ID RL13_HUMAN Reviewed; 211 AA. AC P26373; B4DLX3; F5H1S2; Q3KQT8; Q567Q8; Q9BPX0; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 217. DE RecName: Full=Large ribosomal subunit protein eL13 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L13; DE AltName: Full=Breast basic conserved protein 1; GN Name=RPL13; Synonyms=BBC1; ORFNames=OK/SW-cl.46; 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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP THR-112. RX PubMed=1301162; DOI=10.1093/hmg/1.2.91; RA Adams S.M., Helps N.R., Sharp M.G.F., Brammar W.J., Walker R.A., RA Varley J.M.; RT "Isolation and characterization of a novel gene with differential RT expression in benign and malignant human breast tumours."; RL Hum. Mol. Genet. 1:91-96(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-112. RC TISSUE=Blood vessel, Brain, Cervix, Lung, Lymph, Pancreas, Placenta, RC and Uterus; 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 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-177, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-77 AND SER-106, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] 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 [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [16] 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 [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-145; LYS-174 AND RP LYS-177, AND IDENTIFICATION BY MASS 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 [18] RP INVOLVEMENT IN SEMDIST, VARIANT SEMDIST PRO-183, FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=31630789; DOI=10.1016/j.ajhg.2019.09.024; RA Le Caignec C., Ory B., Lamoureux F., O'Donohue M.F., Orgebin E., RA Lindenbaum P., Teletchea S., Saby M., Hurst A., Nelson K., Gilbert S.R., RA Wilnai Y., Zeitlin L., Segev E., Tesfaye R., Nizon M., Cogne B., RA Bezieau S., Geoffroy L., Hamel A., Mayrargue E., de Courtivron B., RA Decock-Giraudaud A., Charrier C., Pichon O., Retiere C., Redon R., RA Pepler A., McWalter K., Da Costa L., Toutain A., Gleizes P.E., RA Baud'huin M., Isidor B.; RT "RPL13 variants cause spondyloepimetaphyseal dysplasia with severe short RT stature."; RL Am. J. Hum. Genet. 105:1040-1047(2019). 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). RN [20] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8} RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x; RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.; RT "Structural snapshots of human pre-60S ribosomal particles before and after RT nuclear export."; RL Nat. Commun. 11:3542-3542(2020). CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex CC responsible for the synthesis of proteins in the cell (PubMed:31630789, CC PubMed:23636399, PubMed:32669547). The small ribosomal subunit (SSU) CC binds messenger RNAs (mRNAs) and translates the encoded message by CC selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). CC The large subunit (LSU) contains the ribosomal catalytic site termed CC the peptidyl transferase center (PTC), which catalyzes the formation of CC peptide bonds, thereby polymerizing the amino acids delivered by tRNAs CC into a polypeptide chain (Probable). The nascent polypeptides leave the CC ribosome through a tunnel in the LSU and interact with protein factors CC that function in enzymatic processing, targeting, and the membrane CC insertion of nascent chains at the exit of the ribosomal tunnel CC (Probable). As part of the LSU, it is probably required for its CC formation and the maturation of rRNAs (PubMed:31630789). Plays a role CC in bone development (PubMed:31630789). {ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:31630789, ECO:0000269|PubMed:32669547}. CC -!- SUBUNIT: Component of the 60S large ribosomal subunit (LSU). CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, CC ECO:0000305|PubMed:31630789}. CC -!- INTERACTION: CC P26373; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-356849, EBI-739624; CC P26373; P42858: HTT; NbExp=10; IntAct=EBI-356849, EBI-466029; CC P26373; Q5S007: LRRK2; NbExp=4; IntAct=EBI-356849, EBI-5323863; CC P26373; Q96DV4: MRPL38; NbExp=2; IntAct=EBI-356849, EBI-720441; CC P26373; P16333: NCK1; NbExp=2; IntAct=EBI-356849, EBI-389883; CC P26373; P27986: PIK3R1; NbExp=2; IntAct=EBI-356849, EBI-79464; CC P26373; Q15554: TERF2; NbExp=2; IntAct=EBI-356849, EBI-706637; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399, CC ECO:0000305|PubMed:31630789}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P26373-1; Sequence=Displayed; CC Name=2; CC IsoId=P26373-2; Sequence=VSP_046028; CC -!- TISSUE SPECIFICITY: Higher levels of expression in benign breast CC lesions than in carcinomas. {ECO:0000269|PubMed:1301162}. CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Isidor-Toutain type CC (SEMDIST) [MIM:618728]: An autosomal dominant bone disease CC characterized by early postnatal growth deficiency, severe short CC stature, genu varum, platyspondyly and severe epiphyseal and CC metaphyseal changes in the lower limbs. {ECO:0000269|PubMed:31630789}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 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; X64707; CAA45963.1; -; mRNA. DR EMBL; AB062392; BAB93479.1; -; mRNA. DR EMBL; AK297198; BAG59685.1; -; mRNA. DR EMBL; AC092123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004954; AAH04954.1; -; mRNA. DR EMBL; BC007345; AAH07345.1; -; mRNA. DR EMBL; BC007563; AAH07563.1; -; mRNA. DR EMBL; BC007805; AAH07805.1; -; mRNA. DR EMBL; BC010994; AAH10994.1; -; mRNA. DR EMBL; BC013078; AAH13078.1; -; mRNA. DR EMBL; BC014167; AAH14167.1; -; mRNA. DR EMBL; BC020804; AAH20804.1; -; mRNA. DR EMBL; BC027463; AAH27463.1; -; mRNA. DR EMBL; BC063378; AAH63378.1; -; mRNA. DR EMBL; BC093063; AAH93063.1; -; mRNA. DR EMBL; BC106058; AAI06059.1; -; mRNA. DR CCDS; CCDS10979.1; -. [P26373-1] DR CCDS; CCDS58492.1; -. [P26373-2] DR PIR; S23753; S23753. DR RefSeq; NP_000968.2; NM_000977.3. [P26373-1] DR RefSeq; NP_001230059.1; NM_001243130.1. DR RefSeq; NP_001230060.1; NM_001243131.1. [P26373-2] DR RefSeq; NP_150254.1; NM_033251.2. [P26373-1] DR PDB; 4UG0; EM; -; LL=1-211. DR PDB; 4V6X; EM; 5.00 A; CL=1-211. DR PDB; 5AJ0; EM; 3.50 A; AL=1-211. DR PDB; 5LKS; EM; 3.60 A; LL=1-211. DR PDB; 5T2C; EM; 3.60 A; r=1-211. DR PDB; 6IP5; EM; 3.90 A; 2F=1-211. DR PDB; 6IP6; EM; 4.50 A; 2F=1-211. DR PDB; 6IP8; EM; 3.90 A; 2F=1-211. DR PDB; 6LQM; EM; 3.09 A; Q=1-211. DR PDB; 6LSR; EM; 3.13 A; Q=1-211. DR PDB; 6LSS; EM; 3.23 A; Q=1-211. DR PDB; 6LU8; EM; 3.13 A; Q=1-211. DR PDB; 6OLE; EM; 3.10 A; M=2-206. DR PDB; 6OLF; EM; 3.90 A; M=2-206. DR PDB; 6OLG; EM; 3.40 A; AL=2-206. DR PDB; 6OLI; EM; 3.50 A; M=2-206. DR PDB; 6OLZ; EM; 3.90 A; AL=2-206. DR PDB; 6OM0; EM; 3.10 A; M=2-206. DR PDB; 6OM7; EM; 3.70 A; M=2-206. DR PDB; 6QZP; EM; 2.90 A; LL=2-211. DR PDB; 6W6L; EM; 3.84 A; M=1-211. DR PDB; 6XA1; EM; 2.80 A; LL=2-205. DR PDB; 6Y0G; EM; 3.20 A; LL=1-211. DR PDB; 6Y2L; EM; 3.00 A; LL=1-211. DR PDB; 6Y57; EM; 3.50 A; LL=1-211. DR PDB; 6Y6X; EM; 2.80 A; LL=2-211. DR PDB; 6Z6L; EM; 3.00 A; LL=1-211. DR PDB; 6Z6M; EM; 3.10 A; LL=1-211. DR PDB; 6Z6N; EM; 2.90 A; LL=1-211. DR PDB; 6ZM7; EM; 2.70 A; LL=1-211. DR PDB; 6ZME; EM; 3.00 A; LL=1-211. DR PDB; 6ZMI; EM; 2.60 A; LL=1-211. DR PDB; 6ZMO; EM; 3.10 A; LL=1-211. DR PDB; 7BHP; EM; 3.30 A; LL=1-211. DR PDB; 7F5S; EM; 2.72 A; LL=1-211. DR PDB; 7OW7; EM; 2.20 A; r=1-211. DR PDB; 7QVP; EM; 3.00 A; LL/ML=1-211. DR PDB; 7XNX; EM; 2.70 A; LL=1-211. DR PDB; 7XNY; EM; 2.50 A; LL=1-211. DR PDB; 8A3D; EM; 1.67 A; r=1-211. DR PDB; 8FKP; EM; 2.85 A; L6=1-211. DR PDB; 8FKQ; EM; 2.76 A; L6=1-211. DR PDB; 8FKR; EM; 2.89 A; L6=1-211. DR PDB; 8FKS; EM; 2.88 A; L6=1-211. DR PDB; 8FKT; EM; 2.81 A; L6=1-211. DR PDB; 8FKU; EM; 2.82 A; L6=1-211. DR PDB; 8FKV; EM; 2.47 A; L6=1-211. DR PDB; 8FKW; EM; 2.50 A; L6=1-211. DR PDB; 8FKX; EM; 2.59 A; L6=1-211. DR PDB; 8FKY; EM; 2.67 A; L6=1-211. DR PDB; 8FKZ; EM; 3.04 A; L6=1-211. DR PDB; 8FL2; EM; 2.67 A; L6=1-211. DR PDB; 8FL3; EM; 2.53 A; L6=1-211. DR PDB; 8FL4; EM; 2.89 A; L6=1-211. DR PDB; 8FL6; EM; 2.62 A; L6=1-211. DR PDB; 8FL7; EM; 2.55 A; L6=1-211. DR PDB; 8FL9; EM; 2.75 A; L6=1-211. DR PDB; 8FLA; EM; 2.63 A; L6=1-211. DR PDB; 8FLB; EM; 2.55 A; L6=1-211. DR PDB; 8FLC; EM; 2.76 A; L6=1-211. DR PDB; 8FLD; EM; 2.58 A; L6=1-211. DR PDB; 8FLE; EM; 2.48 A; L6=1-211. DR PDB; 8FLF; EM; 2.65 A; L6=1-211. DR PDB; 8G5Y; EM; 2.29 A; LL=1-211. DR PDB; 8G5Z; EM; 2.64 A; LL=2-207. DR PDB; 8G60; EM; 2.54 A; LL=1-211. DR PDB; 8G61; EM; 2.94 A; LL=1-211. DR PDB; 8GLP; EM; 1.67 A; LL=1-211. DR PDB; 8IDT; EM; 2.80 A; Q=1-211. DR PDB; 8IDY; EM; 3.00 A; Q=1-211. DR PDB; 8IE3; EM; 3.30 A; Q=1-211. DR PDB; 8INE; EM; 3.20 A; Q=1-211. DR PDB; 8INF; EM; 3.00 A; Q=1-211. DR PDB; 8INK; EM; 3.20 A; Q=1-211. DR PDB; 8IPD; EM; 3.20 A; Q=1-211. DR PDB; 8IPX; EM; 4.30 A; Q=1-211. DR PDB; 8IPY; EM; 3.20 A; Q=1-211. DR PDB; 8IR1; EM; 3.30 A; Q=1-211. DR PDB; 8IR3; EM; 3.50 A; Q=1-211. DR PDB; 8JDJ; EM; 2.50 A; Q=1-211. DR PDB; 8JDK; EM; 2.26 A; Q=1-211. DR PDB; 8JDL; EM; 2.42 A; Q=1-211. DR PDB; 8JDM; EM; 2.67 A; Q=1-211. DR PDBsum; 4UG0; -. DR PDBsum; 4V6X; -. DR PDBsum; 5AJ0; -. DR PDBsum; 5LKS; -. DR PDBsum; 5T2C; -. DR PDBsum; 6IP5; -. DR PDBsum; 6IP6; -. DR PDBsum; 6IP8; -. DR PDBsum; 6LQM; -. DR PDBsum; 6LSR; -. DR PDBsum; 6LSS; -. DR PDBsum; 6LU8; -. 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; 6W6L; -. DR PDBsum; 6XA1; -. DR PDBsum; 6Y0G; -. DR PDBsum; 6Y2L; -. DR PDBsum; 6Y57; -. DR PDBsum; 6Y6X; -. DR PDBsum; 6Z6L; -. DR PDBsum; 6Z6M; -. DR PDBsum; 6Z6N; -. DR PDBsum; 6ZM7; -. DR PDBsum; 6ZME; -. DR PDBsum; 6ZMI; -. DR PDBsum; 6ZMO; -. DR PDBsum; 7BHP; -. DR PDBsum; 7F5S; -. DR PDBsum; 7OW7; -. DR PDBsum; 7QVP; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8A3D; -. DR PDBsum; 8FKP; -. DR PDBsum; 8FKQ; -. DR PDBsum; 8FKR; -. DR PDBsum; 8FKS; -. DR PDBsum; 8FKT; -. DR PDBsum; 8FKU; -. DR PDBsum; 8FKV; -. DR PDBsum; 8FKW; -. DR PDBsum; 8FKX; -. DR PDBsum; 8FKY; -. DR PDBsum; 8FKZ; -. DR PDBsum; 8FL2; -. DR PDBsum; 8FL3; -. DR PDBsum; 8FL4; -. DR PDBsum; 8FL6; -. DR PDBsum; 8FL7; -. DR PDBsum; 8FL9; -. DR PDBsum; 8FLA; -. DR PDBsum; 8FLB; -. DR PDBsum; 8FLC; -. DR PDBsum; 8FLD; -. DR PDBsum; 8FLE; -. DR PDBsum; 8FLF; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8GLP; -. DR PDBsum; 8IDT; -. DR PDBsum; 8IDY; -. DR PDBsum; 8IE3; -. DR PDBsum; 8INE; -. DR PDBsum; 8INF; -. DR PDBsum; 8INK; -. DR PDBsum; 8IPD; -. DR PDBsum; 8IPX; -. DR PDBsum; 8IPY; -. DR PDBsum; 8IR1; -. DR PDBsum; 8IR3; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR AlphaFoldDB; P26373; -. DR EMDB; EMD-0948; -. DR EMDB; EMD-0963; -. DR EMDB; EMD-0964; -. DR EMDB; EMD-0978; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10709; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-12189; -. DR EMDB; EMD-13094; -. DR EMDB; EMD-14181; -. DR EMDB; EMD-15113; -. DR EMDB; EMD-29252; -. DR EMDB; EMD-29253; -. DR EMDB; EMD-29254; -. DR EMDB; EMD-29255; -. DR EMDB; EMD-29256; -. DR EMDB; EMD-29257; -. DR EMDB; EMD-29258; -. DR EMDB; EMD-29259; -. DR EMDB; EMD-29260; -. DR EMDB; EMD-29261; -. DR EMDB; EMD-29262; -. DR EMDB; EMD-29265; -. DR EMDB; EMD-29266; -. DR EMDB; EMD-29267; -. DR EMDB; EMD-29268; -. DR EMDB; EMD-29269; -. DR EMDB; EMD-29271; -. DR EMDB; EMD-29272; -. DR EMDB; EMD-29273; -. DR EMDB; EMD-29274; -. 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-31465; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-35370; -. DR EMDB; EMD-35371; -. DR EMDB; EMD-35375; -. DR EMDB; EMD-35596; -. DR EMDB; EMD-35597; -. DR EMDB; EMD-35599; -. DR EMDB; EMD-35639; -. DR EMDB; EMD-35649; -. DR EMDB; EMD-35651; -. DR EMDB; EMD-35672; -. DR EMDB; EMD-35673; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P26373; -. DR BioGRID; 112057; 681. DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit. DR ComplexPortal; CPX-7664; 60S cytosolic large ribosomal subunit, testis-specific variant. DR ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant. DR CORUM; P26373; -. DR IntAct; P26373; 143. DR MINT; P26373; -. DR STRING; 9606.ENSP00000307889; -. DR GlyGen; P26373; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P26373; -. DR MetOSite; P26373; -. DR PhosphoSitePlus; P26373; -. DR SwissPalm; P26373; -. DR BioMuta; RPL13; -. DR DMDM; 21903462; -. DR EPD; P26373; -. DR jPOST; P26373; -. DR MassIVE; P26373; -. DR MaxQB; P26373; -. DR PaxDb; 9606-ENSP00000307889; -. DR PeptideAtlas; P26373; -. DR ProteomicsDB; 25745; -. DR ProteomicsDB; 54328; -. [P26373-1] DR Pumba; P26373; -. DR TopDownProteomics; P26373-1; -. [P26373-1] DR TopDownProteomics; P26373-2; -. [P26373-2] DR Antibodypedia; 17428; 167 antibodies from 27 providers. DR DNASU; 6137; -. DR Ensembl; ENST00000311528.10; ENSP00000307889.5; ENSG00000167526.14. [P26373-1] DR Ensembl; ENST00000393099.3; ENSP00000376811.3; ENSG00000167526.14. [P26373-1] DR Ensembl; ENST00000452368.7; ENSP00000438959.2; ENSG00000167526.14. [P26373-2] DR Ensembl; ENST00000567815.5; ENSP00000455009.1; ENSG00000167526.14. [P26373-1] DR GeneID; 6137; -. DR KEGG; hsa:6137; -. DR MANE-Select; ENST00000311528.10; ENSP00000307889.5; NM_000977.4; NP_000968.2. DR UCSC; uc002fnm.3; human. [P26373-1] DR AGR; HGNC:10303; -. DR CTD; 6137; -. DR DisGeNET; 6137; -. DR GeneCards; RPL13; -. DR HGNC; HGNC:10303; RPL13. DR HPA; ENSG00000167526; Low tissue specificity. DR MalaCards; RPL13; -. DR MIM; 113703; gene. DR MIM; 618728; phenotype. DR neXtProt; NX_P26373; -. DR OpenTargets; ENSG00000167526; -. DR PharmGKB; PA34670; -. DR VEuPathDB; HostDB:ENSG00000167526; -. DR eggNOG; KOG3295; Eukaryota. DR GeneTree; ENSGT00390000007818; -. DR HOGENOM; CLU_075696_1_0_1; -. DR InParanoid; P26373; -. DR OMA; IQKNHFR; -. DR OrthoDB; 150071at2759; -. DR PhylomeDB; P26373; -. DR TreeFam; TF300073; -. DR PathwayCommons; P26373; -. 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; P26373; -. DR SIGNOR; P26373; -. DR BioGRID-ORCS; 6137; 860 hits in 1136 CRISPR screens. DR ChiTaRS; RPL13; human. DR GeneWiki; RPL13; -. DR GenomeRNAi; 6137; -. DR Pharos; P26373; Tbio. DR PRO; PR:P26373; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P26373; Protein. DR Bgee; ENSG00000167526; Expressed in left ovary and 205 other cell types or tissues. DR ExpressionAtlas; P26373; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. 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:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. 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:UniProtKB. DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl. DR GO; GO:0060348; P:bone development; IMP:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0006412; P:translation; TAS:ProtInc. DR Gene3D; 1.20.5.110; -; 1. DR HAMAP; MF_00499; Ribosomal_eL13; 1. DR InterPro; IPR001380; Ribosomal_eL13. DR InterPro; IPR018256; Ribosomal_eL13_CS. DR PANTHER; PTHR11722; 60S RIBOSOMAL PROTEIN L13; 1. DR PANTHER; PTHR11722:SF4; 60S RIBOSOMAL PROTEIN L13; 1. DR Pfam; PF01294; Ribosomal_L13e; 1. DR PROSITE; PS01104; RIBOSOMAL_L13E; 1. DR Genevisible; P26373; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Disease variant; Dwarfism; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT CHAIN 1..211 FT /note="Large ribosomal subunit protein eL13" FT /id="PRO_0000192919" FT MOD_RES 16 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:23186163" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 177 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 123 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 145 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 174 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 174 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 177 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 88..134 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046028" FT VARIANT 112 FT /note="A -> T (in dbSNP:rs9930567)" FT /evidence="ECO:0000269|PubMed:1301162, FT ECO:0000269|PubMed:15489334" FT /id="VAR_051801" FT VARIANT 170 FT /note="T -> P (in dbSNP:rs1062450)" FT /id="VAR_051802" FT VARIANT 183 FT /note="R -> P (in SEMDIST)" FT /evidence="ECO:0000269|PubMed:31630789" FT /id="VAR_083551" FT CONFLICT 9 FT /note="V -> A (in Ref. 3; BAG59685)" FT /evidence="ECO:0000305" SQ SEQUENCE 211 AA; 24261 MW; DB9FC57768E6BEDE CRC64; MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPVRNV YKKEKARVIT EEEKNFKAFA SLRMARANAR LFGIRAKRAK EAAEQDVEKK K //