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Protein

60S acidic ribosomal protein P2

Gene

RpLP2

Organism
Drosophila melanogaster (Fruit fly)
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

  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • cytoplasmic translation Source: FlyBase
  • translational elongation Source: InterPro

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P2
Alternative name(s):
Acidic ribosomal protein RPA1
Gene namesi
Name:RpLP2
Synonyms:rpA1, RpP1
ORF Names:CG4918
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003274. RpLP2.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: FlyBase
  • cytosolic ribosome Source: FlyBase
  • ribosome Source: FlyBase

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001576521 – 11360S acidic ribosomal protein P2Add BLAST113

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei100Phosphoserine1 Publication1
Modified residuei102Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05389.
PRIDEiP05389.

PTM databases

iPTMnetiP05389.

Expressioni

Gene expression databases

BgeeiFBgn0003274.
GenevisibleiP05389. DM.

Interactioni

Subunit structurei

P1 and P2 exist as dimers at the large ribosomal subunit.

Protein-protein interaction databases

BioGridi62568. 16 interactors.
DIPiDIP-19859N.
IntActiP05389. 5 interactors.
MINTiMINT-784895.
STRINGi7227.FBpp0089424.

Structurei

3D structure databases

ProteinModelPortaliP05389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
InParanoidiP05389.
KOiK02943.
OMAiAFFNFTM.
OrthoDBiEOG091G14BD.
PhylomeDBiP05389.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch. 1 hit.
InterProiView protein in InterPro
IPR027534. Ribosomal_L12.

Sequencei

Sequence statusi: Complete.

P05389-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYVAAYLLA VLGGKDSPAN SDLEKILSSV GVEVDAERLT KVIKELAGKS
60 70 80 90 100
IDDLIKEGRE KLSSMPVGGG GAVAAADAAP AAAAGGDKKE AKKEEKKEES
110
ESEDDDMGFA LFE
Length:113
Mass (Da):11,757
Last modified:November 1, 1988 - v1
Checksum:iDDA5F5A4219BD65A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21S → G in CAA29026 (PubMed:3103101).Curated1
Sequence conflicti21S → G in AAM51113 (PubMed:12537569).Curated1
Sequence conflicti76A → V in AAM51113 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05016 Genomic DNA. Translation: CAA28672.1.
X05466 mRNA. Translation: CAA29026.1.
AE013599 Genomic DNA. Translation: AAF57979.1.
AY119253 mRNA. Translation: AAM51113.1.
PIRiA26401. R6FFP2.
RefSeqiNP_523764.1. NM_079040.4.

Genome annotation databases

EnsemblMetazoaiFBtr0087105; FBpp0086252; FBgn0003274.
GeneIDi36855.
KEGGidme:Dmel_CG4918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05016 Genomic DNA. Translation: CAA28672.1.
X05466 mRNA. Translation: CAA29026.1.
AE013599 Genomic DNA. Translation: AAF57979.1.
AY119253 mRNA. Translation: AAM51113.1.
PIRiA26401. R6FFP2.
RefSeqiNP_523764.1. NM_079040.4.

3D structure databases

ProteinModelPortaliP05389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62568. 16 interactors.
DIPiDIP-19859N.
IntActiP05389. 5 interactors.
MINTiMINT-784895.
STRINGi7227.FBpp0089424.

PTM databases

iPTMnetiP05389.

Proteomic databases

PaxDbiP05389.
PRIDEiP05389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087105; FBpp0086252; FBgn0003274.
GeneIDi36855.
KEGGidme:Dmel_CG4918.

Organism-specific databases

CTDi6181.
FlyBaseiFBgn0003274. RpLP2.

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
InParanoidiP05389.
KOiK02943.
OMAiAFFNFTM.
OrthoDBiEOG091G14BD.
PhylomeDBiP05389.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiRpLP2. fly.
GenomeRNAii36855.
PROiPR:P05389.

Gene expression databases

BgeeiFBgn0003274.
GenevisibleiP05389. DM.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch. 1 hit.
InterProiView protein in InterPro
IPR027534. Ribosomal_L12.
ProtoNetiSearch...

Entry informationi

Entry nameiRLA2_DROME
AccessioniPrimary (citable) accession number: P05389
Secondary accession number(s): A4UZK7, Q8MRV1, Q9V7R6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 7, 2017
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.