RL11_HUMAN
ID RL11_HUMAN Reviewed; 178 AA.
AC P62913; P25121; P39026; Q8TDH2; Q9Y674;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=60S ribosomal protein L11;
DE AltName: Full=CLL-associated antigen KW-12;
DE AltName: Full=Large ribosomal subunit protein uL5 {ECO:0000303|PubMed:24524803};
GN Name=RPL11;
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).
RX PubMed=7748210;
RA Mishin V.P., Filipenko M.L., Muravlev A.I., Karpova G.G., Mertvetsov N.P.;
RT "Cloning and determination of the primary structure of DNA complementary to
RT the mRNA of human ribosomal protein L11.";
RL Bioorg. Khim. 21:158-160(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bhat K.S.;
RT "Expressed sequence tags from a human cell line.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12815950;
RA Voronina E.N., Kolokol'tsova T.D., Nechaeva E.A., Filipenko M.L.;
RT "Structural and functional analysis of the human ribosomal protein L11
RT gene.";
RL Mol. Biol. (Mosk.) 37:425-435(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tonsil;
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 2-13; 89-95; 119-145 AND 157-164, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Quadroni M., Bienvenut W.V.;
RL Submitted (NOV-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-178 (ISOFORM 1).
RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M.,
RA Barrett P., Gribben J.G.;
RT "Identification of novel tumor antigens in CLL by SEREX: assessment of
RT their potential as targets for immunotherapeutic approaches.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-52.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [8]
RP ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
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 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 [10]
RP FUNCTION, AND VARIANT DBA7 GLU-161 DEL.
RX PubMed=19061985; DOI=10.1016/j.ajhg.2008.11.004;
RA Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F.,
RA Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C.,
RA Meerpohl J.J., Atsidaftos E., Lipton J.M., Gleizes P.-E., Beggs A.H.;
RT "Ribosomal protein L5 and L11 mutations are associated with cleft palate
RT and abnormal thumbs in Diamond-Blackfan anemia patients.";
RL Am. J. Hum. Genet. 83:769-780(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-85, 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MDM2.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 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 [20]
RP INTERACTION WITH NOP53.
RX PubMed=24556985; DOI=10.1073/pnas.1400705111;
RA Yoon J.C., Ling A.J., Isik M., Lee D.Y., Steinbaugh M.J., Sack L.M.,
RA Boduch A.N., Blackwell T.K., Sinclair D.A., Elledge S.J.;
RT "GLTSCR2/PICT1 links mitochondrial stress and Myc signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3781-3786(2014).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP INTERACTION WITH NOP53, AND SUBCELLULAR LOCATION.
RX PubMed=27829214; DOI=10.18632/oncotarget.13082;
RA Chen H., Han L., Tsai H., Wang Z., Wu Y., Duo Y., Cao W., Chen L., Tan Z.,
RA Xu N., Huang X., Zhuang J., Huang L.;
RT "PICT-1 is a key nucleolar sensor in DNA damage response signaling that
RT regulates apoptosis through the RPL11-MDM2-p53 pathway.";
RL Oncotarget 7:83241-83257(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-52 AND LYS-154, AND
RP IDENTIFICATION BY MASS 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 [24]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION,
RP SUBUNIT, AND 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 [25] {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 [26]
RP VARIANT DBA7 HIS-20.
RX PubMed=19191325; DOI=10.1002/humu.20874;
RA Cmejla R., Cmejlova J., Handrkova H., Petrak J., Petrtylova K., Mihal V.,
RA Stary J., Cerna Z., Jabali Y., Pospisilova D.;
RT "Identification of mutations in the ribosomal protein L5 (RPL5) and
RT ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan
RT anemia.";
RL Hum. Mutat. 30:321-327(2009).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell (PubMed:32669547,
CC PubMed:19191325). The small ribosomal subunit (SSU) binds messenger
CC RNAs (mRNAs) and translates the encoded message by selecting cognate
CC aminoacyl-transfer RNA (tRNA) molecules (PubMed:32669547,
CC PubMed:19191325). The large subunit (LSU) contains the ribosomal
CC catalytic site termed the peptidyl transferase center (PTC), which
CC catalyzes the formation of peptide bonds, thereby polymerizing the
CC amino acids delivered by tRNAs into a polypeptide chain
CC (PubMed:32669547, PubMed:19191325). The nascent polypeptides leave the
CC ribosome through a tunnel in the LSU and interact with protein factors
CC that function in enzymatic processing, targeting, and the membrane
CC insertion of nascent chains at the exit of the ribosomal tunnel
CC (PubMed:32669547, PubMed:19191325). As part of the 5S RNP/5S
CC ribonucleoprotein particle it is an essential component of the LSU,
CC required for its formation and the maturation of rRNAs
CC (PubMed:19061985, PubMed:12962325, PubMed:24120868). It also couples
CC ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it
CC accumulates in the nucleoplasm and inhibits MDM2, when ribosome
CC biogenesis is perturbed, mediating the stabilization and the activation
CC of TP53 (PubMed:24120868). Promotes nucleolar location of PML (By
CC similarity). {ECO:0000250|UniProtKB:Q9CXW4,
CC ECO:0000269|PubMed:12962325, ECO:0000269|PubMed:19061985,
CC ECO:0000269|PubMed:19191325, ECO:0000269|PubMed:24120868,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU)
CC (PubMed:32669547, PubMed:19191325). Part of a LSU subcomplex, the 5S
CC RNP which is composed of the 5S RNA, RPL5 and RPL11 (PubMed:24120868).
CC Interacts with PML (By similarity). Interacts with MDM2; negatively
CC regulates MDM2-mediated TP53 ubiquitination and degradation
CC (PubMed:24120868). Interacts with NOP53; retains RPL11 into the
CC nucleolus (PubMed:24556985, PubMed:27829214).
CC {ECO:0000250|UniProtKB:Q9CXW4, ECO:0000269|PubMed:19191325,
CC ECO:0000269|PubMed:24120868, ECO:0000269|PubMed:24556985,
CC ECO:0000269|PubMed:27829214, ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC P62913; Q13554: CAMK2B; NbExp=3; IntAct=EBI-354380, EBI-1058722;
CC P62913; P08238: HSP90AB1; NbExp=2; IntAct=EBI-354380, EBI-352572;
CC P62913; Q6A162: KRT40; NbExp=3; IntAct=EBI-354380, EBI-10171697;
CC P62913; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-354380, EBI-10172290;
CC P62913; Q00987: MDM2; NbExp=11; IntAct=EBI-354380, EBI-389668;
CC P62913; P01106: MYC; NbExp=3; IntAct=EBI-354380, EBI-447544;
CC P62913; Q15843: NEDD8; NbExp=5; IntAct=EBI-354380, EBI-716247;
CC P62913-2; Q92997: DVL3; NbExp=3; IntAct=EBI-11027771, EBI-739789;
CC P62913-2; Q92551: IP6K1; NbExp=3; IntAct=EBI-11027771, EBI-751911;
CC P62913-2; Q92993: KAT5; NbExp=3; IntAct=EBI-11027771, EBI-399080;
CC P62913-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11027771, EBI-11742507;
CC P62913-2; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-11027771, EBI-1051317;
CC P62913-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-11027771, EBI-9090795;
CC P62913-2; P61981: YWHAG; NbExp=3; IntAct=EBI-11027771, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:27829214}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9CXW4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62913-1, P39026-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P62913-2, P39026-2;
CC Sequence=VSP_008320;
CC -!- DISEASE: Diamond-Blackfan anemia 7 (DBA7) [MIM:612562]: 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:19061985, ECO:0000269|PubMed:19191325}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; X79234; CAA55816.1; -; mRNA.
DR EMBL; L05092; AAC15856.1; -; mRNA.
DR EMBL; AF101385; AAD20460.3; -; Genomic_DNA.
DR EMBL; BC018970; AAH18970.1; -; mRNA.
DR EMBL; AF432212; AAL99919.1; -; mRNA.
DR EMBL; AB007171; BAA25831.1; -; Genomic_DNA.
DR CCDS; CCDS238.1; -.
DR CCDS; CCDS85940.1; -. [P62913-2]
DR PIR; S45049; S45049.
DR RefSeq; NP_000966.2; NM_000975.3. [P62913-1]
DR RefSeq; NP_001186731.1; NM_001199802.1. [P62913-2]
DR PDB; 4UG0; EM; -; LJ=1-178.
DR PDB; 4V6X; EM; 5.00 A; CJ=1-178.
DR PDB; 4XXB; X-ray; 2.40 A; A=1-178.
DR PDB; 5AJ0; EM; 3.50 A; AJ=1-178.
DR PDB; 5LKS; EM; 3.60 A; LJ=1-178.
DR PDB; 5T2C; EM; 3.60 A; q=1-178.
DR PDB; 6IP5; EM; 3.90 A; 2E=1-178.
DR PDB; 6IP6; EM; 4.50 A; 2E=1-178.
DR PDB; 6IP8; EM; 3.90 A; 2E=1-178.
DR PDB; 6LQM; EM; 3.09 A; N=1-178.
DR PDB; 6LSR; EM; 3.13 A; N=1-178.
DR PDB; 6LSS; EM; 3.23 A; N=1-178.
DR PDB; 6LU8; EM; 3.13 A; N=1-178.
DR PDB; 6OLE; EM; 3.10 A; L=9-177.
DR PDB; 6OLF; EM; 3.90 A; L=9-177.
DR PDB; 6OLG; EM; 3.40 A; AJ=9-177.
DR PDB; 6OLI; EM; 3.50 A; L=9-177.
DR PDB; 6OLZ; EM; 3.90 A; AJ=9-177.
DR PDB; 6OM0; EM; 3.10 A; L=9-177.
DR PDB; 6OM7; EM; 3.70 A; L=9-177.
DR PDB; 6QZP; EM; 2.90 A; LJ=3-178.
DR PDB; 6W6L; EM; 3.84 A; L=1-178.
DR PDB; 6XA1; EM; 2.80 A; LJ=3-178.
DR PDB; 6Y0G; EM; 3.20 A; LJ=1-178.
DR PDB; 6Y2L; EM; 3.00 A; LJ=1-178.
DR PDB; 6Y57; EM; 3.50 A; LJ=1-178.
DR PDB; 6Y6X; EM; 2.80 A; LJ=3-178.
DR PDB; 6Z6L; EM; 3.00 A; LJ=1-178.
DR PDB; 6Z6M; EM; 3.10 A; LJ=1-178.
DR PDB; 6Z6N; EM; 2.90 A; LJ=1-178.
DR PDB; 6ZM7; EM; 2.70 A; LJ=1-178.
DR PDB; 6ZME; EM; 3.00 A; LJ=1-178.
DR PDB; 6ZMI; EM; 2.60 A; LJ=1-178.
DR PDB; 6ZMO; EM; 3.10 A; LJ=1-178.
DR PDB; 7BHP; EM; 3.30 A; LJ=1-178.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 4XXB; -.
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; P62913; -.
DR SMR; P62913; -.
DR BioGRID; 112055; 482.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62913; -.
DR IntAct; P62913; 105.
DR MINT; P62913; -.
DR STRING; 9606.ENSP00000363676; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR MoonProt; P62913; -.
DR GlyGen; P62913; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62913; -.
DR MetOSite; P62913; -.
DR PhosphoSitePlus; P62913; -.
DR SwissPalm; P62913; -.
DR BioMuta; RPL11; -.
DR DMDM; 51702795; -.
DR SWISS-2DPAGE; P62913; -.
DR EPD; P62913; -.
DR jPOST; P62913; -.
DR MassIVE; P62913; -.
DR MaxQB; P62913; -.
DR PaxDb; P62913; -.
DR PeptideAtlas; P62913; -.
DR PRIDE; P62913; -.
DR ProteomicsDB; 57452; -.
DR ProteomicsDB; 57453; -. [P62913-2]
DR TopDownProteomics; P62913-1; -. [P62913-1]
DR Antibodypedia; 1241; 332 antibodies from 31 providers.
DR DNASU; 6135; -.
DR Ensembl; ENST00000374550.8; ENSP00000363676.4; ENSG00000142676.14. [P62913-2]
DR Ensembl; ENST00000643754.2; ENSP00000496250.1; ENSG00000142676.14. [P62913-1]
DR GeneID; 6135; -.
DR KEGG; hsa:6135; -.
DR MANE-Select; ENST00000643754.2; ENSP00000496250.1; NM_000975.5; NP_000966.2.
DR CTD; 6135; -.
DR DisGeNET; 6135; -.
DR GeneCards; RPL11; -.
DR GeneReviews; RPL11; -.
DR HGNC; HGNC:10301; RPL11.
DR HPA; ENSG00000142676; Low tissue specificity.
DR MalaCards; RPL11; -.
DR MIM; 604175; gene.
DR MIM; 612562; phenotype.
DR neXtProt; NX_P62913; -.
DR OpenTargets; ENSG00000142676; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34664; -.
DR VEuPathDB; HostDB:ENSG00000142676; -.
DR eggNOG; KOG0397; Eukaryota.
DR GeneTree; ENSGT00910000144211; -.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; P62913; -.
DR OMA; QTETIKW; -.
DR PhylomeDB; P62913; -.
DR TreeFam; TF300017; -.
DR PathwayCommons; P62913; -.
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; P62913; -.
DR SIGNOR; P62913; -.
DR BioGRID-ORCS; 6135; 830 hits in 1079 CRISPR screens.
DR ChiTaRS; RPL11; human.
DR GeneWiki; RPL11; -.
DR GenomeRNAi; 6135; -.
DR Pharos; P62913; Tbio.
DR PRO; PR:P62913; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P62913; protein.
DR Bgee; ENSG00000142676; Expressed in ganglionic eminence and 208 other tissues.
DR ExpressionAtlas; P62913; baseline and differential.
DR Genevisible; P62913; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0008097; F:5S rRNA binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IMP:CAFA.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000435; P:negative regulation of protein neddylation; IDA:CAFA.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IMP:CAFA.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:CAFA.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:CAFA.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0006605; P:protein targeting; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Diamond-Blackfan anemia; Direct protein sequencing; Disease variant;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..178
FT /note="60S ribosomal protein L11"
FT /id="PRO_0000125082"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 3
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008320"
FT VARIANT 20
FT /note="L -> H (in DBA7)"
FT /evidence="ECO:0000269|PubMed:19191325"
FT /id="VAR_055448"
FT VARIANT 161
FT /note="Missing (in DBA7)"
FT /evidence="ECO:0000269|PubMed:19061985"
FT /id="VAR_055449"
FT CONFLICT 31
FT /note="D -> G (in Ref. 1; CAA55816)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="T -> A (in Ref. 1; CAA55816)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="Y -> L (in Ref. 1; CAA55816)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="K -> E (in Ref. 1; CAA55816)"
FT /evidence="ECO:0000305"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4XXB"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4XXB"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:4XXB"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:4XXB"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4XXB"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4XXB"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4XXB"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4XXB"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:4XXB"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4XXB"
SQ SEQUENCE 178 AA; 20252 MW; 26EC965C9239774E CRC64;
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF
GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD
PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKY DGIILPGK
