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RS14A_DROME
ID   RS14A_DROME             Reviewed;         151 AA.
AC   C0HKA0; P14130; Q0KHV1; Q8SZL7; Q9V3R5;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=40S ribosomal protein S14a {ECO:0000305};
GN   Name=RpS14a {ECO:0000312|FlyBase:FBgn0004403};
GN   ORFNames=CG1524 {ECO:0000312|FlyBase:FBgn0004403};
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 [GENOMIC DNA].
RX   PubMed=3141788; DOI=10.1128/mcb.8.10.4314-4321.1988;
RA   Brown S.J., Rhoads D.D., Stewart M.J., van Slyke B., Chen I.-T.,
RA   Johnson T.K., Denell R.E., Roufa D.J.;
RT   "Ribosomal protein S14 is encoded by a pair of highly conserved, adjacent
RT   genes on the X chromosome of Drosophila melanogaster.";
RL   Mol. Cell. Biol. 8:4314-4321(1988).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo, and Head;
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   [5]
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 universal ribosomal protein uS11 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL48136.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M21045; AAA28852.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF46298.1; -; Genomic_DNA.
DR   EMBL; AY070665; AAL48136.1; ALT_FRAME; mRNA.
DR   PIR; A30815; A30815.
DR   RefSeq; NP_001284995.1; NM_001298066.1.
DR   RefSeq; NP_524884.1; NM_080145.5.
DR   RefSeq; NP_536352.1; NM_080427.4.
DR   RefSeq; NP_727218.1; NM_167137.2.
DR   PDB; 4V6W; EM; 6.00 A; AO=1-151.
DR   PDB; 6XU6; EM; 3.50 A; AO=25-151.
DR   PDB; 6XU7; EM; 4.90 A; AO=18-151.
DR   PDB; 6XU8; EM; 3.00 A; AO=25-151.
DR   PDBsum; 4V6W; -.
DR   PDBsum; 6XU6; -.
DR   PDBsum; 6XU7; -.
DR   PDBsum; 6XU8; -.
DR   AlphaFoldDB; C0HKA0; -.
DR   SMR; C0HKA0; -.
DR   STRING; 7227.FBpp0071050; -.
DR   PRIDE; C0HKA0; -.
DR   DNASU; 47219; -.
DR   EnsemblMetazoa; FBtr0071094; FBpp0071050; FBgn0004403.
DR   EnsemblMetazoa; FBtr0071095; FBpp0071051; FBgn0004403.
DR   EnsemblMetazoa; FBtr0071096; FBpp0071052; FBgn0004404.
DR   EnsemblMetazoa; FBtr0345291; FBpp0311458; FBgn0004404.
DR   GeneID; 47218; -.
DR   GeneID; 47219; -.
DR   KEGG; dme:Dmel_CG1524; -.
DR   KEGG; dme:Dmel_CG1527; -.
DR   CTD; 47218; -.
DR   CTD; 47219; -.
DR   FlyBase; FBgn0004403; RpS14a.
DR   VEuPathDB; VectorBase:FBgn0004403; -.
DR   VEuPathDB; VectorBase:FBgn0004404; -.
DR   eggNOG; KOG0407; Eukaryota.
DR   OMA; KWGVAHI; -.
DR   OrthoDB; 1408000at2759; -.
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-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
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   BioGRID-ORCS; 47218; 0 hits in 1 CRISPR screen.
DR   BioGRID-ORCS; 47219; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; RpS14a; fly.
DR   PRO; PR:C0HKA0; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0004403; Expressed in wing disc and 25 other tissues.
DR   ExpressionAtlas; C0HKA0; baseline and differential.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA 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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.420.80; -; 1.
DR   HAMAP; MF_01310; Ribosomal_S11; 1.
DR   InterPro; IPR001971; Ribosomal_S11.
DR   InterPro; IPR018102; Ribosomal_S11_CS.
DR   InterPro; IPR036967; Ribosomal_S11_sf.
DR   PANTHER; PTHR11759; PTHR11759; 1.
DR   Pfam; PF00411; Ribosomal_S11; 1.
DR   PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR   PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..151
FT                   /note="40S ribosomal protein S14a"
FT                   /id="PRO_0000123342"
FT   REGION          131..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   151 AA;  16265 MW;  7FD3C0E7A32C4216 CRC64;
     MAPRKAKVQK EEVQVQLGPQ VRDGEIVFGV AHIYASFNDT FVHVTDLSGR ETIARVTGGM
     KVKADRDEAS PYAAMLAAQD VAEKCKTLGI TALHIKLRAT GGNKTKTPGP GAQSALRALA
     RSSMKIGRIE DVTPIPSDST RRKGGRRGRR L
 
 
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