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RS19A_DROME
ID   RS19A_DROME             Reviewed;         156 AA.
AC   P39018; A4V4N1; B7Z0Y8; Q9VXE1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=40S ribosomal protein S19a;
GN   Name=RpS19a; Synonyms=RpS19; ORFNames=CG4464;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Canton-S;
RX   PubMed=8367309; DOI=10.1093/nar/21.16.3897;
RA   Baumgartner S.W., Martin D., Chiquet-Ehrismann R.;
RT   "Drosophila ribosomal protein S19 cDNA sequence.";
RL   Nucleic Acids Res. 21:3897-3897(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Willig T.-N.D., Peters L.L., Parra M.K., Tchernia G., Mohandas N.;
RT   "RPS19 gene in Mus musculus and Drosophila melanogaster, and conserved
RT   features among 40 different species.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
RX   PubMed=23636399; DOI=10.1038/nature12104;
RA   Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA   Wilson D.N., Beckmann R.;
RT   "Structures of the human and Drosophila 80S ribosome.";
RL   Nature 497:80-85(2013).
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS19 family.
CC       {ECO:0000305}.
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DR   EMBL; X73153; CAA51677.1; -; mRNA.
DR   EMBL; AF216206; AAF65682.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09412.1; -; Genomic_DNA.
DR   EMBL; AY118868; AAM50728.1; -; mRNA.
DR   RefSeq; NP_001285338.1; NM_001298409.1.
DR   RefSeq; NP_001285339.1; NM_001298410.1.
DR   RefSeq; NP_523376.1; NM_078652.4.
DR   RefSeq; NP_727992.1; NM_167526.3.
DR   RefSeq; NP_727993.1; NM_167527.3.
DR   PDB; 4V6W; EM; 6.00 A; AT=1-156.
DR   PDB; 6XU6; EM; 3.50 A; AT=6-148.
DR   PDB; 6XU7; EM; 4.90 A; AT=6-148.
DR   PDB; 6XU8; EM; 3.00 A; AT=6-144.
DR   PDBsum; 4V6W; -.
DR   PDBsum; 6XU6; -.
DR   PDBsum; 6XU7; -.
DR   PDBsum; 6XU8; -.
DR   AlphaFoldDB; P39018; -.
DR   SMR; P39018; -.
DR   BioGRID; 58971; 91.
DR   IntAct; P39018; 20.
DR   MINT; P39018; -.
DR   STRING; 7227.FBpp0074086; -.
DR   PaxDb; P39018; -.
DR   PRIDE; P39018; -.
DR   DNASU; 32635; -.
DR   EnsemblMetazoa; FBtr0074311; FBpp0074086; FBgn0010412.
DR   EnsemblMetazoa; FBtr0074312; FBpp0074087; FBgn0010412.
DR   EnsemblMetazoa; FBtr0074313; FBpp0074088; FBgn0010412.
DR   EnsemblMetazoa; FBtr0340149; FBpp0309135; FBgn0010412.
DR   EnsemblMetazoa; FBtr0345129; FBpp0311350; FBgn0010412.
DR   GeneID; 32635; -.
DR   KEGG; dme:Dmel_CG4464; -.
DR   CTD; 32635; -.
DR   FlyBase; FBgn0010412; RpS19a.
DR   VEuPathDB; VectorBase:FBgn0010412; -.
DR   eggNOG; KOG3411; Eukaryota.
DR   GeneTree; ENSGT00940000164207; -.
DR   HOGENOM; CLU_108559_0_1_1; -.
DR   InParanoid; P39018; -.
DR   OMA; YIDGPVG; -.
DR   OrthoDB; 1434984at2759; -.
DR   PhylomeDB; P39018; -.
DR   Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-DME-72649; Translation initiation complex formation.
DR   Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   SignaLink; P39018; -.
DR   BioGRID-ORCS; 32635; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 32635; -.
DR   PRO; PR:P39018; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0010412; Expressed in mouthpart and 23 other tissues.
DR   ExpressionAtlas; P39018; baseline and differential.
DR   Genevisible; P39018; DM.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR   GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001266; Ribosomal_S19e.
DR   InterPro; IPR018277; Ribosomal_S19e_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11710; PTHR11710; 1.
DR   Pfam; PF01090; Ribosomal_S19e; 1.
DR   SMART; SM01413; Ribosomal_S19e; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00628; RIBOSOMAL_S19E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..156
FT                   /note="40S ribosomal protein S19a"
FT                   /id="PRO_0000153824"
FT   CONFLICT        37
FT                   /note="V -> I (in Ref. 1; CAA51677)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   156 AA;  17291 MW;  E70529088E255DEA CRC64;
     MPGVTVKDID QHAVTKAVAV FLKKTGKLKV PDQMDIVKTA KFKELAPYDP DWFYVRCASI
     LRHLYHRSPA GVGSITKIYG GRKRNGVHPS HFCRAADGAA RKALQALEHA RLVEKHPDGG
     RKLSSIGQRD LDRIANQIVF KQRDAAKQTG PIVISK
 
 
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