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Protein

40S ribosomal protein S23

Gene

Rps23

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

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S23
Gene namesi
Name:Rps23
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1913725. Rps23.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 14314240S ribosomal protein S23PRO_0000146458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-succinyllysine1 Publication
Modified residuei62 – 6213-hydroxyprolineBy similarity
Modified residuei135 – 1351N6-acetyllysineBy similarity

Post-translational modificationi

Hydroxylation at Pro-62 affects translation termination efficiency.By similarity

Keywords - PTMi

Acetylation, Hydroxylation

Proteomic databases

MaxQBiP62267.
PaxDbiP62267.
PRIDEiP62267.

PTM databases

PhosphoSiteiP62267.

Expressioni

Gene expression databases

BgeeiP62267.
CleanExiMM_RPS23.
ExpressionAtlasiP62267. baseline and differential.
GenevisibleiP62267. MM.

Interactioni

Protein-protein interaction databases

BioGridi211500. 3 interactions.
IntActiP62267. 5 interactions.
MINTiMINT-1857177.
STRINGi10090.ENSMUSP00000054490.

Structurei

3D structure databases

ProteinModelPortaliP62267.
SMRiP62267. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

eggNOGiCOG0048.
GeneTreeiENSGT00550000074784.
HOVERGENiHBG054200.
InParanoidiP62267.
KOiK02973.
OMAiMPGKKSP.
OrthoDBiEOG77DJ7H.
TreeFamiTF300871.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005680. Ribosomal_S23_euk/arc.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00982. uS12_E_A. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI
60 70 80 90 100
VLEKVGVEAK QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV
110 120 130 140
LVAGFGRKGH AVGDIPGVRF KVVKVANVSL LALYKGKKER PRS
Length:143
Mass (Da):15,808
Last modified:January 23, 2007 - v3
Checksum:i8417A48B8CF0A8E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002573 mRNA. Translation: BAB22198.1.
AK010594 mRNA. Translation: BAB27050.1.
AK010608 mRNA. Translation: BAB27058.1.
AK012438 mRNA. Translation: BAB28238.1.
AK013720 mRNA. Translation: BAB28969.1.
AK050580 mRNA. Translation: BAC34329.1.
AK088085 mRNA. Translation: BAC40136.1.
AK166994 mRNA. Translation: BAE39173.1.
AK168587 mRNA. Translation: BAE40456.1.
BC002145 mRNA. Translation: AAH02145.1.
BC054435 mRNA. Translation: AAH54435.1.
BC078418 mRNA. Translation: AAH78418.1.
CCDSiCCDS26674.1.
RefSeqiNP_077137.1. NM_024175.3.
UniGeneiMm.306302.

Genome annotation databases

EnsembliENSMUST00000051955; ENSMUSP00000054490; ENSMUSG00000049517.
GeneIDi66475.
KEGGimmu:66475.
UCSCiuc007rjq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002573 mRNA. Translation: BAB22198.1.
AK010594 mRNA. Translation: BAB27050.1.
AK010608 mRNA. Translation: BAB27058.1.
AK012438 mRNA. Translation: BAB28238.1.
AK013720 mRNA. Translation: BAB28969.1.
AK050580 mRNA. Translation: BAC34329.1.
AK088085 mRNA. Translation: BAC40136.1.
AK166994 mRNA. Translation: BAE39173.1.
AK168587 mRNA. Translation: BAE40456.1.
BC002145 mRNA. Translation: AAH02145.1.
BC054435 mRNA. Translation: AAH54435.1.
BC078418 mRNA. Translation: AAH78418.1.
CCDSiCCDS26674.1.
RefSeqiNP_077137.1. NM_024175.3.
UniGeneiMm.306302.

3D structure databases

ProteinModelPortaliP62267.
SMRiP62267. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211500. 3 interactions.
IntActiP62267. 5 interactions.
MINTiMINT-1857177.
STRINGi10090.ENSMUSP00000054490.

PTM databases

PhosphoSiteiP62267.

Proteomic databases

MaxQBiP62267.
PaxDbiP62267.
PRIDEiP62267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051955; ENSMUSP00000054490; ENSMUSG00000049517.
GeneIDi66475.
KEGGimmu:66475.
UCSCiuc007rjq.2. mouse.

Organism-specific databases

CTDi6228.
MGIiMGI:1913725. Rps23.

Phylogenomic databases

eggNOGiCOG0048.
GeneTreeiENSGT00550000074784.
HOVERGENiHBG054200.
InParanoidiP62267.
KOiK02973.
OMAiMPGKKSP.
OrthoDBiEOG77DJ7H.
TreeFamiTF300871.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi321794.
PROiP62267.
SOURCEiSearch...

Gene expression databases

BgeeiP62267.
CleanExiMM_RPS23.
ExpressionAtlasiP62267. baseline and differential.
GenevisibleiP62267. MM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005680. Ribosomal_S23_euk/arc.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00982. uS12_E_A. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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 and NOD.
    Tissue: Hippocampus, Kidney 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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRS23_MOUSE
AccessioniPrimary (citable) accession number: P62267
Secondary accession number(s): P39028, Q542K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 112 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

External Data

Dasty 3

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 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.