RS2_RAT
ID RS2_RAT Reviewed; 293 AA.
AC P27952; Q4G062;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=40S ribosomal protein S2;
GN Name=Rps2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 111-128.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1939063; DOI=10.1016/s0021-9258(18)54884-5;
RA Suzuki K., Olvera J., Wool I.G.;
RT "Primary structure of rat ribosomal protein S2. A ribosomal protein with
RT arginine-glycine tandem repeats and RGGF motifs that are associated with
RT nucleolar localization and binding to ribonucleic acids.";
RL J. Biol. Chem. 266:20007-20010(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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; X57432; CAA40679.1; -; mRNA.
DR EMBL; BC098726; AAH98726.1; -; mRNA.
DR PIR; S18828; R3RTS2.
DR RefSeq; NP_114026.3; NM_031838.3.
DR AlphaFoldDB; P27952; -.
DR SMR; P27952; -.
DR BioGRID; 249832; 3.
DR IntAct; P27952; 6.
DR MINT; P27952; -.
DR STRING; 10116.ENSRNOP00000019508; -.
DR iPTMnet; P27952; -.
DR PhosphoSitePlus; P27952; -.
DR jPOST; P27952; -.
DR PaxDb; P27952; -.
DR PRIDE; P27952; -.
DR Ensembl; ENSRNOT00000019508; ENSRNOP00000019508; ENSRNOG00000014179.
DR GeneID; 83789; -.
DR KEGG; rno:83789; -.
DR UCSC; RGD:619887; rat.
DR CTD; 6187; -.
DR RGD; 619887; Rps2.
DR eggNOG; KOG0877; Eukaryota.
DR GeneTree; ENSGT00940000153095; -.
DR HOGENOM; CLU_065898_0_2_1; -.
DR InParanoid; P27952; -.
DR OMA; KSPYQEH; -.
DR OrthoDB; 1197354at2759; -.
DR PhylomeDB; P27952; -.
DR PRO; PR:P27952; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014179; Expressed in spleen and 18 other tissues.
DR Genevisible; P27952; RN.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IMP:RGD.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:RGD.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IMP:RGD.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:RGD.
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 1: Evidence at protein level;
KW Acetylation; Citrullination; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; 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_0000131675"
FT REPEAT 9..11
FT /note="1-1"
FT REPEAT 12..14
FT /note="1-2"
FT REPEAT 15..17
FT /note="1-3"
FT REPEAT 22..25
FT /note="2-1"
FT REPEAT 26..29
FT /note="2-2"
FT REPEAT 34..35
FT /note="3-1"
FT REPEAT 36..37
FT /note="3-2"
FT REPEAT 38..39
FT /note="3-3"
FT REPEAT 40..41
FT /note="3-4"
FT REPEAT 42..43
FT /note="3-5"
FT REPEAT 44..45
FT /note="3-6"
FT REPEAT 46..47
FT /note="3-7"
FT REPEAT 48..49
FT /note="3-8"
FT REPEAT 51..52
FT /note="3-9"
FT DOMAIN 102..165
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..17
FT /note="3 X 3 AA tandem repeats of G-G-P"
FT REGION 22..29
FT /note="2 X 4 AA tandem repeats of R-G-G-F"
FT REGION 34..52
FT /note="9 X 2 AA tandem repeats of R-G"
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"
SQ SEQUENCE 293 AA; 31231 MW; 9092DB564AA624C9 CRC64;
MADDAGAAGG PGGPGGPGLG GRGGFRGGFG SGLRGRGRGR GRGRGRGRGA RGGKAEDKEW
IPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ
RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV
PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT
FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT
