P24534 · EF1B_HUMAN
- ProteinElongation factor 1-beta
- GeneEEF1B2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids225 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.
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 | |
Cellular Component | cytosol | |
Cellular Component | eukaryotic translation elongation factor 1 complex | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | translation elongation factor activity | |
Biological Process | translational elongation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation factor 1-beta
- Short namesEF-1-beta
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP24534
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 458 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000155021 | 2-225 | UniProt | Elongation factor 1-beta | |||
Sequence: GFGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPADLCHALRWYNHIKSYEKEKASLPGVKKALGKYGPADVEDTTGSGATDSKDDDDIDLFGSDDEEESEEAKRLREERLAQYESKKAKKPALVAKSSILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDYVQSMDVAAFNKI | |||||||
Modified residue | 7 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 8 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 42 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 93 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 95 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 106 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 147 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 174 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylation affects the GDP/GTP exchange rate.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Induction
By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress.
Gene expression databases
Organism-specific databases
Interaction
Subunit
EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P24534 | EEF1G P26641 | 12 | EBI-354334, EBI-351467 | |
BINARY | P24534 | EEF1G P26641-2 | 3 | EBI-354334, EBI-10177695 | |
BINARY | P24534 | HTT P42858 | 7 | EBI-354334, EBI-466029 | |
BINARY | P24534 | SPRYD4 Q8WW59 | 3 | EBI-354334, EBI-8602056 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-84 | GST C-terminal | ||||
Sequence: GFGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPADLCHALRWYNHIKSYEKEKASLPGVKKALGKYGPADV | ||||||
Region | 78-115 | Disordered | ||||
Sequence: KYGPADVEDTTGSGATDSKDDDDIDLFGSDDEEESEEA |
Sequence similarities
Belongs to the EF-1-beta/EF-1-delta family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length225
- Mass (Da)24,764
- Last updated2007-01-23 v3
- ChecksumCDE763ADBF127822
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X60489 EMBL· GenBank· DDBJ | CAA43019.1 EMBL· GenBank· DDBJ | mRNA | ||
X60656 EMBL· GenBank· DDBJ | CAA43063.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007079 EMBL· GenBank· DDBJ | AAP35742.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456825 EMBL· GenBank· DDBJ | CAG33106.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291910 EMBL· GenBank· DDBJ | BAF84599.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007383 EMBL· GenBank· DDBJ | AAY15062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471063 EMBL· GenBank· DDBJ | EAW70381.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000211 EMBL· GenBank· DDBJ | AAH00211.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004931 EMBL· GenBank· DDBJ | AAH04931.1 EMBL· GenBank· DDBJ | mRNA | ||
BC067787 EMBL· GenBank· DDBJ | AAH67787.1 EMBL· GenBank· DDBJ | mRNA |