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 27-MAR-2024, entry version 217. DE RecName: Full=Small ribosomal subunit protein eS10 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S10; 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 UBIQUITINATION AT LYS-138 AND LYS-139, AND MUTAGENESIS OF 138-LYS-LYS-139. RX PubMed=28685749; DOI=10.1038/ncomms16056; RA Garzia A., Jafarnejad S.M., Meyer C., Chapat C., Gogakos T., Morozov P., RA Amiri M., Shapiro M., Molina H., Tuschl T., Sonenberg N.; RT "The E3 ubiquitin ligase and RNA-binding protein ZNF598 orchestrates RT ribosome quality control of premature polyadenylated mRNAs."; RL Nat. Commun. 8:16056-16056(2017). RN [15] RP UBIQUITINATION AT LYS-138 AND LYS-139, DEUBIQUITINATION, AND MUTAGENESIS OF RP 138-LYS-LYS-139. RX PubMed=32011234; DOI=10.7554/elife.54023; RA Garshott D.M., Sundaramoorthy E., Leonard M., Bennett E.J.; RT "Distinct regulatory ribosomal ubiquitylation events are reversible and RT hierarchically organized."; RL Elife 9:0-0(2020). RN [16] RP DEUBIQUITINATION BY USP10. RX PubMed=31981475; DOI=10.1016/j.molcel.2019.12.024; RA Meyer C., Garzia A., Morozov P., Molina H., Tuschl T.; RT "The G3BP1-family-USP10 deubiquitinase complex rescues ubiquitinated 40S RT subunits of ribosomes stalled in translation from lysosomal degradation."; RL Mol. Cell 77:1193-1205(2020). RN [17] RP DEUBIQUITINATION. RX PubMed=36445135; DOI=10.1128/mcb.00265-22; RA Snaurova R., Vdovin A., Durech M., Nezval J., Zihala D., Jelinek T., RA Hajek R., Simicek M.; RT "Deubiquitinase OTUD1 resolves stalled translation on polyA and rare codon RT rich mRNAs."; RL Mol. Cell. Biol. 42:e0026522-e0026522(2022). RN [18] RP UBIQUITINATION AT LYS-138 AND LYS-139, AND MUTAGENESIS OF 138-LYS-LYS-139. RX PubMed=36302773; DOI=10.1038/s41467-022-34097-9; RA Narita M., Denk T., Matsuo Y., Sugiyama T., Kikuguchi C., Ito S., Sato N., RA Suzuki T., Hashimoto S., Machova I., Tesina P., Beckmann R., Inada T.; RT "A distinct mammalian disome collision interface harbors K63-linked RT polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation."; RL Nat. Commun. 13:6411-6411(2022). RN [19] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. 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 (PubMed:23636399). The CC ribosome is a large ribonucleoprotein complex responsible for the CC synthesis of proteins in the cell (PubMed:23636399). CC {ECO:0000269|PubMed:23636399}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23636399). CC The methylated form interacts with NPM1 (PubMed:20159986). CC {ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:23636399}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20159986, CC ECO:0000269|PubMed:23636399}. Nucleus, nucleolus CC {ECO:0000269|PubMed:20159986}. Note=Localized in the granular component CC (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. {ECO:0000269|PubMed:20159986}. 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, PubMed:28685749, CC PubMed:32011234, PubMed:36302773). Deubiquitinated by OTUD3 and USP21, CC antagonizing ZNF598 activity (PubMed:32011234). Deubiquitinated by CC OTUD1, antagonizing ZNF598 activity and stimulating formation of CC polysomes: deubiquitination by OTUD1 promotes stability and translation CC of a subset mRNAs with a high abundance of rare codons can limit the CC translation rate (PubMed:36445135). Deubiquitinated by USP10 CC (PubMed:31981475). {ECO:0000269|PubMed:28065601, CC ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:28685749, CC ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:32011234, CC ECO:0000269|PubMed:36302773, ECO:0000269|PubMed:36445135}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QP6; EM; 4.70 A; a=1-165. DR PDB; 7QP7; EM; 3.70 A; a=1-165. DR PDB; 7QVP; EM; 3.00 A; RK/SK=1-165. DR PDB; 7R4X; EM; 2.15 A; K=1-165. DR PDB; 7TQL; EM; 3.40 A; M=1-97. DR PDB; 7XNX; EM; 2.70 A; SK=1-165. DR PDB; 7XNY; EM; 2.50 A; SK=1-165. DR PDB; 8G5Y; EM; 2.29 A; SK=1-165. DR PDB; 8G60; EM; 2.54 A; SK=1-165. DR PDB; 8G61; EM; 2.94 A; SK=1-165. DR PDB; 8G6J; EM; 2.80 A; SK=1-165. DR PDB; 8GLP; EM; 1.67 A; SK=1-165. DR PDB; 8JDJ; EM; 2.50 A; 7=1-165. DR PDB; 8JDK; EM; 2.26 A; 7=1-165. DR PDB; 8JDL; EM; 2.42 A; 7=1-165. DR PDB; 8JDM; EM; 2.67 A; 7=1-165. DR PDB; 8PPK; EM; 2.98 A; K=1-165. DR PDB; 8PPL; EM; 2.65 A; AK=1-165. DR PDB; 8T4S; EM; 2.60 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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7QVP; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8T4S; -. DR AlphaFoldDB; P46783; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10772; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11301; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11322; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11440; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11517; -. DR EMDB; EMD-11518; -. DR EMDB; EMD-11519; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14181; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-4350; -. DR EMDB; EMD-4351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-4353; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P46783; -. DR BioGRID; 112118; 560. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P46783; -. DR IntAct; P46783; 102. 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; 9606-ENSP00000481646; -. DR PeptideAtlas; P46783; -. DR ProteomicsDB; 55765; -. DR Pumba; P46783; -. DR TopDownProteomics; P46783; -. DR Antibodypedia; 45705; 254 antibodies from 30 providers. DR DNASU; 6204; -. DR Ensembl; ENST00000464218.5; ENSP00000494440.1; ENSG00000124614.17. DR Ensembl; ENST00000467531.5; ENSP00000494190.1; ENSG00000124614.17. DR Ensembl; ENST00000621356.3; ENSP00000481646.1; ENSG00000124614.17. DR Ensembl; ENST00000648437.1; ENSP00000497917.1; ENSG00000124614.17. 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 AGR; HGNC:10383; -. 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; Diamond-Blackfan 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; YRRRDQE; -. DR OrthoDB; 154729at2759; -. 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-9735869; SARS-CoV-1 modulates host translation machinery. 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; 426 hits in 1154 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 primordial germ cell in gonad and 95 other cell types or tissues. DR ExpressionAtlas; P46783; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS: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; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; IC:UniProtKB. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR005326; Plectin_eS10_N. DR InterPro; IPR037447; Ribosomal_eS10. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR12146; 40S RIBOSOMAL PROTEIN S10; 1. DR PANTHER; PTHR12146:SF10; 40S RIBOSOMAL PROTEIN S10; 1. DR Pfam; PF03501; S10_plectin; 1. DR Genevisible; P46783; HS. 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="Small ribosomal subunit protein eS10" 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, ECO:0000269|PubMed:28685749, FT ECO:0000269|PubMed:32011234, ECO:0000269|PubMed:36302773" 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, ECO:0000269|PubMed:28685749, FT ECO:0000269|PubMed:32011234, ECO:0000269|PubMed:36302773" 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, ECO:0000269|PubMed:28685749, FT ECO:0000269|PubMed:32011234, ECO:0000269|PubMed:36302773" 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..17 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 18..25 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 33..35 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 36..39 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 42..54 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 57..63 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 73..83 FT /evidence="ECO:0007829|PDB:7R4X" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:7R4X" 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 //