RL14_MOUSE
ID RL14_MOUSE Reviewed; 217 AA.
AC Q9CR57; Q9D8Q1;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=60S ribosomal protein L14;
GN Name=Rpl14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-85 AND LYS-206, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(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:0000250|UniProtKB:P50914}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P50914}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50914}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 family.
CC {ECO:0000305}.
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DR EMBL; AK007807; BAB25272.1; -; mRNA.
DR EMBL; AK012277; BAB28136.1; -; mRNA.
DR EMBL; AK013912; BAB29051.1; -; mRNA.
DR CCDS; CCDS40809.1; -.
DR RefSeq; NP_080250.1; NM_025974.2.
DR PDB; 6SWA; EM; 3.10 A; L=1-217.
DR PDB; 7CPU; EM; 2.82 A; LM=1-217.
DR PDB; 7CPV; EM; 3.03 A; LM=1-217.
DR PDB; 7LS1; EM; 3.30 A; G1=1-217.
DR PDB; 7LS2; EM; 3.10 A; G1=1-217.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; Q9CR57; -.
DR SMR; Q9CR57; -.
DR BioGRID; 211949; 98.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; Q9CR57; -.
DR IntAct; Q9CR57; 6.
DR MINT; Q9CR57; -.
DR STRING; 10090.ENSMUSP00000131489; -.
DR iPTMnet; Q9CR57; -.
DR PhosphoSitePlus; Q9CR57; -.
DR SwissPalm; Q9CR57; -.
DR CPTAC; non-CPTAC-3667; -.
DR EPD; Q9CR57; -.
DR jPOST; Q9CR57; -.
DR MaxQB; Q9CR57; -.
DR PaxDb; Q9CR57; -.
DR PeptideAtlas; Q9CR57; -.
DR PRIDE; Q9CR57; -.
DR ProteomicsDB; 255017; -.
DR TopDownProteomics; Q9CR57; -.
DR DNASU; 67115; -.
DR Ensembl; ENSMUST00000165532; ENSMUSP00000131489; ENSMUSG00000025794.
DR GeneID; 67115; -.
DR KEGG; mmu:67115; -.
DR UCSC; uc009scr.1; mouse.
DR CTD; 9045; -.
DR MGI; MGI:1914365; Rpl14.
DR VEuPathDB; HostDB:ENSMUSG00000025794; -.
DR eggNOG; KOG3421; Eukaryota.
DR GeneTree; ENSGT00390000007888; -.
DR HOGENOM; CLU_082438_0_0_1; -.
DR InParanoid; Q9CR57; -.
DR OMA; RWANCAW; -.
DR OrthoDB; 1433759at2759; -.
DR PhylomeDB; Q9CR57; -.
DR TreeFam; TF314356; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 67115; 30 hits in 70 CRISPR screens.
DR ChiTaRS; Rpl14; mouse.
DR PRO; PR:Q9CR57; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CR57; protein.
DR Bgee; ENSMUSG00000025794; Expressed in morula and 221 other tissues.
DR ExpressionAtlas; Q9CR57; baseline and differential.
DR Genevisible; Q9CR57; MM.
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; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR CDD; cd06088; KOW_RPL14; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002784; Ribosomal_L14e_dom.
DR InterPro; IPR039660; Ribosomal_protein_L14.
DR InterPro; IPR041985; RPL14_KOW.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11127; PTHR11127; 1.
DR Pfam; PF01929; Ribosomal_L14e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..217
FT /note="60S ribosomal protein L14"
FT /id="PRO_0000132032"
FT REPEAT 173..177
FT /note="1-1; approximate"
FT REPEAT 178..182
FT /note="1-2"
FT REPEAT 183..187
FT /note="1-3"
FT REPEAT 188..192
FT /note="1-4"
FT REPEAT 195..197
FT /note="2-1"
FT REPEAT 198..200
FT /note="2-2"
FT REGION 162..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..192
FT /note="4 X 5 AA tandem repeats of Q-K-A-[APS]-X"
FT REGION 195..200
FT /note="2 X 3 AA tandem repeats of K-G-Q"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50914"
FT MOD_RES 85
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 85
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P50914"
FT CONFLICT 26
FT /note="A -> T (in Ref. 1; BAB25272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 23564 MW; 1DB57CAA155D05A9 CRC64;
MVFRRYVEVG RVAYISFGPH AGKLVAIVDV IDQNRALVDG PCTRVRRQAM PFKCMQLTDF
ILKFPHSARQ KYVRKAWEKA DINTKWAATR WAKKIDARER KAKMTDFDRF KVMKAKKMRN
RIIKTEVKKL QRAAILKASP KKAAVAKAAI AAAAAAAAAK AKVPAKKATG PGKKAAGQKA
PAQKAAGQKA APPAKGQKGQ KTPAQKAPAP KAAGKKA
