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Protein

60S ribosomal protein L5

Gene

Rpl5

Organism
Mus musculus (Mouse)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:102854. Rpl5.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleusnucleolus By similarity

GO - Cellular componenti

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_0000131433Add
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-acetyllysineCombined sources
Modified residuei272 – 2721PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP47962.
PaxDbiP47962.
PRIDEiP47962.

PTM databases

iPTMnetiP47962.
PhosphoSiteiP47962.
SwissPalmiP47962.

Expressioni

Gene expression databases

BgeeiP47962.
CleanExiMM_RPL5.
ExpressionAtlasiP47962. baseline and differential.
GenevisibleiP47962. MM.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Mdm2P238043EBI-773940,EBI-641788

Protein-protein interaction databases

BioGridi433810. 5 interactions.
IntActiP47962. 11 interactions.
MINTiMINT-1857930.
STRINGi10090.ENSMUSP00000080854.

Structurei

3D structure databases

ProteinModelPortaliP47962.
SMRiP47962. Positions 15-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

eggNOGiKOG0875. Eukaryota.
COG0256. LUCA.
HOGENOMiHOG000105947.
HOVERGENiHBG009347.
InParanoidiP47962.
KOiK02932.
OMAiVICQVVY.
OrthoDBiEOG7VB2FW.
PhylomeDBiP47962.
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.

P47962-1 [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 GQVEVNGGEY 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):34,401
Last modified:January 23, 2007 - v3
Checksum:i30D74B9E66E17C65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008489 mRNA. Translation: BAB25695.1.
AK013107 mRNA. Translation: BAB28652.1.
BC026934 mRNA. Translation: AAH26934.1.
BC083318 mRNA. Translation: AAH83318.1.
Z35311 Genomic DNA. No translation available.
X83590 mRNA. Translation: CAA58570.1.
CCDSiCCDS39199.1.
PIRiS50100.
RefSeqiNP_058676.1. NM_016980.2.
UniGeneiMm.277897.
Mm.426204.
Mm.491107.

Genome annotation databases

EnsembliENSMUST00000082223; ENSMUSP00000080854; ENSMUSG00000058558.
GeneIDi100503670.
KEGGimmu:100503670.
UCSCiuc008ynh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008489 mRNA. Translation: BAB25695.1.
AK013107 mRNA. Translation: BAB28652.1.
BC026934 mRNA. Translation: AAH26934.1.
BC083318 mRNA. Translation: AAH83318.1.
Z35311 Genomic DNA. No translation available.
X83590 mRNA. Translation: CAA58570.1.
CCDSiCCDS39199.1.
PIRiS50100.
RefSeqiNP_058676.1. NM_016980.2.
UniGeneiMm.277897.
Mm.426204.
Mm.491107.

3D structure databases

ProteinModelPortaliP47962.
SMRiP47962. Positions 15-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi433810. 5 interactions.
IntActiP47962. 11 interactions.
MINTiMINT-1857930.
STRINGi10090.ENSMUSP00000080854.

PTM databases

iPTMnetiP47962.
PhosphoSiteiP47962.
SwissPalmiP47962.

Proteomic databases

EPDiP47962.
PaxDbiP47962.
PRIDEiP47962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000082223; ENSMUSP00000080854; ENSMUSG00000058558.
GeneIDi100503670.
KEGGimmu:100503670.
UCSCiuc008ynh.2. mouse.

Organism-specific databases

CTDi6125.
MGIiMGI:102854. Rpl5.

Phylogenomic databases

eggNOGiKOG0875. Eukaryota.
COG0256. LUCA.
HOGENOMiHOG000105947.
HOVERGENiHBG009347.
InParanoidiP47962.
KOiK02932.
OMAiVICQVVY.
OrthoDBiEOG7VB2FW.
PhylomeDBiP47962.
TreeFamiTF300044.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiRpl5. mouse.
NextBioi33367520.
PROiP47962.
SOURCEiSearch...

Gene expression databases

BgeeiP47962.
CleanExiMM_RPL5.
ExpressionAtlasiP47962. baseline and differential.
GenevisibleiP47962. MM.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Small intestine.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and mammals."
    Qu L.H., Nicoloso M., Michot B., Azum M.C., Caizergues-Ferrer M., Renalier M.H., Bachellerie J.-P.
    Nucleic Acids Res. 22:4073-4081(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-179.
  4. Zach O.R.F.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 206-297.
    Strain: NMRE.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL5_MOUSE
AccessioniPrimary (citable) accession number: P47962
Secondary accession number(s): Q9CR19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 145 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.