RL11B_SCHPO
ID RL11B_SCHPO Reviewed; 174 AA.
AC P0CT78; Q10157; Q9UTS3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=60S ribosomal protein L11-B;
GN Name=rpl1102; Synonyms=rpl11b; ORFNames=SPBC17G9.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee J.-J., Kim H.-G., Lim C.-J.;
RT "Cloning and nucleotide sequence of the cDNA encoding the ribosomal protein
RT L11 from Schizosaccharomyces pombe.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- MISCELLANEOUS: There are two genes for L11 in S.pombe.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13719.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF201080; AAF13719.1; ALT_INIT; mRNA.
DR EMBL; CU329671; CAB52808.1; -; Genomic_DNA.
DR PIR; T38395; T38395.
DR RefSeq; NP_594150.1; NM_001019574.2.
DR RefSeq; NP_595899.1; NM_001021806.2.
DR AlphaFoldDB; P0CT78; -.
DR SMR; P0CT78; -.
DR STRING; 284812.P0CT78; -.
DR iPTMnet; P0CT78; -.
DR EnsemblFungi; SPAC26A3.07c.1; SPAC26A3.07c.1:pep; SPAC26A3.07c.
DR EnsemblFungi; SPBC17G9.10.1; SPBC17G9.10.1:pep; SPBC17G9.10.
DR GeneID; 2539846; -.
DR GeneID; 2541591; -.
DR KEGG; spo:SPAC26A3.07c; -.
DR KEGG; spo:SPBC17G9.10; -.
DR PomBase; SPBC17G9.10; rpl1102.
DR VEuPathDB; FungiDB:SPAC26A3.07c; -.
DR VEuPathDB; FungiDB:SPBC17G9.10; -.
DR OMA; MDFYCIM; -.
DR PhylomeDB; P0CT78; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P0CT78; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..174
FT /note="60S ribosomal protein L11-B"
FT /id="PRO_0000433412"
SQ SEQUENCE 174 AA; 19891 MW; E7057DCD8A7B74D4 CRC64;
MAEKAQNPMK ELRISKLVLN ISLGESGDRL TRAAKVLEQL SGQTPVFSKA RYTIRRFGIR
RNEKIACHVT VRGPKAEEIL ERGLKVKEYE LKKRNFSATG NFGFGIQEHI DLGIKYDPSI
GIYGMDFYVV MDRPGMRVAR RKAQRGRVGY THKINAEDTI NWFKQKYDAV VLGK
