="PRO_0000219136"
FT REPEAT 127..134
FT /note="1"
FT REPEAT 135..142
FT /note="2"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..142
FT /note="2 X 8 AA tandem repeats of A-X-A-K-A-P-A-[KQ]"
FT COMPBIAS 1..22
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47914"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47914"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47914"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47914"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 160 AA; 17587 MW; 420E1A9ED9709C01 CRC64;
MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN KKGLKKMQAN
NAKAVSARAE AIKALVKPQA IKPKMPKGPK LKRLAFIAHP KLGKRIRSYM AKGQRLCQPK
PKVQTKAGAK APAKAQASAP AQAPKGAQAP KGAQAPVKAP
