ID   RL36_HUMAN              Reviewed;         105 AA.
AC   Q9Y3U8; B2R4Y1; D6W634; Q6FIG1; Q9UQF6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=Large ribosomal subunit protein eL36 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L36;
GN   Name=RPL36;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Blood, Kidney, 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   [8]
RP   PROTEIN SEQUENCE OF 2-10, 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   [9]
RP   PROTEIN SEQUENCE OF 2-13; 46-55 AND 88-98, CLEAVAGE OF INITIATOR
RP   METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RA   Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [10]
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, 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   [12]
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   [13]
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   [14]
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   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), SUBCELLULAR LOCATION,
RP   SUBUNIT, AND FUNCTION.
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   [16] {ECO:0007744|PDB:5AJ0}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP   SUBUNIT, AND FUNCTION.
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   [17] {ECO:0007744|PDB:4UG0}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), SUBCELLULAR LOCATION,
RP   SUBUNIT, AND FUNCTION.
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   [18] {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:25901680, PubMed:25957688, PubMed:32669547).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399,
CC       PubMed:25901680, PubMed:25957688, PubMed:32669547).
CC       {ECO:0000269|PubMed:23636399, 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:25901680, PubMed:25957688, PubMed:32669547).
CC       {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC       ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC       ECO:0000305|PubMed:12962325}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC       Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC       Note=Detected on cytosolic polysomes (PubMed:25957688).
CC       {ECO:0000250|UniProtKB:Q2YGT9, ECO:0000269|PubMed:25957688}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL36 family.
CC       {ECO:0000305}.
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DR   EMBL; AB061833; BAB79471.1; -; Genomic_DNA.
DR   EMBL; AL050273; CAB43374.1; -; mRNA.
DR   EMBL; AF077043; AAD27776.1; -; mRNA.
DR   EMBL; CR533465; CAG38496.1; -; mRNA.
DR   EMBL; AK311990; BAG34928.1; -; mRNA.
DR   EMBL; CH471139; EAW69155.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69158.1; -; Genomic_DNA.
DR   EMBL; BC003052; AAH03052.1; -; mRNA.
DR   EMBL; BC004971; AAH04971.1; -; mRNA.
DR   EMBL; BC091508; AAH91508.1; -; mRNA.
DR   CCDS; CCDS12147.1; -.
DR   PIR; T08720; T08720.
DR   RefSeq; NP_056229.2; NM_015414.3.
DR   RefSeq; NP_378669.1; NM_033643.2.
DR   PDB; 4UG0; EM; -; Li=1-105.
DR   PDB; 4V6X; EM; 5.00 A; Ci=1-105.
DR   PDB; 5AJ0; EM; 3.50 A; Ai=1-105.
DR   PDB; 5LKS; EM; 3.60 A; Li=1-105.
DR   PDB; 5T2C; EM; 3.60 A; c=1-105.
DR   PDB; 6IP5; EM; 3.90 A; 2c=1-105.
DR   PDB; 6IP6; EM; 4.50 A; 2c=1-105.
DR   PDB; 6IP8; EM; 3.90 A; 2c=1-105.
DR   PDB; 6LQM; EM; 3.09 A; K=1-105.
DR   PDB; 6LSR; EM; 3.13 A; K=1-105.
DR   PDB; 6LSS; EM; 3.23 A; K=1-105.
DR   PDB; 6LU8; EM; 3.13 A; K=1-105.
DR   PDB; 6OLE; EM; 3.10 A; j=5-101.
DR   PDB; 6OLF; EM; 3.90 A; j=5-101.
DR   PDB; 6OLG; EM; 3.40 A; Ai=5-101.
DR   PDB; 6OLI; EM; 3.50 A; j=5-101.
DR   PDB; 6OLZ; EM; 3.90 A; Ai=5-101.
DR   PDB; 6OM0; EM; 3.10 A; j=5-101.
DR   PDB; 6OM7; EM; 3.70 A; j=5-101.
DR   PDB; 6QZP; EM; 2.90 A; Li=2-103.
DR   PDB; 6W6L; EM; 3.84 A; j=1-105.
DR   PDB; 6XA1; EM; 2.80 A; Li=2-103.
DR   PDB; 6Y0G; EM; 3.20 A; Li=1-105.
DR   PDB; 6Y2L; EM; 3.00 A; Li=1-105.
DR   PDB; 6Y57; EM; 3.50 A; Li=1-105.
DR   PDB; 6Y6X; EM; 2.80 A; Li=2-103.
DR   PDB; 6Z6L; EM; 3.00 A; Li=1-105.
DR   PDB; 6Z6M; EM; 3.10 A; Li=1-105.
DR   PDB; 6Z6N; EM; 2.90 A; Li=1-105.
DR   PDB; 6ZM7; EM; 2.70 A; Li=1-105.
DR   PDB; 6ZME; EM; 3.00 A; Li=1-105.
DR   PDB; 6ZMI; EM; 2.60 A; Li=1-105.
DR   PDB; 6ZMO; EM; 3.10 A; Li=1-105.
DR   PDB; 7BHP; EM; 3.30 A; Li=1-105.
DR   PDB; 7F5S; EM; 2.72 A; Li=1-105.
DR   PDB; 7OW7; EM; 2.20 A; c=1-105.
DR   PDB; 7QGG; EM; 2.86 A; j=1-105.
DR   PDB; 7QVP; EM; 3.00 A; Li/Mi=1-105.
DR   PDB; 7XNX; EM; 2.70 A; Li=1-105.
DR   PDB; 7XNY; EM; 2.50 A; Li=1-105.
DR   PDB; 8A3D; EM; 1.67 A; c=1-105.
DR   PDB; 8FKP; EM; 2.85 A; LU=1-105.
DR   PDB; 8FKQ; EM; 2.76 A; LU=1-105.
DR   PDB; 8FKR; EM; 2.89 A; LU=1-105.
DR   PDB; 8FKS; EM; 2.88 A; LU=1-105.
DR   PDB; 8FKT; EM; 2.81 A; LU=1-105.
DR   PDB; 8FKU; EM; 2.82 A; LU=1-105.
DR   PDB; 8FKV; EM; 2.47 A; LU=1-105.
DR   PDB; 8FKW; EM; 2.50 A; LU=1-105.
DR   PDB; 8FKX; EM; 2.59 A; LU=1-105.
DR   PDB; 8FKY; EM; 2.67 A; LU=1-105.
DR   PDB; 8FKZ; EM; 3.04 A; LU=1-105.
DR   PDB; 8FL2; EM; 2.67 A; LU=1-105.
DR   PDB; 8FL3; EM; 2.53 A; LU=1-105.
DR   PDB; 8FL4; EM; 2.89 A; LU=1-105.
DR   PDB; 8FL6; EM; 2.62 A; LU=1-105.
DR   PDB; 8FL7; EM; 2.55 A; LU=1-105.
DR   PDB; 8FL9; EM; 2.75 A; LU=1-105.
DR   PDB; 8FLA; EM; 2.63 A; LU=1-105.
DR   PDB; 8FLB; EM; 2.55 A; LU=1-105.
DR   PDB; 8FLC; EM; 2.76 A; LU=1-105.
DR   PDB; 8FLD; EM; 2.58 A; LU=1-105.
DR   PDB; 8FLE; EM; 2.48 A; LU=1-105.
DR   PDB; 8FLF; EM; 2.65 A; LU=1-105.
DR   PDB; 8G5Y; EM; 2.29 A; Li=1-105.
DR   PDB; 8G5Z; EM; 2.64 A; Li=2-103.
DR   PDB; 8G60; EM; 2.54 A; Li=1-105.
DR   PDB; 8G61; EM; 2.94 A; Li=1-105.
DR   PDB; 8G6J; EM; 2.80 A; Li=1-105.
DR   PDB; 8GLP; EM; 1.67 A; Li=1-105.
DR   PDB; 8IDT; EM; 2.80 A; K=1-105.
DR   PDB; 8IDY; EM; 3.00 A; K=1-105.
DR   PDB; 8IE3; EM; 3.30 A; K=1-105.
DR   PDB; 8INE; EM; 3.20 A; K=1-105.
DR   PDB; 8INF; EM; 3.00 A; K=1-105.
DR   PDB; 8INK; EM; 3.20 A; K=1-105.
DR   PDB; 8IPD; EM; 3.20 A; K=1-105.
DR   PDB; 8IPX; EM; 4.30 A; K=1-105.
DR   PDB; 8IPY; EM; 3.20 A; K=1-105.
DR   PDB; 8IR1; EM; 3.30 A; K=1-105.
DR   PDB; 8IR3; EM; 3.50 A; K=1-105.
DR   PDB; 8JDJ; EM; 2.50 A; n=1-105.
DR   PDB; 8JDK; EM; 2.26 A; n=1-105.
DR   PDB; 8JDL; EM; 2.42 A; n=1-105.
DR   PDB; 8JDM; EM; 2.67 A; n=1-105.
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; 7QGG; -.
DR   PDBsum; 7QVP; -.
DR   PDBsum; 7XNX; -.
DR   PDBsum; 7XNY; -.
DR   PDBsum; 8A3D; -.
DR   PDBsum; 8FKP; -.
DR   PDBsum; 8FKQ; -.
DR   PDBsum; 8FKR; -.
DR   PDBsum; 8FKS; -.
DR   PDBsum; 8FKT; -.
DR   PDBsum; 8FKU; -.
DR   PDBsum; 8FKV; -.
DR   PDBsum; 8FKW; -.
DR   PDBsum; 8FKX; -.
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; Q9Y3U8; -.
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-13954; -.
DR   EMDB; EMD-14181; -.
DR   EMDB; EMD-15113; -.
DR   EMDB; EMD-29252; -.
DR   EMDB; EMD-29253; -.
DR   EMDB; EMD-29254; -.
DR   EMDB; EMD-29255; -.
DR   EMDB; EMD-29256; -.
DR   EMDB; EMD-29257; -.
DR   EMDB; EMD-29258; -.
DR   EMDB; EMD-29259; -.
DR   EMDB; EMD-29260; -.
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; Q9Y3U8; -.
DR   BioGRID; 117388; 503.
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; Q9Y3U8; -.
DR   IntAct; Q9Y3U8; 90.
DR   MINT; Q9Y3U8; -.
DR   STRING; 9606.ENSP00000464342; -.
DR   GlyGen; Q9Y3U8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y3U8; -.
DR   MetOSite; Q9Y3U8; -.
DR   PhosphoSitePlus; Q9Y3U8; -.
DR   SwissPalm; Q9Y3U8; -.
DR   BioMuta; RPL36; -.
DR   DMDM; 7388073; -.
DR   EPD; Q9Y3U8; -.
DR   jPOST; Q9Y3U8; -.
DR   MassIVE; Q9Y3U8; -.
DR   MaxQB; Q9Y3U8; -.
DR   PaxDb; 9606-ENSP00000464342; -.
DR   PeptideAtlas; Q9Y3U8; -.
DR   ProteomicsDB; 86079; -.
DR   Pumba; Q9Y3U8; -.
DR   TopDownProteomics; Q9Y3U8; -.
DR   Antibodypedia; 23940; 194 antibodies from 26 providers.
DR   DNASU; 25873; -.
DR   Ensembl; ENST00000347512.8; ENSP00000252543.3; ENSG00000130255.13.
DR   Ensembl; ENST00000394580.2; ENSP00000378081.2; ENSG00000130255.13.
DR   Ensembl; ENST00000577222.5; ENSP00000464342.1; ENSG00000130255.13.
DR   Ensembl; ENST00000579649.5; ENSP00000462609.1; ENSG00000130255.13.
DR   GeneID; 25873; -.
DR   KEGG; hsa:25873; -.
DR   MANE-Select; ENST00000347512.8; ENSP00000252543.3; NM_033643.3; NP_378669.1.
DR   UCSC; uc002mcv.4; human.
DR   AGR; HGNC:13631; -.
DR   CTD; 25873; -.
DR   DisGeNET; 25873; -.
DR   GeneCards; RPL36; -.
DR   HGNC; HGNC:13631; RPL36.
DR   HPA; ENSG00000130255; Low tissue specificity.
DR   MIM; 617893; gene.
DR   neXtProt; NX_Q9Y3U8; -.
DR   OpenTargets; ENSG00000130255; -.
DR   PharmGKB; PA34730; -.
DR   VEuPathDB; HostDB:ENSG00000130255; -.
DR   eggNOG; KOG3452; Eukaryota.
DR   GeneTree; ENSGT00390000011943; -.
DR   HOGENOM; CLU_140672_2_0_1; -.
DR   InParanoid; Q9Y3U8; -.
DR   OMA; NKGHKTE; -.
DR   OrthoDB; 1341689at2759; -.
DR   PhylomeDB; Q9Y3U8; -.
DR   TreeFam; TF314463; -.
DR   PathwayCommons; Q9Y3U8; -.
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; Q9Y3U8; -.
DR   SIGNOR; Q9Y3U8; -.
DR   BioGRID-ORCS; 25873; 845 hits in 1138 CRISPR screens.
DR   ChiTaRS; RPL36; human.
DR   GeneWiki; RPL36; -.
DR   GenomeRNAi; 25873; -.
DR   Pharos; Q9Y3U8; Tbio.
DR   PRO; PR:Q9Y3U8; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9Y3U8; Protein.
DR   Bgee; ENSG00000130255; Expressed in ganglionic eminence and 202 other cell types or tissues.
DR   ExpressionAtlas; Q9Y3U8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
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; 1.10.10.1760; 60S ribosomal protein L36; 1.
DR   InterPro; IPR000509; Ribosomal_eL36.
DR   InterPro; IPR038097; Ribosomal_eL36_sf.
DR   PANTHER; PTHR10114; 60S RIBOSOMAL PROTEIN L36; 1.
DR   PANTHER; PTHR10114:SF28; 60S RIBOSOMAL PROTEIN L36; 1.
DR   Pfam; PF01158; Ribosomal_L36e; 1.
DR   PROSITE; PS01190; RIBOSOMAL_L36E; 1.
DR   Genevisible; Q9Y3U8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.9"
FT   CHAIN           2..105
FT                   /note="Large ribosomal subunit protein eL36"
FT                   /id="PRO_0000195007"
FT   MOD_RES         62
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         67
FT                   /note="K -> E (in dbSNP:rs11556110)"
FT                   /id="VAR_051804"
FT   CONFLICT        29
FT                   /note="R -> H (in Ref. 3; AAD27776)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   105 AA;  12254 MW;  FEE8850A62080EB3 CRC64;
     MALRYPMAVG LNKGHKVTKN VSKPRHSRRR GRLTKHTKFV RDMIREVCGF APYERRAMEL
     LKVSKDKRAL KFIKKRVGTH IRAKRKREEL SNVLAAMRKA AAKKD
//