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Protein

60S ribosomal protein L5

Gene

RPL5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs (PubMed:12962325, PubMed:19061985, PubMed:24120868, PubMed:23636399). It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53 (PubMed:24120868).4 Publications

GO - Molecular functioni

  • 5S rRNA binding Source: CAFA
  • mRNA 3'-UTR binding Source: CAFA
  • mRNA 5'-UTR binding Source: CAFA
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central
  • ubiquitin ligase inhibitor activity Source: CAFA
  • ubiquitin protein ligase binding Source: CAFA

GO - Biological processi

  • negative regulation of protein neddylation Source: CAFA
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: CAFA
  • negative regulation of ubiquitin protein ligase activity Source: CAFA
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of gene expression Source: CAFA
  • positive regulation of translation Source: CAFA
  • protein stabilization Source: CAFA
  • regulation of signal transduction by p53 class mediator Source: UniProtKB
  • ribosomal large subunit assembly Source: UniProtKB
  • ribosomal large subunit biogenesis Source: UniProtKB
  • rRNA processing Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: ProtInc
  • translational initiation Source: Reactome
  • viral transcription Source: Reactome

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-9010553. Regulation of expression of SLITs and ROBOs.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiP46777.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L5
Alternative name(s):
Large ribosomal subunit protein uL181 Publication
Gene namesi
Name:RPL5
ORF Names:MSTP030
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000122406.12.
HGNCiHGNC:10360. RPL5.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 6 (DBA6)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
See also OMIM:612561
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055450140G → S in DBA6. 1 PublicationCorresponds to variant dbSNP:rs121434406Ensembl.1
Natural variantiVAR_055451285A → V in DBA6. 1 Publication1

Keywords - Diseasei

Diamond-Blackfan anemia, Disease mutation

Organism-specific databases

DisGeNETi6125.
GeneReviewsiRPL5.
MalaCardsiRPL5.
MIMi612561. phenotype.
OpenTargetsiENSG00000122406.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34755.

Polymorphism and mutation databases

BioMutaiRPL5.
DMDMi81175191.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001314312 – 29760S ribosomal protein L5Add BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineCombined sources1
Modified residuei5N6-acetyllysineCombined sources1
Modified residuei48N6-acetyllysineCombined sources1
Modified residuei185PhosphoserineCombined sources1
Modified residuei220N6-acetyllysine; alternateBy similarity1
Cross-linki220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei232PhosphothreonineCombined sources1
Modified residuei272PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46777.
MaxQBiP46777.
PaxDbiP46777.
PeptideAtlasiP46777.
PRIDEiP46777.
TopDownProteomicsiP46777.

PTM databases

iPTMnetiP46777.
PhosphoSitePlusiP46777.
SwissPalmiP46777.

Expressioni

Gene expression databases

BgeeiENSG00000122406.
CleanExiHS_RPL5.
ExpressionAtlasiP46777. baseline and differential.
GenevisibleiP46777. HS.

Organism-specific databases

HPAiHPA043717.

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). Part of a LSU subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11 (PubMed:24120868). Interacts with isoform 1 of NVL in an ATP-dependent manner (PubMed:15469983). Interacts with RRP1B (PubMed:20926688).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: CAFA

Protein-protein interaction databases

BioGridi112045. 229 interactors.
CORUMiP46777.
DIPiDIP-31152N.
IntActiP46777. 41 interactors.
MINTiMINT-1034099.
STRINGi9606.ENSP00000359345.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LD1-297[»]
4V6Xelectron microscopy5.00CD1-297[»]
5AJ0electron microscopy3.50AD1-297[»]
5LKSelectron microscopy3.60LD1-297[»]
5T2Celectron microscopy3.60G1-297[»]
ProteinModelPortaliP46777.
SMRiP46777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0875. Eukaryota.
COG0256. LUCA.
GeneTreeiENSGT00390000008456.
HOVERGENiHBG009347.
InParanoidiP46777.
KOiK02932.
OMAiVAEYMES.
OrthoDBiEOG091G0GZO.
PhylomeDBiP46777.
TreeFamiTF300044.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiView protein in InterPro
IPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiView protein in Pfam
PF14204. Ribosomal_L18_c. 1 hit.
PF17144. Ribosomal_L5e. 1 hit.
PRINTSiPR00058. RIBOSOMALL5.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR
60 70 80 90 100
MIVRVTNRDI ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC
110 120 130 140 150
TGLLLARRLL NRFGMDKIYE GQVEVTGDEY NVESIDGQPG AFTCYLDAGL
160 170 180 190 200
ARTTTGNKVF GALKGAVDGG LSIPHSTKRF PGYDSESKEF NAEVHRKHIM
210 220 230 240 250
GQNVADYMRY LMEEDEDAYK KQFSQYIKNS VTPDMMEEMY KKAHAAIREN
260 270 280 290
PVYEKKPKKE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES
Length:297
Mass (Da):34,363
Last modified:January 23, 2007 - v3
Checksum:i07CA9FBA842BD2A3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78A → R in AAA85654 (PubMed:7772601).Curated1
Sequence conflicti176S → R (PubMed:7937132).Curated1
Sequence conflicti264K → E in BAD96324 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055450140G → S in DBA6. 1 PublicationCorresponds to variant dbSNP:rs121434406Ensembl.1
Natural variantiVAR_052009210Y → C1 PublicationCorresponds to variant dbSNP:rs11540832Ensembl.1
Natural variantiVAR_055451285A → V in DBA6. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14966 mRNA. Translation: AAA85654.1.
AF113210 mRNA. Translation: AAG39281.1.
AK222604 mRNA. Translation: BAD96324.1.
AL162740 Genomic DNA. No translation available.
BC109370 mRNA. Translation: AAI09371.1.
U76609 mRNA. Translation: AAB18361.1.
Z35312 Genomic DNA. No translation available.
CCDSiCCDS741.1.
PIRiS55912.
RefSeqiNP_000960.2. NM_000969.3.
UniGeneiHs.532359.
Hs.568386.

Genome annotation databases

EnsembliENST00000370321; ENSP00000359345; ENSG00000122406.
GeneIDi6125.
KEGGihsa:6125.
UCSCiuc001doz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRL5_HUMAN
AccessioniPrimary (citable) accession number: P46777
Secondary accession number(s): Q32LZ3, Q53HH6, Q9H3F4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 174 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families