P78344 · IF4G2_HUMAN
- ProteinEukaryotic translation initiation factor 4 gamma 2
- GeneEIF4G2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids907 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.
Miscellaneous
This gene has been shown to be extensively edited in the liver of APOBEC1 transgenic animal model. Its aberrant editing could contribute to the potent oncogenesis induced by overexpression of APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a fundamental translational repressor.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | adherens junction | |
Cellular Component | axon | |
Cellular Component | cytosol | |
Cellular Component | eukaryotic translation initiation factor 4F complex | |
Cellular Component | membrane | |
Molecular Function | cadherin binding | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | translation factor activity, RNA binding | |
Molecular Function | translation initiation factor activity | |
Biological Process | cell death | |
Biological Process | heart development | |
Biological Process | macromolecule biosynthetic process | |
Biological Process | negative regulation of autophagy | |
Biological Process | positive regulation of axon extension | |
Biological Process | positive regulation of cell growth | |
Biological Process | positive regulation of dendritic spine development | |
Biological Process | positive regulation of translation | |
Biological Process | regulation of cell cycle | |
Biological Process | regulation of translational initiation | |
Biological Process | translational initiation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 4 gamma 2
- Short nameseIF-4-gamma 2; eIF-4G 2; eIF4G 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP78344
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048923 | 236 | in dbSNP:rs34885591 | |||
Sequence: L → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 815 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000213325 | 1-907 | UniProt | Eukaryotic translation initiation factor 4 gamma 2 | |||
Sequence: MESAIAEGGASRFSASSGGGGSRGAPQHYPKTAGNSEFLGKTPGQNAQKWIPARSTRRDDNSAANNSANEKERHDAIFRKVRGILNKLTPEKFDKLCLELLNVGVESKLILKGVILLIVDKALEEPKYSSLYAQLCLRLAEDAPNFDGPAAEGQPGQKQSTTFRRLLISKLQDEFENRTRNVDVYDKRENPLLPEEEEQRAIAKIKMLGNIKFIGELGKLDLIHESILHKCIKTLLEKKKRVQLKDMGEDLECLCQIMRTVGPRLDHERAKSLMDQYFARMCSLMLSKELPARIRFLLQDTVELREHHWVPRKAFLDNGPKTINQIRQDAVKDLGVFIPAPMAQGMRSDFFLEGPFMPPRMKMDRDPLGGLADMFGQMPGSGIGTGPGVIQDRFSPTMGRHRSNQLFNGHGGHIMPPTQSQFGEMGGKFMKSQGLSQLYHNQSQGLLSQLQGQSKDMPPRFSKKGQLNADEISLRPAQSFLMNKNQVPKLQPQITMIPPSAQPPRTQTPPLGQTPQLGLKTNPPLIQEKPAKTSKKPPPSKEELLKLTETVVTEYLNSGNANEAVNGVREMRAPKHFLPEMLSKVIILSLDRSDEDKEKASSLISLLKQEGIATSDNFMQAFLNVLDQCPKLEVDIPLVKSYLAQFAARAIISELVSISELAQPLESGTHFPLFLLCLQQLAKLQDREWLTELFQQSKVNMQKMLPEIDQNKDRMLEILEGKGLSFLFPLLKLEKELLKQIKLDPSPQTIYKWIKDNISPKLHVDKGFVNILMTSFLQYISSEVNPPSDETDSSSAPSKEQLEQEKQLLLSFKPVMQKFLHDHVDLQVSALYALQVHCYNSNFPKGMLLRFFVHFYDMEIIEEEAFLAWKEDITQEFPGKGKALFQVNQWLTWLETAEEEESEEEAD | |||||||
Modified residue | 11 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 16 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 89 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 360 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 395 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 431 | UniProt | N6-methyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 443 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 443 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 479 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 505 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 508 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 514 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 514 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 575 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 602 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 902 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 902 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation; hyperphosphorylated during mitosis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed in all adult tissues examined, with high levels in skeletal muscle and heart. Also expressed in fetal brain, lung, liver and kidney.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the serine/threonine protein kinases MKNK1 and MKNK2 (PubMed:9878069).
Binds EIF4A and EIF3 (PubMed:9030685, PubMed:9049310).
Interacts with MIF4GD (PubMed:18025107).
Interacts with DAZAP2 (PubMed:17984221).
Binds EIF4A and EIF3 (PubMed:9030685, PubMed:9049310).
Interacts with MIF4GD (PubMed:18025107).
Interacts with DAZAP2 (PubMed:17984221).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P78344 | EIF2S2 P20042 | 4 | EBI-296519, EBI-711977 | |
BINARY | P78344 | EIF4A1 P60842 | 5 | EBI-296519, EBI-73449 | |
BINARY | P78344 | HSPB1 P04792 | 3 | EBI-296519, EBI-352682 | |
XENO | P78344 | PRO_0000308465 P29991 | 4 | EBI-296519, EBI-8826747 | |
BINARY | P78344-1 | EIF4A1 P60842 | 3 | EBI-16040248, EBI-73449 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-71 | Disordered | ||||
Sequence: MESAIAEGGASRFSASSGGGGSRGAPQHYPKTAGNSEFLGKTPGQNAQKWIPARSTRRDDNSAANNSANEK | ||||||
Compositional bias | 38-63 | Polar residues | ||||
Sequence: FLGKTPGQNAQKWIPARSTRRDDNSA | ||||||
Domain | 78-308 | MIF4G | ||||
Sequence: FRKVRGILNKLTPEKFDKLCLELLNVGVESKLILKGVILLIVDKALEEPKYSSLYAQLCLRLAEDAPNFDGPAAEGQPGQKQSTTFRRLLISKLQDEFENRTRNVDVYDKRENPLLPEEEEQRAIAKIKMLGNIKFIGELGKLDLIHESILHKCIKTLLEKKKRVQLKDMGEDLECLCQIMRTVGPRLDHERAKSLMDQYFARMCSLMLSKELPARIRFLLQDTVELREHH | ||||||
Region | 498-541 | Disordered | ||||
Sequence: PPSAQPPRTQTPPLGQTPQLGLKTNPPLIQEKPAKTSKKPPPSK | ||||||
Domain | 543-666 | MI | ||||
Sequence: ELLKLTETVVTEYLNSGNANEAVNGVREMRAPKHFLPEMLSKVIILSLDRSDEDKEKASSLISLLKQEGIATSDNFMQAFLNVLDQCPKLEVDIPLVKSYLAQFAARAIISELVSISELAQPLE | ||||||
Domain | 720-904 | W2 | ||||
Sequence: EGKGLSFLFPLLKLEKELLKQIKLDPSPQTIYKWIKDNISPKLHVDKGFVNILMTSFLQYISSEVNPPSDETDSSSAPSKEQLEQEKQLLLSFKPVMQKFLHDHVDLQVSALYALQVHCYNSNFPKGMLLRFFVHFYDMEIIEEEAFLAWKEDITQEFPGKGKALFQVNQWLTWLETAEEEESEE |
Sequence similarities
Belongs to the eukaryotic initiation factor 4G family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P78344-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length907
- Mass (Da)102,362
- Last updated1997-05-01 v1
- Checksum4EF050B5EEA4DF91
P78344-2
- Name2
- Differences from canonical
- 434-471: Missing
Computationally mapped potential isoform sequences
There are 15 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3DQV9 | D3DQV9_HUMAN | EIF4G2 | 907 | ||
H0YEC5 | H0YEC5_HUMAN | EIF4G2 | 244 | ||
H0YEW3 | H0YEW3_HUMAN | EIF4G2 | 20 | ||
H0YEN8 | H0YEN8_HUMAN | EIF4G2 | 112 | ||
H0YEI7 | H0YEI7_HUMAN | EIF4G2 | 84 | ||
H0YDC0 | H0YDC0_HUMAN | EIF4G2 | 116 | ||
H0YD77 | H0YD77_HUMAN | EIF4G2 | 282 | ||
H0YD99 | H0YD99_HUMAN | EIF4G2 | 84 | ||
H0YE22 | H0YE22_HUMAN | EIF4G2 | 234 | ||
H0YE87 | H0YE87_HUMAN | EIF4G2 | 46 | ||
H0YE44 | H0YE44_HUMAN | EIF4G2 | 88 | ||
H0YCF8 | H0YCF8_HUMAN | EIF4G2 | 129 | ||
H0YCH5 | H0YCH5_HUMAN | EIF4G2 | 444 | ||
H0Y3P2 | H0Y3P2_HUMAN | EIF4G2 | 869 | ||
E9PKF8 | E9PKF8_HUMAN | EIF4G2 | 185 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 38-63 | Polar residues | ||||
Sequence: FLGKTPGQNAQKWIPARSTRRDDNSA | ||||||
Sequence conflict | 169 | in Ref. 2; AAC51166 | ||||
Sequence: S → P | ||||||
Sequence conflict | 233 | in Ref. 2; AAC51166 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 245 | in Ref. 2; AAC51166 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 351 | in Ref. 2; AAC51166 | ||||
Sequence: F → L | ||||||
Alternative sequence | VSP_038726 | 434-471 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 441 | in Ref. 6; AAH18746 | ||||
Sequence: N → S | ||||||
Sequence conflict | 531 | in Ref. 2; AAC51166 | ||||
Sequence: A → G | ||||||
Sequence conflict | 534 | in Ref. 6; AAH43149 | ||||
Sequence: S → N | ||||||
Sequence conflict | 613 | in Ref. 2; AAC51166 | ||||
Sequence: A → G | ||||||
Sequence conflict | 861 | in Ref. 2; AAC51166 | ||||
Sequence: I → S | ||||||
Sequence conflict | 899 | in Ref. 2; AAC51166 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73824 EMBL· GenBank· DDBJ | AAB49973.1 EMBL· GenBank· DDBJ | mRNA | ||
U76111 EMBL· GenBank· DDBJ | AAC51166.1 EMBL· GenBank· DDBJ | mRNA | ||
X89713 EMBL· GenBank· DDBJ | CAA61857.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK223548 EMBL· GenBank· DDBJ | BAD97268.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AC116535 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC014930 EMBL· GenBank· DDBJ | AAH14930.2 EMBL· GenBank· DDBJ | mRNA | ||
BC018746 EMBL· GenBank· DDBJ | AAH18746.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018975 EMBL· GenBank· DDBJ | AAH18975.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039851 EMBL· GenBank· DDBJ | AAH39851.1 EMBL· GenBank· DDBJ | mRNA | ||
BC043149 EMBL· GenBank· DDBJ | AAH43149.2 EMBL· GenBank· DDBJ | mRNA | ||
BC111415 EMBL· GenBank· DDBJ | AAI11416.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111548 EMBL· GenBank· DDBJ | AAI11549.2 EMBL· GenBank· DDBJ | mRNA | ||
AB063323 EMBL· GenBank· DDBJ | BAB93515.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |