ID   RL30_HUMAN              Reviewed;         115 AA.
AC   P62888; B2R591; P04645; Q502Z6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Large ribosomal subunit protein eL30 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L30;
GN   Name=RPL30;
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=Placenta;
RA   Filipenko M.L., Karpova G.G.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bhat K.S.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11875025; DOI=10.1101/gr.214202;
RA   Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA   Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT   "The human ribosomal protein genes: sequencing and comparative analysis of
RT   73 genes.";
RL   Genome Res. 12:379-390(2002).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic stem cell, and Mammary gland;
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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP   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-26, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP   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   IDENTIFICATION BY MASS SPECTROMETRY [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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-16, 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   [15]
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   [16]
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   [17]
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   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, 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   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).
RX   PubMed=22139155; DOI=10.1107/s1744309111045131;
RA   Kawaguchi A., Ose T., Yao M., Tanaka I.;
RT   "Crystallization and preliminary X-ray structure analysis of human
RT   ribosomal protein L30e.";
RL   Acta Crystallogr. F 67:1516-1518(2011).
RN   [20]
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   [21] {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 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). {ECO:0000269|PubMed:23636399,
CC       ECO:0000269|PubMed:32669547}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC   -!- INTERACTION:
CC       P62888; Q5S007: LRRK2; NbExp=3; IntAct=EBI-353116, EBI-5323863;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family.
CC       {ECO:0000305}.
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DR   EMBL; L05095; AAC15858.1; -; mRNA.
DR   EMBL; X79238; CAA55820.1; -; mRNA.
DR   EMBL; AB070559; BAB79491.1; -; Genomic_DNA.
DR   EMBL; AK312102; BAG35038.1; -; mRNA.
DR   EMBL; CH471060; EAW91770.1; -; Genomic_DNA.
DR   EMBL; BC032700; AAH32700.1; -; mRNA.
DR   EMBL; BC095426; AAH95426.1; -; mRNA.
DR   CCDS; CCDS34928.1; -.
DR   PIR; S45004; S45004.
DR   RefSeq; NP_000980.1; NM_000989.3.
DR   PDB; 3VI6; X-ray; 1.59 A; A=1-115.
DR   PDB; 4UG0; EM; -; Lc=1-115.
DR   PDB; 4V6X; EM; 5.00 A; Cc=1-115.
DR   PDB; 5AJ0; EM; 3.50 A; Ac=1-115.
DR   PDB; 5LKS; EM; 3.60 A; Lc=1-115.
DR   PDB; 5T2C; EM; 3.60 A; W=1-115.
DR   PDB; 6IP5; EM; 3.90 A; 2W=1-115.
DR   PDB; 6IP6; EM; 4.50 A; 2W=1-115.
DR   PDB; 6IP8; EM; 3.90 A; 2W=1-115.
DR   PDB; 6LQM; EM; 3.09 A; E=1-115.
DR   PDB; 6LSR; EM; 3.13 A; E=1-115.
DR   PDB; 6LSS; EM; 3.23 A; E=1-115.
DR   PDB; 6LU8; EM; 3.13 A; E=1-115.
DR   PDB; 6OLE; EM; 3.10 A; d=7-109.
DR   PDB; 6OLF; EM; 3.90 A; d=7-109.
DR   PDB; 6OLG; EM; 3.40 A; Ac=7-109.
DR   PDB; 6OLI; EM; 3.50 A; d=7-109.
DR   PDB; 6OLZ; EM; 3.90 A; Ac=7-109.
DR   PDB; 6OM0; EM; 3.10 A; d=7-109.
DR   PDB; 6OM7; EM; 3.70 A; d=7-109.
DR   PDB; 6QZP; EM; 2.90 A; Lc=9-106.
DR   PDB; 6W6L; EM; 3.84 A; d=1-115.
DR   PDB; 6XA1; EM; 2.80 A; Lc=9-106.
DR   PDB; 6Y0G; EM; 3.20 A; Lc=1-115.
DR   PDB; 6Y2L; EM; 3.00 A; Lc=1-115.
DR   PDB; 6Y57; EM; 3.50 A; Lc=1-115.
DR   PDB; 6Y6X; EM; 2.80 A; Lc=9-106.
DR   PDB; 6Z6L; EM; 3.00 A; Lc=1-115.
DR   PDB; 6Z6M; EM; 3.10 A; Lc=1-115.
DR   PDB; 6Z6N; EM; 2.90 A; Lc=1-115.
DR   PDB; 6ZM7; EM; 2.70 A; Lc=1-115.
DR   PDB; 6ZME; EM; 3.00 A; Lc=1-115.
DR   PDB; 6ZMI; EM; 2.60 A; Lc=1-115.
DR   PDB; 6ZMO; EM; 3.10 A; Lc=1-115.
DR   PDB; 7BHP; EM; 3.30 A; Lc=1-115.
DR   PDB; 7F5S; EM; 2.72 A; Lc=1-115.
DR   PDB; 7OW7; EM; 2.20 A; W=1-115.
DR   PDB; 7QVP; EM; 3.00 A; Lc/Mc=1-115.
DR   PDB; 7XNX; EM; 2.70 A; Lc=1-115.
DR   PDB; 7XNY; EM; 2.50 A; Lc=1-115.
DR   PDB; 8A3D; EM; 1.67 A; W=1-115.
DR   PDB; 8FKY; EM; 2.67 A; LO=1-115.
DR   PDB; 8FKZ; EM; 3.04 A; LO=1-115.
DR   PDB; 8FL2; EM; 2.67 A; LO=1-115.
DR   PDB; 8FL3; EM; 2.53 A; LO=1-115.
DR   PDB; 8FL4; EM; 2.89 A; LO=1-115.
DR   PDB; 8FL6; EM; 2.62 A; LO=1-115.
DR   PDB; 8FL7; EM; 2.55 A; LO=1-115.
DR   PDB; 8FL9; EM; 2.75 A; LO=1-115.
DR   PDB; 8FLA; EM; 2.63 A; LO=1-115.
DR   PDB; 8FLB; EM; 2.55 A; LO=1-115.
DR   PDB; 8FLC; EM; 2.76 A; LO=1-115.
DR   PDB; 8FLD; EM; 2.58 A; LO=1-115.
DR   PDB; 8FLE; EM; 2.48 A; LO=1-115.
DR   PDB; 8FLF; EM; 2.65 A; LO=1-115.
DR   PDB; 8G5Y; EM; 2.29 A; Lc=1-115.
DR   PDB; 8G5Z; EM; 2.64 A; Lc=9-106.
DR   PDB; 8G60; EM; 2.54 A; Lc=1-115.
DR   PDB; 8G61; EM; 2.94 A; Lc=1-115.
DR   PDB; 8G6J; EM; 2.80 A; Lc=1-115.
DR   PDB; 8GLP; EM; 1.67 A; Lc=1-115.
DR   PDB; 8IDT; EM; 2.80 A; E=1-115.
DR   PDB; 8IDY; EM; 3.00 A; E=1-115.
DR   PDB; 8IE3; EM; 3.30 A; E=1-115.
DR   PDB; 8INE; EM; 3.20 A; E=1-115.
DR   PDB; 8INF; EM; 3.00 A; E=1-115.
DR   PDB; 8INK; EM; 3.20 A; E=1-115.
DR   PDB; 8IPD; EM; 3.20 A; E=1-115.
DR   PDB; 8IPX; EM; 4.30 A; E=1-115.
DR   PDB; 8IPY; EM; 3.20 A; E=1-115.
DR   PDB; 8IR1; EM; 3.30 A; E=1-115.
DR   PDB; 8IR3; EM; 3.50 A; E=1-115.
DR   PDB; 8JDJ; EM; 2.50 A; h=1-115.
DR   PDB; 8JDK; EM; 2.26 A; h=1-115.
DR   PDB; 8JDL; EM; 2.42 A; h=1-115.
DR   PDB; 8JDM; EM; 2.67 A; h=1-115.
DR   PDBsum; 3VI6; -.
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; 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; 8G6J; -.
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; P62888; -.
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-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-29771; -.
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; P62888; -.
DR   BioGRID; 112075; 449.
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; P62888; -.
DR   IntAct; P62888; 182.
DR   MINT; P62888; -.
DR   STRING; 9606.ENSP00000428085; -.
DR   GlyGen; P62888; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62888; -.
DR   MetOSite; P62888; -.
DR   PhosphoSitePlus; P62888; -.
DR   SwissPalm; P62888; -.
DR   BioMuta; RPL30; -.
DR   DMDM; 51702805; -.
DR   CPTAC; CPTAC-434; -.
DR   CPTAC; CPTAC-435; -.
DR   EPD; P62888; -.
DR   jPOST; P62888; -.
DR   MassIVE; P62888; -.
DR   MaxQB; P62888; -.
DR   PaxDb; 9606-ENSP00000428085; -.
DR   PeptideAtlas; P62888; -.
DR   ProteomicsDB; 57445; -.
DR   Pumba; P62888; -.
DR   TopDownProteomics; P62888; -.
DR   Antibodypedia; 1242; 301 antibodies from 31 providers.
DR   DNASU; 6156; -.
DR   Ensembl; ENST00000287038.8; ENSP00000287038.3; ENSG00000156482.11.
DR   Ensembl; ENST00000521291.5; ENSP00000428085.1; ENSG00000156482.11.
DR   GeneID; 6156; -.
DR   KEGG; hsa:6156; -.
DR   MANE-Select; ENST00000287038.8; ENSP00000287038.3; NM_000989.4; NP_000980.1.
DR   UCSC; uc003yif.4; human.
DR   AGR; HGNC:10333; -.
DR   CTD; 6156; -.
DR   DisGeNET; 6156; -.
DR   GeneCards; RPL30; -.
DR   HGNC; HGNC:10333; RPL30.
DR   HPA; ENSG00000156482; Low tissue specificity.
DR   MIM; 180467; gene.
DR   neXtProt; NX_P62888; -.
DR   OpenTargets; ENSG00000156482; -.
DR   PharmGKB; PA34714; -.
DR   VEuPathDB; HostDB:ENSG00000156482; -.
DR   eggNOG; KOG2988; Eukaryota.
DR   GeneTree; ENSGT00390000012138; -.
DR   InParanoid; P62888; -.
DR   OMA; YFQGGNN; -.
DR   OrthoDB; 374852at2759; -.
DR   PhylomeDB; P62888; -.
DR   TreeFam; TF300252; -.
DR   PathwayCommons; P62888; -.
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; P62888; -.
DR   SIGNOR; P62888; -.
DR   BioGRID-ORCS; 6156; 688 hits in 1103 CRISPR screens.
DR   ChiTaRS; RPL30; human.
DR   GeneWiki; RPL30; -.
DR   GenomeRNAi; 6156; -.
DR   Pharos; P62888; Tbio.
DR   PRO; PR:P62888; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P62888; Protein.
DR   Bgee; ENSG00000156482; Expressed in parietal pleura and 208 other cell types or tissues.
DR   ExpressionAtlas; P62888; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   GO; GO:0006412; P:translation; TAS:UniProtKB.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   HAMAP; MF_00481; Ribosomal_eL30; 1.
DR   InterPro; IPR000231; Ribosomal_eL30.
DR   InterPro; IPR039109; Ribosomal_eL30-like.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR022991; Ribosomal_eL30_CS.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   PANTHER; PTHR11449:SF1; 60S RIBOSOMAL PROTEIN L30; 1.
DR   PANTHER; PTHR11449; RIBOSOMAL PROTEIN L30; 1.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
DR   PROSITE; PS00709; RIBOSOMAL_L30E_1; 1.
DR   PROSITE; PS00993; RIBOSOMAL_L30E_2; 1.
DR   SWISS-2DPAGE; P62888; -.
DR   Genevisible; P62888; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..115
FT                   /note="Large ribosomal subunit protein eL30"
FT                   /id="PRO_0000146120"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         26
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CROSSLNK        26
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   HELIX           15..24
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   HELIX           31..39
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   HELIX           54..66
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:3VI6"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:3VI6"
SQ   SEQUENCE   115 AA;  12784 MW;  95186B081E39748C CRC64;
     MVAAKKTKKS LESINSRLQL VMKSGKYVLG YKQTLKMIRQ GKAKLVILAN NCPALRKSEI
     EYYAMLAKTG VHHYSGNNIE LGTACGKYYR VCTLAIIDPG DSDIIRSMPE QTGEK
//