Overview
| Uniprot ID | Q2VIR3 |
|---|
| Protein Name | Eukaryotic translation initiation factor 2 subunit 3B |
|---|
| Gene Name | EIF2S3B |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 266 |
IRSFDVNKPGCEVDD |
| 59 |
HGKSTVVKAISGVHT |
Function
Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity)
Protein Sequence
10
MAGGEAGVTL
20
GQPHLSRQDL
30
TTLDVTKLTP
40
LSHEVISRQA
50
TINIGTIGHV
60
AHGKSTVVKA
70
ISGVHTVRFK
80
NELERNITIK
90
LGYANAKIYQ
100
LDDPSCPRPE
110
CYRSCGSSMP
120
DEFPTDIPGT
130
KGNFRLVRHV
140
SFVDCPGHDI
150
LMATMLNGAA
160
VMDAALLLIA
170
GNESCPQPQT
180
SEHLAAIEIM
190
KLKHILILQN
200
KIDLVKERQA
210
KEQYEQILAF
220
VQGTVAEGAP
230
IIPISAQLKY
240
NIEVVCEYIV
250
KKIPVPPRDF
260
TSEPRLIVIR
270
SFDVNKPGCE
280
VDDLKGGVAG
290
GSILKGVLKV
300
GQETEVRPGI
310
VSKDSEGKLM
320
CKSIFSKIVS
330
LFAEHNDLQY
340
AAPGGLIGVG
350
TKIDPTLCRA
360
DRMVGQILGA
370
VGALPEIFTE
380
LEISYFLLRR
390
LLGVRTEGDK
400
KAAKVQKLSK
410
NEVLMVNIGS
420
LSTGGRVSAV
430
KADLGKIVLT
440
NPVCTEVGEK
450
IALSRRVEKH
460
WRLIGWGQIR
470
RGVTIKPTVD
DD
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005850 |
eukaryotic translation initiation factor 2 complex |
| Molecular Function |
GO:0005525 |
GTP binding |
| Molecular Function |
GO:0003924 |
GTPase activity |
| Molecular Function |
GO:0003743 |
translation initiation factor activity |
| Molecular Function |
GO:0000049 |
tRNA binding |
| Biological Process |
GO:0001731 |
formation of translation preinitiation complex |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.