Q8N9N8 · EIF1A_HUMAN
- ProteinProbable RNA-binding protein EIF1AD
- GeneEIF1AD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids165 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role into cellular response to oxidative stress. Decreases cell proliferation.
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 | cytosol | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | RNA binding | |
Molecular Function | translation initiation factor activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable RNA-binding protein EIF1AD
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8N9N8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_037851 | 23 | in dbSNP:rs17849919 | |||
Sequence: D → N | ||||||
Natural variant | VAR_037852 | 159 | in dbSNP:rs2276017 | |||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 185 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_0000314151 | 1-165 | UniProt | Probable RNA-binding protein EIF1AD | |||
Sequence: MSQATKRKHVVKEVLGEHIVPSDQQQIVRVLRTPGNNLHEVETAQGQRFLVSMPSKYRKNIWIKRGDFLIVDPIEEGEKVKAEISFVLCKDHVRSLQKEGFWPEAFSEVAEKHNNRNRQTQPELPAEPQLSGEESSSEDDSDLFVNTNRRQYHESEEESEEEEAA | |||||||
Modified residue | 33 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 131 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 135 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 136 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 137 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 155 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 159 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the glioblastoma cell line U-87MG, the embryonic kidney cell line HEK293, the pancreatic carcinoma cell line PANC-1, the breast carcinoma cell line MCF-7, the lung cancer cell line NCI-H460, and the chronic myelogenous leukemia cell line K-562.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with GAPDH and STAT1.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-89 | S1-like | ||||
Sequence: TKRKHVVKEVLGEHIVPSDQQQIVRVLRTPGNNLHEVETAQGQRFLVSMPSKYRKNIWIKRGDFLIVDPIEEGEKVKAEISFVLC | ||||||
Motif | 6-12 | Nuclear localization signal | ||||
Sequence: KRKHVVK | ||||||
Motif | 56-65 | Nuclear localization signal | ||||
Sequence: KYRKNIWIKR | ||||||
Region | 112-165 | Disordered | ||||
Sequence: KHNNRNRQTQPELPAEPQLSGEESSSEDDSDLFVNTNRRQYHESEEESEEEEAA |
Sequence similarities
Belongs to the EIF1AD family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length165
- Mass (Da)19,053
- Last updated2002-10-01 v1
- Checksum33FB5ACB777084B2
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK094129 EMBL· GenBank· DDBJ | BAC04293.1 EMBL· GenBank· DDBJ | mRNA | ||
AK311891 EMBL· GenBank· DDBJ | BAG34832.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471076 EMBL· GenBank· DDBJ | EAW74478.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005131 EMBL· GenBank· DDBJ | AAH05131.1 EMBL· GenBank· DDBJ | mRNA |