O75794 · CD123_HUMAN
- ProteinTranslation initiation factor eIF2 assembly protein
- GeneCDC123
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP-dependent protein-folding chaperone for the eIF2 complex (PubMed:35031321, PubMed:37507029).
Binds to the gamma subunit of the eIF2 complex which allows the subunit to assemble with the alpha and beta subunits (By similarity).
Binds to the gamma subunit of the eIF2 complex which allows the subunit to assemble with the alpha and beta subunits (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 104 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 107 | ATP (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 109 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 111 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 167 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 168 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 169 | ATP (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 170 | ATP (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 177 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 179 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 193 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 233 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 248 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | protein folding chaperone | |
Biological Process | eukaryotic translation initiation factor 2 complex assembly |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranslation initiation factor eIF2 assembly protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75794
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 233 | Severely disrupts assembly factor activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 246 | Severely disrupts assembly factor activity. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 322 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 chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000228662 | 1-336 | UniProt | Translation initiation factor eIF2 assembly protein | |||
Sequence: MKKEHVLHCQFSAWYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEAEEIQWSDDENTATLTAPEFPEFATKVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCTDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELISENNLNGDFSEVDAQEQDSPAFRCTNSEVTVQPSPYLSYRLPKDFVDLSTGEDAHKLIDFLKLKRNQQEDD | |||||||
Modified residue | 60 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the highest expression in testis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the eIF2 complex gamma subunit EIF2S3 (via C-terminus); the interaction is direct (PubMed:35031321, PubMed:37507029).
Interacts with the eIF2 complex alpha subunit EIF2S1 (PubMed:31836389, PubMed:35031321).
Interacts with the eIF2 complex beta subunit EIF2S2 (PubMed:31836389, PubMed:35031321).
Interacts with the eIF2 complex alpha subunit EIF2S1 (PubMed:31836389, PubMed:35031321).
Interacts with the eIF2 complex beta subunit EIF2S2 (PubMed:31836389, PubMed:35031321).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75794 | EIF2S2 P20042 | 4 | EBI-2808248, EBI-711977 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)39,135
- Last updated1998-11-01 v1
- ChecksumB13CF241D06C9D25
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 93 | in Ref. 1; BAA03593 | ||||
Sequence: A → P | ||||||
Sequence conflict | 317 | in Ref. 1; BAA03593 | ||||
Sequence: E → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D14878 EMBL· GenBank· DDBJ | BAA03593.1 EMBL· GenBank· DDBJ | mRNA | ||
U27112 EMBL· GenBank· DDBJ | AAC34738.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456966 EMBL· GenBank· DDBJ | CAG33247.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289362 EMBL· GenBank· DDBJ | BAF82051.1 EMBL· GenBank· DDBJ | mRNA | ||
AL512770 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471072 EMBL· GenBank· DDBJ | EAW86317.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001600 EMBL· GenBank· DDBJ | AAH01600.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009598 EMBL· GenBank· DDBJ | AAH09598.1 EMBL· GenBank· DDBJ | mRNA |