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Protein

40S ribosomal protein S10

Gene

Rps10

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

Functioni

Component of the 40S ribosomal subunit.By similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. structural constituent of ribosome Source: Ensembl

GO - Biological processi

  1. ribosomal small subunit assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_253640. Peptide chain elongation.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S10
Gene namesi
Name:Rps10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1914347. Rps10.

Subcellular locationi

Cytoplasm By similarity. Nucleusnucleolus By similarity
Note: Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosolic small ribosomal subunit Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. focal adhesion Source: MGI
  5. membrane Source: MGI
  6. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16516540S ribosomal protein S10PRO_0000116361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphotyrosine1 Publication
Modified residuei146 – 1461Phosphoserine1 Publication
Modified residuei158 – 1581Symmetric dimethylarginineBy similarity
Modified residuei160 – 1601Symmetric dimethylarginineBy similarity

Post-translational modificationi

Methylated by PRMT5. Methylation is necessary for its interaction with NPS1, its localization in the granular component (GC) region of the nucleolus, for the proper assembly of ribosomes, protein synthesis and optimal cell proliferation (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP63325.
PaxDbiP63325.
PRIDEiP63325.

PTM databases

PhosphoSiteiP63325.

Expressioni

Gene expression databases

BgeeiP63325.
CleanExiMM_RPS10.
ExpressionAtlasiP63325. baseline and differential.
GenevestigatoriP63325.

Interactioni

Subunit structurei

Component of the small ribosomal subunit. Interacts with PRMT5. The methylated form interacts with NPM1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211937. 3 interactions.
IntActiP63325. 3 interactions.
MINTiMINT-1857301.

Structurei

3D structure databases

ProteinModelPortaliP63325.
SMRiP63325. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S10e family.Curated

Phylogenomic databases

eggNOGiCOG5045.
HOGENOMiHOG000216624.
HOVERGENiHBG001253.
InParanoidiP63325.
KOiK02947.
OMAiVDKNVPN.
OrthoDBiEOG7VB2H1.
PhylomeDBiP63325.
TreeFamiTF319100.

Family and domain databases

InterProiIPR005326. S10_plectin_N.
[Graphical view]
PfamiPF03501. S10_plectin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ
60 70 80 90 100
SLKSRGYVKE QFAWRHFYWY LTNEGIQYLR DYLHLPPEIV PATLRRSRPE
110 120 130 140 150
TGRPRPKGPE GERPARFTRG EADRDTYRRS AVPPGADKKA EAGAGSATEF
160
QFRGGFGRGR GQPPQ
Length:165
Mass (Da):18,916
Last modified:October 11, 2004 - v1
Checksum:i75B7005BA57AABA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008797 mRNA. Translation: BAB25901.1.
AK011065 mRNA. Translation: BAB27372.1.
AK002558 mRNA. No translation available.
BC003853 mRNA. Translation: AAH03853.1.
BC019725 mRNA. Translation: AAH19725.1.
CCDSiCCDS37522.1.
PIRiH59404.
RefSeqiNP_080239.1. NM_025963.3.
UniGeneiMm.275810.
Mm.383217.

Genome annotation databases

EnsembliENSMUST00000114881; ENSMUSP00000110531; ENSMUSG00000052146.
ENSMUST00000114882; ENSMUSP00000110532; ENSMUSG00000052146.
ENSMUST00000178774; ENSMUSP00000136042; ENSMUSG00000052146.
GeneIDi67097.
KEGGimmu:67097.
UCSCiuc008bph.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008797 mRNA. Translation: BAB25901.1.
AK011065 mRNA. Translation: BAB27372.1.
AK002558 mRNA. No translation available.
BC003853 mRNA. Translation: AAH03853.1.
BC019725 mRNA. Translation: AAH19725.1.
CCDSiCCDS37522.1.
PIRiH59404.
RefSeqiNP_080239.1. NM_025963.3.
UniGeneiMm.275810.
Mm.383217.

3D structure databases

ProteinModelPortaliP63325.
SMRiP63325. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211937. 3 interactions.
IntActiP63325. 3 interactions.
MINTiMINT-1857301.

PTM databases

PhosphoSiteiP63325.

Proteomic databases

MaxQBiP63325.
PaxDbiP63325.
PRIDEiP63325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114881; ENSMUSP00000110531; ENSMUSG00000052146.
ENSMUST00000114882; ENSMUSP00000110532; ENSMUSG00000052146.
ENSMUST00000178774; ENSMUSP00000136042; ENSMUSG00000052146.
GeneIDi67097.
KEGGimmu:67097.
UCSCiuc008bph.1. mouse.

Organism-specific databases

CTDi6204.
MGIiMGI:1914347. Rps10.

Phylogenomic databases

eggNOGiCOG5045.
HOGENOMiHOG000216624.
HOVERGENiHBG001253.
InParanoidiP63325.
KOiK02947.
OMAiVDKNVPN.
OrthoDBiEOG7VB2H1.
PhylomeDBiP63325.
TreeFamiTF319100.

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_253640. Peptide chain elongation.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

NextBioi323566.
PROiP63325.
SOURCEiSearch...

Gene expression databases

BgeeiP63325.
CleanExiMM_RPS10.
ExpressionAtlasiP63325. baseline and differential.
GenevestigatoriP63325.

Family and domain databases

InterProiIPR005326. S10_plectin_N.
[Graphical view]
PfamiPF03501. S10_plectin. 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.
    Tissue: Kidney, Liver and Stomach.
  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 gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRS10_MOUSE
AccessioniPrimary (citable) accession number: P63325
Secondary accession number(s): P09900, Q9DCR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 4, 2015
This is version 96 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

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.