EIF5B
entrez
9669
canonical
uniprot
O60841
canonical
ensembl
ENSG00000158417
resolver
ensp
ENSP00000289371
resolver
enst
ENST00000289371
resolver
genesymbol
EIF5B
resolver
genesymbol_syn
IF2
resolver
genesymbol_syn
KIAA0741
resolver
hgnc
HGNC:30793
resolver
uniprot
O95805
resolver
uniprot
Q53RV7
resolver
uniprot
Q53SI8
resolver
uniprot
Q8N5A0
resolver
uniprot
Q9UF81
resolver
uniprot
Q9UMN7
resolver
uniprot_entry
IF2P_HUMAN
resolver
uniprot_entry
Q8N5A0_HUMAN
resolver
uniprot_sec
O95805
resolver
uniprot_sec
Q53RV7
resolver
uniprot_sec
Q53SI8
resolver
uniprot_sec
Q9UF81
resolver
uniprot_sec
Q9UMN7
resolver
amino_acid_sequence
MGKKQKNKSEDSTKDDIDLDALAAEIEGAGAAKEQEPQKSKGKKKKEKKKQDFDEDDILKELEELSLEAQGIKADRETVAVKPTENNEEEFTSKDKKKKGQKGKKQSFDDNDSEELEDKDSKSKKTAKPKVEMYSGSDDDDDFNKLPKKAKGKAQKSNKKWDGSEEDEDNSKKIKERSRINSSGESGDESDEFLQSRKGQKKNQKNKPGPNIESGNEDDDASFKIKTVAQKKAEKKERERKKRDEEKAKLRKLKEKEELETGKKDQSKQKESQRKFEEETVKSKVTVDTGVIPASEEKAETPTAAEDDNEGDKKKKDKKKKKGEKEEKEKEKKKGPSKATVKAMQEALAKLKEEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEATLKLLQAQGVEVPSKDSLPKKRPIYEDKKRKKIPQQLESKEVSESMELCAAVEVMEQGVPEKEETPPPVEPEEEEDTEDAGLDDWEAMASDEETEKVEGNKVHIEVKENPEEEEEEEEEEEEDEESEEEEEEEGESEGSEGDEEDEKVSDEKDSGKTLDKKPSKEMSSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHSKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKEDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKIKILPQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII
uniprot
proteins
ec_number
3.6.5.3
uniprot
proteins
function
FUNCTION: Plays a role in translation initiation (PubMed:10659855, PubMed:35732735). Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon (PubMed:10659855, PubMed:35732735). Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex (PubMed:12569173, PubMed:35732735). Is released after formation of the 80S initiation complex (PubMed:35732735). Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes (PubMed:10659855, PubMed:35732735). In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit (PubMed:10659855). {ECO:0000269|PubMed:10659855, ECO:0000269|PubMed:12569173, ECO:0000269|PubMed:35732735}.
uniprot
proteins
mass_dalton
138827
uniprot
proteins
mutagenesis
MUTAGEN 640; /note="V->G: Loss of activity in vivo. Retains full activity in vitro."; /evidence="ECO:0000269|PubMed:10200264"; MUTAGEN 706; /note="H->E: Loss of activity; both in vivo and in vitro. Loss of EIF5B release from the 80S initiation complex, certainly due to loss of ability to hydrolyze GTP."; /evidence="ECO:0000269|PubMed:10200264, ECO:0000269|PubMed:35732735"; MUTAGEN 706; /note="H->Q: Loss of activity in vivo. Partial activity in vitro."; /evidence="ECO:0000269|PubMed:10200264"; MUTAGEN 759; /note="D->N: Loss of activity; both in vivo and in vitro."; /evidence="ECO:0000269|PubMed:10200264"; MUTAGEN 1105; /note="R->A: Disruption of contacts with the Met-tRNA acceptor stem; when associated with A-1174."; /evidence="ECO:0000269|PubMed:35732735"; MUTAGEN 1174; /note="R->A: Disruption of contacts with the Met-tRNA acceptor stem; when associated with A-1105."; /evidence="ECO:0000269|PubMed:35732735"; MUTAGEN 1188..1189; /note="RQ->ER: Disruption of contacts with eIF1A (EIF1AX); when associated with E-1199 and 1218-R-R-1219."; /evidence="ECO:0000269|PubMed:35732735"; MUTAGEN 1199; /note="R->E: Disruption of contacts with eIF1A (EIF1AX); when associated with 1188-E-E-1189 and 1218-R-R-1219."; /evidence="ECO:0000269|PubMed:35732735"; MUTAGEN 1218..1219; /note="EI->RR: Disruption of contacts with eIF1A (EIF1AX); when associated with 1188-E-R-1189 and E-1199."; /evidence="ECO:0000269|PubMed:35732735
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Cleaved and inactivated by the protease 3C of poliovirus, Coxsackievirus B3 and Human rhinovirus 14, allowing the virus to shutoff the host cell translation. {ECO:0000269|PubMed:18572216}.
uniprot
proteins
protein_family
Classic translation factor GTPase family
uniprot
proteins
protein_family
IF-2 subfamily
uniprot
proteins
protein_family
TRAFAC class translation factor GTPase superfamily
uniprot
proteins
pubmed
10200264
uniprot
proteins
pubmed
10432305
uniprot
proteins
pubmed
10659855
uniprot
proteins
pubmed
11124703
uniprot
proteins
pubmed
12569173
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18572216
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
30211544
uniprot
proteins
pubmed
35732735
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1220
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}.
uniprot
proteins