ID RL10_HUMAN Reviewed; 214 AA. AC P27635; A3KQT0; D3DWW6; Q16470; Q2HXT7; Q53FH7; Q6FGN8; Q8TDA5; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 5. DT 27-MAR-2024, entry version 230. DE RecName: Full=Large ribosomal subunit protein uL16 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L10 {ECO:0000305}; DE AltName: Full=Laminin receptor homolog; DE AltName: Full=Protein QM; DE AltName: Full=Ribosomal protein L10 {ECO:0000312|HGNC:HGNC:10298}; DE AltName: Full=Tumor suppressor QM; GN Name=RPL10 {ECO:0000312|HGNC:HGNC:10298}; Synonyms=DXS648E, QM; 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]. RX PubMed=1658743; DOI=10.1093/nar/19.20.5763; RA Dowdy S.F., Lai K.M., Weissman B.E., Matsui Y., Hogan B.L.M., RA Stanbridge E.S.; RT "The isolation and characterization of a novel cDNA demonstrating an RT altered mRNA level in nontumorigenic Wilms' microcell hybrid cells."; RL Nucleic Acids Res. 19:5763-5769(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1303197; DOI=10.1093/hmg/1.4.269; RA van den Ouweland A.M.W., Kioschis P., Verdijk M., Tamanini F., Toniolo D., RA Poustka A., van Oost B.A.; RT "Identification and characterization of a new gene in the human Xq28 RT region."; RL Hum. Mol. Genet. 1:269-273(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mammary gland; RA Kroepelin M.; RT "Sequence analysis of a novel gene expressed in normal and in tumor-derived RT tissue."; RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1339145; DOI=10.1093/hmg/1.7.529; RA Kaneko K., Kobayashi H., Onodera O., Miyatake T., Tsuji S.; RT "Genomic organization of a cDNA (QM) demonstrating an altered mRNA level in RT nontumorigenic Wilms' microcell hybrid cells and its localization to RT Xq28."; RL Hum. Mol. Genet. 1:529-533(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-202. RX PubMed=12138090; DOI=10.1074/jbc.m201859200; RA Oh H.S., Kwon H., Sun S.K., Yang C.-H.; RT "QM, a putative tumor suppressor, regulates proto-oncogene c-Yes."; RL J. Biol. Chem. 277:36489-36498(2002). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-202. RC TISSUE=Mammary cancer, Ovarian carcinoma, Pancreatic cancer, and RC Prostatic carcinoma; RX PubMed=16627977; DOI=10.4161/cbt.5.5.2610; RA Shen X.J., Ali-Fehmi R., Weng C.R., Sarkar F.H., Grignon D., Liao D.J.; RT "Loss of heterozygosity and microsatellite instability at the Xq28 and the RT A/G heterozygosity of the QM gene are associated with ovarian cancer."; RL Cancer Biol. Ther. 5:523-528(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thymus; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=8733135; DOI=10.1093/hmg/5.5.659; RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.; RT "Long-range sequence analysis in Xq28: thirteen known and six candidate RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."; RL Hum. Mol. Genet. 5:659-668(1996). RN [10] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-202. RC TISSUE=Brain, Mammary gland, and Placenta; 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 [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-147. RX PubMed=1534224; DOI=10.1016/s0006-291x(05)80005-1; RA Bignon C., Roux-Dosseto M., Zeigler M.E., Wicha M.S., Martin P.M.; RT "cDNA cloning and genomic analysis of a new multigene family sharing common RT phylogenetic and expression profiles with the laminin receptor gene."; RL Biochem. Biophys. Res. Commun. 184:1165-1172(1992). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-214. 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 [15] RP PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, RP AND SUBUNIT. RX PubMed=12962325; DOI=10.1023/a:1025068419698; RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.; RT "Characterization and analysis of posttranslational modifications of the RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and RT Edman sequencing."; RL J. Protein Chem. 22:249-258(2003). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-182. RX PubMed=18258260; DOI=10.1016/j.jmb.2008.01.003; RA Nishimura M., Kaminishi T., Takemoto C., Kawazoe M., Yoshida T., Tanaka A., RA Sugano S., Shirouzu M., Ohkubo T., Yokoyama S., Kobayashi Y.; RT "Crystal structure of human ribosomal protein L10 core domain reveals RT eukaryote-specific motifs in addition to the conserved fold."; RL J. Mol. Biol. 377:421-430(2008). RN [23] RP INVOLVEMENT IN AUTSX5, AND VARIANTS MET-206 AND GLN-213. RX PubMed=16940977; DOI=10.1038/sj.mp.4001883; RA Klauck S.M., Felder B., Kolb-Kokocinski A., Schuster C., Chiocchetti A., RA Schupp I., Wellenreuther R., Schmoetzer G., Poustka F., RA Breitenbach-Koller L., Poustka A.; RT "Mutations in the ribosomal protein gene RPL10 suggest a novel modulating RT disease mechanism for autism."; RL Mol. Psychiatry 11:1073-1084(2006). RN [24] RP VARIANT GLN-213, AND INVOLVEMENT IN AUTSX5. RX PubMed=21567917; DOI=10.1002/ajmg.a.33977; RA Chiocchetti A., Pakalapati G., Duketis E., Wiemann S., Poustka A., RA Poustka F., Klauck S.M.; RT "Mutation and expression analyses of the ribosomal protein gene RPL10 in an RT extended German sample of patients with autism spectrum disorder."; RL Am. J. Med. Genet. A 155:1472-1475(2011). RN [25] RP VARIANT MRXS35 GLU-78, CHARACTERIZATION OF VARIANT MRXS35 GLU-78, RP INVOLVEMENT IN MRXS35, VARIANT ASN-202, CHARACTERIZATION OF VARIANTS RP ASN-202; MET-206 AND GLN-213, AND FUNCTION. RX PubMed=25316788; DOI=10.1534/genetics.114.168211; RA Brooks S.S., Wall A.L., Golzio C., Reid D.W., Kondyles A., Willer J.R., RA Botti C., Nicchitta C.V., Katsanis N., Davis E.E.; RT "A novel ribosomopathy caused by dysfunction of RPL10 disrupts RT neurodevelopment and causes X-linked microcephaly in humans."; RL Genetics 198:723-733(2014). RN [26] RP VARIANT MRXS35 SER-161. RX PubMed=25846674; DOI=10.1002/ajmg.a.37094; RA Thevenon J., Michot C., Bole C., Nitschke P., Nizon M., Faivre L., RA Munnich A., Lyonnet S., Bonnefont J.P., Portes V.D., Amiel J.; RT "RPL10 mutation segregating in a family with X-linked syndromic RT Intellectual Disability."; RL Am. J. Med. Genet. A 167A:1908-1912(2015). RN [27] RP VARIANT MRXS35 VAL-64, CHARACTERIZATION OF VARIANT MRXS35 VAL-64, AND RP FUNCTION. RX PubMed=26290468; DOI=10.1002/humu.22860; RA Zanni G., Kalscheuer V.M., Friedrich A., Barresi S., Alfieri P., RA Di Capua M., Haas S.A., Piccini G., Karl T., Klauck S.M., Bellacchio E., RA Emma F., Cappa M., Bertini E., Breitenbach-Koller L.; RT "A novel mutation in RPL10 (Ribosomal Protein L10) causes X-Linked RT intellectual disability, cerebellar hypoplasia, and spondylo-epiphyseal RT dysplasia."; RL Hum. Mutat. 36:1155-1158(2015). CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:26290468). CC Plays a role in the formation of actively translating ribosomes CC (PubMed:26290468). May play a role in the embryonic brain development CC (PubMed:25316788). {ECO:0000269|PubMed:25316788, CC ECO:0000269|PubMed:26290468, ECO:0000305|PubMed:12962325}. CC -!- SUBUNIT: Component of the large ribosomal subunit. Mature ribosomes CC consist of a small (40S) and a large (60S) subunit. The 40S subunit CC contains about 33 different proteins and 1 molecule of RNA (18S). The CC 60S subunit contains about 49 different proteins and 3 molecules of RNA CC (28S, 5.8S and 5S). {ECO:0000305|PubMed:12962325}. CC -!- INTERACTION: CC P27635; P54253: ATXN1; NbExp=3; IntAct=EBI-352398, EBI-930964; CC P27635; P12931: SRC; NbExp=6; IntAct=EBI-352398, EBI-621482; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ZWV3}. CC -!- DEVELOPMENTAL STAGE: Down-regulated during adipocyte, kidney, and heart CC differentiation. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q6ZWV3}. CC -!- PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:Q6ZWV3}. CC -!- DISEASE: Autism, X-linked 5 (AUTSX5) [MIM:300847]: A complex CC multifactorial, pervasive developmental disorder characterized by CC impairments in reciprocal social interaction and communication, CC restricted and stereotyped patterns of interests and activities, and CC the presence of developmental abnormalities by 3 years of age. Most CC individuals with autism also manifest moderate intellectual disability. CC {ECO:0000269|PubMed:16940977, ECO:0000269|PubMed:21567917}. CC Note=Disease susceptibility is associated with variants affecting the CC gene represented in this entry. RPL10 is involved in autism only in CC rare cases. Two hypomorphic variants affecting the translation process CC have been found in families with autism spectrum disorders, suggesting CC that aberrant translation may play a role in disease mechanisms. CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 35 CC (MRXS35) [MIM:300998]: A syndrome characterized by intellectual CC deficit, delayed psychomotor development, poor speech, and dysmorphic CC features. {ECO:0000269|PubMed:25316788, ECO:0000269|PubMed:25846674, CC ECO:0000269|PubMed:26290468}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB22173.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42148/RPL10"; 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; M64241; AAA63253.1; -; mRNA. DR EMBL; M81806; AAA36021.1; -; Genomic_DNA. DR EMBL; M73791; AAA36378.1; -; mRNA. DR EMBL; S64169; AAB27665.1; -; Genomic_DNA. DR EMBL; S64168; AAB27665.1; JOINED; Genomic_DNA. DR EMBL; AF486812; AAL88713.1; -; mRNA. DR EMBL; DQ369703; ABC88559.1; -; mRNA. DR EMBL; DQ369704; ABC88560.1; -; mRNA. DR EMBL; DQ369705; ABC88561.1; -; mRNA. DR EMBL; DQ369706; ABC88562.1; -; mRNA. DR EMBL; DQ369707; ABC88563.1; -; mRNA. DR EMBL; DQ369708; ABC88564.1; -; mRNA. DR EMBL; DQ369709; ABC88565.1; -; mRNA. DR EMBL; DQ369710; ABC88566.1; -; mRNA. DR EMBL; DQ369711; ABC88567.1; -; mRNA. DR EMBL; DQ369712; ABC88568.1; -; mRNA. DR EMBL; DQ369713; ABC88569.1; -; mRNA. DR EMBL; DQ369714; ABC88570.1; -; mRNA. DR EMBL; DQ369715; ABC88571.1; -; mRNA. DR EMBL; DQ369716; ABC88572.1; -; mRNA. DR EMBL; CR456797; CAG33078.1; -; mRNA. DR EMBL; CR542069; CAG46866.1; -; mRNA. DR EMBL; AK223309; BAD97029.1; -; mRNA. DR EMBL; L44140; AAA92646.1; -; Genomic_DNA. DR EMBL; BX936346; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX936347; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72737.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72739.1; -; Genomic_DNA. DR EMBL; BC003358; AAH03358.1; -; mRNA. DR EMBL; BC026276; AAH26276.1; -; mRNA. DR EMBL; BC071918; AAH71918.1; -; mRNA. DR EMBL; S35960; AAB22173.1; ALT_FRAME; mRNA. DR EMBL; AB007170; BAA28595.1; -; Genomic_DNA. DR CCDS; CCDS14746.1; -. DR PIR; A42735; A42735. DR RefSeq; NP_001243506.2; NM_001256577.2. DR RefSeq; NP_001243509.2; NM_001256580.2. DR RefSeq; NP_001290553.1; NM_001303624.1. DR RefSeq; NP_001290554.1; NM_001303625.1. DR RefSeq; NP_001290555.1; NM_001303626.1. DR RefSeq; NP_006004.3; NM_006013.4. DR PDB; 2PA2; X-ray; 2.50 A; A/B=34-182. DR PDB; 5AJ0; EM; 3.50 A; AI=1-214. DR PDB; 6OLE; EM; 3.10 A; K=3-213. DR PDB; 6OLF; EM; 3.90 A; K=3-213. DR PDB; 6OLG; EM; 3.40 A; AI=3-213. DR PDB; 6OLI; EM; 3.50 A; K=3-213. DR PDB; 6OLZ; EM; 3.90 A; AI=3-213. DR PDB; 6OM0; EM; 3.10 A; K=3-213. DR PDB; 6OM7; EM; 3.70 A; K=3-213. DR PDB; 6W6L; EM; 3.84 A; K=1-214. DR PDB; 7F5S; EM; 2.72 A; LI=1-214. DR PDB; 8A3D; EM; 1.67 A; p=1-214. DR PDB; 8FLD; EM; 2.58 A; BE=1-214. DR PDB; 8FLE; EM; 2.48 A; BE=1-214. DR PDB; 8FLF; EM; 2.65 A; BE=1-214. DR PDB; 8G5Y; EM; 2.29 A; LI=1-214. DR PDB; 8G5Z; EM; 2.64 A; LI=2-214. DR PDB; 8G60; EM; 2.54 A; LI=1-214. DR PDB; 8G61; EM; 2.94 A; LI=1-214. DR PDB; 8G6J; EM; 2.80 A; LI=1-214. DR PDB; 8GLP; EM; 1.67 A; LI=1-214. DR PDBsum; 2PA2; -. DR PDBsum; 5AJ0; -. DR PDBsum; 6OLE; -. DR PDBsum; 6OLF; -. DR PDBsum; 6OLG; -. DR PDBsum; 6OLI; -. DR PDBsum; 6OLZ; -. DR PDBsum; 6OM0; -. DR PDBsum; 6OM7; -. DR PDBsum; 6W6L; -. DR PDBsum; 7F5S; -. DR PDBsum; 8A3D; -. DR PDBsum; 8FLD; -. DR PDBsum; 8FLE; -. DR PDBsum; 8FLF; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR AlphaFoldDB; P27635; -. DR EMDB; EMD-15113; -. DR EMDB; EMD-29275; -. DR EMDB; EMD-29276; -. DR EMDB; EMD-29277; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-31465; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-40205; -. DR SMR; P27635; -. DR BioGRID; 112054; 708. DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit. DR ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant. DR CORUM; P27635; -. DR DIP; DIP-1133N; -. DR IntAct; P27635; 340. DR MINT; P27635; -. DR STRING; 9606.ENSP00000413436; -. DR DrugBank; DB11638; Artenimol. DR MoonProt; P27635; -. DR GlyGen; P27635; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P27635; -. DR MetOSite; P27635; -. DR PhosphoSitePlus; P27635; -. DR SwissPalm; P27635; -. DR BioMuta; RPL10; -. DR DMDM; 148887414; -. DR EPD; P27635; -. DR jPOST; P27635; -. DR MassIVE; P27635; -. DR MaxQB; P27635; -. DR PaxDb; 9606-ENSP00000413436; -. DR PeptideAtlas; P27635; -. DR ProteomicsDB; 54403; -. DR Pumba; P27635; -. DR TopDownProteomics; P27635; -. DR Antibodypedia; 1254; 324 antibodies from 31 providers. DR DNASU; 6134; -. DR Ensembl; ENST00000344746.8; ENSP00000341730.4; ENSG00000147403.18. DR Ensembl; ENST00000369817.7; ENSP00000358832.2; ENSG00000147403.18. DR GeneID; 6134; -. DR KEGG; hsa:6134; -. DR MANE-Select; ENST00000369817.7; ENSP00000358832.2; NM_006013.5; NP_006004.3. DR AGR; HGNC:10298; -. DR CTD; 6134; -. DR DisGeNET; 6134; -. DR GeneCards; RPL10; -. DR HGNC; HGNC:10298; RPL10. DR HPA; ENSG00000147403; Low tissue specificity. DR MalaCards; RPL10; -. DR MIM; 300847; phenotype. DR MIM; 300998; phenotype. DR MIM; 312173; gene. DR neXtProt; NX_P27635; -. DR OpenTargets; ENSG00000147403; -. DR Orphanet; 459070; X-linked intellectual disability-cerebellar hypoplasia-spondylo-epiphyseal dysplasia syndrome. DR Orphanet; 435938; X-linked microcephaly-growth retardation-prognathism-cryptorchidism syndrome. DR PharmGKB; PA34660; -. DR VEuPathDB; HostDB:ENSG00000147403; -. DR eggNOG; KOG0857; Eukaryota. DR GeneTree; ENSGT00390000003897; -. DR InParanoid; P27635; -. DR OMA; KLYGVHG; -. DR OrthoDB; 1116065at2759; -. DR PhylomeDB; P27635; -. DR TreeFam; TF300082; -. DR PathwayCommons; P27635; -. 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-72689; Formation of a pool of free 40S subunits. 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-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; P27635; -. DR SIGNOR; P27635; -. DR BioGRID-ORCS; 6134; 212 hits in 760 CRISPR screens. DR ChiTaRS; RPL10; human. DR EvolutionaryTrace; P27635; -. DR GeneWiki; RPL10; -. DR GenomeRNAi; 6134; -. DR Pharos; P27635; Tbio. DR PRO; PR:P27635; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P27635; Protein. DR Bgee; ENSG00000147403; Expressed in left ovary and 97 other cell types or tissues. DR ExpressionAtlas; P27635; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase. DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase. DR GO; GO:1990403; P:embryonic brain development; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:CAFA. DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB. DR GO; GO:0006412; P:translation; NAS:UniProtKB. DR CDD; cd01433; Ribosomal_L16_L10e; 1. DR Gene3D; 3.30.60.300; -; 1. DR Gene3D; 3.90.1170.10; Ribosomal protein L10e/L16; 1. DR InterPro; IPR047873; Ribosomal_uL16. DR InterPro; IPR018255; Ribosomal_uL16_CS_euk_arc. DR InterPro; IPR016180; Ribosomal_uL16_dom. DR InterPro; IPR001197; Ribosomal_uL16_euk_arch. DR InterPro; IPR036920; Ribosomal_uL16_sf. DR NCBIfam; TIGR00279; uL16_euk_arch; 1. DR PANTHER; PTHR11726; 60S RIBOSOMAL PROTEIN L10; 1. DR PANTHER; PTHR11726:SF10; 60S RIBOSOMAL PROTEIN L10; 1. DR Pfam; PF00252; Ribosomal_L16; 1. DR PIRSF; PIRSF005590; Ribosomal_L10; 1. DR SUPFAM; SSF54686; Ribosomal protein L16p/L10e; 1. DR PROSITE; PS01257; RIBOSOMAL_L10E; 1. DR Genevisible; P27635; HS. PE 1: Evidence at protein level; KW 3D-structure; Autism; Autism spectrum disorder; Citrullination; Cytoplasm; KW Developmental protein; Direct protein sequencing; Disease variant; KW Intellectual disability; Isopeptide bond; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Translation regulation; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12962325" FT CHAIN 2..214 FT /note="Large ribosomal subunit protein uL16" FT /id="PRO_0000147105" FT MOD_RES 32 FT /note="Citrulline" FT /evidence="ECO:0000250|UniProtKB:Q6ZWV3" FT CROSSLNK 175 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 188 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT VARIANT 64 FT /note="A -> V (in MRXS35; increased the formation of FT actively translating ribosomes when expressed in a yeast FT heterologous system)" FT /evidence="ECO:0000269|PubMed:26290468" FT /id="VAR_079288" FT VARIANT 78 FT /note="K -> E (in MRXS35; loss of function; fails to rescue FT embryonic brain development when expressed in a zebrafish FT heterologous system; dbSNP:rs1131692040)" FT /evidence="ECO:0000269|PubMed:25316788" FT /id="VAR_079289" FT VARIANT 161 FT /note="G -> S (in MRXS35; uncertain significance; FT dbSNP:rs1131692041)" FT /evidence="ECO:0000269|PubMed:25846674" FT /id="VAR_079290" FT VARIANT 202 FT /note="S -> N (rescues embryonic brain development when FT expressed in a zebrafish heterologous system; FT dbSNP:rs4909)" FT /evidence="ECO:0000269|PubMed:12138090, FT ECO:0000269|PubMed:1303197, ECO:0000269|PubMed:1339145, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1658743, FT ECO:0000269|PubMed:16627977, ECO:0000269|PubMed:25316788, FT ECO:0000269|PubMed:9582194, ECO:0000269|Ref.10, FT ECO:0000269|Ref.3, ECO:0000269|Ref.7, ECO:0000269|Ref.8" FT /id="VAR_006922" FT VARIANT 206 FT /note="L -> M (risk factor for AUTSX5; no effect on FT function; rescues embryonic brain development when FT expressed in a zebrafish heterologous system; FT dbSNP:rs387906727)" FT /evidence="ECO:0000269|PubMed:16940977, FT ECO:0000269|PubMed:25316788" FT /id="VAR_027795" FT VARIANT 213 FT /note="H -> Q (risk factor for AUTSX5; no effect on FT function; rescues embryonic brain development when FT expressed in a zebrafish heterologous system; FT dbSNP:rs782521991)" FT /evidence="ECO:0000269|PubMed:16940977, FT ECO:0000269|PubMed:21567917, ECO:0000269|PubMed:25316788" FT /id="VAR_027796" FT CONFLICT 23 FT /note="Missing (in Ref. 5; AAL88713)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="F -> L (in Ref. 8; BAD97029)" FT /evidence="ECO:0000305" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:2PA2" FT HELIX 62..80 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 133..140 FT /evidence="ECO:0007829|PDB:2PA2" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:2PA2" FT HELIX 145..155 FT /evidence="ECO:0007829|PDB:2PA2" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:2PA2" FT STRAND 163..169 FT /evidence="ECO:0007829|PDB:2PA2" SQ SEQUENCE 214 AA; 24577 MW; 0860CECC8BF674FE CRC64; MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLCG HMVSDEYEQL SSEALEAARI CANKYMVKSC GKDGFHIRVR LHPFHVIRIN KMLSCAGADR LQTGMRGAFG KPQGTVARVH IGQVIMSIRT KLQNKEHVIE ALRRAKFKFP GRQKIHISKK WGFTKFNADE FEDMVAEKRL IPDGCGVKYI PSRGPLDKWR ALHS //