RL15_HUMAN
ID RL15_HUMAN Reviewed; 204 AA.
AC P61313; P39030; P41051; Q5U0C0; Q642I1; Q6IPX6; Q8WYP2; Q96C44; Q9H2E5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=60S ribosomal protein L15;
DE AltName: Full=Large ribosomal subunit protein eL15 {ECO:0000303|PubMed:24524803};
GN Name=RPL15; Synonyms=EC45; ORFNames=TCBAP0781;
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] (ISOFORM 1).
RA Herzog H.;
RT "cDNA encoding the human homologue of yeast ribosomal protein YL10.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang Q., Yang C., Zhou J., Liu Z., Wang X., Zhou C., Wu M.;
RT "Cloning and characterization of EC45 gene, encoding human ribosomal
RT protein L15 and overexpressing in esophageal cancer.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Tanaka T., Shimizu N., Kenmochi N.;
RT "Structures of 69 human ribosomal protein genes: cloning, sequencing, and
RT comparative analysis.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.;
RT "Cloning of a new isoform of ribosomal protein L15 in testis.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RA Villalon D.K., Luna R.A., Margolin J.K., Tsang Y.T.M., Hale S.M., Mei G.,
RA Bouck J., Gibbs R.A.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Small intestine;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone, Brain, Cervix, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
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 INTERACTION WITH IFIT1.
RX PubMed=21612406; DOI=10.1089/dna.2010.1149;
RA Hsu Y.A., Lin H.J., Sheu J.J., Shieh F.K., Chen S.Y., Lai C.H., Tsai F.J.,
RA Wan L., Chen B.H.;
RT "A novel interaction between interferon-inducible protein p56 and ribosomal
RT protein L15 in gastric cancer cells.";
RL DNA Cell Biol. 30:671-679(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [18]
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 [19]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
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-83, 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), 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 [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), 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).
RN [24]
RP INVOLVEMENT IN DBA12.
RX PubMed=23812780; DOI=10.1007/s00439-013-1326-z;
RA Landowski M., O'Donohue M.F., Buros C., Ghazvinian R., Montel-Lehry N.,
RA Vlachos A., Sieff C.A., Newburger P.E., Niewiadomska E., Matysiak M.,
RA Glader B., Atsidaftos E., Lipton J.M., Beggs A.H., Gleizes P.E.,
RA Gazda H.T.;
RT "Novel deletion of RPL15 identified by array-comparative genomic
RT hybridization in Diamond-Blackfan anemia.";
RL Hum. Genet. 132:1265-1274(2013).
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 (PubMed:23636399,
CC PubMed:32669547). Interacts with IFIT1 (via TPR repeats 1-4)
CC (PubMed:21612406). {ECO:0000269|PubMed:21612406,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P61313; P54253: ATXN1; NbExp=3; IntAct=EBI-443462, EBI-930964;
CC P61313; P42858: HTT; NbExp=3; IntAct=EBI-443462, EBI-466029;
CC P61313; P50222: MEOX2; NbExp=3; IntAct=EBI-443462, EBI-748397;
CC P61313; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-443462, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61313-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61313-2; Sequence=VSP_045144;
CC -!- DISEASE: Diamond-Blackfan anemia 12 (DBA12) [MIM:615550]: 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:23812780}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36583.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L25899; AAA36583.1; ALT_FRAME; mRNA.
DR EMBL; AF279903; AAG44837.1; -; mRNA.
DR EMBL; AB061823; BAB79461.1; -; Genomic_DNA.
DR EMBL; AY347528; AAQ24859.1; -; mRNA.
DR EMBL; AF283772; AAG15591.1; -; mRNA.
DR EMBL; AK290694; BAF83383.1; -; mRNA.
DR EMBL; AK292000; BAF84689.1; -; mRNA.
DR EMBL; BT019672; AAV38478.1; -; mRNA.
DR EMBL; AC124914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64338.1; -; Genomic_DNA.
DR EMBL; BC081565; AAH81565.1; -; mRNA.
DR EMBL; BC014837; AAH14837.1; -; mRNA.
DR EMBL; BC068198; AAH68198.1; -; mRNA.
DR EMBL; BC070328; AAH70328.1; -; mRNA.
DR EMBL; BC071672; AAH71672.1; -; mRNA.
DR CCDS; CCDS2640.1; -. [P61313-1]
DR CCDS; CCDS58818.1; -. [P61313-2]
DR RefSeq; NP_001240308.1; NM_001253379.1. [P61313-1]
DR RefSeq; NP_001240309.1; NM_001253380.1. [P61313-1]
DR RefSeq; NP_001240311.1; NM_001253382.1. [P61313-1]
DR RefSeq; NP_001240312.1; NM_001253383.1. [P61313-1]
DR RefSeq; NP_001240313.1; NM_001253384.1. [P61313-2]
DR RefSeq; NP_002939.2; NM_002948.3. [P61313-1]
DR PDB; 4UG0; EM; -; LN=1-204.
DR PDB; 4V6X; EM; 5.00 A; CN=1-204.
DR PDB; 5AJ0; EM; 3.50 A; AN=1-204.
DR PDB; 5LKS; EM; 3.60 A; LN=1-204.
DR PDB; 5T2C; EM; 3.60 A; t=1-204.
DR PDB; 6IP5; EM; 3.90 A; 2H=1-204.
DR PDB; 6IP6; EM; 4.50 A; 2H=1-204.
DR PDB; 6IP8; EM; 3.90 A; 2H=1-204.
DR PDB; 6LQM; EM; 3.09 A; U=1-204.
DR PDB; 6LSR; EM; 3.13 A; U=1-204.
DR PDB; 6LSS; EM; 3.23 A; U=1-204.
DR PDB; 6LU8; EM; 3.13 A; U=1-204.
DR PDB; 6OLE; EM; 3.10 A; O=2-204.
DR PDB; 6OLF; EM; 3.90 A; O=2-204.
DR PDB; 6OLG; EM; 3.40 A; AN=2-204.
DR PDB; 6OLI; EM; 3.50 A; O=2-204.
DR PDB; 6OLZ; EM; 3.90 A; AN=2-204.
DR PDB; 6OM0; EM; 3.10 A; O=2-204.
DR PDB; 6OM7; EM; 3.70 A; O=2-204.
DR PDB; 6QZP; EM; 2.90 A; LN=2-204.
DR PDB; 6W6L; EM; 3.84 A; O=1-204.
DR PDB; 6XA1; EM; 2.80 A; LN=2-204.
DR PDB; 6Y0G; EM; 3.20 A; LN=1-204.
DR PDB; 6Y2L; EM; 3.00 A; LN=1-204.
DR PDB; 6Y57; EM; 3.50 A; LN=1-204.
DR PDB; 6Y6X; EM; 2.80 A; LN=2-204.
DR PDB; 6Z6L; EM; 3.00 A; LN=1-204.
DR PDB; 6Z6M; EM; 3.10 A; LN=1-204.
DR PDB; 6Z6N; EM; 2.90 A; LN=1-204.
DR PDB; 6ZM7; EM; 2.70 A; LN=1-204.
DR PDB; 6ZME; EM; 3.00 A; LN=1-204.
DR PDB; 6ZMI; EM; 2.60 A; LN=1-204.
DR PDB; 6ZMO; EM; 3.10 A; LN=1-204.
DR PDB; 7BHP; EM; 3.30 A; LN=1-204.
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; P61313; -.
DR SMR; P61313; -.
DR BioGRID; 112058; 459.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P61313; -.
DR IntAct; P61313; 106.
DR MINT; P61313; -.
DR STRING; 9606.ENSP00000309334; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR GlyGen; P61313; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61313; -.
DR PhosphoSitePlus; P61313; -.
DR SwissPalm; P61313; -.
DR BioMuta; RPL15; -.
DR SWISS-2DPAGE; P61313; -.
DR EPD; P61313; -.
DR jPOST; P61313; -.
DR MassIVE; P61313; -.
DR MaxQB; P61313; -.
DR PaxDb; P61313; -.
DR PeptideAtlas; P61313; -.
DR PRIDE; P61313; -.
DR ProteomicsDB; 57293; -. [P61313-1]
DR ProteomicsDB; 65913; -.
DR TopDownProteomics; P61313-1; -. [P61313-1]
DR Antibodypedia; 11374; 251 antibodies from 30 providers.
DR DNASU; 6138; -.
DR Ensembl; ENST00000307839.10; ENSP00000309334.5; ENSG00000174748.22. [P61313-1]
DR Ensembl; ENST00000354811.5; ENSP00000346867.5; ENSG00000174748.22. [P61313-1]
DR Ensembl; ENST00000413699.7; ENSP00000416692.1; ENSG00000174748.22. [P61313-1]
DR Ensembl; ENST00000415719.5; ENSP00000388529.1; ENSG00000174748.22. [P61313-1]
DR Ensembl; ENST00000456530.7; ENSP00000398788.2; ENSG00000174748.22. [P61313-2]
DR Ensembl; ENST00000611050.4; ENSP00000483260.1; ENSG00000174748.22. [P61313-1]
DR Ensembl; ENST00000644185.1; ENSP00000493759.1; ENSG00000174748.22. [P61313-1]
DR GeneID; 6138; -.
DR KEGG; hsa:6138; -.
DR MANE-Select; ENST00000307839.10; ENSP00000309334.5; NM_002948.5; NP_002939.2.
DR UCSC; uc003ccn.4; human. [P61313-1]
DR CTD; 6138; -.
DR DisGeNET; 6138; -.
DR GeneCards; RPL15; -.
DR GeneReviews; RPL15; -.
DR HGNC; HGNC:10306; RPL15.
DR HPA; ENSG00000174748; Low tissue specificity.
DR MalaCards; RPL15; -.
DR MIM; 604174; gene.
DR MIM; 615550; phenotype.
DR neXtProt; NX_P61313; -.
DR OpenTargets; ENSG00000174748; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34674; -.
DR VEuPathDB; HostDB:ENSG00000174748; -.
DR eggNOG; KOG1678; Eukaryota.
DR GeneTree; ENSGT00910000144184; -.
DR InParanoid; P61313; -.
DR OMA; KYMQELY; -.
DR PhylomeDB; P61313; -.
DR TreeFam; TF300050; -.
DR PathwayCommons; P61313; -.
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; P61313; -.
DR SIGNOR; P61313; -.
DR BioGRID-ORCS; 6138; 806 hits in 1048 CRISPR screens.
DR ChiTaRS; RPL15; human.
DR GeneWiki; RPL15; -.
DR GenomeRNAi; 6138; -.
DR Pharos; P61313; Tbio.
DR PRO; PR:P61313; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P61313; protein.
DR Bgee; ENSG00000174748; Expressed in cortical plate and 205 other tissues.
DR ExpressionAtlas; P61313; baseline and differential.
DR Genevisible; P61313; HS.
DR GO; GO:0031672; C:A band; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005840; C:ribosome; TAS:ProtInc.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
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; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 3.40.1120.10; -; 1.
DR InterPro; IPR024794; Rbsml_L15e_core_dom_sf.
DR InterPro; IPR000439; Ribosomal_L15e.
DR InterPro; IPR020925; Ribosomal_L15e_CS.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR PANTHER; PTHR11847; PTHR11847; 1.
DR Pfam; PF00827; Ribosomal_L15e; 1.
DR SMART; SM01384; Ribosomal_L15e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS01194; RIBOSOMAL_L15E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Diamond-Blackfan anemia;
KW Isopeptide bond; Lipoprotein; Myristate; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..204
FT /note="60S ribosomal protein L15"
FT /id="PRO_0000127527"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61314"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 121..204
FT /note="VGEDSTYKFFEVILIDPFHKAIRRNPDTQWITKPVHKHREMRGLTSAGRKSR
FT GLGKGHKFHHTIGGSRRAAWRRRNTLQLHRYR -> MESHSHSGGSAVGQSRLTATSVS
FT RV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045144"
FT CONFLICT 101
FT /note="V -> L (in Ref. 5; AAG44837)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="F -> A (in Ref. 1; AAA36583 and 3; BAB79461)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="V -> D (in Ref. 1; AAA36583)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="F -> S (in Ref. 10; AAH14837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 24146 MW; A6E3AD1A76C9506F CRC64;
MGAYKYIQEL WRKKQSDVMR FLLRVRCWQY RQLSALHRAP RPTRPDKARR LGYKAKQGYV
IYRIRVRRGG RKRPVPKGAT YGKPVHHGVN QLKFARSLQS VAEERAGRHC GALRVLNSYW
VGEDSTYKFF EVILIDPFHK AIRRNPDTQW ITKPVHKHRE MRGLTSAGRK SRGLGKGHKF
HHTIGGSRRA AWRRRNTLQL HRYR
