RL27A_PONAB
ID RL27A_PONAB Reviewed; 148 AA.
AC Q5REY2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=60S ribosomal protein L27a;
GN Name=RPL27A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:P46776}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P46776}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46776}.
CC -!- PTM: Hydroxylated on His-39 by MINA. {ECO:0000250|UniProtKB:P46776}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 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; CR857381; CAH89675.1; -; mRNA.
DR RefSeq; NP_001124757.1; NM_001131285.1.
DR AlphaFoldDB; Q5REY2; -.
DR SMR; Q5REY2; -.
DR IntAct; Q5REY2; 1.
DR MINT; Q5REY2; -.
DR STRING; 9601.ENSPPYP00000017756; -.
DR Ensembl; ENSPPYT00000033876; ENSPPYP00000024613; ENSPPYG00000029639.
DR GeneID; 100936083; -.
DR KEGG; pon:100936083; -.
DR CTD; 6157; -.
DR eggNOG; KOG1742; Eukaryota.
DR GeneTree; ENSGT00390000005534; -.
DR InParanoid; Q5REY2; -.
DR OrthoDB; 1445443at2759; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 4.10.990.10; -; 1.
DR HAMAP; MF_01341; Ribosomal_L15; 1.
DR InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR027386; Rbsml_prot_L15/27a_N.
DR InterPro; IPR030878; Ribosomal_L15.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L27A; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydroxylation; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..148
FT /note="60S ribosomal protein L27a"
FT /id="PRO_0000104883"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="(3S)-3-hydroxyhistidine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46776"
SQ SEQUENCE 148 AA; 16561 MW; CB5E09C91507798F CRC64;
MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGLHH HRINFDKYHP GYFGKVGMKH
YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKTGAAPI IDVVRSGYYK VLGKGKLPKQ
PVIVKAKFFS RRAEEKIKSV GGACVLVA