RL27A_MOUSE
ID RL27A_MOUSE Reviewed; 148 AA.
AC P14115; Q9CQ16; Q9R1X6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 5.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=60S ribosomal protein L27a;
DE AltName: Full=L29;
GN Name=Rpl27a;
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 [MRNA].
RC TISSUE=Kidney;
RX PubMed=2434927; DOI=10.1093/nar/15.3.1019;
RA Belhumeur P., Paterno G.D., Boileau G., Claverie J.-M., Skup D.;
RT "Isolation and characterisation of a murine cDNA clone highly homologous to
RT the yeast L29 ribosomal protein gene.";
RL Nucleic Acids Res. 15:1019-1029(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10449908; DOI=10.1159/000015303;
RA Kusuda J., Hirai M., Tanuma R., Hirata M., Hashimoto K.;
RT "Genomic structure and chromosome location of RPL27A/Rpl27a, the genes
RT encoding human and mouse ribosomal protein L27A.";
RL Cytogenet. Cell Genet. 85:248-251(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11528127; DOI=10.1159/000056999;
RA Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA Zabel B., Hankeln T., Schmidt E.R.;
RT "Comparative genomic sequencing reveals a strikingly similar architecture
RT of a conserved syntenic region on human chromosome 11p15.3 (including gene
RT ST5) and mouse chromosome 7.";
RL Cytogenet. Cell Genet. 93:284-290(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow macrophage, Embryonic stem cell, Pancreas, and
RC Small intestine;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Kidney;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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).
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:P46776}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P46776}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46776}.
CC -!- PTM: Hydroxylated on His-39 by MINA. {ECO:0000250|UniProtKB:P46776}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC {ECO:0000305}.
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DR EMBL; X05021; CAA28678.1; -; mRNA.
DR EMBL; AB020237; BAA77362.1; -; Genomic_DNA.
DR EMBL; AJ307670; CAC38113.1; -; Genomic_DNA.
DR EMBL; AK007837; BAB25295.1; -; mRNA.
DR EMBL; AK008531; BAB25724.1; -; mRNA.
DR EMBL; AK010286; BAB26822.1; -; mRNA.
DR EMBL; AK150907; BAE29949.1; -; mRNA.
DR EMBL; AK167792; BAE39822.1; -; mRNA.
DR EMBL; AK167915; BAE39922.1; -; mRNA.
DR EMBL; CH466531; EDL16941.1; -; Genomic_DNA.
DR EMBL; BC056958; AAH56958.1; -; mRNA.
DR EMBL; BC081430; AAH81430.1; -; mRNA.
DR EMBL; BC086939; AAH86939.1; -; mRNA.
DR CCDS; CCDS40083.1; -.
DR PIR; S11557; R5MS27.
DR RefSeq; NP_036105.2; NM_011975.3.
DR PDB; 6SWA; EM; 3.10 A; Y=1-148.
DR PDB; 7LS1; EM; 3.30 A; U2=1-148.
DR PDB; 7LS2; EM; 3.10 A; U2=1-148.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P14115; -.
DR SMR; P14115; -.
DR BioGRID; 205001; 52.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR IntAct; P14115; 1.
DR STRING; 10090.ENSMUSP00000076607; -.
DR iPTMnet; P14115; -.
DR PhosphoSitePlus; P14115; -.
DR SwissPalm; P14115; -.
DR EPD; P14115; -.
DR jPOST; P14115; -.
DR MaxQB; P14115; -.
DR PaxDb; P14115; -.
DR PeptideAtlas; P14115; -.
DR PRIDE; P14115; -.
DR ProteomicsDB; 255019; -.
DR Antibodypedia; 24122; 174 antibodies from 29 providers.
DR DNASU; 26451; -.
DR Ensembl; ENSMUST00000143107; ENSMUSP00000123410; ENSMUSG00000046364.
DR GeneID; 26451; -.
DR KEGG; mmu:26451; -.
DR UCSC; uc009jdr.1; mouse.
DR CTD; 6157; -.
DR MGI; MGI:1347076; Rpl27a.
DR VEuPathDB; HostDB:ENSMUSG00000046364; -.
DR eggNOG; KOG1742; Eukaryota.
DR GeneTree; ENSGT00390000005534; -.
DR HOGENOM; CLU_109163_1_0_1; -.
DR InParanoid; P14115; -.
DR OMA; WGRVGQH; -.
DR OrthoDB; 1445443at2759; -.
DR PhylomeDB; P14115; -.
DR TreeFam; TF313742; -.
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; 26451; 24 hits in 69 CRISPR screens.
DR ChiTaRS; Rpl27a; mouse.
DR PRO; PR:P14115; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P14115; protein.
DR Bgee; ENSMUSG00000046364; Expressed in epiblast (generic) and 63 other tissues.
DR ExpressionAtlas; P14115; baseline and differential.
DR Genevisible; P14115; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IGI:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; IGI:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IGI:MGI.
DR Gene3D; 4.10.990.10; -; 1.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR027386; Rbsml_prot_L15/27a_N.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydroxylation; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..148
FT /note="60S ribosomal protein L27a"
FT /id="PRO_0000104880"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="(3S)-3-hydroxyhistidine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT CONFLICT 30
FT /note="G -> S (in Ref. 1; CAA28678)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="L -> P (in Ref. 1; CAA28678 and 2; BAA77362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16605 MW; D6E11FA50E24D206 CRC64;
MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGMHH HRINFDKYHP GYFGKVGMRH
YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKTGVAPI IDVVRSGYYK VLGKGKLPKQ
PVIVKAKFFS RRAEEKIKGV GGACVLVA
