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RS18_CANLF
ID   RS18_CANLF              Reviewed;         152 AA.
AC   Q5TJE9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=40S ribosomal protein S18;
GN   Name=RPS18;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA   Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA   Ollier W.E.R., Binns M.M.;
RT   "Genomic sequence of the class II region of the canine MHC: comparison with
RT   the MHC of other mammalian species.";
RL   Genomics 85:48-59(2005).
CC   -!- FUNCTION: Located at the top of the head of the 40S subunit, it
CC       contacts several helices of the 18S rRNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ630366; CAI11439.1; -; Genomic_DNA.
DR   RefSeq; NP_001041547.1; NM_001048082.1.
DR   PDB; 4V5Z; EM; 8.70 A; m=1-152.
DR   PDBsum; 4V5Z; -.
DR   AlphaFoldDB; Q5TJE9; -.
DR   SMR; Q5TJE9; -.
DR   STRING; 9612.ENSCAFP00000001357; -.
DR   PaxDb; Q5TJE9; -.
DR   PRIDE; Q5TJE9; -.
DR   Ensembl; ENSCAFT00030024505; ENSCAFP00030021390; ENSCAFG00030013216.
DR   Ensembl; ENSCAFT00030024575; ENSCAFP00030021460; ENSCAFG00030013216.
DR   Ensembl; ENSCAFT00040038692; ENSCAFP00040033750; ENSCAFG00040020851.
DR   Ensembl; ENSCAFT00040038732; ENSCAFP00040033785; ENSCAFG00040020851.
DR   Ensembl; ENSCAFT00845036787; ENSCAFP00845028802; ENSCAFG00845020845.
DR   Ensembl; ENSCAFT00845036893; ENSCAFP00845028884; ENSCAFG00845020845.
DR   GeneID; 403685; -.
DR   KEGG; cfa:403685; -.
DR   CTD; 6222; -.
DR   VEuPathDB; HostDB:ENSCAFG00845020845; -.
DR   eggNOG; KOG3311; Eukaryota.
DR   GeneTree; ENSGT00390000012691; -.
DR   HOGENOM; CLU_103849_0_1_1; -.
DR   InParanoid; Q5TJE9; -.
DR   OMA; IRAYRGI; -.
DR   OrthoDB; 1343043at2759; -.
DR   TreeFam; TF317649; -.
DR   Reactome; R-CFA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-CFA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-CFA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-CFA-72649; Translation initiation complex formation.
DR   Reactome; R-CFA-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-CFA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-CFA-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-CFA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-CFA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-CFA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   EvolutionaryTrace; Q5TJE9; -.
DR   Proteomes; UP000002254; Chromosome 12.
DR   Bgee; ENSCAFG00000000950; Expressed in ovary and 48 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:AgBase.
DR   GO; GO:0015935; C:small ribosomal subunit; ISS:AgBase.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 4.10.910.10; -; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR   InterPro; IPR001892; Ribosomal_S13.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
FT   CHAIN           2..152
FT                   /note="40S ribosomal protein S18"
FT                   /id="PRO_0000132211"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
FT   MOD_RES         94
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
FT   MOD_RES         106
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
FT   CROSSLNK        91
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
FT   CROSSLNK        94
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62269"
SQ   SEQUENCE   152 AA;  17719 MW;  4DAF0662C3F37F22 CRC64;
     MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT
     EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH
     RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK
 
 
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