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DENR_BOVIN
ID   DENR_BOVIN              Reviewed;         198 AA.
AC   Q2HJ47;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Density-regulated protein;
DE            Short=DRP;
GN   Name=DENR;
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=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the translation of target mRNAs by
CC       scanning and recognition of the initiation codon. Involved in
CC       translation initiation; promotes recruitment of aminoacetyled initiator
CC       tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA
CC       and mRNA from recycled 40S subunits following ABCE1-mediated
CC       dissociation of post-termination ribosomal complexes into subunits (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MCTS1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
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DR   EMBL; BC113316; AAI13317.1; -; mRNA.
DR   RefSeq; NP_001039993.1; NM_001046528.1.
DR   RefSeq; XP_001252166.1; XM_001252165.6.
DR   RefSeq; XP_015330995.1; XM_015475509.1.
DR   AlphaFoldDB; Q2HJ47; -.
DR   SMR; Q2HJ47; -.
DR   STRING; 9913.ENSBTAP00000046224; -.
DR   PaxDb; Q2HJ47; -.
DR   PeptideAtlas; Q2HJ47; -.
DR   PRIDE; Q2HJ47; -.
DR   Ensembl; ENSBTAT00000045998; ENSBTAP00000043335; ENSBTAG00000032433.
DR   Ensembl; ENSBTAT00000078420; ENSBTAP00000057926; ENSBTAG00000049723.
DR   GeneID; 614238; -.
DR   KEGG; bta:614238; -.
DR   CTD; 8562; -.
DR   VEuPathDB; HostDB:ENSBTAG00000032433; -.
DR   VEuPathDB; HostDB:ENSBTAG00000049723; -.
DR   eggNOG; KOG3239; Eukaryota.
DR   GeneTree; ENSGT00390000014349; -.
DR   HOGENOM; CLU_073511_1_0_1; -.
DR   InParanoid; Q2HJ47; -.
DR   OMA; VIYCGVC; -.
DR   OrthoDB; 1490022at2759; -.
DR   TreeFam; TF105912; -.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000032433; Expressed in biceps femoris and 106 other tissues.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR   GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR   InterPro; IPR005873; DENR_eukaryotes.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   TIGRFAMs; TIGR01159; DRP1; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   CHAIN           2..198
FT                   /note="Density-regulated protein"
FT                   /id="PRO_0000322640"
FT   DOMAIN          115..182
FT                   /note="SUI1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         86
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43583"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQJ6"
SQ   SEQUENCE   198 AA;  22217 MW;  E1CCFEB236B09286 CRC64;
     MAADISESGG HDCRGDQRSN TKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
     FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
     PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
     KWPEVDDDSI EDLGEVKK
 
 
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