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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.16
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.16
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.16
Involvement in disease	Defects in RPS10 are the cause of Diamond-Blackfan anemia type 9 (DBA9) [MIM:613308]. It is 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. Ref.17
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	endocrine pancreas development Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome translational elongation 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 Ref.6. Source: UniProtKB nucleolus Inferred from direct assay Ref.16. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.16. 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 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15
	Modified residue	130	1	Phosphoserine Ref.11
	Modified residue	146	1	Phosphoserine Ref.12 Ref.13 Ref.15
	Modified residue	158	1	Symmetric dimethylarginine Ref.16
	Modified residue	160	1	Symmetric dimethylarginine Ref.16
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.16
	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.16

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: 7772601] [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: 14702039] [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: 14574404] [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: 15489334] [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: 8706699] [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: 9582194] [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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, MASS SPECTROMETRY.
[9]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[10]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[11]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12 AND SER-146, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12 AND SER-146, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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: 20159986] [Abstract] Cited for: SUBCELLULAR LOCATION, METHYLATION AT ARG-158 AND ARG-160, INTERACTION WITH PRMT5 AND NPM1, MUTAGENESIS OF ARG-158 AND ARG-160.
[17]	"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: 20116044] [Abstract] Cited for: INVOLVEMENT IN DBA9.
[18]	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)
[19]	"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: 21269460] [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. BX255972 Genomic DNA. Translation: CAH73100.1. 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.
SMR	P46783. Positions 1-100.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46783. 12 interactions.
MINT	MINT-5001020.
STRING	P46783.
PTM databases
PhosphoSite	P46783.
Polymorphism databases
DMDM	1173177.
Proteomic databases
PRIDE	P46783.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326199; ENSP00000347271; ENSG00000124614.
GeneID	6204.
KEGG	hsa:6204.
UCSC	uc003ojm.1. human.
Organism-specific databases
CTD	6204.
GeneCards	GC06M034432.
H-InvDB	HIX0009603. HIX0201612.
HGNC	HGNC:10383. RPS10.
MIM	603632. gene. 613308. phenotype.
neXtProt	NX_P46783.
Orphanet	124. Blackfan-Diamond disease.
PharmGKB	PA34779.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06592.
HOVERGEN	HBG001253.
OrthoDB	EOG47SSFW.
PhylomeDB	P46783.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111217. Metabolism. REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
Bgee	P46783.
CleanEx	HS_RPS10.
Genevestigator	P46783.
GermOnline	ENSG00000124614. Homo sapiens.
Family and domain databases
InterPro	IPR005326. S10_plectin_N. [Graphical view]
KO	K02947.
Pfam	PF03501. S10_plectin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 114 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.