RL13_HUMAN
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 03-AUG-2022, entry version 208.
DE RecName: Full=60S ribosomal protein L13;
DE AltName: Full=Breast basic conserved protein 1;
DE AltName: Full=Large ribosomal subunit protein eL13 {ECO:0000303|PubMed:24524803};
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, and
RC 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}.
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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 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 AlphaFoldDB; P26373; -.
DR SMR; P26373; -.
DR BioGRID; 112057; 613.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P26373; -.
DR IntAct; P26373; 132.
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; P26373; -.
DR PeptideAtlas; P26373; -.
DR PRIDE; P26373; -.
DR ProteomicsDB; 25745; -.
DR ProteomicsDB; 54328; -. [P26373-1]
DR TopDownProteomics; P26373-1; -. [P26373-1]
DR TopDownProteomics; P26373-2; -. [P26373-2]
DR Antibodypedia; 17428; 145 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 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; NQQIPHN; -.
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; 824 hits in 1056 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 203 other tissues.
DR ExpressionAtlas; P26373; baseline and differential.
DR Genevisible; P26373; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
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; IC:FlyBase.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR HAMAP; MF_00499; Ribosomal_L13e; 1.
DR InterPro; IPR001380; Ribosomal_L13e.
DR InterPro; IPR018256; Ribosomal_L13e_CS.
DR PANTHER; PTHR11722; PTHR11722; 1.
DR Pfam; PF01294; Ribosomal_L13e; 1.
DR PROSITE; PS01104; RIBOSOMAL_L13E; 1.
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="60S ribosomal protein L13"
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
