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Protein

60S acidic ribosomal protein P2

Gene

Rplp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the elongation step of protein synthesis.

GO - Molecular functioni

  • iron ion binding Source: RGD
  • large ribosomal subunit rRNA binding Source: GO_Central
  • ribonucleoprotein complex binding Source: RGD
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

  • cellular response to cAMP Source: RGD
  • cellular response to Thyroid stimulating hormone Source: RGD
  • cytoplasmic translation Source: GO_Central
  • positive regulation of translation Source: RGD
  • translational elongation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-RNO-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P2
Gene namesi
Name:Rplp2
Synonyms:Rp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi621775. Rplp2.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: RGD
  • preribosome, large subunit precursor Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001576441 – 11560S acidic ribosomal protein P2Add BLAST115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei21N6-acetyllysine; alternateBy similarity1
Modified residuei21N6-succinyllysine; alternateBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei86PhosphoserineBy similarity1
Modified residuei102PhosphoserineCombined sources1
Modified residuei105PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP02401.
PRIDEiP02401.

PTM databases

iPTMnetiP02401.
PhosphoSitePlusiP02401.

Expressioni

Gene expression databases

BgeeiENSRNOG00000002116.
GenevisibleiP02401. RN.

Interactioni

Subunit structurei

Heterodimer with RPLP1 at the lateral ribosomal stalk of the large ribosomal subunit.By similarity

Protein-protein interaction databases

BioGridi250823. 1 interactor.
IntActiP02401. 1 interactor.
MINTiMINT-4578930.
STRINGi10116.ENSRNOP00000053863.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP02401.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG091G14BD.
PhylomeDBiP02401.
TreeFamiTF320650.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch. 1 hit.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYVASYLLA ALGGNSNPSA KDIKKILDSV GIEADDERLN KVISELNGKN
60 70 80 90 100
IEDVIAQGVG KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE
110
ESEESDDDMG FGLFD
Length:115
Mass (Da):11,692
Last modified:November 1, 1991 - v2
Checksum:i503B346F9F49591B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15098 mRNA. Translation: CAA33201.1.
X55153 Genomic DNA. Translation: CAA38953.1.
BC099697 mRNA. Translation: AAH99697.1.
PIRiS22320. R6RTP2.
RefSeqiNP_001025192.1. NM_001030021.1.
XP_003749061.1. XM_003749013.2.
XP_008772967.1. XM_008774745.1.
UniGeneiRn.144648.
Rn.226833.
Rn.976.

Genome annotation databases

EnsembliENSRNOT00000038691; ENSRNOP00000038214; ENSRNOG00000002116.
ENSRNOT00000057030; ENSRNOP00000053863; ENSRNOG00000037607.
GeneIDi100911575.
140662.
KEGGirno:100911575.
rno:140662.
UCSCiRGD:621775. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15098 mRNA. Translation: CAA33201.1.
X55153 Genomic DNA. Translation: CAA38953.1.
BC099697 mRNA. Translation: AAH99697.1.
PIRiS22320. R6RTP2.
RefSeqiNP_001025192.1. NM_001030021.1.
XP_003749061.1. XM_003749013.2.
XP_008772967.1. XM_008774745.1.
UniGeneiRn.144648.
Rn.226833.
Rn.976.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250823. 1 interactor.
IntActiP02401. 1 interactor.
MINTiMINT-4578930.
STRINGi10116.ENSRNOP00000053863.

PTM databases

iPTMnetiP02401.
PhosphoSitePlusiP02401.

Proteomic databases

PaxDbiP02401.
PRIDEiP02401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000038691; ENSRNOP00000038214; ENSRNOG00000002116.
ENSRNOT00000057030; ENSRNOP00000053863; ENSRNOG00000037607.
GeneIDi100911575.
140662.
KEGGirno:100911575.
rno:140662.
UCSCiRGD:621775. rat.

Organism-specific databases

CTDi6181.
RGDi621775. Rplp2.

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP02401.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG091G14BD.
PhylomeDBiP02401.
TreeFamiTF320650.

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-RNO-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP02401.

Gene expression databases

BgeeiENSRNOG00000002116.
GenevisibleiP02401. RN.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch. 1 hit.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRLA2_RAT
AccessioniPrimary (citable) accession number: P02401
Secondary accession number(s): Q499W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. 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.