RL10_HUMAN
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 03-AUG-2022, entry version 221.
DE RecName: Full=60S ribosomal protein L10 {ECO:0000305};
DE AltName: Full=Laminin receptor homolog;
DE AltName: Full=Large ribosomal subunit protein uL16 {ECO:0000303|PubMed:24524803};
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 SUSCEPTIBILITY TO AUTISM, AND VARIANTS AUTSX5 MET-206 AND
RP 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 AUTSX5 GLN-213.
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 CHARACTERIZATION OF VARIANTS AUTSX5 MET-206 AND GLN-213, INVOLVEMENT IN
RP MRXS35, VARIANT ASN-202, CHARACTERIZATION OF VARIANT ASN-202, 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 -!- 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 ECO:0000269|PubMed:25316788}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry. RPL10 is
CC involved in autism only in rare cases. Two hypomorphic variants
CC affecting the translation process have been found in families with
CC autism spectrum disorders, suggesting that aberrant translation may
CC 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="http://atlasgeneticsoncology.org/Genes/RPL10ID42148chXq28.html";
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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 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 AlphaFoldDB; P27635; -.
DR SMR; P27635; -.
DR BioGRID; 112054; 647.
DR CORUM; P27635; -.
DR DIP; DIP-1133N; -.
DR IntAct; P27635; 339.
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; P27635; -.
DR PeptideAtlas; P27635; -.
DR PRIDE; P27635; -.
DR ProteomicsDB; 54403; -.
DR TopDownProteomics; P27635; -.
DR Antibodypedia; 1254; 298 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 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 OrthoDB; 1215841at2759; -.
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; 179 hits in 687 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 95 other tissues.
DR ExpressionAtlas; P27635; baseline and differential.
DR Genevisible; P27635; HS.
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:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
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:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR InterPro; IPR001197; Ribosomal_L10e.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR018255; Ribosomal_L10e_CS.
DR PANTHER; PTHR11726; PTHR11726; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR00279; uL16_euk_arch; 1.
DR PROSITE; PS01257; RIBOSOMAL_L10E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autism; Autism spectrum disorder; Citrullination;
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="60S ribosomal protein L10"
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; unknown pathological
FT significance; 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 (in AUTSX5; associated with disease
FT susceptibility; no effect on function; rescues embryonic
FT brain development when expressed in a zebrafish
FT heterologous system; dbSNP:rs387906727)"
FT /evidence="ECO:0000269|PubMed:16940977,
FT ECO:0000269|PubMed:25316788"
FT /id="VAR_027795"
FT VARIANT 213
FT /note="H -> Q (in AUTSX5; associated with disease
FT susceptibility; no effect on function; rescues embryonic
FT brain development when expressed in a zebrafish
FT heterologous system; 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
