RS2_BOVIN
ID RS2_BOVIN Reviewed; 293 AA.
AC O18789; A2V9C7; Q3T0W5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=40S ribosomal protein S2;
GN Name=RPS2;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-293.
RC TISSUE=Aorta;
RA Lileinsiek B., Rocha M., Umansky V., Benner A., Lin Y., Ziegler R.,
RA Nawroth P.P., Schirrmacher V.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. Plays a role in the assembly and function of the 40S ribosomal
CC subunit. Mutations in this protein affects the control of translational
CC fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC ribosome assembly. {ECO:0000250|UniProtKB:P25443}.
CC -!- SUBUNIT: Interacts with zinc finger protein ZNF277 (via zinc-finger
CC domains); the interaction is direct; the interaction is extra-
CC ribosomal. Interaction with ZNF277 competes with the binding of RPS2 to
CC protein arginine methyltransferase PRMT3.
CC {ECO:0000250|UniProtKB:P15880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15880}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P15880}. Note=Probably
CC localized to nucleolus and cytoplasm in complex with ZNF277.
CC {ECO:0000250|UniProtKB:P15880}.
CC -!- PTM: Citrullinated by PADI4 in the Arg/Gly-rich region. {ECO:0000250}.
CC -!- PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple
CC sites in the Arg/Gly-rich region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; BC102227; AAI02228.1; -; mRNA.
DR EMBL; AF013215; AAB65437.1; -; mRNA.
DR RefSeq; NP_001028785.1; NM_001033613.2.
DR AlphaFoldDB; O18789; -.
DR SMR; O18789; -.
DR STRING; 9913.ENSBTAP00000012544; -.
DR PaxDb; O18789; -.
DR PeptideAtlas; O18789; -.
DR PRIDE; O18789; -.
DR GeneID; 286867; -.
DR KEGG; bta:286867; -.
DR CTD; 6187; -.
DR eggNOG; KOG0877; Eukaryota.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; O18789; -.
DR OrthoDB; 1197354at2759; -.
DR TreeFam; TF300806; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Citrullination; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CHAIN 2..293
FT /note="40S ribosomal protein S2"
FT /id="PRO_0000131671"
FT DOMAIN 102..165
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 275
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15880"
FT CONFLICT 48
FT /note="R -> G (in Ref. 2; AAB65437)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> P (in Ref. 2; AAB65437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31235 MW; 40C19794ECCBDA7B CRC64;
MADDAGAAGG PGGPGGPGMG GRGGFRGGFG SGVRGRGRGR GRGRGRGRGA RGGKAEDKEW
LPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ
RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV
PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT
FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT
