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RS9_RAT
ID   RS9_RAT                 Reviewed;         194 AA.
AC   P29314; Q6P9W7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=40S ribosomal protein S9;
GN   Name=Rps9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8503895; DOI=10.1006/bbrc.1993.1596;
RA   Chan Y.-L., Paz V., Olvera J., Wool I.G.;
RT   "The primary structure of rat ribosomal protein S9.";
RL   Biochem. Biophys. Res. Commun. 193:106-112(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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).
CC   -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC       containing untranslated mRNAs. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
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DR   EMBL; X66370; CAA47013.1; -; mRNA.
DR   EMBL; BC060560; AAH60560.1; -; mRNA.
DR   PIR; JN0587; S21497.
DR   RefSeq; NP_001300864.1; NM_001313935.1.
DR   RefSeq; NP_112370.2; NM_031108.4.
DR   AlphaFoldDB; P29314; -.
DR   SMR; P29314; -.
DR   BioGRID; 249644; 5.
DR   IntAct; P29314; 8.
DR   STRING; 10116.ENSRNOP00000015234; -.
DR   iPTMnet; P29314; -.
DR   PhosphoSitePlus; P29314; -.
DR   jPOST; P29314; -.
DR   PaxDb; P29314; -.
DR   PRIDE; P29314; -.
DR   Ensembl; ENSRNOT00000086622; ENSRNOP00000074779; ENSRNOG00000058909.
DR   GeneID; 103689992; -.
DR   GeneID; 81772; -.
DR   KEGG; rno:103689992; -.
DR   UCSC; RGD:619889; rat.
DR   CTD; 103689992; -.
DR   CTD; 6203; -.
DR   RGD; 619889; Rps9.
DR   eggNOG; KOG3301; Eukaryota.
DR   GeneTree; ENSGT00550000074829; -.
DR   HOGENOM; CLU_089738_0_0_1; -.
DR   InParanoid; P29314; -.
DR   OMA; ARQFITH; -.
DR   OrthoDB; 1310788at2759; -.
DR   PhylomeDB; P29314; -.
DR   TreeFam; TF300795; -.
DR   Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-RNO-72649; Translation initiation complex formation.
DR   Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P29314; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000058909; Expressed in thymus and 19 other tissues.
DR   ExpressionAtlas; P29314; baseline and differential.
DR   Genevisible; P29314; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:1990932; F:5.8S rRNA binding; IDA:RGD.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR   GO; GO:0045182; F:translation regulator activity; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; ISO:RGD.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR018079; Ribosomal_S4_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01018; uS4_arch; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Ubl conjugation.
FT   CHAIN           1..194
FT                   /note="40S ribosomal protein S9"
FT                   /id="PRO_0000132692"
FT   DOMAIN          108..182
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   REGION          162..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZWN5"
FT   MOD_RES         116
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZWN5"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46781"
FT   MOD_RES         155
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46781"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46781"
FT   CROSSLNK        93
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46781"
FT   CROSSLNK        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P46781"
FT   CONFLICT        138
FT                   /note="R -> L (in Ref. 1; CAA47013)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="R -> L (in Ref. 1; CAA47013)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22591 MW;  E9CE3CBD59524F81 CRC64;
     MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL AKIRKAAREL
     LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL KIEDFLERRL QTQVFKLGLA
     KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK
     GQGGAGAGDD EEED
 
 
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