P46783 (RS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S10

Gene names

Name:

RPS10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
Subcellular location	Cytoplasm. Nucleus › nucleolus. Note: Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Co-localizes with NPS1 in the GC region of the nucleolus. Ref.10
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.10
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.11
Sequence similarities	Belongs to the ribosomal protein S10e family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Disease	Diamond-Blackfan anemia
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB nucleolus Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 165	165	40S ribosomal protein S10		PRO_0000116360
Amino acid modifications
	Modified residue	12	1	Phosphotyrosine Ref.8
	Modified residue	146	1	Phosphoserine By similarity
	Modified residue	158	1	Symmetric dimethylarginine Ref.10
	Modified residue	160	1	Symmetric dimethylarginine Ref.10
Experimental info
	Mutagenesis	158	1	R → 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.10
	Mutagenesis	160	1	R → 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.10

Sequences

	Sequence		Length	Mass (Da)
	P46783 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 64106DFCD97AABA3	FASTA	165	18,898
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, MASS SPECTROMETRY.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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.
[11]	"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.
[12]	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)
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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.
IPI	IPI00008438.
PIR	S55918.
RefSeq	NP_001005.1. NM_001014.4. NP_001190174.1. NM_001203245.2. NP_001191020.1. NM_001204091.1.
UniGene	Hs.406620. Hs.645317.
3D structure databases
ProteinModelPortal	P46783.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46783. 18 interactions.
MINT	MINT-5001020.
STRING	9606.ENSP00000347271.
PTM databases
PhosphoSite	P46783.
Polymorphism databases
DMDM	1173177.
Proteomic databases
PaxDb	P46783.
PRIDE	P46783.
Protocols and materials databases
DNASU	6204.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326199; ENSP00000347271; ENSG00000124614.
GeneID	6204.
KEGG	hsa:6204.
UCSC	uc003ojm.3. human.
Organism-specific databases
CTD	6204.
GeneCards	GC06M034514.
H-InvDB	HIX0201612.
HGNC	HGNC:10383. RPS10.
HPA	HPA047268. HPA048084.
MIM	603632. gene. 613308. phenotype.
neXtProt	NX_P46783.
Orphanet	124. Blackfan-Diamond disease.
PharmGKB	PA34779.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5045.
HOVERGEN	HBG001253.
KO	K02947.
OrthoDB	EOG47SSFW.
PhylomeDB	P46783.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P46783.
Bgee	P46783.
CleanEx	HS_RPS10.
Genevestigator	P46783.
GermOnline	ENSG00000124614. Homo sapiens.
Family and domain databases
InterPro	IPR005326. S10_plectin_N. [Graphical view]
Pfam	PF03501. S10_plectin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	6204.
NextBio	24095.
SOURCE	Search...

Entry information

Entry name

RS10_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.