Q8BPU7 · ELMO1_MOUSE

  • Protein
    Engulfment and cell motility protein 1
  • Gene
    Elmo1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentglutamatergic synapse
Cellular Componentguanyl-nucleotide exchange factor complex
Cellular Componentplasma membrane
Cellular Componentpostsynapse
Molecular Functionguanyl-nucleotide exchange factor activity
Molecular FunctionSH3 domain binding
Biological Processactin cytoskeleton organization
Biological Processactin filament organization
Biological Processactin filament-based process
Biological Processapoptotic process
Biological Processcell motility
Biological Processphagocytosis
Biological Processphagocytosis, engulfment
Biological ProcessRac protein signal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Engulfment and cell motility protein 1
  • Alternative names
    • Protein ced-12 homolog

Gene names

    • Name
      Elmo1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8BPU7
  • Secondary accessions
    • Q8BSY9
    • Q8K2C5
    • Q91ZU3

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Cell membrane
Note: Translocation to plasma membrane seems to be mediated by DOCK1 and CRK.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001537131-727Engulfment and cell motility protein 1
Modified residue18Phosphotyrosine; by HCK
Modified residue100N6-acetyllysine
Modified residue105N6-acetyllysine
Modified residue216Phosphotyrosine; by HCK
Modified residue344Phosphoserine
Modified residue395Phosphotyrosine; by HCK
Modified residue511Phosphotyrosine; by HCK
Modified residue720Phosphotyrosine; by HCK

Post-translational modification

Phosphorylated by HCK.

Keywords

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q8BPU7-1Dock1 Q8BUR413EBI-644162, EBI-646023

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain319-492ELMO
Domain555-676PH
Motif707-714SH3-binding

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

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.

  • Length
    727
  • Mass (Da)
    83,936
  • Last updated
    2003-05-16 v2
  • Checksum
    21B1BB9195504D28
MPPPSDIVKVAIEWPGAYPKLMEIDQKKPLSAIIKEVCDGWSLANHEYFALQHADSSNFYITEKNRNEIKNGTILRLTTSPAQNAQQLHERIQSSSMDAKLEALKDLASLSRDVTFAQEFINLDGISLLTQMVESGTERYQKLQKIMKPCFGDMLSFTLTAFVELMDHGIVSWDTFSVAFIKKIASFVNKSAIDISILQRSLAILESMVLNSHDLYQKVAQEITIGQLIPHLQGTDQEIQTYTIAVINALFLKAPDERRQEMANILAQKQLRYIILTHVIRAQRAINNEMAHQLYVLQVLTFNLLEDRMMTKMDPQDQAQRDIIFELRRIAFDAESEPNNSSGSMEKRKSMYTRDYKKLGFINHVNPAMDFTQTPPGMLALDNMLYFAKHHQDAYIRIVLENSSREDKHECPFGRSSIELTKMLCEILKVGELPSETCNDFHPMFFTHDRSFEEFFCICIQLLNKTWKEMRATSEDFNKVMQVVKEQVMRALTTKPSSLDQFKSKLQNLSYTEILKIRQSERMNQEDFQSRPILELKEKIQPEILELIKQQRLNRLVEGTCFRKLNARRRQDKFWYCRLSPNHKVLHYGDLEESPQGEVPHDSLQDKLPVADIKAVVTGKDCPHMKEKGALKQNKEVLELAFSILYDSNCQLNFIAPDKHEYCIWTDGLNALLGKDMMSDLTRNDLDTLLSMEIKLRLLDLENIQIPDAPPPIPKEPSNYDFVYDCN

Q8BPU7-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8BPU7-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 398-420: IVLENSSREDKHECPFGRSSIEL → VSMLASLRYCQCRMEFCFPTYAQ
    • 421-727: Missing

Q8BPU7-4

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1Y7VLM1A0A1Y7VLM1_MOUSEElmo125
A0A1Y7VIX9A0A1Y7VIX9_MOUSEElmo1193

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0074811-480in isoform 2 and isoform 4
Sequence conflict9in Ref. 2; BAC25925
Sequence conflict315in Ref. 2; BAC25925
Alternative sequenceVSP_007482398-420in isoform 3
Alternative sequenceVSP_007483421-727in isoform 3
Alternative sequenceVSP_007484636-642in isoform 4
Alternative sequenceVSP_007485643-727in isoform 4

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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