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RL37_BOVIN
ID   RL37_BOVIN              Reviewed;          97 AA.
AC   P79244; A6QLM5; Q3T109;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=60S ribosomal protein L37;
GN   Name=RPL37;
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 (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-93.
RX   PubMed=7588717; DOI=10.1111/j.1432-1033.1995.tb20874.x;
RA   Su S., Bird R.C.;
RT   "Cell cycle, differentiation and tissue-independent expression of ribosomal
RT   protein L37.";
RL   Eur. J. Biochem. 232:789-797(1995).
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:P61927}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P61927}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61927}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC       {ECO:0000305}.
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DR   EMBL; BC102179; AAI02180.1; -; mRNA.
DR   EMBL; BC148017; AAI48018.1; -; mRNA.
DR   EMBL; S79980; AAD14319.1; -; mRNA.
DR   RefSeq; NP_001071600.1; NM_001078132.2.
DR   AlphaFoldDB; P79244; -.
DR   SMR; P79244; -.
DR   STRING; 9913.ENSBTAP00000006781; -.
DR   PaxDb; P79244; -.
DR   PRIDE; P79244; -.
DR   Ensembl; ENSBTAT00000006781; ENSBTAP00000006781; ENSBTAG00000005142.
DR   GeneID; 768317; -.
DR   KEGG; bta:768317; -.
DR   CTD; 6167; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005142; -.
DR   eggNOG; KOG3475; Eukaryota.
DR   GeneTree; ENSGT00390000005254; -.
DR   HOGENOM; CLU_150908_0_0_1; -.
DR   InParanoid; P79244; -.
DR   OMA; RMAYLKH; -.
DR   OrthoDB; 1560654at2759; -.
DR   TreeFam; TF300260; -.
DR   Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-BTA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Proteomes; UP000009136; Chromosome 20.
DR   Bgee; ENSBTAG00000005142; Expressed in retropharyngeal lymph node and 104 other tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0097371; F:MDM2/MDM4 family protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:Ensembl.
DR   GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IEA:Ensembl.
DR   GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.20.25.30; -; 1.
DR   HAMAP; MF_00547; Ribosomal_L37e; 1.
DR   InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR   InterPro; IPR001569; Ribosomal_L37e.
DR   InterPro; IPR018267; Ribosomal_L37e_CS.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   Pfam; PF01907; Ribosomal_L37e; 1.
DR   SUPFAM; SSF57829; SSF57829; 1.
DR   PROSITE; PS01077; RIBOSOMAL_L37E; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..97
FT                   /note="60S ribosomal protein L37"
FT                   /id="PRO_0000139704"
FT   ZN_FING         19..37
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P49166"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P49166"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P49166"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P49166"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61927"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61927"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61927"
FT   CONFLICT        16
FT                   /note="H -> D (in Ref. 2; AAD14319)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   97 AA;  11078 MW;  F565A11E983027C9 CRC64;
     MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG
     TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS
 
 
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