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Protein

40S ribosomal protein S25

Gene

Rps25

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
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:
40S ribosomal protein S25
Gene namesi
Name:Rps25
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1922867. Rps25.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12512540S ribosomal protein S25PRO_0000192870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-acetyllysineCombined sources
Modified residuei52 – 521N6-acetyllysine; alternateCombined sources
Modified residuei52 – 521N6-succinyllysine; alternateCombined sources
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei66 – 661N6-acetyllysineBy similarity
Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
Modified residuei94 – 941N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP62852.
PaxDbiP62852.
PRIDEiP62852.

PTM databases

iPTMnetiP62852.
PhosphoSiteiP62852.
SwissPalmiP62852.

Expressioni

Gene expression databases

BgeeiP62852.
CleanExiMM_RPS25.
ExpressionAtlasiP62852. baseline.
GenevisibleiP62852. MM.

Interactioni

Protein-protein interaction databases

BioGridi217620. 3 interactions.
IntActiP62852. 3 interactions.
MINTiMINT-1857365.
STRINGi10090.ENSMUSP00000079180.

Structurei

3D structure databases

ProteinModelPortaliP62852.
SMRiP62852. Positions 41-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S25e family.Curated

Phylogenomic databases

eggNOGiKOG1767. Eukaryota.
COG4901. LUCA.
HOGENOMiHOG000203673.
HOVERGENiHBG054579.
InParanoidiP62852.
KOiK02975.
OMAiPTYKYVS.
OrthoDBiEOG722JC9.
PhylomeDBiP62852.
TreeFamiTF314909.

Family and domain databases

InterProiIPR004977. Ribosomal_S25.
[Graphical view]
PANTHERiPTHR12850. PTHR12850. 1 hit.
PfamiPF03297. Ribosomal_S25. 1 hit.
[Graphical view]
ProDomiPD012268. Ribosomal_S25. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P62852-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKDDKKKK DAGKSAKKDK DPVNKSGGKA KKKKWSKGKV RDKLNNLVLF
60 70 80 90 100
DKATYDKLCK EVPNYKLITP AVVSERLKIR GSLARAALQE LLSKGLIKLV
110 120
SKHRAQVIYT RNTKGGDAPA AGEDA
Length:125
Mass (Da):13,742
Last modified:August 16, 2004 - v1
Checksum:iB8E05F04FCF2F1A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012696 mRNA. Translation: BAB28417.1.
AK077450 mRNA. Translation: BAC36806.1.
BC002088 mRNA. Translation: AAH02088.1.
BC027208 mRNA. Translation: AAH27208.1.
BC079541 mRNA. Translation: AAH79541.1.
CCDSiCCDS40600.1.
RefSeqiNP_077228.1. NM_024266.3.
UniGeneiMm.292027.
Mm.391885.
Mm.427157.

Genome annotation databases

EnsembliENSMUST00000080300; ENSMUSP00000079180; ENSMUSG00000009927.
GeneIDi75617.
KEGGimmu:75617.
UCSCiuc009pdm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012696 mRNA. Translation: BAB28417.1.
AK077450 mRNA. Translation: BAC36806.1.
BC002088 mRNA. Translation: AAH02088.1.
BC027208 mRNA. Translation: AAH27208.1.
BC079541 mRNA. Translation: AAH79541.1.
CCDSiCCDS40600.1.
RefSeqiNP_077228.1. NM_024266.3.
UniGeneiMm.292027.
Mm.391885.
Mm.427157.

3D structure databases

ProteinModelPortaliP62852.
SMRiP62852. Positions 41-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217620. 3 interactions.
IntActiP62852. 3 interactions.
MINTiMINT-1857365.
STRINGi10090.ENSMUSP00000079180.

PTM databases

iPTMnetiP62852.
PhosphoSiteiP62852.
SwissPalmiP62852.

Proteomic databases

EPDiP62852.
PaxDbiP62852.
PRIDEiP62852.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080300; ENSMUSP00000079180; ENSMUSG00000009927.
GeneIDi75617.
KEGGimmu:75617.
UCSCiuc009pdm.1. mouse.

Organism-specific databases

CTDi6230.
MGIiMGI:1922867. Rps25.

Phylogenomic databases

eggNOGiKOG1767. Eukaryota.
COG4901. LUCA.
HOGENOMiHOG000203673.
HOVERGENiHBG054579.
InParanoidiP62852.
KOiK02975.
OMAiPTYKYVS.
OrthoDBiEOG722JC9.
PhylomeDBiP62852.
TreeFamiTF314909.

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-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
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

NextBioi24185.
PROiP62852.
SOURCEiSearch...

Gene expression databases

BgeeiP62852.
CleanExiMM_RPS25.
ExpressionAtlasiP62852. baseline.
GenevisibleiP62852. MM.

Family and domain databases

InterProiIPR004977. Ribosomal_S25.
[Graphical view]
PANTHERiPTHR12850. PTHR12850. 1 hit.
PfamiPF03297. Ribosomal_S25. 1 hit.
[Graphical view]
ProDomiPD012268. Ribosomal_S25. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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.
  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 and Czech II.
    Tissue: Brain and Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "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-43 AND LYS-52, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiRS25_MOUSE
AccessioniPrimary (citable) accession number: P62852
Secondary accession number(s): P25111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: March 16, 2016
This is version 104 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.