Q8BPU7 · ELMO1_MOUSE
- ProteinEngulfment and cell motility protein 1
- GeneElmo1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids727 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1 (By similarity).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | glutamatergic synapse | |
Cellular Component | guanyl-nucleotide exchange factor complex | |
Cellular Component | plasma membrane | |
Cellular Component | postsynapse | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | SH3 domain binding | |
Biological Process | actin cytoskeleton organization | |
Biological Process | actin filament organization | |
Biological Process | actin filament-based process | |
Biological Process | apoptotic process | |
Biological Process | cell motility | |
Biological Process | phagocytosis | |
Biological Process | phagocytosis, engulfment | |
Biological Process | Rac protein signal transduction |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEngulfment and cell motility protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8BPU7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Translocation to plasma membrane seems to be mediated by DOCK1 and CRK.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000153713 | 1-727 | Engulfment and cell motility protein 1 | |||
Sequence: MPPPSDIVKVAIEWPGAYPKLMEIDQKKPLSAIIKEVCDGWSLANHEYFALQHADSSNFYITEKNRNEIKNGTILRLTTSPAQNAQQLHERIQSSSMDAKLEALKDLASLSRDVTFAQEFINLDGISLLTQMVESGTERYQKLQKIMKPCFGDMLSFTLTAFVELMDHGIVSWDTFSVAFIKKIASFVNKSAIDISILQRSLAILESMVLNSHDLYQKVAQEITIGQLIPHLQGTDQEIQTYTIAVINALFLKAPDERRQEMANILAQKQLRYIILTHVIRAQRAINNEMAHQLYVLQVLTFNLLEDRMMTKMDPQDQAQRDIIFELRRIAFDAESEPNNSSGSMEKRKSMYTRDYKKLGFINHVNPAMDFTQTPPGMLALDNMLYFAKHHQDAYIRIVLENSSREDKHECPFGRSSIELTKMLCEILKVGELPSETCNDFHPMFFTHDRSFEEFFCICIQLLNKTWKEMRATSEDFNKVMQVVKEQVMRALTTKPSSLDQFKSKLQNLSYTEILKIRQSERMNQEDFQSRPILELKEKIQPEILELIKQQRLNRLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKDMMSDLTRNDLDTLLSMEIKLRLLDLENIQIPDAPPPIPKEPSNYDFVYDCN | ||||||
Modified residue | 18 | Phosphotyrosine; by HCK | ||||
Sequence: Y | ||||||
Modified residue | 100 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 105 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 216 | Phosphotyrosine; by HCK | ||||
Sequence: Y | ||||||
Modified residue | 344 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 395 | Phosphotyrosine; by HCK | ||||
Sequence: Y | ||||||
Modified residue | 511 | Phosphotyrosine; by HCK | ||||
Sequence: Y | ||||||
Modified residue | 720 | Phosphotyrosine; by HCK | ||||
Sequence: Y |
Post-translational modification
Phosphorylated by HCK.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts directly with the SH3-domain of DOCK1 via its SH3-binding site. Probably forms a heterotrimeric complex with DOCK1 and RAC1 (By similarity).
Interacts with PLEKHG6. Interacts with HCK (via SH3 domain) (By similarity).
Interacts with ADGRB1 (PubMed:17960134).
Interacts with ADGRB3 (By similarity).
Interacts with DOCK5 (PubMed:27505886).
Interacts with PLEKHG6. Interacts with HCK (via SH3 domain) (By similarity).
Interacts with ADGRB1 (PubMed:17960134).
Interacts with ADGRB3 (By similarity).
Interacts with DOCK5 (PubMed:27505886).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8BPU7-1 | Dock1 Q8BUR4 | 13 | EBI-644162, EBI-646023 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 319-492 | ELMO | ||||
Sequence: AQRDIIFELRRIAFDAESEPNNSSGSMEKRKSMYTRDYKKLGFINHVNPAMDFTQTPPGMLALDNMLYFAKHHQDAYIRIVLENSSREDKHECPFGRSSIELTKMLCEILKVGELPSETCNDFHPMFFTHDRSFEEFFCICIQLLNKTWKEMRATSEDFNKVMQVVKEQVMRAL | ||||||
Domain | 555-676 | PH | ||||
Sequence: RLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKD | ||||||
Motif | 707-714 | SH3-binding | ||||
Sequence: PDAPPPIP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8BPU7-1
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
- Length727
- Mass (Da)83,936
- Last updated2003-05-16 v2
- Checksum21B1BB9195504D28
Q8BPU7-2
- Name2
- Differences from canonical
- 1-480: Missing
Q8BPU7-3
- Name3
Q8BPU7-4
- Name4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1Y7VLM1 | A0A1Y7VLM1_MOUSE | Elmo1 | 25 | ||
A0A1Y7VIX9 | A0A1Y7VIX9_MOUSE | Elmo1 | 193 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007481 | 1-480 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 9 | in Ref. 2; BAC25925 | ||||
Sequence: K → E | ||||||
Sequence conflict | 315 | in Ref. 2; BAC25925 | ||||
Sequence: P → H | ||||||
Alternative sequence | VSP_007482 | 398-420 | in isoform 3 | |||
Sequence: IVLENSSREDKHECPFGRSSIEL → VSMLASLRYCQCRMEFCFPTYAQ | ||||||
Alternative sequence | VSP_007483 | 421-727 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_007484 | 636-642 | in isoform 4 | |||
Sequence: EVLELAF → VWFSKSL | ||||||
Alternative sequence | VSP_007485 | 643-727 | in isoform 4 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF398883 EMBL· GenBank· DDBJ | AAL14464.1 EMBL· GenBank· DDBJ | mRNA | ||
AK028389 EMBL· GenBank· DDBJ | BAC25925.1 EMBL· GenBank· DDBJ | mRNA | ||
AK053306 EMBL· GenBank· DDBJ | BAC35336.1 EMBL· GenBank· DDBJ | mRNA | ||
BC024727 EMBL· GenBank· DDBJ | AAH24727.1 EMBL· GenBank· DDBJ | mRNA | ||
BC031782 EMBL· GenBank· DDBJ | AAH31782.1 EMBL· GenBank· DDBJ | mRNA |