Q9UPY6 · WASF3_HUMAN

  • Protein
    Actin-binding protein WASF3
  • Gene
    WASF3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Downstream effector molecules involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape.

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 Componentcytoskeleton
Cellular Componentextracellular exosome
Cellular Componentglial cell projection
Cellular Componentglutamatergic synapse
Cellular Componentlamellipodium
Cellular Componentpostsynapse
Cellular ComponentSCAR complex
Molecular Functionactin binding
Molecular FunctionArp2/3 complex binding
Molecular Functionprotein kinase A regulatory subunit binding
Biological Processactin cytoskeleton organization
Biological Processactin filament polymerization
Biological Processcytoskeleton organization
Biological Processlamellipodium assembly
Biological Processmodification of postsynaptic actin cytoskeleton
Biological Processoligodendrocyte development
Biological Processpositive regulation of Arp2/3 complex-mediated actin nucleation
Biological Processpositive regulation of myelination
Biological Processprotein-containing complex assembly
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Actin-binding protein WASF3
  • Alternative names
    • Protein WAVE-3
    • Verprolin homology domain-containing protein 3
    • Wiskott-Aldrich syndrome protein family member 3 (WASP family protein member 3)

Gene names

    • Name
      WASF3
    • Synonyms
      KIAA0900, SCAR3, WAVE3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9UPY6
  • Secondary accessions
    • O94974
    • Q86VQ2

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_052953415in dbSNP:rs17084492

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 580 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001889961-502UniProtActin-binding protein WASF3
Modified residue151UniProtPhosphotyrosine; by ABL1
Modified residue (large scale data)235PRIDEPhosphoserine
Modified residue248UniProtPhosphotyrosine; by ABL1
Modified residue337UniProtPhosphotyrosine; by ABL1
Modified residue486UniProtPhosphotyrosine; by ABL1

Post-translational modification

Phosphorylation by ABL1 promotes lamellipodia formation and cell migration.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in ovary and brain.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Binds actin and the Arp2/3 complex.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for coiled coil, compositional bias, region, domain.

TypeIDPosition(s)Description
Coiled coil57-93
Coiled coil162-206
Compositional bias169-193Basic and acidic residues
Region169-210Disordered
Compositional bias223-262Polar residues
Region223-443Disordered
Compositional bias300-315Pro residues
Compositional bias338-355Pro residues
Compositional bias388-412Pro residues
Domain440-457WH2

Domain

Binds the Arp2/3 complex through the C-terminal region and actin through verprolin homology (VPH) domain.

Sequence similarities

Belongs to the SCAR/WAVE family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9UPY6-1

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
    502
  • Mass (Da)
    55,293
  • Last updated
    2005-02-01 v2
  • Checksum
    C0655CE181BD3C57
MPLVKRNIEPRHLCRGALPEGITSELECVTNSTLAAIIRQLSSLSKHAEDIFGELFNEANNFYIRANSLQDRIDRLAVKVTQLDSTVEEVSLQDINMKKAFKSSTVQDQQVVSKNSIPNPVADIYNQSDKPPPLNILTPYRDDKKDGLKFYTDPSYFFDLWKEKMLQDTEDKRKEKRRQKEQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQPVTPSYAAGDVPPHGPASQAAEHEYRPPSASARHMALNRPQQPPPPPPPQAPEGSQASAPMAPADYGMLPAQIIEYYNPSGPPPPPPPPVIPSAQTAFVSPLQMPMQPPFPASASSTHAAPPHPPSTGLLVTAPPPPGPPPPPPGPPGPGSSLSSSPMHGPPVAEAKRQEPAQPPISDARSDLLAAIRMGIQLKKVQEQREQEAKREPVGNDVATILSRRIAVEYSDSDDDSEFDENDWSD

Q9UPY6-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 181-239: EQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTR → REKHKLNPNRNQQVNVRKVRTRKEEWERRKMGIEFMSDAKKLEQAGSAKEDRVPSG

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A590UJ74A0A590UJ74_HUMANWASF3359

Sequence caution

The sequence BAA74923.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias169-193Basic and acidic residues
Alternative sequenceVSP_054517181-239in isoform 2
Compositional bias223-262Polar residues
Compositional bias300-315Pro residues
Sequence conflict307-308in Ref. 1 and 2
Compositional bias338-355Pro residues
Compositional bias388-412Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB026543
EMBL· GenBank· DDBJ
BAA81796.1
EMBL· GenBank· DDBJ
mRNA
AF454702
EMBL· GenBank· DDBJ
AAL51032.1
EMBL· GenBank· DDBJ
mRNA
AB020707
EMBL· GenBank· DDBJ
BAA74923.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AL159978
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL163538
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL353789
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471075
EMBL· GenBank· DDBJ
EAX08388.1
EMBL· GenBank· DDBJ
Genomic DNA
BC050283
EMBL· GenBank· DDBJ
AAH50283.1
EMBL· GenBank· DDBJ
mRNA
AF134305
EMBL· GenBank· DDBJ
AAD33054.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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