Q62834 · CD123_RAT
- ProteinTranslation initiation factor eIF2 assembly protein
- GeneCdc123
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
ATP-dependent protein-folding chaperone for the eIF2 complex (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).
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
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 | 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
Names & Taxonomy
Protein names
- Recommended nameTranslation initiation factor eIF2 assembly protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ62834
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 109 | in 3Y1tsD123 cell line; reversibly arrested in G1 phase of cell cycle at the restrictive temperature of 39.8 degrees Celsius; due to extensive degradation by the proteasome | ||||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000228665 | 1-336 | Translation initiation factor eIF2 assembly protein | |||
Sequence: MKKEHVSHCQFSAWYPLFRSLTIKSVILPLPQNVKDYLLDDGTLVVSGREDPPTCSQPDSGDEAEETQWSDDESTATLTAPEFPEFNTQVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKSLSDIFLLFKSSDFITHDFTQPFIHCNDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEICRCIQDFFKEHLQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELTSENNLRGDVSEADALEQDSPAFRCTNSEVTVQPSPYLSYGLPKDFVDLSTGEDAHKLIDFLKLKRNQQEDD | ||||||
Modified residue | 60 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated.
The Val-109 variant is degraded by the proteasome suggesting that it is polyubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Frequently detected in granular vesicles, in the cytoplasm of some epithelial, stromal and sperm cells and in varicosities lining nervous fibers, while it appears to be absent in endothelial and smooth muscle cells (at protein level). Widely expressed. Expressed at high level in testis.
Gene expression databases
Interaction
Subunit
Interacts with the eIF2 complex gamma subunit EIF2S3 (via C-terminus); the interaction is direct. Interacts with the eIF2 complex alpha subunit EIF2S1. Interacts with the eIF2 complex beta subunit EIF2S2.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 48-73 | Disordered | ||||
Sequence: GREDPPTCSQPDSGDEAEETQWSDDE |
Sequence similarities
Belongs to the CDC123 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)38,812
- Last updated1996-11-01 v1
- Checksum6E1D1379A2612934
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6A9Q9 | A0A8I6A9Q9_RAT | Cdc123 | 316 | ||
A0A8I5ZX90 | A0A8I5ZX90_RAT | Cdc123 | 336 | ||
A0A8L2QDG3 | A0A8L2QDG3_RAT | Cdc123 | 331 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U34843 EMBL· GenBank· DDBJ | AAB60521.1 EMBL· GenBank· DDBJ | mRNA | ||
BC061527 EMBL· GenBank· DDBJ | AAH61527.1 EMBL· GenBank· DDBJ | mRNA |