RS6_BOVIN
ID RS6_BOVIN Reviewed; 249 AA.
AC Q5E995;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=40S ribosomal protein S6;
GN Name=RPS6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 40S small ribosomal subunit (By similarity).
CC Plays an important role in controlling cell growth and proliferation
CC through the selective translation of particular classes of mRNA (By
CC similarity). {ECO:0000250|UniProtKB:P62753}.
CC -!- PTM: Ribosomal protein S6 is the major substrate of protein kinases in
CC eukaryote ribosomes. The phosphorylation is stimulated by growth
CC factors, tumor promoting agents, and mitogens. It is dephosphorylated
CC at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and
CC RPS6KA3; phosphorylation at these sites facilitates the assembly of the
CC pre-initiation complex. {ECO:0000250|UniProtKB:P62753}.
CC -!- PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-
CC 137 by KDM8. {ECO:0000250|UniProtKB:P62753}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family.
CC {ECO:0000305}.
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DR EMBL; BT021025; AAX09042.1; -; mRNA.
DR EMBL; AY911358; AAW82123.1; -; mRNA.
DR EMBL; BC102493; AAI02494.1; -; mRNA.
DR RefSeq; NP_001015548.1; NM_001015548.2.
DR AlphaFoldDB; Q5E995; -.
DR SMR; Q5E995; -.
DR STRING; 9913.ENSBTAP00000049139; -.
DR iPTMnet; Q5E995; -.
DR PaxDb; Q5E995; -.
DR PeptideAtlas; Q5E995; -.
DR PRIDE; Q5E995; -.
DR Ensembl; ENSBTAT00000014877; ENSBTAP00000049139; ENSBTAG00000023462.
DR GeneID; 787914; -.
DR KEGG; bta:787914; -.
DR CTD; 6194; -.
DR VEuPathDB; HostDB:ENSBTAG00000023462; -.
DR eggNOG; KOG1646; Eukaryota.
DR GeneTree; ENSGT00390000009819; -.
DR InParanoid; Q5E995; -.
DR OMA; FYEKRMS; -.
DR OrthoDB; 1326714at2759; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000023462; Expressed in myometrium and 105 other tissues.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0042593; P:glucose homeostasis; ISS:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR InterPro; IPR014401; Ribosomal_S6_euk.
DR InterPro; IPR001377; Ribosomal_S6e.
DR InterPro; IPR018282; Ribosomal_S6e_CS.
DR PANTHER; PTHR11502; PTHR11502; 1.
DR Pfam; PF01092; Ribosomal_S6e; 1.
DR PIRSF; PIRSF002129; Ribosom_S6_euk; 1.
DR SMART; SM01405; Ribosomal_S6e; 1.
DR PROSITE; PS00578; RIBOSOMAL_S6E; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydroxylation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..249
FT /note="40S ribosomal protein S6"
FT /id="PRO_0000239293"
FT REGION 217..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="(3R)-3-hydroxyarginine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 235
FT /note="Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 236
FT /note="Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62753"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62753"
SQ SEQUENCE 249 AA; 28667 MW; 071F5258853C9DDF CRC64;
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG
FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD
IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKDGKKPR TKAPKIQRLV
TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS
TSKSESSQK
