RL23A_HUMAN
ID RL23A_HUMAN Reviewed; 156 AA.
AC P62750; B2R5B2; P29316; P39024; Q92774;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=60S ribosomal protein L23a;
DE AltName: Full=Large ribosomal subunit protein uL23 {ECO:0000303|PubMed:24524803};
GN Name=RPL23A;
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].
RC TISSUE=Melanoma;
RA Jiang H., Lin J., Tao J., Fisher P.B.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Reddy K.B., Lin C.W., Howe P.H.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8662070; DOI=10.1007/bf02660056;
RA Fan W., Cai W., Parimoo S., Lennon G.G., Weissman S.M.;
RT "Identification of seven new human MHC class I region genes around the HLA-
RT F locus.";
RL Immunogenetics 44:97-103(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9417910; DOI=10.1006/geno.1997.5038;
RA Fan W., Christensen M., Eichler E., Zhang X., Lennon G.;
RT "Cloning, sequencing, gene organization, and localization of the human
RT ribosomal protein RPL23A gene.";
RL Genomics 46:234-239(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-156.
RC TISSUE=Liver;
RA Bonaldo M., Soares M.B.;
RT "Identification and localization of six liver expressed genes on human
RT chromosome 13.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH IPO5; IPO7; KPNB1 AND TNPO1, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
RA Jaekel S., Goerlich D.;
RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of
RT ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [10]
RP INTERACTION WITH INTERACTION WITH IPO5; IPO7; IPO8; KPNB1 AND TNPO1.
RX PubMed=11682607; DOI=10.1242/jcs.114.19.3479;
RA Dean K.A., von Ahsen O., Goerlich D., Fried H.M.;
RT "Signal recognition particle protein 19 is imported into the nucleus by
RT importin 8 (RanBP8) and transportin.";
RL J. Cell Sci. 114:3479-3485(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, 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 [14]
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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
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 [18]
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 [19]
RP FUNCTION, INTERACTION WITH LYAR; GNL2 AND MDM2, AND INDUCTION BY GNL2.
RX PubMed=26203195; DOI=10.1074/jbc.m115.637280;
RA Datta D., Anbarasu K., Rajabather S., Priya R.S., Desai P., Mahalingam S.;
RT "Nucleolar GTP-binding protein-1 (NGP-1) promotes G1 to S phase transition
RT by activating cyclin-dependent kinase inhibitor p21 Cip1/Waf1.";
RL J. Biol. Chem. 290:21536-21552(2015).
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-14, 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 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 [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).
RN [24]
RP VARIANT THR-99.
RX PubMed=22431104; DOI=10.1002/humu.22081;
RA Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A., Davies S.M.,
RA Kattamis A., Doherty L., Landowski M., Buros C., Ghazvinian R., Sieff C.A.,
RA Newburger P.E., Niewiadomska E., Matysiak M., Glader B., Atsidaftos E.,
RA Lipton J.M., Gleizes P.E., Beggs A.H.;
RT "Frameshift mutation in p53 regulator RPL26 is associated with multiple
RT physical abnormalities and a specific pre-ribosomal RNA processing defect
RT in diamond-blackfan anemia.";
RL Hum. Mutat. 33:1037-1044(2012).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). The ribosome is a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:23636399,
CC PubMed:32669547). Binds a specific region on the 26S rRNA
CC (PubMed:23636399, PubMed:32669547). May promote p53/TP53 degradation
CC possibly through the stimulation of MDM2-mediated TP53
CC polyubiquitination (PubMed:26203195). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:26203195, ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). Interacts with LYAR and GNL2 (PubMed:26203195).
CC Interacts with MDM2; this interaction may promote MDM2-mediated
CC p53/TP53 polyubiquitination (PubMed:26203195). Directly interacts (via
CC BIB domain) with IPO5, IPO7, KPNB1 and TNPO1; these interactions are
CC involved in RPL23A nuclear import for the assembly of ribosomal
CC subunits (PubMed:9687515, PubMed:11682607). Interacts with IPO8
CC (PubMed:11682607). {ECO:0000269|PubMed:11682607,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:26203195,
CC ECO:0000269|PubMed:32669547, ECO:0000269|PubMed:9687515}.
CC -!- INTERACTION:
CC P62750; Q5S007: LRRK2; NbExp=2; IntAct=EBI-353254, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:9687515}. Nucleus {ECO:0000269|PubMed:9687515}.
CC Note=Although RPL23A is functional within the cytoplasm, the assembly
CC of ribosomal subunits occurs in the nucleus. RPL23A nuclear import is
CC mediated by IPO5/RanBP5, IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn.
CC {ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9687515}.
CC -!- INDUCTION: May be down-regulated by GNL2 (at protein level).
CC {ECO:0000269|PubMed:26203195}.
CC -!- DOMAIN: The N-terminal beta-like import receptor binding (BIB) domain
CC mediates interaction with IPO5, IPO7, KPNB1 and TNPO1.
CC {ECO:0000269|PubMed:9687515}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000250|UniProtKB:P62751}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P62751}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
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DR EMBL; U43701; AAB03210.1; -; mRNA.
DR EMBL; U02032; AAA03341.1; -; mRNA.
DR EMBL; U37230; AAB17510.1; -; mRNA.
DR EMBL; AF001689; AAC51934.1; -; Genomic_DNA.
DR EMBL; AK312123; BAG35059.1; -; mRNA.
DR EMBL; CH471159; EAW51132.1; -; Genomic_DNA.
DR EMBL; BC014459; AAH14459.1; -; mRNA.
DR EMBL; BC058041; AAH58041.1; -; mRNA.
DR EMBL; L13799; AAA35681.1; -; mRNA.
DR CCDS; CCDS11241.1; -.
DR RefSeq; NP_000975.2; NM_000984.5.
DR PDB; 4UG0; EM; -; LX=1-156.
DR PDB; 4V6X; EM; 5.00 A; CX=1-156.
DR PDB; 5AJ0; EM; 3.50 A; AX=1-156.
DR PDB; 5LKS; EM; 3.60 A; LX=1-156.
DR PDB; 5T2C; EM; 3.60 A; R=1-156.
DR PDB; 6IP5; EM; 3.90 A; 2R=1-156.
DR PDB; 6IP6; EM; 4.50 A; 2R=1-156.
DR PDB; 6IP8; EM; 3.90 A; 2R=1-156.
DR PDB; 6LQM; EM; 3.09 A; g=1-156.
DR PDB; 6LSR; EM; 3.13 A; g=1-156.
DR PDB; 6LSS; EM; 3.23 A; g=1-156.
DR PDB; 6LU8; EM; 3.13 A; g=1-156.
DR PDB; 6OLE; EM; 3.10 A; Y=39-155.
DR PDB; 6OLF; EM; 3.90 A; Y=39-155.
DR PDB; 6OLG; EM; 3.40 A; AX=39-155.
DR PDB; 6OLI; EM; 3.50 A; Y=39-155.
DR PDB; 6OLZ; EM; 3.90 A; AX=39-155.
DR PDB; 6OM0; EM; 3.10 A; Y=39-155.
DR PDB; 6OM7; EM; 3.70 A; Y=39-155.
DR PDB; 6QZP; EM; 2.90 A; LX=37-156.
DR PDB; 6SXO; EM; 3.30 A; LX=1-156.
DR PDB; 6W6L; EM; 3.84 A; Y=1-156.
DR PDB; 6XA1; EM; 2.80 A; LX=37-156.
DR PDB; 6Y0G; EM; 3.20 A; LX=1-156.
DR PDB; 6Y2L; EM; 3.00 A; LX=1-156.
DR PDB; 6Y57; EM; 3.50 A; LX=1-156.
DR PDB; 6Y6X; EM; 2.80 A; LX=37-156.
DR PDB; 6Z6L; EM; 3.00 A; LX=1-156.
DR PDB; 6Z6M; EM; 3.10 A; LX=1-156.
DR PDB; 6Z6N; EM; 2.90 A; LX=1-156.
DR PDB; 6ZM7; EM; 2.70 A; LX=1-156.
DR PDB; 6ZME; EM; 3.00 A; LX=1-156.
DR PDB; 6ZMI; EM; 2.60 A; LX=1-156.
DR PDB; 6ZMO; EM; 3.10 A; LX=1-156.
DR PDB; 7BHP; EM; 3.30 A; LX=1-156.
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; 6SXO; -.
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; P62750; -.
DR SMR; P62750; -.
DR BioGRID; 112067; 531.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62750; -.
DR IntAct; P62750; 113.
DR MINT; P62750; -.
DR STRING; 9606.ENSP00000389103; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB08437; Puromycin.
DR GlyGen; P62750; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62750; -.
DR MetOSite; P62750; -.
DR PhosphoSitePlus; P62750; -.
DR SwissPalm; P62750; -.
DR BioMuta; RPL23A; -.
DR DMDM; 51338637; -.
DR SWISS-2DPAGE; P62750; -.
DR EPD; P62750; -.
DR jPOST; P62750; -.
DR MassIVE; P62750; -.
DR MaxQB; P62750; -.
DR PaxDb; P62750; -.
DR PeptideAtlas; P62750; -.
DR PRIDE; P62750; -.
DR ProteomicsDB; 57421; -.
DR TopDownProteomics; P62750; -.
DR Antibodypedia; 26533; 274 antibodies from 26 providers.
DR DNASU; 6147; -.
DR Ensembl; ENST00000422514.7; ENSP00000389103.2; ENSG00000198242.14.
DR GeneID; 6147; -.
DR KEGG; hsa:6147; -.
DR MANE-Select; ENST00000422514.7; ENSP00000389103.2; NM_000984.6; NP_000975.2.
DR UCSC; uc002hci.4; human.
DR CTD; 6147; -.
DR DisGeNET; 6147; -.
DR GeneCards; RPL23A; -.
DR HGNC; HGNC:10317; RPL23A.
DR HPA; ENSG00000198242; Low tissue specificity.
DR MIM; 602326; gene.
DR neXtProt; NX_P62750; -.
DR OpenTargets; ENSG00000198242; -.
DR PharmGKB; PA34691; -.
DR VEuPathDB; HostDB:ENSG00000198242; -.
DR eggNOG; KOG1751; Eukaryota.
DR GeneTree; ENSGT00950000182901; -.
DR HOGENOM; CLU_037562_0_2_1; -.
DR InParanoid; P62750; -.
DR OMA; IPHVPRM; -.
DR OrthoDB; 1436090at2759; -.
DR PhylomeDB; P62750; -.
DR TreeFam; TF314116; -.
DR PathwayCommons; P62750; -.
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; P62750; -.
DR SIGNOR; P62750; -.
DR BioGRID-ORCS; 6147; 776 hits in 1047 CRISPR screens.
DR ChiTaRS; RPL23A; human.
DR GeneWiki; RPL23A; -.
DR GenomeRNAi; 6147; -.
DR Pharos; P62750; Tbio.
DR PRO; PR:P62750; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P62750; protein.
DR Bgee; ENSG00000198242; Expressed in left ovary and 97 other tissues.
DR ExpressionAtlas; P62750; baseline and differential.
DR Genevisible; P62750; 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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:1904841; F:TORC2 complex binding; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR019985; Ribosomal_L23.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR005633; Ribosomal_L23/L25_N.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR11620; PTHR11620; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR Pfam; PF03939; Ribosomal_L23eN; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR TIGRFAMs; TIGR03636; uL23_arch; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT CHAIN 2..156
FT /note="60S ribosomal protein L23a"
FT /id="PRO_0000129467"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..74
FT /note="Beta-like import receptor binding (BIB) domain"
FT /evidence="ECO:0000269|PubMed:9687515"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..64
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT MOD_RES 41
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 45
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62751"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 99
FT /note="I -> T (rare variant found in Diamond-Blackfan
FT anemia patients; unknown pathological significance;
FT dbSNP:rs151327030)"
FT /evidence="ECO:0000269|PubMed:22431104"
FT /id="VAR_069221"
FT CONFLICT 2
FT /note="A -> IP (in Ref. 2; AAA03341)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="K -> N (in Ref. 3; AAB17510)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="K -> S (in Ref. 3; AAB17510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17695 MW; 3980E77B47FAB70E CRC64;
MAPKAKKEAP APPKAEAKAK ALKAKKAVLK GVHSHKKKKI RTSPTFRRPK TLRLRRQPKY
PRKSAPRRNK LDHYAIIKFP LTTESAMKKI EDNNTLVFIV DVKANKHQIK QAVKKLYDID
VAKVNTLIRP DGEKKAYVRL APDYDALDVA NKIGII
