RS3A_CALJA
ID RS3A_CALJA Reviewed; 264 AA.
AC B0KW94;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
GN Name=RPS3A {ECO:0000255|HAMAP-Rule:MF_03122};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role during erythropoiesis through regulation of
CC transcription factor DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (28S, 5.8S and 5S). Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Binds with high affinity to
CC IPO4. Interacts with DDIT3. {ECO:0000255|HAMAP-Rule:MF_03122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03122}. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC {ECO:0000255|HAMAP-Rule:MF_03122}.
CC -!- PTM: ADP-ribosylated at Tyr-155 by PARP1 in presence of HPF1.
CC {ECO:0000250|UniProtKB:P61247}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03122}.
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DR EMBL; DP000567; ABY79117.1; -; Genomic_DNA.
DR RefSeq; XP_002744350.1; XM_002744304.4.
DR AlphaFoldDB; B0KW94; -.
DR SMR; B0KW94; -.
DR STRING; 9483.ENSCJAP00000000618; -.
DR GeneID; 100394558; -.
DR KEGG; cjc:100394558; -.
DR eggNOG; KOG1628; Eukaryota.
DR InParanoid; B0KW94; -.
DR OrthoDB; 1207239at2759; -.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
DR InterPro; IPR027500; Ribosomal_S1/3_euk.
DR InterPro; IPR001593; Ribosomal_S3Ae.
DR Pfam; PF01015; Ribosomal_S3Ae; 1.
DR SMART; SM01397; Ribosomal_S3Ae; 1.
PE 3: Inferred from homology;
KW Acetylation; ADP-ribosylation; Cytoplasm; Differentiation; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..264
FT /note="40S ribosomal protein S3a"
FT /id="PRO_0000389294"
FT REGION 233..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97351"
FT MOD_RES 155
FT /note="ADP-ribosyltyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97351"
FT MOD_RES 249
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT MOD_RES 256
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61247"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61247"
SQ SEQUENCE 264 AA; 29892 MW; ED0F87B3B0B6049B CRC64;
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD
GLKGRVFEVS LADFQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM
IEAHVDVKTT DGYLLRLFCV GFTKKHNNQI RKTSYAQHQQ VCQIRKKMME IMTREVQTND
LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKI PKFELGKLME LHGEGSSSGK
ATGDETGAKV ERADGYEPPV QESV
