RS10_HUMAN
ID RS10_HUMAN Reviewed; 165 AA.
AC P46783; B2R4E3; Q5TZC0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=40S ribosomal protein S10;
DE AltName: Full=Small ribosomal subunit protein eS10 {ECO:0000303|PubMed:24524803};
GN Name=RPS10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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, S10
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Egorov T.A.,
RA 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; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA 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 WITH
RP 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 methyltransferase
RT 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 Diamond-
RT Blackfan anemia.";
RL Am. J. Hum. Genet. 86:222-228(2010).
RN [10]
RP ERRATUM OF PUBMED:20116044.
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 NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [12]
RP UBIQUITINATION AT LYS-138 AND LYS-139, AND MUTAGENESIS OF 138-LYS-LYS-139.
RX PubMed=28065601; DOI=10.1016/j.molcel.2016.11.039;
RA Juszkiewicz S., Hegde R.S.;
RT "Initiation of quality control during poly(A) translation requires site-
RT specific ribosome ubiquitination.";
RL Mol. Cell 65:743-750(2016).
RN [13]
RP UBIQUITINATION AT LYS-138 AND LYS-139, AND MUTAGENESIS OF 138-LYS-LYS-139.
RX PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026;
RA Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.;
RT "ZNF598 and RACK1 regulate mammalian ribosome-associated quality control
RT function by mediating regulatory 40S ribosomal ubiquitylation.";
RL Mol. Cell 65:751-760(2017).
RN [14]
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 {ECO:0000269|PubMed:20159986}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20159986}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:20159986}. Note=Localized in the granular
CC component (GC) region of the nucleolus. Methylation is required for its
CC localization in the GC region. Colocalizes with NPS1 in the GC region
CC of the nucleolus.
CC -!- PTM: Methylated by PRMT5. Methylation is necessary for its interaction
CC with NPS1, its localization in the granular component (GC) region of
CC the nucleolus, for the proper assembly of ribosomes, protein synthesis
CC and optimal cell proliferation. {ECO:0000269|PubMed:20159986}.
CC -!- PTM: Monoubiquitinated by ZNF598 when a ribosome has stalled during
CC translation of poly(A) sequences, leading to preclude synthesis of a
CC long poly-lysine tail and initiate the ribosome quality control (RQC)
CC pathway to degrade the potentially detrimental aberrant nascent
CC polypeptide (PubMed:28065601, PubMed:28132843).
CC {ECO:0000269|PubMed:28065601, ECO:0000269|PubMed:28132843}.
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 anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies.
CC {ECO:0000269|PubMed:20116044}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family.
CC {ECO:0000305}.
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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 CCDS; CCDS4792.1; -.
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 PDB; 4UG0; EM; -; SK=1-165.
DR PDB; 4V6X; EM; 5.00 A; AK=1-165.
DR PDB; 5A2Q; EM; 3.90 A; K=1-165.
DR PDB; 5AJ0; EM; 3.50 A; BK=1-165.
DR PDB; 5FLX; EM; 3.90 A; K=1-165.
DR PDB; 5LKS; EM; 3.60 A; SK=1-165.
DR PDB; 5OA3; EM; 4.30 A; K=1-165.
DR PDB; 5T2C; EM; 3.60 A; Av=1-165.
DR PDB; 5VYC; X-ray; 6.00 A; K1/K2/K3/K4/K5/K6=1-165.
DR PDB; 6FEC; EM; 6.30 A; t=1-98.
DR PDB; 6G51; EM; 4.10 A; K=1-165.
DR PDB; 6G53; EM; 4.50 A; K=1-165.
DR PDB; 6G5H; EM; 3.60 A; K=1-165.
DR PDB; 6G5I; EM; 3.50 A; K=1-165.
DR PDB; 6IP5; EM; 3.90 A; 2u=1-165.
DR PDB; 6IP6; EM; 4.50 A; 2u=1-165.
DR PDB; 6IP8; EM; 3.90 A; 2u=1-165.
DR PDB; 6OLE; EM; 3.10 A; SK=1-98.
DR PDB; 6OLF; EM; 3.90 A; SK=1-98.
DR PDB; 6OLG; EM; 3.40 A; BK=1-98.
DR PDB; 6OLI; EM; 3.50 A; SK=1-98.
DR PDB; 6OLZ; EM; 3.90 A; BK=1-98.
DR PDB; 6OM0; EM; 3.10 A; SK=1-98.
DR PDB; 6OM7; EM; 3.70 A; SK=1-98.
DR PDB; 6QZP; EM; 2.90 A; SK=1-98.
DR PDB; 6XA1; EM; 2.80 A; SK=1-95.
DR PDB; 6Y0G; EM; 3.20 A; SK=1-165.
DR PDB; 6Y2L; EM; 3.00 A; SK=1-165.
DR PDB; 6Y57; EM; 3.50 A; SK=1-165.
DR PDB; 6YBS; EM; 3.10 A; a=1-165.
DR PDB; 6Z6L; EM; 3.00 A; SK=1-165.
DR PDB; 6Z6M; EM; 3.10 A; SK=1-165.
DR PDB; 6Z6N; EM; 2.90 A; SK=1-165.
DR PDB; 6ZLW; EM; 2.60 A; M=1-165.
DR PDB; 6ZM7; EM; 2.70 A; SK=1-165.
DR PDB; 6ZME; EM; 3.00 A; SK=1-165.
DR PDB; 6ZMI; EM; 2.60 A; SK=1-165.
DR PDB; 6ZMO; EM; 3.10 A; SK=1-165.
DR PDB; 6ZMT; EM; 3.00 A; M=1-165.
DR PDB; 6ZMW; EM; 3.70 A; a=1-165.
DR PDB; 6ZN5; EM; 3.20 A; M=3-97.
DR PDB; 6ZOJ; EM; 2.80 A; K=1-165.
DR PDB; 6ZOL; EM; 2.80 A; K=1-165.
DR PDB; 6ZON; EM; 3.00 A; u=1-165.
DR PDB; 6ZP4; EM; 2.90 A; u=1-165.
DR PDB; 6ZUO; EM; 3.10 A; K=1-165.
DR PDB; 6ZV6; EM; 2.90 A; K=1-165.
DR PDB; 6ZVH; EM; 2.90 A; K=1-98.
DR PDB; 6ZVJ; EM; 3.80 A; u=1-95.
DR PDB; 6ZXD; EM; 3.20 A; K=1-165.
DR PDB; 6ZXE; EM; 3.00 A; K=1-165.
DR PDB; 6ZXF; EM; 3.70 A; K=1-165.
DR PDB; 6ZXG; EM; 2.60 A; K=1-165.
DR PDB; 6ZXH; EM; 2.70 A; K=1-165.
DR PDB; 7A09; EM; 3.50 A; u=1-165.
DR PDB; 7K5I; EM; 2.90 A; K=1-165.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P46783; -.
DR SMR; P46783; -.
DR BioGRID; 112118; 478.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P46783; -.
DR IntAct; P46783; 101.
DR MINT; P46783; -.
DR STRING; 9606.ENSP00000481646; -.
DR GlyGen; P46783; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46783; -.
DR PhosphoSitePlus; P46783; -.
DR SwissPalm; P46783; -.
DR BioMuta; RPS10; -.
DR DMDM; 1173177; -.
DR EPD; P46783; -.
DR jPOST; P46783; -.
DR MassIVE; P46783; -.
DR MaxQB; P46783; -.
DR PaxDb; P46783; -.
DR PeptideAtlas; P46783; -.
DR PRIDE; P46783; -.
DR ProteomicsDB; 55765; -.
DR TopDownProteomics; P46783; -.
DR Antibodypedia; 45705; 229 antibodies from 30 providers.
DR DNASU; 6204; -.
DR Ensembl; ENST00000464218.5; ENSP00000494440.1; ENSG00000124614.16.
DR Ensembl; ENST00000467531.5; ENSP00000494190.1; ENSG00000124614.16.
DR Ensembl; ENST00000621356.3; ENSP00000481646.1; ENSG00000124614.16.
DR Ensembl; ENST00000648437.1; ENSP00000497917.1; ENSG00000124614.16.
DR GeneID; 6204; -.
DR KEGG; hsa:6204; -.
DR MANE-Select; ENST00000648437.1; ENSP00000497917.1; NM_001014.5; NP_001005.1.
DR UCSC; uc003ojm.4; human.
DR CTD; 6204; -.
DR DisGeNET; 6204; -.
DR GeneCards; RPS10; -.
DR GeneReviews; RPS10; -.
DR HGNC; HGNC:10383; RPS10.
DR HPA; ENSG00000124614; Low tissue specificity.
DR MalaCards; RPS10; -.
DR MIM; 603632; gene.
DR MIM; 613308; phenotype.
DR neXtProt; NX_P46783; -.
DR OpenTargets; ENSG00000124614; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34779; -.
DR VEuPathDB; HostDB:ENSG00000124614; -.
DR eggNOG; KOG3344; Eukaryota.
DR GeneTree; ENSGT00440000034918; -.
DR HOGENOM; CLU_089349_3_1_1; -.
DR InParanoid; P46783; -.
DR OMA; GFNPEFR; -.
DR OrthoDB; 1588066at2759; -.
DR PhylomeDB; P46783; -.
DR TreeFam; TF319100; -.
DR PathwayCommons; P46783; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P46783; -.
DR SIGNOR; P46783; -.
DR BioGRID-ORCS; 6204; 416 hits in 1085 CRISPR screens.
DR GeneWiki; RPS10; -.
DR GenomeRNAi; 6204; -.
DR Pharos; P46783; Tbio.
DR PRO; PR:P46783; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P46783; protein.
DR Bgee; ENSG00000124614; Expressed in left ovary and 93 other tissues.
DR ExpressionAtlas; P46783; baseline and differential.
DR Genevisible; P46783; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037447; Rps10.
DR InterPro; IPR005326; S10_plectin_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12146; PTHR12146; 1.
DR Pfam; PF03501; S10_plectin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..165
FT /note="40S ribosomal protein S10"
FT /id="PRO_0000116360"
FT REGION 92..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63325"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63325"
FT MOD_RES 153
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P63325"
FT MOD_RES 158
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:20159986"
FT MOD_RES 160
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:20159986"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT MUTAGEN 138..139
FT /note="KK->RR: Abolishes monoubiquitination by ZNF598,
FT leading to enhanced readthrough on the poly(A)-stall
FT sequences."
FT /evidence="ECO:0000269|PubMed:28065601,
FT ECO:0000269|PubMed:28132843"
FT MUTAGEN 158
FT /note="R->K: Weakly methylated. Complete loss of
FT methylation; inefficient assembly into ribosomes;
FT instability; increased degradation by the proteasomal
FT pathway; decreased interaction with NPM1; absence of
FT localization in the granular component (GC) region of the
FT nucleolus; when associated with K-160."
FT /evidence="ECO:0000269|PubMed:20159986"
FT MUTAGEN 160
FT /note="R->K: Weakly methylated. Complete loss of
FT methylation; inefficient assembly into ribosomes;
FT instability; increased degradation by the proteasomal
FT pathway; decreased interaction with NPM1; absence of
FT localization in the granular component (GC) region of the
FT nucleolus; when associated with K-158."
FT /evidence="ECO:0000269|PubMed:20159986"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6ZLW"
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
