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Protein

60S acidic ribosomal protein P2

Gene

Rplp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

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-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 P2
Gene namesi
Name:Rplp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1914436. Rplp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11511560S acidic ribosomal protein P2PRO_0000157641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei21 – 211N6-acetyllysine; alternateCombined sources
Modified residuei21 – 211N6-succinyllysine; alternateCombined sources
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP99027.
MaxQBiP99027.
PaxDbiP99027.
PRIDEiP99027.
TopDownProteomicsiP99027.

2D gel databases

REPRODUCTION-2DPAGEIPI00139795.
SWISS-2DPAGEP99027.

PTM databases

iPTMnetiP99027.
PhosphoSiteiP99027.

Expressioni

Gene expression databases

BgeeiP99027.
CleanExiMM_RPLP2.
GenevisibleiP99027. MM.

Interactioni

Subunit structurei

Heterodimer with RPLP1 at the lateral ribosomal stalk of the large ribosomal subunit.By similarity

Protein-protein interaction databases

BioGridi212002. 4 interactions.
IntActiP99027. 8 interactions.
MINTiMINT-4132684.
STRINGi10090.ENSMUSP00000081474.

Structurei

3D structure databases

ProteinModelPortaliP99027.
SMRiP99027. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP99027.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG7JMGHH.
PhylomeDBiP99027.
TreeFamiTF320650.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P99027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN
60 70 80 90 100
IEDVIAQGVG KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE
110
ESEESDDDMG FGLFD
Length:115
Mass (Da):11,651
Last modified:April 13, 2004 - v3
Checksum:iAAF3FE3A0FA756BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191S → N in BAB28297 (PubMed:16141072).Curated
Sequence conflicti61 – 611K → R in BAB28297 (PubMed:16141072).Curated
Sequence conflicti81 – 811A → T in BAB28297 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002419 mRNA. Translation: BAB22086.1.
AK008344 mRNA. Translation: BAB25616.1.
AK010618 mRNA. Translation: BAB27066.1.
AK012402 mRNA. Translation: BAB28217.1.
AK012526 mRNA. Translation: BAB28297.1.
AK028140 mRNA. Translation: BAC25768.1.
AK028149 mRNA. Translation: BAC25777.1.
AK088737 mRNA. Translation: BAC40539.1.
AK134206 mRNA. Translation: BAE22051.1.
AK166774 mRNA. Translation: BAE39010.1.
BC012413 mRNA. Translation: AAH12413.1.
CCDSiCCDS40187.1.
RefSeqiNP_080296.3. NM_026020.6.
XP_006536292.1. XM_006536229.1.
UniGeneiMm.380435.

Genome annotation databases

EnsembliENSMUST00000084434; ENSMUSP00000081474; ENSMUSG00000025508.
ENSMUST00000106003; ENSMUSP00000101625; ENSMUSG00000025508.
ENSMUST00000106004; ENSMUSP00000101626; ENSMUSG00000025508.
GeneIDi67186.
KEGGimmu:67186.
UCSCiuc009klf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002419 mRNA. Translation: BAB22086.1.
AK008344 mRNA. Translation: BAB25616.1.
AK010618 mRNA. Translation: BAB27066.1.
AK012402 mRNA. Translation: BAB28217.1.
AK012526 mRNA. Translation: BAB28297.1.
AK028140 mRNA. Translation: BAC25768.1.
AK028149 mRNA. Translation: BAC25777.1.
AK088737 mRNA. Translation: BAC40539.1.
AK134206 mRNA. Translation: BAE22051.1.
AK166774 mRNA. Translation: BAE39010.1.
BC012413 mRNA. Translation: AAH12413.1.
CCDSiCCDS40187.1.
RefSeqiNP_080296.3. NM_026020.6.
XP_006536292.1. XM_006536229.1.
UniGeneiMm.380435.

3D structure databases

ProteinModelPortaliP99027.
SMRiP99027. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212002. 4 interactions.
IntActiP99027. 8 interactions.
MINTiMINT-4132684.
STRINGi10090.ENSMUSP00000081474.

PTM databases

iPTMnetiP99027.
PhosphoSiteiP99027.

2D gel databases

REPRODUCTION-2DPAGEIPI00139795.
SWISS-2DPAGEP99027.

Proteomic databases

EPDiP99027.
MaxQBiP99027.
PaxDbiP99027.
PRIDEiP99027.
TopDownProteomicsiP99027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084434; ENSMUSP00000081474; ENSMUSG00000025508.
ENSMUST00000106003; ENSMUSP00000101625; ENSMUSG00000025508.
ENSMUST00000106004; ENSMUSP00000101626; ENSMUSG00000025508.
GeneIDi67186.
KEGGimmu:67186.
UCSCiuc009klf.1. mouse.

Organism-specific databases

CTDi6181.
MGIiMGI:1914436. Rplp2.

Phylogenomic databases

eggNOGiKOG3449. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074828.
HOGENOMiHOG000229897.
HOVERGENiHBG014761.
InParanoidiP99027.
KOiK02943.
OMAiVISELHG.
OrthoDBiEOG7JMGHH.
PhylomeDBiP99027.
TreeFamiTF320650.

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

NextBioi323828.
PROiP99027.
SOURCEiSearch...

Gene expression databases

BgeeiP99027.
CleanExiMM_RPLP2.
GenevisibleiP99027. MM.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]
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, Head and Thymus.
  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].
  3. Cited for: PROTEIN SEQUENCE OF 1-10.
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-102 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-86; SER-102 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "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-21, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiRLA2_MOUSE
AccessioniPrimary (citable) accession number: P99027
Secondary accession number(s): Q3TKY3, Q9CQ99, Q9CZJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 13, 2004
Last modified: May 11, 2016
This is version 121 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.