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Protein

40S ribosomal protein S10

Gene

RPS10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the 40S ribosomal subunit.

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S10
Gene namesi
Name:RPS10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10383. RPS10.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleusnucleolus 1 Publication

  • 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.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 9 (DBA9)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.

See also OMIM:613308

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581R → K: Weakly methylated. Complete loss of methylation; inefficient assembly into ribosomes; instability; increased degradation by the proteasomal pathway; decreased interaction with NPM1; absence of localization in the granular component (GC) region of the nucleolus; when associated with K-160. 1 Publication
Mutagenesisi160 – 1601R → K: Weakly methylated. Complete loss of methylation; inefficient assembly into ribosomes; instability; increased degradation by the proteasomal pathway; decreased interaction with NPM1; absence of localization in the granular component (GC) region of the nucleolus; when associated with K-158. 1 Publication

Keywords - Diseasei

Diamond-Blackfan anemia

Organism-specific databases

MIMi613308. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34779.

Polymorphism and mutation databases

BioMutaiRPS10.
DMDMi1173177.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16516540S ribosomal protein S10PRO_0000116360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphotyrosineBy similarity
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei158 – 1581Symmetric dimethylarginine1 Publication
Modified residuei160 – 1601Symmetric dimethylarginine1 Publication

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.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP46783.
PaxDbiP46783.
PRIDEiP46783.

PTM databases

PhosphoSiteiP46783.

Expressioni

Gene expression databases

BgeeiP46783.
CleanExiHS_RPS10.
ExpressionAtlasiP46783. baseline.
GenevestigatoriP46783.

Organism-specific databases

HPAiHPA047268.
HPA048084.

Interactioni

Subunit structurei

Component of the small ribosomal subunit. Interacts with PRMT5. The methylated form interacts with NPM1.1 Publication

Protein-protein interaction databases

BioGridi112118. 114 interactions.
IntActiP46783. 27 interactions.
MINTiMINT-5001020.
STRINGi9606.ENSP00000347271.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AK1-165[»]
ProteinModelPortaliP46783.
SMRiP46783. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S10e family.Curated

Phylogenomic databases

eggNOGiCOG5045.
GeneTreeiENSGT00440000034918.
HOVERGENiHBG001253.
InParanoidiP46783.
KOiK02947.
PhylomeDBiP46783.
TreeFamiTF319100.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P46783-1 [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
TGRPRPKGLE GERPARLTRG EADRDTYRRS AVPPGADKKA EAGAGSATEF
160
QFRGGFGRGR GQPPQ
Length:165
Mass (Da):18,898
Last modified:November 1, 1995 - v1
Checksum:i64106DFCD97AABA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14972 mRNA. Translation: AAA85660.1.
AK311797 mRNA. Translation: BAG34740.1.
AL157372 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03784.1.
BC001032 mRNA. Translation: AAH01032.1.
BC001955 mRNA. Translation: AAH01955.1.
BC005012 mRNA. Translation: AAH05012.1.
BC070235 mRNA. Translation: AAH70235.1.
BC071946 mRNA. Translation: AAH71946.1.
BC073799 mRNA. Translation: AAH73799.1.
AB007151 Genomic DNA. Translation: BAA25817.1.
CCDSiCCDS4792.1.
PIRiS55918.
RefSeqiNP_001005.1. NM_001014.4.
NP_001190174.1. NM_001203245.2.
NP_001191020.1. NM_001204091.1.
UniGeneiHs.406620.
Hs.645317.

Genome annotation databases

EnsembliENST00000326199; ENSP00000347271; ENSG00000124614.
ENST00000621356; ENSP00000481646; ENSG00000124614.
GeneIDi6204.
KEGGihsa:6204.
UCSCiuc003ojm.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14972 mRNA. Translation: AAA85660.1.
AK311797 mRNA. Translation: BAG34740.1.
AL157372 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03784.1.
BC001032 mRNA. Translation: AAH01032.1.
BC001955 mRNA. Translation: AAH01955.1.
BC005012 mRNA. Translation: AAH05012.1.
BC070235 mRNA. Translation: AAH70235.1.
BC071946 mRNA. Translation: AAH71946.1.
BC073799 mRNA. Translation: AAH73799.1.
AB007151 Genomic DNA. Translation: BAA25817.1.
CCDSiCCDS4792.1.
PIRiS55918.
RefSeqiNP_001005.1. NM_001014.4.
NP_001190174.1. NM_001203245.2.
NP_001191020.1. NM_001204091.1.
UniGeneiHs.406620.
Hs.645317.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AK1-165[»]
ProteinModelPortaliP46783.
SMRiP46783. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112118. 114 interactions.
IntActiP46783. 27 interactions.
MINTiMINT-5001020.
STRINGi9606.ENSP00000347271.

PTM databases

PhosphoSiteiP46783.

Polymorphism and mutation databases

BioMutaiRPS10.
DMDMi1173177.

Proteomic databases

MaxQBiP46783.
PaxDbiP46783.
PRIDEiP46783.

Protocols and materials databases

DNASUi6204.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326199; ENSP00000347271; ENSG00000124614.
ENST00000621356; ENSP00000481646; ENSG00000124614.
GeneIDi6204.
KEGGihsa:6204.
UCSCiuc003ojm.3. human.

Organism-specific databases

CTDi6204.
GeneCardsiGC06M035731.
GeneReviewsiRPS10.
H-InvDBHIX0201612.
HGNCiHGNC:10383. RPS10.
HPAiHPA047268.
HPA048084.
MIMi603632. gene.
613308. phenotype.
neXtProtiNX_P46783.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34779.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5045.
GeneTreeiENSGT00440000034918.
HOVERGENiHBG001253.
InParanoidiP46783.
KOiK02947.
PhylomeDBiP46783.
TreeFamiTF319100.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

GeneWikiiRPS10.
GenomeRNAii6204.
NextBioi24095.
PROiP46783.
SOURCEiSearch...

Gene expression databases

BgeeiP46783.
CleanExiHS_RPS10.
ExpressionAtlasiP46783. baseline.
GenevestigatoriP46783.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
    Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
    Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Lymph, Placenta and Skin.
  6. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
    Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
    Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15.
    Tissue: Placenta.
  7. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-85.
  8. "Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis."
    Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.
    J. Biol. Chem. 285:12695-12705(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, METHYLATION AT ARG-158 AND ARG-160, INTERACTION WITH PRMT5 AND NPM1, MUTAGENESIS OF ARG-158 AND ARG-160.
  9. Cited for: INVOLVEMENT IN DBA9.
  10. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRS10_HUMAN
AccessioniPrimary (citable) accession number: P46783
Secondary accession number(s): B2R4E3, Q5TZC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 27, 2015
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. 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.