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Protein

60S acidic ribosomal protein P0

Gene

Rplp0

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

GO - Molecular functioni

GO - Biological processi

  • cellular response to interleukin-4 Source: MGI
  • cytoplasmic translation Source: GO_Central
  • ribosome biogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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-6791226. Major pathway of rRNA processing in the nucleolus.
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 acidic ribosomal protein P0
Alternative name(s):
60S ribosomal protein L10E
Gene namesi
Name:Rplp0
Synonyms:Arbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1927636. Rplp0.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31731760S acidic ribosomal protein P0PRO_0000154759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591PhosphothreonineBy similarity
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei304 – 3041PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP14869.
PaxDbiP14869.
PeptideAtlasiP14869.
PRIDEiP14869.

PTM databases

iPTMnetiP14869.
PhosphoSiteiP14869.
SwissPalmiP14869.

Expressioni

Gene expression databases

BgeeiP14869.
CleanExiMM_RPLP0.
ExpressionAtlasiP14869. baseline and differential.
GenevisibleiP14869. MM.

Interactioni

Subunit structurei

P0 forms a pentameric complex by interaction with dimers of P1 and P2. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with APEX1. Interacts with FMR1.By similarity

Protein-protein interaction databases

BioGridi198181. 5 interactions.
IntActiP14869. 10 interactions.
MINTiMINT-1862816.
STRINGi10090.ENSMUSP00000083705.

Structurei

3D structure databases

ProteinModelPortaliP14869.
SMRiP14869. Positions 7-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

eggNOGiKOG0815. Eukaryota.
COG0244. LUCA.
HOGENOMiHOG000210987.
HOVERGENiHBG000711.
InParanoidiP14869.
KOiK02941.
OMAiIGTNDNP.
OrthoDBiEOG71K63M.
PhylomeDBiP14869.
TreeFamiTF300849.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.

Sequencei

Sequence statusi: Complete.

P14869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK
60 70 80 90 100
AVVLMGKNTM MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD
110 120 130 140 150
MLLANKVPAA ARAGAIAPCE VTVPAQNTGL GPEKTSFFQA LGITTKISRG
160 170 180 190 200
TIEILSDVQL IKTGDKVGAS EATLLNMLNI SPFSFGLIIQ QVFDNGSIYN
210 220 230 240 250
PEVLDITEQA LHSRFLEGVR NVASVCLQIG YPTVASVPHS IINGYKRVLA
260 270 280 290 300
LSVETEYTFP LTEKVKAFLA DPSAFAAAAP AAAATTAAPA AAAAPAKAEA
310
KEESEESDED MGFGLFD
Length:317
Mass (Da):34,216
Last modified:April 13, 2004 - v3
Checksum:i7985E1D7B235EAD0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621T → A in AAH03833 (PubMed:15489334).Curated
Sequence conflicti262 – 2621T → A in AAH11106 (PubMed:15489334).Curated
Sequence conflicti262 – 2621T → A in AAH11291 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15267 mRNA. Translation: CAA33338.1.
AK010267 mRNA. Translation: BAB26807.1.
AK012606 mRNA. Translation: BAB28352.1.
AK029816 mRNA. Translation: BAC26631.1.
AK081678 mRNA. Translation: BAC38288.1.
BC003833 mRNA. Translation: AAH03833.1.
BC011106 mRNA. Translation: AAH11106.1.
BC011291 mRNA. Translation: AAH11291.1.
CCDSiCCDS19594.1.
PIRiS05305. R5MS10.
RefSeqiNP_031501.1. NM_007475.5.
UniGeneiMm.371545.
Mm.5286.

Genome annotation databases

EnsembliENSMUST00000086519; ENSMUSP00000083705; ENSMUSG00000067274.
GeneIDi11837.
KEGGimmu:11837.
UCSCiuc008zed.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15267 mRNA. Translation: CAA33338.1.
AK010267 mRNA. Translation: BAB26807.1.
AK012606 mRNA. Translation: BAB28352.1.
AK029816 mRNA. Translation: BAC26631.1.
AK081678 mRNA. Translation: BAC38288.1.
BC003833 mRNA. Translation: AAH03833.1.
BC011106 mRNA. Translation: AAH11106.1.
BC011291 mRNA. Translation: AAH11291.1.
CCDSiCCDS19594.1.
PIRiS05305. R5MS10.
RefSeqiNP_031501.1. NM_007475.5.
UniGeneiMm.371545.
Mm.5286.

3D structure databases

ProteinModelPortaliP14869.
SMRiP14869. Positions 7-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198181. 5 interactions.
IntActiP14869. 10 interactions.
MINTiMINT-1862816.
STRINGi10090.ENSMUSP00000083705.

PTM databases

iPTMnetiP14869.
PhosphoSiteiP14869.
SwissPalmiP14869.

Proteomic databases

EPDiP14869.
PaxDbiP14869.
PeptideAtlasiP14869.
PRIDEiP14869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086519; ENSMUSP00000083705; ENSMUSG00000067274.
GeneIDi11837.
KEGGimmu:11837.
UCSCiuc008zed.2. mouse.

Organism-specific databases

CTDi6175.
MGIiMGI:1927636. Rplp0.

Phylogenomic databases

eggNOGiKOG0815. Eukaryota.
COG0244. LUCA.
HOGENOMiHOG000210987.
HOVERGENiHBG000711.
InParanoidiP14869.
KOiK02941.
OMAiIGTNDNP.
OrthoDBiEOG71K63M.
PhylomeDBiP14869.
TreeFamiTF300849.

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-6791226. Major pathway of rRNA processing in the nucleolus.
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

PROiP14869.
SOURCEiSearch...

Gene expression databases

BgeeiP14869.
CleanExiMM_RPLP0.
ExpressionAtlasiP14869. baseline and differential.
GenevisibleiP14869. MM.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse homologue of the human acidic ribosomal phosphoprotein PO: a highly conserved polypeptide that is under translational control."
    Krowczynska A.M., Coutts M., Makrides S., Brawerman G.
    Nucleic Acids Res. 17:6408-6408(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Head and Testis.
  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].
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 135-146 AND 150-162.
    Tissue: Brain.

Entry informationi

Entry nameiRLA0_MOUSE
AccessioniPrimary (citable) accession number: P14869
Secondary accession number(s): Q99L54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 13, 2004
Last modified: July 6, 2016
This is version 147 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. 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.