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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
 
 
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