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RS14_CRIGR
ID   RS14_CRIGR              Reviewed;         151 AA.
AC   P62265; P06366;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=40S ribosomal protein S14;
GN   Name=RPS14; Synonyms=EMTB;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3839563; DOI=10.1128/mcb.5.7.1655-1659.1985;
RA   Rhoads D.D., Roufa D.J.;
RT   "Emetine resistance of Chinese hamster cells: structures of wild-type and
RT   mutant ribosomal protein S14 mRNAs.";
RL   Mol. Cell. Biol. 5:1655-1659(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2267626; DOI=10.1007/bf01233092;
RA   Diaz J.J., Rhoads D.D., Roufa D.J.;
RT   "Genetic analysis of a vital mammalian housekeeping locus using CHO cells
RT   that express a transfected mutant allele.";
RL   Somat. Cell Mol. Genet. 16:517-528(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1921707; DOI=10.1093/oxfordjournals.molbev.a040665;
RA   Rhoads D.D., Roufa D.J.;
RT   "Molecular evolution of the mammalian ribosomal protein gene, RPS14.";
RL   Mol. Biol. Evol. 8:503-514(1991).
CC   -!- MISCELLANEOUS: Mutations in S14 can lead to resistance to the protein
CC       synthesis inhibitor emetine.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC       {ECO:0000305}.
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DR   EMBL; M11241; AAA37016.1; -; mRNA.
DR   EMBL; M35008; AAA37017.1; -; Genomic_DNA.
DR   PIR; A02725; R4HY14.
DR   RefSeq; NP_001231448.1; NM_001244519.1.
DR   AlphaFoldDB; P62265; -.
DR   SMR; P62265; -.
DR   STRING; 10029.NP_001231448.1; -.
DR   Ensembl; ENSCGRT00001023942; ENSCGRP00001019698; ENSCGRG00001019064.
DR   GeneID; 100689292; -.
DR   KEGG; cge:100689292; -.
DR   CTD; 6208; -.
DR   eggNOG; KOG0407; Eukaryota.
DR   GeneTree; ENSGT00390000000703; -.
DR   OMA; KWGVAHI; -.
DR   OrthoDB; 1408000at2759; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:Ensembl.
DR   GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
DR   GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Isopeptide bond; Phosphoprotein; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..151
FT                   /note="40S ribosomal protein S14"
FT                   /id="PRO_0000123336"
FT   REGION          131..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62263"
FT   MOD_RES         133
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62263"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62263"
FT   CROSSLNK        61
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62263"
FT   CROSSLNK        63
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62263"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62263"
SQ   SEQUENCE   151 AA;  16273 MW;  4F4387F9FADAC278 CRC64;
     MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM
     KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA
     RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L
 
 
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