EF1B_BOVIN
ID EF1B_BOVIN Reviewed; 225 AA.
AC Q5E983; A6QLF3; Q56JY7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
GN Name=EEF1B;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC to EF-1-alpha to GTP. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation affects the GDP/GTP exchange rate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; BT021037; AAX09054.1; -; mRNA.
DR EMBL; AY911340; AAW82108.1; -; mRNA.
DR EMBL; BC147944; AAI47945.1; -; mRNA.
DR RefSeq; NP_001014936.1; NM_001014936.1.
DR AlphaFoldDB; Q5E983; -.
DR BMRB; Q5E983; -.
DR SMR; Q5E983; -.
DR STRING; 9913.ENSBTAP00000029304; -.
DR PaxDb; Q5E983; -.
DR PeptideAtlas; Q5E983; -.
DR PRIDE; Q5E983; -.
DR Ensembl; ENSBTAT00000029304; ENSBTAP00000029304; ENSBTAG00000021979.
DR Ensembl; ENSBTAT00000078391; ENSBTAP00000058501; ENSBTAG00000021979.
DR GeneID; 520875; -.
DR KEGG; bta:520875; -.
DR CTD; 1933; -.
DR VEuPathDB; HostDB:ENSBTAG00000021979; -.
DR VGNC; VGNC:54422; EEF1B2.
DR eggNOG; KOG1668; Eukaryota.
DR GeneTree; ENSGT00950000183014; -.
DR HOGENOM; CLU_050172_0_0_1; -.
DR InParanoid; Q5E983; -.
DR OMA; FEVKPWD; -.
DR OrthoDB; 1464823at2759; -.
DR TreeFam; TF313134; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000021979; Expressed in myometrium and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM01182; EF-1_beta_acid; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Elongation factor; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..225
FT /note="Elongation factor 1-beta"
FT /id="PRO_0000155020"
FT DOMAIN 2..90
FT /note="GST C-terminal"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70251"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT MOD_RES 106
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P34826"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P24534"
FT CONFLICT 94
FT /note="D -> G (in Ref. 2; AAW82108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24805 MW; 326B28F3B26A5454 CRC64;
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSGPPPADLC HALRWYNHIK
SYEKEKASLP GVKKALGKYG PANVEDTTES GATDSKDDDD IDLFGSDDEE ESEEAKRLRE
ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV
GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF DEYVQSMDVA AFNKI
