RL13A_HUMAN
ID RL13A_HUMAN Reviewed; 203 AA.
AC P40429; A8K505;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=60S ribosomal protein L13a;
DE AltName: Full=23 kDa highly basic protein;
DE AltName: Full=Large ribosomal subunit protein uL13 {ECO:0000303|PubMed:24524803};
GN Name=RPL13A;
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=1282492; DOI=10.1016/s0888-7543(05)80117-x;
RA Price S.R., Nightingale M.S., Bobak D.A., Tsuchiya M., Moss J., Vaughan M.;
RT "Conservation of a 23-kDa human transplantation antigen in mammalian
RT species.";
RL Genomics 14:959-964(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10580157; DOI=10.1016/s0378-1119(99)00429-1;
RA Higa S., Yoshihama M., Tanaka T., Kenmochi N.;
RT "Gene organization and sequence of the region containing the ribosomal
RT protein genes RPL13A and RPS11 in the human genome and conserved features
RT in the mouse genome.";
RL Gene 240:371-377(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Lymph, Muscle, Pancreas, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-12; 38-49; 104-115 AND 135-159, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=14567916; DOI=10.1016/s0092-8674(03)00773-6;
RA Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E.,
RA Fox P.L.;
RT "Regulated release of L13a from the 60S ribosomal subunit as a mechanism of
RT transcript-specific translational control.";
RL Cell 115:187-198(2003).
RN [8]
RP ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY, 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 [9]
RP IDENTIFICATION IN THE GAIT COMPLEX.
RX PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
RA Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M.,
RA Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific
RT silencing of translation.";
RL Cell 119:195-208(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH EIF4G1.
RX PubMed=17218275; DOI=10.1016/j.molcel.2006.11.028;
RA Kapasi P., Chaudhuri S., Vyas K., Baus D., Komar A.A., Fox P.L.,
RA Merrick W.C., Mazumder B.;
RT "L13a blocks 48S assembly: role of a general initiation factor in mRNA-
RT specific translational control.";
RL Mol. Cell 25:113-126(2007).
RN [11]
RP FUNCTION.
RX PubMed=17921318; DOI=10.1261/rna.694007;
RA Chaudhuri S., Vyas K., Kapasi P., Komar A.A., Dinman J.D., Barik S.,
RA Mazumder B.;
RT "Human ribosomal protein L13a is dispensable for canonical ribosome
RT function but indispensable for efficient rRNA methylation.";
RL RNA 13:2224-2237(2007).
RN [12]
RP PHOSPHORYLATION AT SER-77, AND MUTAGENESIS OF SER-77.
RX PubMed=18995835; DOI=10.1016/j.molcel.2008.09.019;
RA Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.;
RT "DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating
RT inflammatory gene expression.";
RL Mol. Cell 32:371-382(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-191, AND IDENTIFICATION BY MASS
RP 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 [15]
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 [16]
RP FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
RX PubMed=23071094; DOI=10.1128/mcb.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
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 [20]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP 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 [23] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS).
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: Associated with ribosomes but is not required for canonical
CC ribosome function and has extra-ribosomal functions (PubMed:14567916,
CC PubMed:17218275, PubMed:23636399, PubMed:32669547). Component of the
CC GAIT (gamma interferon-activated inhibitor of translation) complex
CC which mediates interferon-gamma-induced transcript-selective
CC translation inhibition in inflammation processes (PubMed:23071094).
CC Upon interferon-gamma activation and subsequent phosphorylation
CC dissociates from the ribosome and assembles into the GAIT complex which
CC binds to stem loop-containing GAIT elements in the 3'-UTR of diverse
CC inflammatory mRNAs (such as ceruplasmin) and suppresses their
CC translation (PubMed:23071094). In the GAIT complex interacts with m7G
CC cap-bound eIF4G at or near the eIF3-binding site and blocks the
CC recruitment of the 43S ribosomal complex (PubMed:23071094). Involved in
CC methylation of rRNA (PubMed:17921318). {ECO:0000269|PubMed:14567916,
CC ECO:0000269|PubMed:17218275, ECO:0000269|PubMed:17921318,
CC ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the 60S ribosome (PubMed:14567916,
CC PubMed:12962325, PubMed:23636399, PubMed:32669547). Component of the
CC GAIT complex (PubMed:15479637). Interacts with EIF4G1
CC (PubMed:17218275). {ECO:0000269|PubMed:14567916,
CC ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:17218275,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399,
CC ECO:0000305|PubMed:14567916}.
CC -!- PTM: Phosphorylation at Ser-77 upon interferon-gamma treatment in
CC monocytes involves a DAPK1-DAPK3 kinase cascade and is causing release
CC from the ribosome, association with the GAIT complex and subsequent
CC involvement in transcript-selective translation inhibition.
CC {ECO:0000269|PubMed:14567916, ECO:0000269|PubMed:18995835}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P19253}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000305}.
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DR EMBL; X56932; CAA40254.1; -; mRNA.
DR EMBL; AB028893; BAA88214.1; -; Genomic_DNA.
DR EMBL; AK291120; BAF83809.1; -; mRNA.
DR EMBL; CH471177; EAW52495.1; -; Genomic_DNA.
DR EMBL; BC000514; AAH00514.1; -; mRNA.
DR EMBL; BC001675; AAH01675.1; -; mRNA.
DR EMBL; BC001836; AAH01836.1; -; mRNA.
DR EMBL; BC062537; AAH62537.1; -; mRNA.
DR EMBL; BC065236; AAH65236.1; -; mRNA.
DR EMBL; BC070223; AAH70223.1; -; mRNA.
DR EMBL; BC071929; AAH71929.1; -; mRNA.
DR CCDS; CCDS12768.1; -.
DR PIR; S29539; S29539.
DR RefSeq; NP_001257420.1; NM_001270491.1.
DR RefSeq; NP_036555.1; NM_012423.3.
DR PDB; 4UG0; EM; -; LO=1-203.
DR PDB; 4V6X; EM; 5.00 A; CO=1-203.
DR PDB; 5AJ0; EM; 3.50 A; AO=1-203.
DR PDB; 5LKS; EM; 3.60 A; LO=1-203.
DR PDB; 5T2C; EM; 3.60 A; I=1-203.
DR PDB; 6IP5; EM; 3.90 A; 2I=1-203.
DR PDB; 6IP6; EM; 4.50 A; 2I=1-203.
DR PDB; 6IP8; EM; 3.90 A; 2I=1-203.
DR PDB; 6LQM; EM; 3.09 A; V=1-203.
DR PDB; 6LSR; EM; 3.13 A; V=1-203.
DR PDB; 6LSS; EM; 3.23 A; V=1-203.
DR PDB; 6LU8; EM; 3.13 A; V=1-203.
DR PDB; 6OLE; EM; 3.10 A; P=5-199.
DR PDB; 6OLF; EM; 3.90 A; P=5-199.
DR PDB; 6OLG; EM; 3.40 A; AO=5-199.
DR PDB; 6OLI; EM; 3.50 A; P=5-199.
DR PDB; 6OLZ; EM; 3.90 A; AO=5-199.
DR PDB; 6OM0; EM; 3.10 A; P=5-199.
DR PDB; 6OM7; EM; 3.70 A; P=5-199.
DR PDB; 6QZP; EM; 2.90 A; LO=3-203.
DR PDB; 6W6L; EM; 3.84 A; P=1-203.
DR PDB; 6XA1; EM; 2.80 A; LO=3-203.
DR PDB; 6Y0G; EM; 3.20 A; LO=1-203.
DR PDB; 6Y2L; EM; 3.00 A; LO=1-203.
DR PDB; 6Y57; EM; 3.50 A; LO=1-203.
DR PDB; 6Y6X; EM; 2.80 A; LO=3-203.
DR PDB; 6Z6L; EM; 3.00 A; LO=1-203.
DR PDB; 6Z6M; EM; 3.10 A; LO=1-203.
DR PDB; 6Z6N; EM; 2.90 A; LO=1-203.
DR PDB; 6ZM7; EM; 2.70 A; LO=1-203.
DR PDB; 6ZME; EM; 3.00 A; LO=1-203.
DR PDB; 6ZMI; EM; 2.60 A; LO=1-203.
DR PDB; 6ZMO; EM; 3.10 A; LO=1-203.
DR PDB; 7BHP; EM; 3.30 A; LO=1-203.
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; P40429; -.
DR SMR; P40429; -.
DR BioGRID; 117068; 478.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P40429; -.
DR IntAct; P40429; 101.
DR MINT; P40429; -.
DR STRING; 9606.ENSP00000375730; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR MoonProt; P40429; -.
DR GlyGen; P40429; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40429; -.
DR MetOSite; P40429; -.
DR PhosphoSitePlus; P40429; -.
DR SwissPalm; P40429; -.
DR BioMuta; RPL13A; -.
DR DMDM; 730451; -.
DR EPD; P40429; -.
DR jPOST; P40429; -.
DR MassIVE; P40429; -.
DR MaxQB; P40429; -.
DR PaxDb; P40429; -.
DR PeptideAtlas; P40429; -.
DR PRIDE; P40429; -.
DR ProteomicsDB; 55374; -.
DR TopDownProteomics; P40429; -.
DR Antibodypedia; 45892; 110 antibodies from 23 providers.
DR DNASU; 23521; -.
DR Ensembl; ENST00000391857.9; ENSP00000375730.4; ENSG00000142541.18.
DR GeneID; 23521; -.
DR KEGG; hsa:23521; -.
DR MANE-Select; ENST00000391857.9; ENSP00000375730.4; NM_012423.4; NP_036555.1.
DR UCSC; uc002pny.5; human.
DR CTD; 23521; -.
DR DisGeNET; 23521; -.
DR GeneCards; RPL13A; -.
DR HGNC; HGNC:10304; RPL13A.
DR HPA; ENSG00000142541; Low tissue specificity.
DR MIM; 619225; gene.
DR neXtProt; NX_P40429; -.
DR OpenTargets; ENSG00000142541; -.
DR PharmGKB; PA38122; -.
DR VEuPathDB; HostDB:ENSG00000142541; -.
DR eggNOG; KOG3204; Eukaryota.
DR GeneTree; ENSGT00390000010799; -.
DR InParanoid; P40429; -.
DR OMA; GMLPWKT; -.
DR OrthoDB; 1312756at2759; -.
DR PhylomeDB; P40429; -.
DR TreeFam; TF300159; -.
DR PathwayCommons; P40429; -.
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; P40429; -.
DR SIGNOR; P40429; -.
DR BioGRID-ORCS; 23521; 551 hits in 1062 CRISPR screens.
DR ChiTaRS; RPL13A; human.
DR GeneWiki; RPL13A; -.
DR GenomeRNAi; 23521; -.
DR Pharos; P40429; Tbio.
DR PRO; PR:P40429; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P40429; protein.
DR Bgee; ENSG00000142541; Expressed in left ovary and 93 other tissues.
DR ExpressionAtlas; P40429; baseline and differential.
DR Genevisible; P40429; HS.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR GO; GO:0015934; C:large ribosomal subunit; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:1901194; P:negative regulation of formation of translation preinitiation complex; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR CDD; cd00392; Ribosomal_L13; 1.
DR Gene3D; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR005755; Ribosomal_L13_euk/arc.
DR InterPro; IPR036899; Ribosomal_L13_sf.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01077; L13_A_E; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325,
FT ECO:0000269|PubMed:25489052, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..203
FT /note="60S ribosomal protein L13a"
FT /id="PRO_0000133769"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12962325,
FT ECO:0000269|PubMed:25489052, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 59
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P19253"
FT MOD_RES 77
FT /note="Phosphoserine; by ZIPK/DAPK3"
FT /evidence="ECO:0000269|PubMed:18995835"
FT MOD_RES 140
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P19253"
FT MOD_RES 191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 77
FT /note="S->A: Loss of interferon-gamma induced
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:18995835"
SQ SEQUENCE 203 AA; 23577 MW; 3E80D0AB77A0D406 CRC64;
MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ
AEKNVEKKID KYTEVLKTHG LLV
