RL27_HUMAN
ID RL27_HUMAN Reviewed; 136 AA.
AC P61353; P08526; Q4G0A9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=60S ribosomal protein L27;
DE AltName: Full=Large ribosomal subunit protein eL27 {ECO:0000303|PubMed:24524803};
GN Name=RPL27;
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=Kidney;
RX PubMed=8148381; DOI=10.1016/0167-4781(94)90295-x;
RA Gallagher R.A., McClean P.M., Malik A.N.;
RT "Cloning and nucleotide sequence of a full length cDNA encoding ribosomal
RT protein L27 from human fetal kidney.";
RL Biochim. Biophys. Acta 1217:329-332(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bhat K.S.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Brain, Eye, 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 [5]
RP PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-93, AND IDENTIFICATION
RP 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 [8]
RP INTERACTION WITH RRPL1.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP FUNCTION, AND INVOLVEMENT IN DBA16.
RX PubMed=25424902; DOI=10.1111/bjh.13229;
RA Wang R., Yoshida K., Toki T., Sawada T., Uechi T., Okuno Y.,
RA Sato-Otsubo A., Kudo K., Kamimaki I., Kanezaki R., Shiraishi Y., Chiba K.,
RA Tanaka H., Terui K., Sato T., Iribe Y., Ohga S., Kuramitsu M.,
RA Hamaguchi I., Ohara A., Hara J., Goi K., Matsubara K., Koike K.,
RA Ishiguro A., Okamoto Y., Watanabe K., Kanno H., Kojima S., Miyano S.,
RA Kenmochi N., Ogawa S., Ito E.;
RT "Loss of function mutations in RPL27 and RPS27 identified by whole-exome
RT sequencing in Diamond-Blackfan anaemia.";
RL Br. J. Haematol. 168:854-864(2015).
RN [14]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [15]
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 [16]
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 [17] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25957688; DOI=10.1016/j.cell.2015.03.052;
RA Behrmann E., Loerke J., Budkevich T.V., Yamamoto K., Schmidt A.,
RA Penczek P.A., Vos M.R., Burger J., Mielke T., Scheerer P., Spahn C.M.;
RT "Structural snapshots of actively translating human ribosomes.";
RL Cell 161:845-857(2015).
RN [18] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
RN [19] {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:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC Required for proper rRNA processing and maturation of 28S and 5.8S
CC rRNAs (PubMed:25424902). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:25424902, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC Interacts with RRP1B (PubMed:20926688). Interacts with DHX33
CC (PubMed:26100019). {ECO:0000269|PubMed:20926688,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:26100019,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC P61353; P42858: HTT; NbExp=6; IntAct=EBI-352760, EBI-466029;
CC P61353; Q14684: RRP1B; NbExp=3; IntAct=EBI-352760, EBI-372051;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Rough endoplasmic reticulum {ECO:0000250|UniProtKB:A1XQU5}.
CC Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in
CC ribosomes that are associated with the rough endoplasmic reticulum (By
CC similarity). {ECO:0000250|UniProtKB:A1XQU5,
CC ECO:0000269|PubMed:25957688}.
CC -!- DISEASE: Diamond-Blackfan anemia 16 (DBA16) [MIM:617408]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies.
CC {ECO:0000269|PubMed:25424902}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family.
CC {ECO:0000305}.
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DR EMBL; L19527; AAA19815.1; -; mRNA.
DR EMBL; AB061851; BAB79492.1; -; Genomic_DNA.
DR EMBL; L05094; AAC15857.1; -; mRNA.
DR EMBL; BC001700; AAH01700.1; -; mRNA.
DR EMBL; BC002588; AAH02588.1; -; mRNA.
DR EMBL; BC007273; AAH07273.1; -; mRNA.
DR EMBL; BC010026; AAH10026.1; -; mRNA.
DR EMBL; BC098560; AAH98560.1; -; mRNA.
DR CCDS; CCDS11449.1; -.
DR PIR; S43505; S43505.
DR RefSeq; NP_000979.1; NM_000988.3.
DR PDB; 4UG0; EM; -; LZ=1-136.
DR PDB; 4V6X; EM; 5.00 A; CZ=1-136.
DR PDB; 5AJ0; EM; 3.50 A; AZ=1-136.
DR PDB; 5LKS; EM; 3.60 A; LZ=1-136.
DR PDB; 5T2C; EM; 3.60 A; T=1-136.
DR PDB; 6IP5; EM; 3.90 A; 2T=1-136.
DR PDB; 6IP6; EM; 4.50 A; 2T=1-136.
DR PDB; 6IP8; EM; 3.90 A; 2T=1-136.
DR PDB; 6LQM; EM; 3.09 A; i=1-136.
DR PDB; 6LSR; EM; 3.13 A; i=1-136.
DR PDB; 6LSS; EM; 3.23 A; i=1-136.
DR PDB; 6LU8; EM; 3.13 A; i=1-136.
DR PDB; 6OLE; EM; 3.10 A; a=3-136.
DR PDB; 6OLF; EM; 3.90 A; a=3-136.
DR PDB; 6OLG; EM; 3.40 A; AZ=3-136.
DR PDB; 6OLI; EM; 3.50 A; a=3-136.
DR PDB; 6OLZ; EM; 3.90 A; AZ=3-136.
DR PDB; 6OM0; EM; 3.10 A; a=3-136.
DR PDB; 6OM7; EM; 3.70 A; a=3-136.
DR PDB; 6QZP; EM; 2.90 A; LZ=2-136.
DR PDB; 6W6L; EM; 3.84 A; a=1-136.
DR PDB; 6XA1; EM; 2.80 A; LZ=2-136.
DR PDB; 6Y0G; EM; 3.20 A; LZ=1-136.
DR PDB; 6Y2L; EM; 3.00 A; LZ=1-136.
DR PDB; 6Y57; EM; 3.50 A; LZ=1-136.
DR PDB; 6Y6X; EM; 2.80 A; LZ=2-136.
DR PDB; 6Z6L; EM; 3.00 A; LZ=1-136.
DR PDB; 6Z6M; EM; 3.10 A; LZ=1-136.
DR PDB; 6Z6N; EM; 2.90 A; LZ=1-136.
DR PDB; 6ZM7; EM; 2.70 A; LZ=1-136.
DR PDB; 6ZME; EM; 3.00 A; LZ=1-136.
DR PDB; 6ZMI; EM; 2.60 A; LZ=1-136.
DR PDB; 6ZMO; EM; 3.10 A; LZ=1-136.
DR PDB; 7BHP; EM; 3.30 A; LZ=1-136.
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; P61353; -.
DR SMR; P61353; -.
DR BioGRID; 112074; 309.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P61353; -.
DR IntAct; P61353; 85.
DR MINT; P61353; -.
DR STRING; 9606.ENSP00000464813; -.
DR GlyGen; P61353; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61353; -.
DR MetOSite; P61353; -.
DR PhosphoSitePlus; P61353; -.
DR SwissPalm; P61353; -.
DR BioMuta; RPL27; -.
DR DMDM; 47117772; -.
DR SWISS-2DPAGE; P61353; -.
DR EPD; P61353; -.
DR jPOST; P61353; -.
DR MassIVE; P61353; -.
DR MaxQB; P61353; -.
DR PaxDb; P61353; -.
DR PeptideAtlas; P61353; -.
DR PRIDE; P61353; -.
DR ProteomicsDB; 57297; -.
DR TopDownProteomics; P61353; -.
DR Antibodypedia; 1240; 215 antibodies from 26 providers.
DR DNASU; 6155; -.
DR Ensembl; ENST00000253788.12; ENSP00000253788.5; ENSG00000131469.15.
DR Ensembl; ENST00000589037.5; ENSP00000467587.1; ENSG00000131469.15.
DR Ensembl; ENST00000589913.6; ENSP00000464813.1; ENSG00000131469.15.
DR GeneID; 6155; -.
DR KEGG; hsa:6155; -.
DR MANE-Select; ENST00000253788.12; ENSP00000253788.5; NM_000988.5; NP_000979.1.
DR UCSC; uc002icj.4; human.
DR CTD; 6155; -.
DR DisGeNET; 6155; -.
DR GeneCards; RPL27; -.
DR GeneReviews; RPL27; -.
DR HGNC; HGNC:10328; RPL27.
DR HPA; ENSG00000131469; Low tissue specificity.
DR MalaCards; RPL27; -.
DR MIM; 607526; gene.
DR MIM; 617408; phenotype.
DR neXtProt; NX_P61353; -.
DR OpenTargets; ENSG00000131469; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34707; -.
DR VEuPathDB; HostDB:ENSG00000131469; -.
DR eggNOG; KOG3418; Eukaryota.
DR GeneTree; ENSGT00390000010721; -.
DR HOGENOM; CLU_067359_0_1_1; -.
DR InParanoid; P61353; -.
DR OMA; HPFPYAI; -.
DR OrthoDB; 1584965at2759; -.
DR PhylomeDB; P61353; -.
DR PathwayCommons; P61353; -.
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; P61353; -.
DR SIGNOR; P61353; -.
DR BioGRID-ORCS; 6155; 786 hits in 1039 CRISPR screens.
DR ChiTaRS; RPL27; human.
DR GeneWiki; RPL27; -.
DR GenomeRNAi; 6155; -.
DR Pharos; P61353; Tbio.
DR PRO; PR:P61353; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P61353; protein.
DR Bgee; ENSG00000131469; Expressed in cervix squamous epithelium and 209 other tissues.
DR ExpressionAtlas; P61353; baseline and differential.
DR Genevisible; P61353; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS: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:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005840; C:ribosome; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR CDD; cd06090; KOW_RPL27; 1.
DR Gene3D; 2.30.30.770; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041991; KOW_RPL27.
DR InterPro; IPR038655; L27e_sf.
DR InterPro; IPR001141; Ribosomal_L27e.
DR InterPro; IPR018262; Ribosomal_L27e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR10497; PTHR10497; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF01777; Ribosomal_L27e; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01107; RIBOSOMAL_L27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Endoplasmic reticulum; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..136
FT /note="60S ribosomal protein L27"
FT /id="PRO_0000126077"
FT DOMAIN 5..40
FT /note="KOW"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 136 AA; 15798 MW; 73F4151495029A32 CRC64;
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP RKVTAAMGKK
KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV FRDPALKRKA RREAKVKFEE
RYKTGKNKWF FQKLRF
