ID EF1B_RABIT Reviewed; 225 AA.
AC P34826;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
GN Name=EEF1B; Synonyms=EF1B;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-106.
RC STRAIN=New Zealand white;
RX PubMed=8547318; DOI=10.1016/0167-4781(95)00166-2;
RA Chen C.J., Traugh J.A.;
RT "Expression of recombinant elongation factor 1 beta from rabbit in
RT Escherichia coli. Phosphorylation by casein kinase II.";
RL Biochim. Biophys. Acta 1264:303-311(1995).
CC -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC to EF-1-alpha to GTP.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC -!- PTM: Phosphorylation affects the GDP/GTP exchange rate.
CC {ECO:0000269|PubMed:8547318}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; X74728; CAA52741.1; -; mRNA.
DR PIR; S62693; S62693.
DR RefSeq; NP_001075868.1; NM_001082399.1.
DR AlphaFoldDB; P34826; -.
DR BMRB; P34826; -.
DR SMR; P34826; -.
DR STRING; 9986.ENSOCUP00000019358; -.
DR iPTMnet; P34826; -.
DR PaxDb; 9986-ENSOCUP00000019358; -.
DR GeneID; 100009286; -.
DR KEGG; ocu:100009286; -.
DR eggNOG; KOG1668; Eukaryota.
DR InParanoid; P34826; -.
DR OrthoDB; 77945at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd00292; EF1B; 1.
DR CDD; cd10308; GST_C_eEF1b_like; 1.
DR Gene3D; 1.20.1050.130; -; 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; IPR049720; EF1B_bsu/dsu.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR PANTHER; PTHR11595; EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER; 1.
DR PANTHER; PTHR11595:SF21; ELONGATION FACTOR 1-BETA; 1.
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; SSF54984; eEF-1beta-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein 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_0000155023"
FT DOMAIN 2..84
FT /note="GST C-terminal"
FT REGION 80..114
FT /note="Disordered"
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:0000269|PubMed:8547318"
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"
SQ SEQUENCE 225 AA; 24749 MW; EE8B095443DF148A CRC64;
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSGPPPADLC HALRWYNHIK
SYEKEKASLP GIKKALGTYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE
ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMVKLEE CVRSIQADGL VWGSSKLVPV
GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI
//
