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Protein

60S acidic ribosomal protein P2

Gene

RPLP2

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

Functioni

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

GO - Molecular functioni

  • large ribosomal subunit rRNA binding Source: GO_Central
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciZFISH:ENSG00000177600-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).
SIGNORiP05387.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P2
Alternative name(s):
Renal carcinoma antigen NY-REN-44
Gene namesi
Name:RPLP2
Synonyms:D11S2243E, RPP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10377. RPLP2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • preribosome, large subunit precursor Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi6181.
OpenTargetsiENSG00000177600.
PharmGKBiPA34776.

Protein family/group databases

Allergomei1276. Hom s P2.

Polymorphism and mutation databases

BioMutaiRPLP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001576401 – 11560S acidic ribosomal protein P2Add BLAST115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei17PhosphoserineCombined sources1
Modified residuei19PhosphoserineCombined sources1
Modified residuei21N6-acetyllysine; alternateCombined sources1
Modified residuei21N6-succinyllysine; alternateBy similarity1
Modified residuei79PhosphoserineCombined sources1
Modified residuei86PhosphoserineCombined sources1
Modified residuei102Phosphoserine1 Publication1
Modified residuei105PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP05387.
PaxDbiP05387.
PeptideAtlasiP05387.
PRIDEiP05387.
TopDownProteomicsiP05387.

2D gel databases

SWISS-2DPAGEP05387.

PTM databases

iPTMnetiP05387.
PhosphoSitePlusiP05387.
SwissPalmiP05387.

Expressioni

Gene expression databases

BgeeiENSG00000177600.
CleanExiHS_RPLP2.
ExpressionAtlasiP05387. baseline and differential.
GenevisibleiP05387. HS.

Organism-specific databases

HPAiHPA053635.

Interactioni

Subunit structurei

Heterodimer with RPLP1 at the lateral ribosomal stalk of the large ribosomal subunit.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RPLP1P053862EBI-352813,EBI-354582

Protein-protein interaction databases

BioGridi112096. 131 interactors.
IntActiP05387. 23 interactors.
MINTiMINT-4999550.
STRINGi9606.ENSP00000322419.

Structurei

Secondary structure

1115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 3Combined sources3
Helixi4 – 13Combined sources10
Helixi20 – 28Combined sources9
Turni29 – 31Combined sources3
Helixi38 – 46Combined sources9
Helixi51 – 55Combined sources5
Beta strandi59 – 61Combined sources3
Beta strandi63 – 66Combined sources4
Turni91 – 94Combined sources4
Helixi112 – 114Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S4JNMR-A103-115[»]
2JDLX-ray2.20C/D105-115[»]
2LBFNMR-B1-69[»]
2W1ONMR-A/B1-69[»]
4BEHNMR-B1-115[»]
4V6Xelectron microscopy5.00Cu/Cv1-115[»]
5DDZX-ray1.50B106-115[»]
ProteinModelPortaliP05387.
SMRiP05387.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05387.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP05387.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG091G14BD.
PhylomeDBiP05387.
TreeFamiTF320650.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P05387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN
60 70 80 90 100
IEDVIAQGIG KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE
110
ESEESDDDMG FGLFD
Length:115
Mass (Da):11,665
Last modified:November 1, 1988 - v1
Checksum:iB5ECFE2510A756BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17887 mRNA. Translation: AAA36472.1.
AB061837 Genomic DNA. Translation: BAB79475.1.
AK311954 mRNA. Translation: BAG34894.1.
CR542212 mRNA. Translation: CAG47008.1.
CR542248 mRNA. Translation: CAG47044.1.
AP006621 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02393.1.
BC005354 mRNA. Translation: AAH05354.1.
BC005920 mRNA. Translation: AAH05920.1.
BC007573 mRNA. Translation: AAH07573.1.
BC062314 mRNA. Translation: AAH62314.1.
CCDSiCCDS7717.1.
PIRiC27125. R6HUP2.
RefSeqiNP_000995.1. NM_001004.3.
UniGeneiHs.437594.

Genome annotation databases

EnsembliENST00000321153; ENSP00000322419; ENSG00000177600.
ENST00000530797; ENSP00000431240; ENSG00000177600.
GeneIDi6181.
KEGGihsa:6181.
UCSCiuc001lrq.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17887 mRNA. Translation: AAA36472.1.
AB061837 Genomic DNA. Translation: BAB79475.1.
AK311954 mRNA. Translation: BAG34894.1.
CR542212 mRNA. Translation: CAG47008.1.
CR542248 mRNA. Translation: CAG47044.1.
AP006621 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02393.1.
BC005354 mRNA. Translation: AAH05354.1.
BC005920 mRNA. Translation: AAH05920.1.
BC007573 mRNA. Translation: AAH07573.1.
BC062314 mRNA. Translation: AAH62314.1.
CCDSiCCDS7717.1.
PIRiC27125. R6HUP2.
RefSeqiNP_000995.1. NM_001004.3.
UniGeneiHs.437594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S4JNMR-A103-115[»]
2JDLX-ray2.20C/D105-115[»]
2LBFNMR-B1-69[»]
2W1ONMR-A/B1-69[»]
4BEHNMR-B1-115[»]
4V6Xelectron microscopy5.00Cu/Cv1-115[»]
5DDZX-ray1.50B106-115[»]
ProteinModelPortaliP05387.
SMRiP05387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112096. 131 interactors.
IntActiP05387. 23 interactors.
MINTiMINT-4999550.
STRINGi9606.ENSP00000322419.

Protein family/group databases

Allergomei1276. Hom s P2.

PTM databases

iPTMnetiP05387.
PhosphoSitePlusiP05387.
SwissPalmiP05387.

Polymorphism and mutation databases

BioMutaiRPLP2.

2D gel databases

SWISS-2DPAGEP05387.

Proteomic databases

EPDiP05387.
PaxDbiP05387.
PeptideAtlasiP05387.
PRIDEiP05387.
TopDownProteomicsiP05387.

Protocols and materials databases

DNASUi6181.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321153; ENSP00000322419; ENSG00000177600.
ENST00000530797; ENSP00000431240; ENSG00000177600.
GeneIDi6181.
KEGGihsa:6181.
UCSCiuc001lrq.2. human.

Organism-specific databases

CTDi6181.
DisGeNETi6181.
GeneCardsiRPLP2.
HGNCiHGNC:10377. RPLP2.
HPAiHPA053635.
MIMi180530. gene.
neXtProtiNX_P05387.
OpenTargetsiENSG00000177600.
PharmGKBiPA34776.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP05387.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG091G14BD.
PhylomeDBiP05387.
TreeFamiTF320650.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000177600-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).
SIGNORiP05387.

Miscellaneous databases

ChiTaRSiRPLP2. human.
EvolutionaryTraceiP05387.
GeneWikiiRPLP2.
GenomeRNAii6181.
PROiP05387.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000177600.
CleanExiHS_RPLP2.
ExpressionAtlasiP05387. baseline and differential.
GenevisibleiP05387. HS.

Family and domain databases

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

Entry informationi

Entry nameiRLA2_HUMAN
AccessioniPrimary (citable) accession number: P05387
Secondary accession number(s): Q6FG96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 30, 2016
This is version 187 of the entry and version 1 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.