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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

Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA.1 Publication

GO - Molecular functioni

  • 5S rRNA binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • ribosomal large subunit assembly Source: GO_Central
  • ribosomal large subunit biogenesis Source: UniProtKB
  • rRNA processing Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational initiation Source: Reactome
  • viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

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.
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-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
Gene namesi
Name:RPL5
ORF Names:MSTP030
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10360. RPL5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401G → S in DBA6. 1 Publication
Corresponds to variant rs121434406 [ dbSNP | Ensembl ].
VAR_055450
Natural varianti285 – 2851A → V in DBA6. 1 Publication
VAR_055451

Keywords - Diseasei

Diamond-Blackfan anemia, Disease mutation

Organism-specific databases

MalaCardsiRPL5.
MIMi612561. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34755.

Polymorphism and mutation databases

BioMutaiRPL5.
DMDMi81175191.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 29729660S ribosomal protein L5PRO_0000131431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineCombined sources
Modified residuei5 – 51N6-acetyllysineCombined sources
Modified residuei48 – 481N6-acetyllysineCombined sources
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei220 – 2201N6-acetyllysine; alternateBy similarity
Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei232 – 2321PhosphothreonineCombined sources
Modified residuei272 – 2721PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

PTM databases

iPTMnetiP46777.
PhosphoSiteiP46777.
SwissPalmiP46777.

Expressioni

Gene expression databases

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

Organism-specific databases

HPAiHPA043717.
HPA054444.

Interactioni

Subunit structurei

Interacts with isoform 1 of NVL in an ATP-dependent manner.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DCCP431467EBI-358018,EBI-1222919
DccQ631554EBI-358018,EBI-1798965From a different organism.
MDM2Q009875EBI-358018,EBI-389668

Protein-protein interaction databases

BioGridi112045. 223 interactions.
DIPiDIP-31152N.
IntActiP46777. 36 interactions.
MINTiMINT-1034099.
STRINGi9606.ENSP00000359345.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LD1-297[»]
4V6Xelectron microscopy5.00CD1-297[»]
5AJ0electron microscopy3.50AD1-297[»]
ProteinModelPortaliP46777.
SMRiP46777. Positions 15-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF14204. Ribosomal_L18_c. 1 hit.
PF17144. Ribosomal_L5e. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781A → R in AAA85654 (PubMed:7772601).Curated
Sequence conflicti176 – 1761S → R (PubMed:7937132).Curated
Sequence conflicti264 – 2641K → E in BAD96324 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401G → S in DBA6. 1 Publication
Corresponds to variant rs121434406 [ dbSNP | Ensembl ].
VAR_055450
Natural varianti210 – 2101Y → C.1 Publication
Corresponds to variant rs11540832 [ dbSNP | Ensembl ].
VAR_052009
Natural varianti285 – 2851A → V in DBA6. 1 Publication
VAR_055451

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. Translation: CAI22505.1.
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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Diamond-Blackfan Anemia mutation database

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. Translation: CAI22505.1.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LD1-297[»]
4V6Xelectron microscopy5.00CD1-297[»]
5AJ0electron microscopy3.50AD1-297[»]
ProteinModelPortaliP46777.
SMRiP46777. Positions 15-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112045. 223 interactions.
DIPiDIP-31152N.
IntActiP46777. 36 interactions.
MINTiMINT-1034099.
STRINGi9606.ENSP00000359345.

PTM databases

iPTMnetiP46777.
PhosphoSiteiP46777.
SwissPalmiP46777.

Polymorphism and mutation databases

BioMutaiRPL5.
DMDMi81175191.

Proteomic databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6125.
GeneCardsiRPL5.
GeneReviewsiRPL5.
HGNCiHGNC:10360. RPL5.
HPAiHPA043717.
HPA054444.
MalaCardsiRPL5.
MIMi603634. gene.
612561. phenotype.
neXtProtiNX_P46777.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34755.
GenAtlasiSearch...

Phylogenomic databases

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

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.
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-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.

Miscellaneous databases

ChiTaRSiRPL5. human.
GeneWikiiRibosomal_protein_L5.
GenomeRNAii6125.
PROiP46777.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF14204. Ribosomal_L18_c. 1 hit.
PF17144. Ribosomal_L5e. 1 hit.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.
ProtoNetiSearch...

Entry informationi

Entry nameiRL5_HUMAN
AccessioniPrimary (citable) accession number: P46777
Secondary accession number(s): Q32LZ3, Q53HH6, Q9H3F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 162 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.