Full text data of RPS10
RPS10
[Confidence: low (only semi-automatic identification from reviews)]
40S ribosomal protein S10
Note: presumably soluble (membrane word is not in UniProt keywords or features)
40S ribosomal protein S10
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46783
ID RS10_HUMAN Reviewed; 165 AA.
AC P46783; B2R4E3; Q5TZC0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=40S ribosomal protein S10;
GN Name=RPS10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-15.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-85.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [8]
RP SUBCELLULAR LOCATION, METHYLATION AT ARG-158 AND ARG-160, INTERACTION
RP WITH PRMT5 AND NPM1, AND MUTAGENESIS OF ARG-158 AND ARG-160.
RX PubMed=20159986; DOI=10.1074/jbc.M110.103911;
RA Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.;
RT "Methylation of ribosomal protein S10 by protein-arginine
RT methyltransferase 5 regulates ribosome biogenesis.";
RL J. Biol. Chem. 285:12695-12705(2010).
RN [9]
RP INVOLVEMENT IN DBA9.
RX PubMed=20116044; DOI=10.1016/j.ajhg.2009.12.015;
RA Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F.,
RA Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E.,
RA Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.;
RT "Ribosomal protein genes RPS10 and RPS26 are commonly mutated in
RT Diamond-Blackfan anemia.";
RL Am. J. Hum. Genet. 86:222-228(2010).
RN [10]
RP ERRATUM.
RA Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F.,
RA Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E.,
RA Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.;
RL Am. J. Hum. Genet. 86:655-655(2010).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Component of the 40S ribosomal subunit.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Interacts with
CC PRMT5. The methylated form interacts with NPM1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC Note=Localized in the granular component (GC) region of the
CC nucleolus. Methylation is required for its localization in the GC
CC region. Colocalizes with NPS1 in the GC region of the nucleolus.
CC -!- PTM: Methylated by PRMT5. Methylation is necessary for its
CC interaction with NPS1, its localization in the granular component
CC (GC) region of the nucleolus, for the proper assembly of
CC ribosomes, protein synthesis and optimal cell proliferation.
CC -!- DISEASE: Diamond-Blackfan anemia 9 (DBA9) [MIM:613308]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan
CC anemia is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40%
CC of Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial
CC (Pierre-Robin syndrome and cleft palate), thumb and urogenital
CC anomalies. Note=The disease is caused by mutations affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ribosomal protein S10e family.
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DR EMBL; U14972; AAA85660.1; -; mRNA.
DR EMBL; AK311797; BAG34740.1; -; mRNA.
DR EMBL; AL157372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03784.1; -; Genomic_DNA.
DR EMBL; BC001032; AAH01032.1; -; mRNA.
DR EMBL; BC001955; AAH01955.1; -; mRNA.
DR EMBL; BC005012; AAH05012.1; -; mRNA.
DR EMBL; BC070235; AAH70235.1; -; mRNA.
DR EMBL; BC071946; AAH71946.1; -; mRNA.
DR EMBL; BC073799; AAH73799.1; -; mRNA.
DR EMBL; AB007151; BAA25817.1; -; Genomic_DNA.
DR PIR; S55918; S55918.
DR RefSeq; NP_001005.1; NM_001014.4.
DR RefSeq; NP_001190174.1; NM_001203245.2.
DR RefSeq; NP_001191020.1; NM_001204091.1.
DR UniGene; Hs.406620; -.
DR UniGene; Hs.645317; -.
DR PDB; 3J3A; EM; 5.00 A; K=1-165.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P46783; -.
DR SMR; P46783; 1-98.
DR IntAct; P46783; 27.
DR MINT; MINT-5001020; -.
DR STRING; 9606.ENSP00000347271; -.
DR PhosphoSite; P46783; -.
DR DMDM; 1173177; -.
DR PaxDb; P46783; -.
DR PRIDE; P46783; -.
DR DNASU; 6204; -.
DR Ensembl; ENST00000326199; ENSP00000347271; ENSG00000124614.
DR GeneID; 6204; -.
DR KEGG; hsa:6204; -.
DR UCSC; uc003ojm.3; human.
DR CTD; 6204; -.
DR GeneCards; GC06M035236; -.
DR H-InvDB; HIX0201612; -.
DR HGNC; HGNC:10383; RPS10.
DR HPA; HPA047268; -.
DR HPA; HPA048084; -.
DR MIM; 603632; gene.
DR MIM; 613308; phenotype.
DR neXtProt; NX_P46783; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34779; -.
DR eggNOG; COG5045; -.
DR HOVERGEN; HBG001253; -.
DR KO; K02947; -.
DR PhylomeDB; P46783; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPS10; -.
DR GenomeRNAi; 6204; -.
DR NextBio; 24095; -.
DR PRO; PR:P46783; -.
DR ArrayExpress; P46783; -.
DR Bgee; P46783; -.
DR CleanEx; HS_RPS10; -.
DR Genevestigator; P46783; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR InterPro; IPR005326; S10_plectin_N.
DR Pfam; PF03501; S10_plectin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 165 40S ribosomal protein S10.
FT /FTId=PRO_0000116360.
FT MOD_RES 146 146 Phosphoserine (By similarity).
FT MOD_RES 158 158 Symmetric dimethylarginine.
FT MOD_RES 160 160 Symmetric dimethylarginine.
FT MUTAGEN 158 158 R->K: Weakly methylated. Complete loss of
FT methylation; inefficient assembly into
FT ribosomes; instability; increased
FT degradation by the proteasomal pathway;
FT decreased interaction with NPM1; absence
FT of localization in the granular component
FT (GC) region of the nucleolus; when
FT associated with K-160.
FT MUTAGEN 160 160 R->K: Weakly methylated. Complete loss of
FT methylation; inefficient assembly into
FT ribosomes; instability; increased
FT degradation by the proteasomal pathway;
FT decreased interaction with NPM1; absence
FT of localization in the granular component
FT (GC) region of the nucleolus; when
FT associated with K-158.
SQ SEQUENCE 165 AA; 18898 MW; 64106DFCD97AABA3 CRC64;
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE
QFAWRHFYWY LTNEGIQYLR DYLHLPPEIV PATLRRSRPE TGRPRPKGLE GERPARLTRG
EADRDTYRRS AVPPGADKKA EAGAGSATEF QFRGGFGRGR GQPPQ
//
ID RS10_HUMAN Reviewed; 165 AA.
AC P46783; B2R4E3; Q5TZC0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=40S ribosomal protein S10;
GN Name=RPS10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-15.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
RA Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-85.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [8]
RP SUBCELLULAR LOCATION, METHYLATION AT ARG-158 AND ARG-160, INTERACTION
RP WITH PRMT5 AND NPM1, AND MUTAGENESIS OF ARG-158 AND ARG-160.
RX PubMed=20159986; DOI=10.1074/jbc.M110.103911;
RA Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.;
RT "Methylation of ribosomal protein S10 by protein-arginine
RT methyltransferase 5 regulates ribosome biogenesis.";
RL J. Biol. Chem. 285:12695-12705(2010).
RN [9]
RP INVOLVEMENT IN DBA9.
RX PubMed=20116044; DOI=10.1016/j.ajhg.2009.12.015;
RA Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F.,
RA Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E.,
RA Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.;
RT "Ribosomal protein genes RPS10 and RPS26 are commonly mutated in
RT Diamond-Blackfan anemia.";
RL Am. J. Hum. Genet. 86:222-228(2010).
RN [10]
RP ERRATUM.
RA Doherty L., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F.,
RA Clinton C., Schneider H.E., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Glader B., Arceci R.J., Farrar J.E.,
RA Atsidaftos E., Lipton J.M., Gleizes P.E., Gazda H.T.;
RL Am. J. Hum. Genet. 86:655-655(2010).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Component of the 40S ribosomal subunit.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Interacts with
CC PRMT5. The methylated form interacts with NPM1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC Note=Localized in the granular component (GC) region of the
CC nucleolus. Methylation is required for its localization in the GC
CC region. Colocalizes with NPS1 in the GC region of the nucleolus.
CC -!- PTM: Methylated by PRMT5. Methylation is necessary for its
CC interaction with NPS1, its localization in the granular component
CC (GC) region of the nucleolus, for the proper assembly of
CC ribosomes, protein synthesis and optimal cell proliferation.
CC -!- DISEASE: Diamond-Blackfan anemia 9 (DBA9) [MIM:613308]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan
CC anemia is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40%
CC of Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial
CC (Pierre-Robin syndrome and cleft palate), thumb and urogenital
CC anomalies. Note=The disease is caused by mutations affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ribosomal protein S10e family.
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DR EMBL; U14972; AAA85660.1; -; mRNA.
DR EMBL; AK311797; BAG34740.1; -; mRNA.
DR EMBL; AL157372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03784.1; -; Genomic_DNA.
DR EMBL; BC001032; AAH01032.1; -; mRNA.
DR EMBL; BC001955; AAH01955.1; -; mRNA.
DR EMBL; BC005012; AAH05012.1; -; mRNA.
DR EMBL; BC070235; AAH70235.1; -; mRNA.
DR EMBL; BC071946; AAH71946.1; -; mRNA.
DR EMBL; BC073799; AAH73799.1; -; mRNA.
DR EMBL; AB007151; BAA25817.1; -; Genomic_DNA.
DR PIR; S55918; S55918.
DR RefSeq; NP_001005.1; NM_001014.4.
DR RefSeq; NP_001190174.1; NM_001203245.2.
DR RefSeq; NP_001191020.1; NM_001204091.1.
DR UniGene; Hs.406620; -.
DR UniGene; Hs.645317; -.
DR PDB; 3J3A; EM; 5.00 A; K=1-165.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; P46783; -.
DR SMR; P46783; 1-98.
DR IntAct; P46783; 27.
DR MINT; MINT-5001020; -.
DR STRING; 9606.ENSP00000347271; -.
DR PhosphoSite; P46783; -.
DR DMDM; 1173177; -.
DR PaxDb; P46783; -.
DR PRIDE; P46783; -.
DR DNASU; 6204; -.
DR Ensembl; ENST00000326199; ENSP00000347271; ENSG00000124614.
DR GeneID; 6204; -.
DR KEGG; hsa:6204; -.
DR UCSC; uc003ojm.3; human.
DR CTD; 6204; -.
DR GeneCards; GC06M035236; -.
DR H-InvDB; HIX0201612; -.
DR HGNC; HGNC:10383; RPS10.
DR HPA; HPA047268; -.
DR HPA; HPA048084; -.
DR MIM; 603632; gene.
DR MIM; 613308; phenotype.
DR neXtProt; NX_P46783; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34779; -.
DR eggNOG; COG5045; -.
DR HOVERGEN; HBG001253; -.
DR KO; K02947; -.
DR PhylomeDB; P46783; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPS10; -.
DR GenomeRNAi; 6204; -.
DR NextBio; 24095; -.
DR PRO; PR:P46783; -.
DR ArrayExpress; P46783; -.
DR Bgee; P46783; -.
DR CleanEx; HS_RPS10; -.
DR Genevestigator; P46783; -.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR InterPro; IPR005326; S10_plectin_N.
DR Pfam; PF03501; S10_plectin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 165 40S ribosomal protein S10.
FT /FTId=PRO_0000116360.
FT MOD_RES 146 146 Phosphoserine (By similarity).
FT MOD_RES 158 158 Symmetric dimethylarginine.
FT MOD_RES 160 160 Symmetric dimethylarginine.
FT MUTAGEN 158 158 R->K: Weakly methylated. Complete loss of
FT methylation; inefficient assembly into
FT ribosomes; instability; increased
FT degradation by the proteasomal pathway;
FT decreased interaction with NPM1; absence
FT of localization in the granular component
FT (GC) region of the nucleolus; when
FT associated with K-160.
FT MUTAGEN 160 160 R->K: Weakly methylated. Complete loss of
FT methylation; inefficient assembly into
FT ribosomes; instability; increased
FT degradation by the proteasomal pathway;
FT decreased interaction with NPM1; absence
FT of localization in the granular component
FT (GC) region of the nucleolus; when
FT associated with K-158.
SQ SEQUENCE 165 AA; 18898 MW; 64106DFCD97AABA3 CRC64;
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE
QFAWRHFYWY LTNEGIQYLR DYLHLPPEIV PATLRRSRPE TGRPRPKGLE GERPARLTRG
EADRDTYRRS AVPPGADKKA EAGAGSATEF QFRGGFGRGR GQPPQ
//
MIM
603632
*RECORD*
*FIELD* NO
603632
*FIELD* TI
*603632 RIBOSOMAL PROTEIN S10; RPS10
*FIELD* TX
DESCRIPTION
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins (see 180466).
CLONING
Adams et al. (1992) isolated an RPS10 cDNA as a human brain EST.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9; 603631), S10 (RPS10), S29 (RPS29; 603633), L5
(RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 165-amino acid human RPS10
differs from rat Rps10 by 2 amino acids; neither protein contains
cysteine residues. Northern blot analysis suggested variable expression
of RPS10 in colorectal cancers compared to adjacent normal tissues,
although no correlation between the level of expression and the severity
of the disease was found.
GENE STRUCTURE
Boria et al. (2010) stated that the RPS10 gene contains 6 exons spanning
8.65 kb.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS10 gene to chromosome 6p.
Boria et al. (2010) stated that the RPS10 gene maps to chromosome
6p21.31.
GENE FUNCTION
Using siRNA knockdown in HeLa cells to analyze the role of RPS10 in
pre-rRNA processing, Doherty et al. (2010) found that depletion of RPS10
led to decreased levels of 18S rRNA, indicating that RPS10 is necessary
for production of the small subunit. RNA blot analysis showed
accumulation of 43S, 26S, and 18S-E pre-rRNAs, consistent with defects
in cleavage at both ends of the 18S rRNA.
MOLECULAR GENETICS
Doherty et al. (2010) sequenced 35 ribosomal protein genes in a cohort
of 117 patients with Diamond-Blackfan anemia (see DBA9, 613308) who were
negative for mutation in 7 known DBA genes and identified 3 mutations in
the RPS10 gene (603632.0001-603632.0003) in 5 patients.
*FIELD* AV
.0001
DIAMOND-BLACKFAN ANEMIA 9
RPS10, MET1ILE
In a male patient with Diamond-Blackfan anemia (613308), Doherty et al.
(2010) identified heterozygosity for a 3G-A transition in exon 1 of the
RPS10 gene, causing a met1-to-thr (M1T) substitution that eliminates the
start codon and is predicted to result in a truncated 144-residue
protein. The mutation was not found in at least 520 control chromosomes.
.0002
DIAMOND-BLACKFAN ANEMIA 9
RPS10, 1-BP INS, 260C
In a female patient who was diagnosed with Diamond-Blackfan anemia
(613308) at 2 months of age, Doherty et al. (2010) identified
heterozygosity for a 1-bp insertion (260insC) in exon 3 of the RPS10
gene, resulting in a frameshift and a premature termination codon. The
mutation was not found in her unaffected father or in at least 520
control chromosomes.
.0003
DIAMOND-BLACKFAN ANEMIA 9
RPS10, ARG113TER
In a male and 2 female probands with Diamond-Blackfan anemia (613308),
Doherty et al. (2010) identified heterozygosity for a 337C-T transition
in exon 4 of the RPS10 gene, resulting in an arg113-to-ter (R113X)
substitution. Two of the patients were responsive to steroid therapy;
the third, a female with a de novo mutation who was diagnosed at birth,
was unresponsive to steroid therapy and was also noted to have a webbed
neck. The mutation was not found in at least 520 control chromosomes.
*FIELD* RF
1. Adams, M. D.; Dubnick, M.; Kerlavage, A. R.; Moreno, R.; Kelley,
J. M.; Utterback, T. R.; Nagle, J. W.; Fields, C.; Venter, J. C.:
Sequence identification of 2,375 human brain genes. Nature 355:
632-634, 1992. Note: Comment: Nature 357: 367-368, 1992.
2. Boria, I.; Garelli, E.; Gazda, H. T.; Aspesi, A.; Quarello, P.;
Pavesi, E.; Ferrante, D.; Meerpohl, J. J.; Kartal, M.; Da Costa, L.;
Proust, A.; Leblanc, T.; and 17 others: The ribosomal basis of
Diamond-Blackfan anemia: mutation and database update. Hum. Mutat. 31:
1269-1279, 2010.
3. 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.: Ribosomal protein genes RPS10 and RPS26 are commonly
mutated in Diamond-Blackfan anemia. Am. J. Hum. Genet. 86: 222-228,
2010. Note: Erratum: Am. J. Hum. Genet 86: 655-656, 2010.
4. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
5. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
6. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
*FIELD* CN
Cassandra L. Kniffin - updated: 03/24/2011
Marla J. F. O'Neill - updated: 3/18/2010
Patti M. Sherman - updated: 9/10/1999
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
wwang: 03/24/2011
alopez: 6/18/2010
wwang: 5/12/2010
carol: 3/18/2010
alopez: 3/6/2001
psherman: 12/7/1999
mgross: 9/20/1999
psherman: 9/10/1999
carol: 3/19/1999
*RECORD*
*FIELD* NO
603632
*FIELD* TI
*603632 RIBOSOMAL PROTEIN S10; RPS10
*FIELD* TX
DESCRIPTION
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins (see 180466).
CLONING
Adams et al. (1992) isolated an RPS10 cDNA as a human brain EST.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9; 603631), S10 (RPS10), S29 (RPS29; 603633), L5
(RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 165-amino acid human RPS10
differs from rat Rps10 by 2 amino acids; neither protein contains
cysteine residues. Northern blot analysis suggested variable expression
of RPS10 in colorectal cancers compared to adjacent normal tissues,
although no correlation between the level of expression and the severity
of the disease was found.
GENE STRUCTURE
Boria et al. (2010) stated that the RPS10 gene contains 6 exons spanning
8.65 kb.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPS10 gene to chromosome 6p.
Boria et al. (2010) stated that the RPS10 gene maps to chromosome
6p21.31.
GENE FUNCTION
Using siRNA knockdown in HeLa cells to analyze the role of RPS10 in
pre-rRNA processing, Doherty et al. (2010) found that depletion of RPS10
led to decreased levels of 18S rRNA, indicating that RPS10 is necessary
for production of the small subunit. RNA blot analysis showed
accumulation of 43S, 26S, and 18S-E pre-rRNAs, consistent with defects
in cleavage at both ends of the 18S rRNA.
MOLECULAR GENETICS
Doherty et al. (2010) sequenced 35 ribosomal protein genes in a cohort
of 117 patients with Diamond-Blackfan anemia (see DBA9, 613308) who were
negative for mutation in 7 known DBA genes and identified 3 mutations in
the RPS10 gene (603632.0001-603632.0003) in 5 patients.
*FIELD* AV
.0001
DIAMOND-BLACKFAN ANEMIA 9
RPS10, MET1ILE
In a male patient with Diamond-Blackfan anemia (613308), Doherty et al.
(2010) identified heterozygosity for a 3G-A transition in exon 1 of the
RPS10 gene, causing a met1-to-thr (M1T) substitution that eliminates the
start codon and is predicted to result in a truncated 144-residue
protein. The mutation was not found in at least 520 control chromosomes.
.0002
DIAMOND-BLACKFAN ANEMIA 9
RPS10, 1-BP INS, 260C
In a female patient who was diagnosed with Diamond-Blackfan anemia
(613308) at 2 months of age, Doherty et al. (2010) identified
heterozygosity for a 1-bp insertion (260insC) in exon 3 of the RPS10
gene, resulting in a frameshift and a premature termination codon. The
mutation was not found in her unaffected father or in at least 520
control chromosomes.
.0003
DIAMOND-BLACKFAN ANEMIA 9
RPS10, ARG113TER
In a male and 2 female probands with Diamond-Blackfan anemia (613308),
Doherty et al. (2010) identified heterozygosity for a 337C-T transition
in exon 4 of the RPS10 gene, resulting in an arg113-to-ter (R113X)
substitution. Two of the patients were responsive to steroid therapy;
the third, a female with a de novo mutation who was diagnosed at birth,
was unresponsive to steroid therapy and was also noted to have a webbed
neck. The mutation was not found in at least 520 control chromosomes.
*FIELD* RF
1. Adams, M. D.; Dubnick, M.; Kerlavage, A. R.; Moreno, R.; Kelley,
J. M.; Utterback, T. R.; Nagle, J. W.; Fields, C.; Venter, J. C.:
Sequence identification of 2,375 human brain genes. Nature 355:
632-634, 1992. Note: Comment: Nature 357: 367-368, 1992.
2. Boria, I.; Garelli, E.; Gazda, H. T.; Aspesi, A.; Quarello, P.;
Pavesi, E.; Ferrante, D.; Meerpohl, J. J.; Kartal, M.; Da Costa, L.;
Proust, A.; Leblanc, T.; and 17 others: The ribosomal basis of
Diamond-Blackfan anemia: mutation and database update. Hum. Mutat. 31:
1269-1279, 2010.
3. 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.: Ribosomal protein genes RPS10 and RPS26 are commonly
mutated in Diamond-Blackfan anemia. Am. J. Hum. Genet. 86: 222-228,
2010. Note: Erratum: Am. J. Hum. Genet 86: 655-656, 2010.
4. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
5. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
6. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
*FIELD* CN
Cassandra L. Kniffin - updated: 03/24/2011
Marla J. F. O'Neill - updated: 3/18/2010
Patti M. Sherman - updated: 9/10/1999
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
wwang: 03/24/2011
alopez: 6/18/2010
wwang: 5/12/2010
carol: 3/18/2010
alopez: 3/6/2001
psherman: 12/7/1999
mgross: 9/20/1999
psherman: 9/10/1999
carol: 3/19/1999
MIM
613308
*RECORD*
*FIELD* NO
613308
*FIELD* TI
#613308 DIAMOND-BLACKFAN ANEMIA 9; DBA9
*FIELD* TX
A number sign (#) is used with this entry because Diamond-Blackfan
read moreanemia-9 is caused by heterozygous mutations in the gene encoding
ribosomal protein S10 (RPS10; 603632) on chromosome 6p.
For a general phenotypic description and a discussion of genetic
heterogeneity of Diamond-Blackfan anemia, see DBA1 (105650).
MOLECULAR GENETICS
Doherty et al. (2010) sequenced 35 ribosomal protein genes in a cohort
of 117 patients with Diamond-Blackfan anemia who were negative for
mutation in 7 known DBA genes and identified 3 mutations in the RPS10
gene in 5 patients (603632.0001-603632.0003). None of the mutations were
found in at least 520 chromosomes from a control population of similar,
largely European origin. Regarding 4 patients for whom information was
available, 3 had been initially responsive to steroids, and 2 were still
being treated with steroids, whereas 2 were red blood cell-transfusion
dependent. Doherty et al. (2010) estimated that RPS10 mutations are
present in about 2.6% of the overall DBA population.
*FIELD* RF
1. 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.: Ribosomal protein genes RPS10 and RPS26 are commonly
mutated in Diamond-Blackfan anemia. Am. J. Hum. Genet. 86: 222-228,
2010. Note: Erratum: Am. J. Hum. Genet 86: 655-656, 2010.
*FIELD* CD
Marla J. F. O'Neill: 3/17/2010
*FIELD* ED
alopez: 06/18/2010
alopez: 6/18/2010
wwang: 5/12/2010
carol: 3/18/2010
*RECORD*
*FIELD* NO
613308
*FIELD* TI
#613308 DIAMOND-BLACKFAN ANEMIA 9; DBA9
*FIELD* TX
A number sign (#) is used with this entry because Diamond-Blackfan
read moreanemia-9 is caused by heterozygous mutations in the gene encoding
ribosomal protein S10 (RPS10; 603632) on chromosome 6p.
For a general phenotypic description and a discussion of genetic
heterogeneity of Diamond-Blackfan anemia, see DBA1 (105650).
MOLECULAR GENETICS
Doherty et al. (2010) sequenced 35 ribosomal protein genes in a cohort
of 117 patients with Diamond-Blackfan anemia who were negative for
mutation in 7 known DBA genes and identified 3 mutations in the RPS10
gene in 5 patients (603632.0001-603632.0003). None of the mutations were
found in at least 520 chromosomes from a control population of similar,
largely European origin. Regarding 4 patients for whom information was
available, 3 had been initially responsive to steroids, and 2 were still
being treated with steroids, whereas 2 were red blood cell-transfusion
dependent. Doherty et al. (2010) estimated that RPS10 mutations are
present in about 2.6% of the overall DBA population.
*FIELD* RF
1. 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.: Ribosomal protein genes RPS10 and RPS26 are commonly
mutated in Diamond-Blackfan anemia. Am. J. Hum. Genet. 86: 222-228,
2010. Note: Erratum: Am. J. Hum. Genet 86: 655-656, 2010.
*FIELD* CD
Marla J. F. O'Neill: 3/17/2010
*FIELD* ED
alopez: 06/18/2010
alopez: 6/18/2010
wwang: 5/12/2010
carol: 3/18/2010