RL10A_BOVIN
ID RL10A_BOVIN Reviewed; 217 AA.
AC Q5E9E6; Q3SZY5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=60S ribosomal protein L10a;
GN Name=RPL10A;
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 STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000250|UniProtKB:P62906}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P62906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62906}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020974; AAX08991.1; -; mRNA.
DR EMBL; BC102653; AAI02654.1; -; mRNA.
DR RefSeq; NP_001015647.1; NM_001015647.1.
DR AlphaFoldDB; Q5E9E6; -.
DR SMR; Q5E9E6; -.
DR STRING; 9913.ENSBTAP00000025963; -.
DR PaxDb; Q5E9E6; -.
DR PeptideAtlas; Q5E9E6; -.
DR PRIDE; Q5E9E6; -.
DR Ensembl; ENSBTAT00000025963; ENSBTAP00000025963; ENSBTAG00000019494.
DR GeneID; 533310; -.
DR KEGG; bta:533310; -.
DR CTD; 4736; -.
DR VEuPathDB; HostDB:ENSBTAG00000019494; -.
DR VGNC; VGNC:54233; RPL10A.
DR eggNOG; KOG1570; Eukaryota.
DR GeneTree; ENSGT00390000008767; -.
DR HOGENOM; CLU_062853_3_0_1; -.
DR InParanoid; Q5E9E6; -.
DR OMA; TMAINFL; -.
DR OrthoDB; 1172076at2759; -.
DR TreeFam; TF300791; -.
DR Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-BTA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000019494; Expressed in isthmus of fallopian tube and 104 other tissues.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62906"
FT CHAIN 2..217
FT /note="60S ribosomal protein L10a"
FT /id="PRO_0000125817"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62906"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P53026"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53026"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62906"
FT MOD_RES 118
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62906"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62906"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62906"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62906"
SQ SEQUENCE 217 AA; 24831 MW; 38F1A31119A751D3 CRC64;
MSSKVSRDTL YEAVREVLHG NQRKRRKFLE TVELQISLKN YDPQKDKRFS GTVRLKSTPR
PKFSVCVLGD QQHCDEAKAV DIPHMDIEAL KKLNKNKKLV KKLAKKYDAF LASESLIKQI
PRILGPGLNK AGKFPSLLTH NENMVAKVDE VKSTIKFQMK KVLCLAVAVG HVKMTDDELV
YNIHLAVNFL VSLLKKNWQN VRALYIKSTM GKPQRLY
