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DescriptionSubName: Full=Ribosomal protein S23 {ECO:0000313|Ensembl:ENSDARP00000035273}; SubName: Full=Zgc:171710 {ECO:0000313|EMBL:AAI71649.1}; SubName: Full=Zgc:171710 protein {ECO:0000313|EMBL:AAI53999.1};
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MyHits synonymsA8KB78_DANRE , A8KB78 , 8FCEB4CB8C40B815
match map segment
ipfam:Ribosom_S12_S23 ipat:RIBOSOMAL_S12  
Legends: 1, ipat:RIBOSOMAL_S12 [T].
ID   A8KB78_DANRE            Unreviewed;       143 AA.
AC   A8KB78;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   10-MAY-2017, entry version 76.
DE   SubName: Full=Ribosomal protein S23 {ECO:0000313|Ensembl:ENSDARP00000035273};
DE   SubName: Full=Zgc:171710 {ECO:0000313|EMBL:AAI71649.1};
DE   SubName: Full=Zgc:171710 protein {ECO:0000313|EMBL:AAI53999.1};
GN   Name=rps23 {ECO:0000313|Ensembl:ENSDARP00000035273,
GN   ECO:0000313|ZFIN:ZDB-GENE-080220-50};
GN   ORFNames=zgc:171710 {ECO:0000313|EMBL:AAI53999.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI53999.1};
RN   [1] {ECO:0000313|EMBL:AAI53999.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gill {ECO:0000313|EMBL:AAI53999.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAI71649.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000035273}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000035273};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [4] {ECO:0000313|Ensembl:ENSDARP00000035273, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000035273,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS12
CC       family. {ECO:0000256|RuleBase:RU003622}.
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DR   EMBL; FP067440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC153998; AAI53999.1; -; mRNA.
DR   EMBL; BC171649; AAI71649.1; -; mRNA.
DR   EMBL; BC171653; AAI71653.1; -; mRNA.
DR   RefSeq; NP_001103591.1; NM_001110121.1.
DR   UniGene; Dr.41813; -.
DR   STRING; 7955.ENSDARP00000035273; -.
DR   Ensembl; ENSDART00000039206; ENSDARP00000035273; ENSDARG00000021838.
DR   GeneID; 100000341; -.
DR   KEGG; dre:100000341; -.
DR   CTD; 6228; -.
DR   ZFIN; ZDB-GENE-080220-50; rps23.
DR   eggNOG; KOG1749; Eukaryota.
DR   eggNOG; COG0048; LUCA.
DR   GeneTree; ENSGT00550000074784; -.
DR   HOGENOM; HOG000040064; -.
DR   HOVERGEN; HBG054200; -.
DR   KO; K02973; -.
DR   OMA; MPGKKSP; -.
DR   OrthoDB; EOG091G0R2G; -.
DR   TreeFam; TF300871; -.
DR   Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DRE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-DRE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-DRE-72649; Translation initiation complex formation.
DR   Reactome; R-DRE-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DRE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-DRE-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-DRE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-DRE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Proteomes; UP000000437; Chromosome 11.
DR   Bgee; ENSDARG00000021838; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd03367; Ribosomal_S23; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006032; Ribosomal_S12/S23.
DR   InterPro; IPR005680; Ribosomal_S23_euk/arc.
DR   PANTHER; PTHR11652; PTHR11652; 1.
DR   Pfam; PF00164; Ribosom_S12_S23; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00982; uS12_E_A; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:A8KB78};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU003622};
KW   Ribosomal protein {ECO:0000256|RuleBase:RU003622}.
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CC   The following FT lines are automated annotations from the MyHits database.
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FT   MYHIT        30    142       ipfam:Ribosom_S12_S23 [T]
FT   MYHIT        60     67       ipat:RIBOSOMAL_S12 [T]
SQ   SEQUENCE   143 AA;  15849 MW;  8FCEB4CB8C40B815 CRC64;
     MGKCRGLRTA RKLRNHRREQ KWHDKQYKKA HLGTALKANP FGGASHAKGI VLEKVGVEAK
     QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF
     KVVKVANVSL LALYKGKKER PRS
//