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Protein

60S ribosomal protein L5

Gene

Rpl5

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

Functioni

Required for rRNA maturation and formation of the 60S ribosomal subunits (By similarity). This protein binds 5S RNA.By similarity

GO - Molecular functioni

  • 5S rRNA binding Source: RGD
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

  • cellular response to inorganic substance Source: RGD
  • positive regulation of phosphatase activity Source: RGD
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

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-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 ribosomal protein L5
Gene namesi
Name:Rpl5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi619825. Rpl5.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleusnucleolus By similarity

GO - Cellular componenti

  • aminoacyl-tRNA synthetase multienzyme complex Source: RGD
  • cytoplasm Source: UniProtKB
  • cytosolic large ribosomal subunit Source: RGD
  • cytosolic ribosome Source: RGD
  • intracellular ribonucleoprotein complex Source: RGD
  • nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 29729660S ribosomal protein L5PRO_0000131436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei48 – 481N6-acetyllysineBy similarity
Modified residuei220 – 2201N6-acetyllysineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP09895.
PRIDEiP09895.

PTM databases

iPTMnetiP09895.
SwissPalmiP09895.

Expressioni

Gene expression databases

GenevisibleiP09895. RN.

Interactioni

Subunit structurei

Interacts with NVL in an ATP-dependent manner.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppp1cbP621422EBI-916235,EBI-352326

Protein-protein interaction databases

IntActiP09895. 2 interactions.
MINTiMINT-4563789.
STRINGi10116.ENSRNOP00000036514.

Structurei

3D structure databases

ProteinModelPortaliP09895.
SMRiP09895. Positions 11-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

eggNOGiKOG0875. Eukaryota.
COG0256. LUCA.
GeneTreeiENSGT00390000008456.
HOGENOMiHOG000105947.
HOVERGENiHBG009347.
InParanoidiP09895.
KOiK02932.
OMAiVICQVVY.
OrthoDBiEOG7VB2FW.
PhylomeDBiP09895.
TreeFamiTF300044.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A.
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.

P09895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFVKVVKNK AYFKRYQVRF RRRREGKTDY YARKRLVIQD KNKYNTPKYR
60 70 80 90 100
MIVRVTNRDI ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC
110 120 130 140 150
TGLLLARRLL NRFGMDKIYE GQVEVNGDEY NVESIDGQPG AFTCYLDAGL
160 170 180 190 200
ARTTTGNKVF GALKGAVDGG LSIPHSTKRF PGYDSESKEF NAEVHRKHIM
210 220 230 240 250
GQNVADYMRY LMEEDEDAYK KQFSQYIKNN VTPDMMEEMY KKAHAAIREN
260 270 280 290
PVYEKKPKRE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES
Length:297
Mass (Da):34,459
Last modified:January 23, 2007 - v3
Checksum:iABBB47AF1EBE4366
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361Missing in AAA42074 (PubMed:3624282).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17419 mRNA. Translation: AAA42074.1.
X06148 mRNA. Translation: CAA29506.1.
BC060561 mRNA. Translation: AAH60561.1.
PIRiS00111. R5RTL5.
RefSeqiNP_112361.1. NM_031099.1.
XP_006250647.1. XM_006250585.2.
UniGeneiRn.92980.

Genome annotation databases

EnsembliENSRNOT00000030428; ENSRNOP00000036514; ENSRNOG00000023529.
GeneIDi81763.
KEGGirno:81763.
UCSCiRGD:619825. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17419 mRNA. Translation: AAA42074.1.
X06148 mRNA. Translation: CAA29506.1.
BC060561 mRNA. Translation: AAH60561.1.
PIRiS00111. R5RTL5.
RefSeqiNP_112361.1. NM_031099.1.
XP_006250647.1. XM_006250585.2.
UniGeneiRn.92980.

3D structure databases

ProteinModelPortaliP09895.
SMRiP09895. Positions 11-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09895. 2 interactions.
MINTiMINT-4563789.
STRINGi10116.ENSRNOP00000036514.

PTM databases

iPTMnetiP09895.
SwissPalmiP09895.

Proteomic databases

PaxDbiP09895.
PRIDEiP09895.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000030428; ENSRNOP00000036514; ENSRNOG00000023529.
GeneIDi81763.
KEGGirno:81763.
UCSCiRGD:619825. rat.

Organism-specific databases

CTDi6125.
RGDi619825. Rpl5.

Phylogenomic databases

eggNOGiKOG0875. Eukaryota.
COG0256. LUCA.
GeneTreeiENSGT00390000008456.
HOGENOMiHOG000105947.
HOVERGENiHBG009347.
InParanoidiP09895.
KOiK02932.
OMAiVICQVVY.
OrthoDBiEOG7VB2FW.
PhylomeDBiP09895.
TreeFamiTF300044.

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-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

NextBioi615554.
PROiP09895.

Gene expression databases

GenevisibleiP09895. RN.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA."
    Chan Y.-L., Lin A., McNally J., Wool I.G.
    J. Biol. Chem. 262:12879-12886(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Molecular cloning and nucleotide sequence of cDNA specific for rat ribosomal protein L5."
    Tamura S., Kuwano Y., Nakayama T., Tanaka S., Tanaka T., Ogata K.
    Eur. J. Biochem. 168:83-87(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  4. "Distinct domains in ribosomal protein L5 mediate 5 S rRNA binding and nucleolar localization."
    Michael W.M., Dreyfuss G.
    J. Biol. Chem. 271:11571-11574(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.

Entry informationi

Entry nameiRL5_RAT
AccessioniPrimary (citable) accession number: P09895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 125 of the entry and version 3 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.