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Protein

60S ribosomal protein L3

Gene

RPL3

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

Functioni

The L3 protein is a component of the large subunit of cytoplasmic ribosomes.

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100316-MONOMER.
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-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).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L3
Alternative name(s):
HIV-1 TAR RNA-binding protein B
Short name:
TARBP-B
Gene namesi
Name:RPL3
ORF Names:OK/SW-cl.32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:10332. RPL3.

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
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi6122.
OpenTargetsiENSG00000100316.
PharmGKBiPA34713.

Chemistry databases

DrugBankiDB04865. Homoharringtonine.

Polymorphism and mutation databases

BioMutaiRPL3.
DMDMi730565.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000772272 – 40360S ribosomal protein L3Add BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13PhosphoserineCombined sources1
Modified residuei136N6-acetyllysineBy similarity1
Modified residuei286N6-acetyllysineBy similarity1
Modified residuei294N6-acetyllysine; alternateCombined sources1
Cross-linki294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei304PhosphoserineCombined sources1
Modified residuei366N6-acetyllysineCombined sources1
Modified residuei373N6-acetyllysineBy similarity1
Cross-linki399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP39023.
MaxQBiP39023.
PaxDbiP39023.
PeptideAtlasiP39023.
PRIDEiP39023.
TopDownProteomicsiP39023.

2D gel databases

SWISS-2DPAGEP39023.

PTM databases

iPTMnetiP39023.
PhosphoSitePlusiP39023.
SwissPalmiP39023.

Expressioni

Gene expression databases

BgeeiENSG00000100316.
CleanExiHS_RPL3.
ExpressionAtlasiP39023. baseline and differential.
GenevisibleiP39023. HS.

Organism-specific databases

HPAiHPA003365.
HPA055361.

Interactioni

Subunit structurei

Interacts with METTL18.1 Publication

Protein-protein interaction databases

BioGridi112042. 178 interactors.
IntActiP39023. 41 interactors.
MINTiMINT-1145548.
STRINGi9606.ENSP00000346001.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LB1-403[»]
4V6Xelectron microscopy5.00CB1-403[»]
5AJ0electron microscopy3.50AB1-403[»]
ProteinModelPortaliP39023.
SMRiP39023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiKOG0746. Eukaryota.
COG0087. LUCA.
GeneTreeiENSGT00390000017606.
HOGENOMiHOG000107319.
HOVERGENiHBG001864.
InParanoidiP39023.
KOiK02925.
OMAiCKFIRVI.
OrthoDBiEOG091G086T.
PhylomeDBiP39023.
TreeFamiTF300555.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P39023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDPSKP VHLTAFLGYK
60 70 80 90 100
AGMTHIVREV DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR
110 120 130 140 150
TFKTVFAEHI SDECKRRFYK NWHKSKKKAF TKYCKKWQDE DGKKQLEKDF
160 170 180 190 200
SSMKKYCQVI RVIAHTQMRL LPLRQKKAHL MEIQVNGGTV AEKLDWARER
210 220 230 240 250
LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL PRKTHRGLRK
260 270 280 290 300
VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK
310 320 330 340 350
NNASTDYDLS DKSINPLGGF VHYGEVTNDF VMLKGCVVGT KKRVLTLRKS
360 370 380 390 400
LLVQTKRRAL EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE

EGA
Length:403
Mass (Da):46,109
Last modified:January 23, 2007 - v2
Checksum:iA607CEE75CF62148
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22S → T in AAA91344 (PubMed:7576925).Curated1
Sequence conflicti260A → V in AAA91344 (PubMed:7576925).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06922011H → R Rare variant found in a Diamond-Blackfan anemia patient; unknown pathological significance. 1 Publication1
Natural variantiVAR_05204078I → T.Corresponds to variant rs11548004dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73460 mRNA. Translation: CAA51839.1.
AB062291 mRNA. Translation: BAB93474.1.
CR456566 mRNA. Translation: CAG30452.1.
AK315693 mRNA. Translation: BAG38056.1.
AL022326 Genomic DNA. Translation: CAA18450.1.
BC002408 mRNA. Translation: AAH02408.1.
BC006483 mRNA. Translation: AAH06483.1.
BC008003 mRNA. Translation: AAH08003.1.
BC012146 mRNA. Translation: AAH12146.1.
BC012786 mRNA. Translation: AAH12786.1.
BC013674 mRNA. Translation: AAH13674.1.
BC014017 mRNA. Translation: AAH14017.1.
BC015032 mRNA. Translation: AAH15032.1.
BC015767 mRNA. Translation: AAH15767.1.
BC063662 mRNA. Translation: AAH63662.1.
BC088373 mRNA. Translation: AAH88373.1.
BC107711 mRNA. Translation: AAI07712.1.
M90054 mRNA. Translation: AAA60291.1.
L22453 mRNA. Translation: AAA91344.1.
AB007166 Genomic DNA. Translation: BAA25828.1.
CCDSiCCDS13988.1.
PIRiS34195.
RefSeqiNP_000958.1. NM_000967.3.
UniGeneiHs.119598.

Genome annotation databases

EnsembliENST00000216146; ENSP00000346001; ENSG00000100316.
GeneIDi6122.
KEGGihsa:6122.
UCSCiuc003axi.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73460 mRNA. Translation: CAA51839.1.
AB062291 mRNA. Translation: BAB93474.1.
CR456566 mRNA. Translation: CAG30452.1.
AK315693 mRNA. Translation: BAG38056.1.
AL022326 Genomic DNA. Translation: CAA18450.1.
BC002408 mRNA. Translation: AAH02408.1.
BC006483 mRNA. Translation: AAH06483.1.
BC008003 mRNA. Translation: AAH08003.1.
BC012146 mRNA. Translation: AAH12146.1.
BC012786 mRNA. Translation: AAH12786.1.
BC013674 mRNA. Translation: AAH13674.1.
BC014017 mRNA. Translation: AAH14017.1.
BC015032 mRNA. Translation: AAH15032.1.
BC015767 mRNA. Translation: AAH15767.1.
BC063662 mRNA. Translation: AAH63662.1.
BC088373 mRNA. Translation: AAH88373.1.
BC107711 mRNA. Translation: AAI07712.1.
M90054 mRNA. Translation: AAA60291.1.
L22453 mRNA. Translation: AAA91344.1.
AB007166 Genomic DNA. Translation: BAA25828.1.
CCDSiCCDS13988.1.
PIRiS34195.
RefSeqiNP_000958.1. NM_000967.3.
UniGeneiHs.119598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LB1-403[»]
4V6Xelectron microscopy5.00CB1-403[»]
5AJ0electron microscopy3.50AB1-403[»]
ProteinModelPortaliP39023.
SMRiP39023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112042. 178 interactors.
IntActiP39023. 41 interactors.
MINTiMINT-1145548.
STRINGi9606.ENSP00000346001.

Chemistry databases

DrugBankiDB04865. Homoharringtonine.

PTM databases

iPTMnetiP39023.
PhosphoSitePlusiP39023.
SwissPalmiP39023.

Polymorphism and mutation databases

BioMutaiRPL3.
DMDMi730565.

2D gel databases

SWISS-2DPAGEP39023.

Proteomic databases

EPDiP39023.
MaxQBiP39023.
PaxDbiP39023.
PeptideAtlasiP39023.
PRIDEiP39023.
TopDownProteomicsiP39023.

Protocols and materials databases

DNASUi6122.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216146; ENSP00000346001; ENSG00000100316.
GeneIDi6122.
KEGGihsa:6122.
UCSCiuc003axi.4. human.

Organism-specific databases

CTDi6122.
DisGeNETi6122.
GeneCardsiRPL3.
H-InvDBHIX0172339.
HGNCiHGNC:10332. RPL3.
HPAiHPA003365.
HPA055361.
MIMi604163. gene.
neXtProtiNX_P39023.
OpenTargetsiENSG00000100316.
PharmGKBiPA34713.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0746. Eukaryota.
COG0087. LUCA.
GeneTreeiENSGT00390000017606.
HOGENOMiHOG000107319.
HOVERGENiHBG001864.
InParanoidiP39023.
KOiK02925.
OMAiCKFIRVI.
OrthoDBiEOG091G086T.
PhylomeDBiP39023.
TreeFamiTF300555.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100316-MONOMER.
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-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).

Miscellaneous databases

ChiTaRSiRPL3. human.
GeneWikiiRPL3.
GenomeRNAii6122.
PROiP39023.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100316.
CleanExiHS_RPL3.
ExpressionAtlasiP39023. baseline and differential.
GenevisibleiP39023. HS.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL3_HUMAN
AccessioniPrimary (citable) accession number: P39023
Secondary accession number(s): B2RDV9, Q15548, Q5I0G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 177 of the entry and version 2 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 22
    Human chromosome 22: 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.