(data stored in ACNUC9543 zone)

SWISSPROT: 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   08-MAY-2019, entry version 139.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   homologous to the yeast L29 ribosomal protein gene.";
RL   Nucleic Acids Res. 15:1019-1029(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10449908;
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;
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
RT   architecture of a conserved syntenic region on human chromosome
RT   11p15.3 (including gene 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- PTM: Hydroxylated on His-39 by MINA. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL15
CC       family. {ECO:0000305}.
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   SMR; P14115; -.
DR   BioGrid; 205001; 4.
DR   IntAct; P14115; 5.
DR   MINT; P14115; -.
DR   STRING; 10090.ENSMUSP00000123410; -.
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   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   eggNOG; KOG1742; Eukaryota.
DR   eggNOG; COG0200; LUCA.
DR   GeneTree; ENSGT00390000005534; -.
DR   HOGENOM; HOG000231263; -.
DR   InParanoid; P14115; -.
DR   KO; K02900; -.
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   PRO; PR:P14115; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000046364; Expressed in 48 organ(s), highest expression level in spleen.
DR   ExpressionAtlas; P14115; baseline and differential.
DR   Genevisible; P14115; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_01341; Ribosomal_L15; 1.
DR   InterPro; IPR036227; L18e/L15P_sf.
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;
DR   PRODOM; P14115.
DR   SWISS-2DPAGE; P14115.
KW   Acetylation; Complete proteome; Hydroxylation; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    148       60S ribosomal protein L27a.
FT                                /FTId=PRO_0000104880.
FT   MOD_RES      39     39       (3S)-3-hydroxyhistidine. {ECO:0000250}.
FT   MOD_RES      47     47       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46776}.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46776}.
FT   MOD_RES      68     68       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     110    110       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46776}.
FT   CONFLICT     30     30       G -> S (in Ref. 1; CAA28678).
FT                                {ECO:0000305}.
FT   CONFLICT     78     78       L -> P (in Ref. 1; CAA28678 and 2;
FT                                BAA77362). {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
//

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