ID RL36A_HUMAN Reviewed; 106 AA.
AC P83881; P09896; P10661; Q08ES5; Q5J9I6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=Large ribosomal subunit protein eL42 {ECO:0000303|PubMed:24524803};
DE AltName: Full=60S ribosomal protein L36a;
DE AltName: Full=60S ribosomal protein L44;
DE AltName: Full=Cell growth-inhibiting gene 15 protein;
DE AltName: Full=Cell migration-inducing gene 6 protein;
GN Name=RPL36A; Synonyms=RPL44; ORFNames=GIG15, MIG6;
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 [GENOMIC DNA].
RX PubMed=9110171; DOI=10.1101/gr.7.4.315;
RA Oeltjen J.C., Malley T.M., Muzny D.M., Miller W., Gibbs R.A., Belmont J.W.;
RT "Large-scale comparative sequence analysis of the human and murine Bruton's
RT tyrosine kinase loci reveals conserved regulatory domains.";
RL Genome Res. 7:315-329(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a migration-inducing gene.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W., Kim H.K.;
RT "Identification of cell growth-inhibiting gene.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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=Eye, Lung, and Testis;
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 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 [9]
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 [10] {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. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {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 P83881; Q96BJ3: AIDA; NbExp=3; IntAct=EBI-1054835, EBI-4401674;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.
CC {ECO:0000305}.
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DR EMBL; U78027; AAB64204.1; -; Genomic_DNA.
DR EMBL; AY305871; AAQ95213.1; -; mRNA.
DR EMBL; CR542198; CAG46995.1; -; mRNA.
DR EMBL; AY927233; AAX08138.1; -; mRNA.
DR EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471115; EAX02860.1; -; Genomic_DNA.
DR EMBL; BC001781; AAH01781.1; -; mRNA.
DR EMBL; BC031015; AAH31015.1; -; mRNA.
DR EMBL; BC062219; AAH62219.1; -; mRNA.
DR EMBL; BC070204; AAH70204.1; -; mRNA.
DR CCDS; CCDS14483.3; -.
DR RefSeq; NP_066357.2; NM_021029.5.
DR PDB; 4UG0; EM; -; Lo=1-106.
DR PDB; 4V6X; EM; 5.00 A; Co=1-106.
DR PDB; 5AJ0; EM; 3.50 A; Ao=1-106.
DR PDB; 5LKS; EM; 3.60 A; Lo=1-106.
DR PDB; 5T2C; EM; 3.60 A; i=1-106.
DR PDB; 6IP5; EM; 3.90 A; 2i=1-106.
DR PDB; 6IP6; EM; 4.50 A; 2i=1-106.
DR PDB; 6IP8; EM; 3.90 A; 2i=1-106.
DR PDB; 6LQM; EM; 3.09 A; W=1-106.
DR PDB; 6LSR; EM; 3.13 A; W=1-106.
DR PDB; 6LSS; EM; 3.23 A; W=1-106.
DR PDB; 6LU8; EM; 3.13 A; W=1-106.
DR PDB; 6OLE; EM; 3.10 A; p=2-106.
DR PDB; 6OLF; EM; 3.90 A; p=2-106.
DR PDB; 6OLG; EM; 3.40 A; Ao=2-106.
DR PDB; 6OLI; EM; 3.50 A; p=2-106.
DR PDB; 6OLZ; EM; 3.90 A; Ao=2-106.
DR PDB; 6OM0; EM; 3.10 A; p=2-106.
DR PDB; 6OM7; EM; 3.70 A; p=2-106.
DR PDB; 6QZP; EM; 2.90 A; Lo=2-106.
DR PDB; 6XA1; EM; 2.80 A; Lo=2-106.
DR PDB; 6Y0G; EM; 3.20 A; Lo=1-106.
DR PDB; 6Y2L; EM; 3.00 A; Lo=1-106.
DR PDB; 6Y57; EM; 3.50 A; Lo=1-106.
DR PDB; 6Y6X; EM; 2.80 A; Lo=2-106.
DR PDB; 6Z6M; EM; 3.10 A; Lo=1-106.
DR PDB; 6Z6N; EM; 2.90 A; Lo=1-106.
DR PDB; 6ZM7; EM; 2.70 A; Lo=1-106.
DR PDB; 6ZME; EM; 3.00 A; Lo=1-106.
DR PDB; 6ZMI; EM; 2.60 A; Lo=1-106.
DR PDB; 6ZMO; EM; 3.10 A; Lo=1-106.
DR PDB; 7BHP; EM; 3.30 A; Lo=1-106.
DR PDB; 7F5S; EM; 2.72 A; Lo=1-106.
DR PDB; 7OW7; EM; 2.20 A; i=1-106.
DR PDB; 8A3D; EM; 1.67 A; i=1-106.
DR PDB; 8IDT; EM; 2.80 A; W=1-106.
DR PDB; 8IDY; EM; 3.00 A; W=1-106.
DR PDB; 8INE; EM; 3.20 A; W=1-106.
DR PDB; 8INF; EM; 3.00 A; W=1-106.
DR PDB; 8JDJ; EM; 2.50 A; t=1-106.
DR PDB; 8JDK; EM; 2.26 A; t=1-106.
DR PDB; 8JDL; EM; 2.42 A; t=1-106.
DR PDB; 8JDM; EM; 2.67 A; t=1-106.
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; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
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; 8A3D; -.
DR PDBsum; 8IDT; -.
DR PDBsum; 8IDY; -.
DR PDBsum; 8INE; -.
DR PDBsum; 8INF; -.
DR PDBsum; 8JDJ; -.
DR PDBsum; 8JDK; -.
DR PDBsum; 8JDL; -.
DR PDBsum; 8JDM; -.
DR AlphaFoldDB; P83881; -.
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-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-15113; -.
DR EMDB; EMD-31465; -.
DR EMDB; EMD-33329; -.
DR EMDB; EMD-33330; -.
DR EMDB; EMD-35370; -.
DR EMDB; EMD-35371; -.
DR EMDB; EMD-35596; -.
DR EMDB; EMD-35597; -.
DR EMDB; EMD-3883; -.
DR EMDB; EMD-4070; -.
DR EMDB; EMD-9701; -.
DR EMDB; EMD-9702; -.
DR EMDB; EMD-9703; -.
DR SMR; P83881; -.
DR BioGRID; 112092; 129.
DR ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR CORUM; P83881; -.
DR IntAct; P83881; 33.
DR MINT; P83881; -.
DR STRING; 9606.ENSP00000404375; -.
DR GlyGen; P83881; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P83881; -.
DR PhosphoSitePlus; P83881; -.
DR SwissPalm; P83881; -.
DR BioMuta; RPL36A; -.
DR DMDM; 47117731; -.
DR EPD; P83881; -.
DR jPOST; P83881; -.
DR MassIVE; P83881; -.
DR MaxQB; P83881; -.
DR PaxDb; 9606-ENSP00000404375; -.
DR PeptideAtlas; P83881; -.
DR ProteomicsDB; 57741; -.
DR Pumba; P83881; -.
DR TopDownProteomics; P83881; -.
DR Antibodypedia; 34835; 136 antibodies from 20 providers.
DR DNASU; 6173; -.
DR Ensembl; ENST00000553110.8; ENSP00000446503.2; ENSG00000241343.10.
DR GeneID; 6173; -.
DR KEGG; hsa:6173; -.
DR MANE-Select; ENST00000553110.8; ENSP00000446503.2; NM_021029.6; NP_066357.3.
DR UCSC; uc065agx.1; human.
DR AGR; HGNC:10359; -.
DR CTD; 6173; -.
DR DisGeNET; 6173; -.
DR GeneCards; RPL36A; -.
DR HGNC; HGNC:10359; RPL36A.
DR HPA; ENSG00000241343; Low tissue specificity.
DR MIM; 300902; gene.
DR neXtProt; NX_P83881; -.
DR OpenTargets; ENSG00000241343; -.
DR PharmGKB; PA164742367; -.
DR VEuPathDB; HostDB:ENSG00000241343; -.
DR eggNOG; KOG3464; Eukaryota.
DR GeneTree; ENSGT00390000018085; -.
DR InParanoid; P83881; -.
DR OrthoDB; 4943739at2759; -.
DR PhylomeDB; P83881; -.
DR PathwayCommons; P83881; -.
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; P83881; -.
DR SIGNOR; P83881; -.
DR BioGRID-ORCS; 6173; 364 hits in 768 CRISPR screens.
DR ChiTaRS; RPL36A; human.
DR GeneWiki; RPL36A; -.
DR GenomeRNAi; 6173; -.
DR Pharos; P83881; Tbio.
DR PRO; PR:P83881; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P83881; Protein.
DR Bgee; ENSG00000241343; Expressed in cortical plate and 100 other cell types or tissues.
DR ExpressionAtlas; P83881; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.10.450.80; -; 1.
DR InterPro; IPR000552; Ribosomal_eL44.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR10369:SF3; 60S RIBOSOMAL PROTEIN L36A; 1.
DR PANTHER; PTHR10369; 60S RIBOSOMAL PROTEIN L36A/L44; 1.
DR Pfam; PF00935; Ribosomal_L44; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS01172; RIBOSOMAL_L44E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..106
FT /note="Large ribosomal subunit protein eL42"
FT /id="PRO_0000149117"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 106 AA; 12441 MW; AE3308265D70BD26 CRC64;
MVNVPKTRRT FCKKCGKHQP HKVTQYKKGK DSLYAQGKRR YDRKQSGYGG QTKPIFRKKA
KTTKKIVLRL ECVEPNCRSK RMLAIKRCKH FELGGDKKRK GQVIQF
//
