RL28_RAT
ID RL28_RAT Reviewed; 137 AA.
AC P17702;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=60S ribosomal protein L28;
GN Name=Rpl28;
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 PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2207170; DOI=10.1016/0167-4781(90)90143-p;
RA Wool I.G., Chan Y.-L., Paz V., Olvera J.;
RT "The primary structure of rat ribosomal proteins: the amino acid sequences
RT of L27a and L28 and corrections in the sequences of S4 and S12.";
RL Biochim. Biophys. Acta 1050:69-73(1990).
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:P46779}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P46779}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46779}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL28 family.
CC {ECO:0000305}.
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DR EMBL; X52619; CAA36846.1; -; mRNA.
DR PIR; S13072; R5RT28.
DR AlphaFoldDB; P17702; -.
DR SMR; P17702; -.
DR IntAct; P17702; 3.
DR MINT; P17702; -.
DR STRING; 10116.ENSRNOP00000055726; -.
DR iPTMnet; P17702; -.
DR PhosphoSitePlus; P17702; -.
DR jPOST; P17702; -.
DR PaxDb; P17702; -.
DR PRIDE; P17702; -.
DR UCSC; RGD:621193; rat.
DR RGD; 621193; Rpl28.
DR eggNOG; KOG3412; Eukaryota.
DR InParanoid; P17702; -.
DR PhylomeDB; P17702; -.
DR PRO; PR:P17702; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR InterPro; IPR029004; L28e/Mak16.
DR InterPro; IPR002672; Ribosomal_L28e.
DR PANTHER; PTHR10544; PTHR10544; 1.
DR Pfam; PF01778; Ribosomal_L28e; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46779"
FT CHAIN 2..137
FT /note="60S ribosomal protein L28"
FT /id="PRO_0000122391"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P46779"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46779"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46779"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46779"
SQ SEQUENCE 137 AA; 15849 MW; 23BFD2382ACB3D7E CRC64;
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEAWPDGKGV
VVVMKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS
QKPVVVKRKR TRPTKSS