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P46783 (RS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S10
Gene names
Name:RPS10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the 40S ribosomal subunit.

Subunit structure

Component of the small ribosomal subunit. Interacts with PRMT5. The methylated form interacts with NPM1. Ref.8

Subcellular location

Cytoplasm. Nucleusnucleolus. 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. Ref.8

Post-translational modification

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. Ref.8

Involvement in disease

Diamond-Blackfan anemia 9 (DBA9) [MIM:613308]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the ribosomal protein S10e family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DiseaseDiamond-Blackfan anemia
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Inferred by curator PubMed 15883184Ref.6. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.8. Source: UniProtKB

ribosome

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16516540S ribosomal protein S10
PRO_0000116360

Amino acid modifications

Modified residue121Phosphotyrosine By similarity
Modified residue1461Phosphoserine By similarity
Modified residue1581Symmetric dimethylarginine Ref.8
Modified residue1601Symmetric dimethylarginine Ref.8

Experimental info

Mutagenesis1581R → 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. Ref.8
Mutagenesis1601R → 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. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P46783 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 64106DFCD97AABA3

FASTA16518,898
        10         20         30         40         50         60 
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE 

        70         80         90        100        110        120 
QFAWRHFYWY LTNEGIQYLR DYLHLPPEIV PATLRRSRPE TGRPRPKGLE GERPARLTRG 

       130        140        150        160 
EADRDTYRRS AVPPGADKKA EAGAGSATEF QFRGGFGRGR GQPPQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Ribosomal protein genes RPS10 and RPS26 are commonly mutated in Diamond-Blackfan anemia."
Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F., Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E., Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.
Am. J. Hum. Genet. 86:222-228(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DBA9.
[10]Erratum
Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F., Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E., Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.
Am. J. Hum. Genet. 86:655-655(2010)
[11]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS55918.
RefSeqNP_001005.1. NM_001014.4.
NP_001190174.1. NM_001203245.2.
NP_001191020.1. NM_001204091.1.
UniGeneHs.406620.
Hs.645317.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00K1-165[»]
ProteinModelPortalP46783.
SMRP46783. Positions 1-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112118. 112 interactions.
IntActP46783. 27 interactions.
MINTMINT-5001020.
STRING9606.ENSP00000347271.

PTM databases

PhosphoSiteP46783.

Polymorphism databases

DMDM1173177.

Proteomic databases

PaxDbP46783.
PRIDEP46783.

Protocols and materials databases

DNASU6204.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326199; ENSP00000347271; ENSG00000124614.
GeneID6204.
KEGGhsa:6204.
UCSCuc003ojm.3. human.

Organism-specific databases

CTD6204.
GeneCardsGC06M035236.
H-InvDBHIX0201612.
HGNCHGNC:10383. RPS10.
HPAHPA047268.
HPA048084.
MIM603632. gene.
613308. phenotype.
neXtProtNX_P46783.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34779.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5045.
HOVERGENHBG001253.
KOK02947.
PhylomeDBP46783.
TreeFamTF319100.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP46783.
CleanExHS_RPS10.
GenevestigatorP46783.

Family and domain databases

InterProIPR005326. S10_plectin_N.
[Graphical view]
PfamPF03501. S10_plectin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPS10.
GenomeRNAi6204.
NextBio24095.
PROP46783.
SOURCESearch...

Entry information

Entry nameRS10_HUMAN
AccessionPrimary (citable) accession number: P46783
Secondary accession number(s): B2R4E3, Q5TZC0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM