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Protein

60S ribosomal protein L23

Gene

Rpl23

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

Functioni

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 ribosomal protein L23
Gene namesi
Name:Rpl23
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1929455. Rpl23.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14014060S ribosomal protein L23PRO_0000128613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei38 – 381PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP62830.
MaxQBiP62830.
PaxDbiP62830.
PRIDEiP62830.

PTM databases

iPTMnetiP62830.

Expressioni

Gene expression databases

BgeeiP62830.
CleanExiMM_RPL23.
ExpressionAtlasiP62830. baseline and differential.
GenevisibleiP62830. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Mdm2P238042EBI-2365752,EBI-641788

Protein-protein interaction databases

BioGridi211121. 6 interactions.
3404800. 1 interaction.
787698. 1 interaction.
IntActiP62830. 13 interactions.
MINTiMINT-1855107.
STRINGi10090.ENSMUSP00000099435.

Structurei

3D structure databases

ProteinModelPortaliP62830.
SMRiP62830. Positions 9-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
HOVERGENiHBG000282.
InParanoidiP62830.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP62830.
TreeFamiTF300913.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRGRGGSS GAKFRISLGL PVGAVINCAD NTGAKNLYII SVKGIKGRLN
60 70 80 90 100
RLPAAGVGDM VMATVKKGKP ELRKKVHPAV VIRQRKSYRR KDGVFLYFED
110 120 130 140
NAGVIVNNKG EMKGSAITGP VAKECADLWP RIASNAGSIA
Length:140
Mass (Da):14,865
Last modified:August 16, 2004 - v1
Checksum:i807E14139B2EB0B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531P → S in BAB22203 (PubMed:16141072).Curated
Sequence conflicti112 – 1121M → I in BAB28415 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF158022 Genomic DNA. Translation: AAD42413.1.
AF287271 mRNA. Translation: AAF88071.1.
AK002579 mRNA. Translation: BAB22203.1.
AK010680 mRNA. Translation: BAB27112.1.
AK012694 mRNA. Translation: BAB28415.1.
AK018730 mRNA. Translation: BAB31373.1.
AK150671 mRNA. Translation: BAE29753.1.
AK168133 mRNA. Translation: BAE40102.1.
BC025918 mRNA. Translation: AAH25918.1.
BC081448 mRNA. Translation: AAH81448.1.
CCDSiCCDS25331.1.
RefSeqiNP_075029.1. NM_022891.3.
XP_003688806.1. XM_003688758.3.
XP_003689266.1. XM_003689218.3.
UniGeneiMm.140380.

Genome annotation databases

EnsembliENSMUST00000103146; ENSMUSP00000099435; ENSMUSG00000071415.
GeneIDi100044627.
100862455.
65019.
KEGGimmu:100044627.
mmu:100862455.
mmu:65019.
UCSCiuc007leu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF158022 Genomic DNA. Translation: AAD42413.1.
AF287271 mRNA. Translation: AAF88071.1.
AK002579 mRNA. Translation: BAB22203.1.
AK010680 mRNA. Translation: BAB27112.1.
AK012694 mRNA. Translation: BAB28415.1.
AK018730 mRNA. Translation: BAB31373.1.
AK150671 mRNA. Translation: BAE29753.1.
AK168133 mRNA. Translation: BAE40102.1.
BC025918 mRNA. Translation: AAH25918.1.
BC081448 mRNA. Translation: AAH81448.1.
CCDSiCCDS25331.1.
RefSeqiNP_075029.1. NM_022891.3.
XP_003688806.1. XM_003688758.3.
XP_003689266.1. XM_003689218.3.
UniGeneiMm.140380.

3D structure databases

ProteinModelPortaliP62830.
SMRiP62830. Positions 9-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211121. 6 interactions.
3404800. 1 interaction.
787698. 1 interaction.
IntActiP62830. 13 interactions.
MINTiMINT-1855107.
STRINGi10090.ENSMUSP00000099435.

PTM databases

iPTMnetiP62830.

Proteomic databases

EPDiP62830.
MaxQBiP62830.
PaxDbiP62830.
PRIDEiP62830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103146; ENSMUSP00000099435; ENSMUSG00000071415.
GeneIDi100044627.
100862455.
65019.
KEGGimmu:100044627.
mmu:100862455.
mmu:65019.
UCSCiuc007leu.2. mouse.

Organism-specific databases

CTDi9349.
MGIiMGI:1929455. Rpl23.

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
HOVERGENiHBG000282.
InParanoidiP62830.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP62830.
TreeFamiTF300913.

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

ChiTaRSiRpl23. mouse.
NextBioi320251.
PROiP62830.
SOURCEiSearch...

Gene expression databases

BgeeiP62830.
CleanExiMM_RPL23.
ExpressionAtlasiP62830. baseline and differential.
GenevisibleiP62830. MM.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization and chromosome location of the murine Rpl23 gene."
    Kleiter N., Artner I., Copeland N.G., Gilbert D.J., Jenkins N.A., Kratochwil K.
    Cytogenet. Cell Genet. 90:227-230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ and FVB.
  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: Bone marrow and Kidney.
  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].
    Strain: C57BL/6J.
    Tissue: Brain and Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRL23_MOUSE
AccessioniPrimary (citable) accession number: P62830
Secondary accession number(s): P23131
, P24048, Q29246, Q3THU4, Q9CZE6, Q9DCQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 11, 2016
This is version 107 of the entry and version 1 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.