Q9UPY6 · WASF3_HUMAN
- ProteinActin-binding protein WASF3
- GeneWASF3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids502 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 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 | cytoskeleton | |
Cellular Component | extracellular exosome | |
Cellular Component | glial cell projection | |
Cellular Component | glutamatergic synapse | |
Cellular Component | lamellipodium | |
Cellular Component | postsynapse | |
Cellular Component | SCAR complex | |
Molecular Function | actin binding | |
Molecular Function | Arp2/3 complex binding | |
Molecular Function | protein kinase A regulatory subunit binding | |
Biological Process | actin cytoskeleton organization | |
Biological Process | actin filament polymerization | |
Biological Process | cytoskeleton organization | |
Biological Process | lamellipodium assembly | |
Biological Process | modification of postsynaptic actin cytoskeleton | |
Biological Process | oligodendrocyte development | |
Biological Process | positive regulation of Arp2/3 complex-mediated actin nucleation | |
Biological Process | positive regulation of myelination | |
Biological Process | protein-containing complex assembly | |
Biological Process | regulation of cell shape |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActin-binding protein WASF3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UPY6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052953 | 415 | in dbSNP:rs17084492 | |||
Sequence: S → L |
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.
Organism-specific databases
Miscellaneous
Chemistry
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_0000188996 | 1-502 | UniProt | Actin-binding protein WASF3 | |||
Sequence: MPLVKRNIEPRHLCRGALPEGITSELECVTNSTLAAIIRQLSSLSKHAEDIFGELFNEANNFYIRANSLQDRIDRLAVKVTQLDSTVEEVSLQDINMKKAFKSSTVQDQQVVSKNSIPNPVADIYNQSDKPPPLNILTPYRDDKKDGLKFYTDPSYFFDLWKEKMLQDTEDKRKEKRRQKEQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQPVTPSYAAGDVPPHGPASQAAEHEYRPPSASARHMALNRPQQPPPPPPPQAPEGSQASAPMAPADYGMLPAQIIEYYNPSGPPPPPPPPVIPSAQTAFVSPLQMPMQPPFPASASSTHAAPPHPPSTGLLVTAPPPPGPPPPPPGPPGPGSSLSSSPMHGPPVAEAKRQEPAQPPISDARSDLLAAIRMGIQLKKVQEQREQEAKREPVGNDVATILSRRIAVEYSDSDDDSEFDENDWSD | |||||||
Modified residue | 151 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 248 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | |||||||
Modified residue | 337 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y | |||||||
Modified residue | 486 | UniProt | Phosphotyrosine; by ABL1 | ||||
Sequence: Y |
Post-translational modification
Phosphorylation by ABL1 promotes lamellipodia formation and cell migration.
Keywords
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UPY6-2 | ABI2 Q9NYB9-2 | 3 | EBI-12026286, EBI-11096309 | |
BINARY | Q9UPY6-2 | BYSL Q13895 | 3 | EBI-12026286, EBI-358049 | |
BINARY | Q9UPY6-2 | CKS1B P61024 | 3 | EBI-12026286, EBI-456371 | |
BINARY | Q9UPY6-2 | KANK2 Q63ZY3 | 3 | EBI-12026286, EBI-2556193 | |
BINARY | Q9UPY6-2 | KIFC3 Q9BVG8-5 | 3 | EBI-12026286, EBI-14069005 | |
BINARY | Q9UPY6-2 | RASAL3 Q86YV0 | 3 | EBI-12026286, EBI-3437896 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 57-93 | |||||
Sequence: NEANNFYIRANSLQDRIDRLAVKVTQLDSTVEEVSLQ | ||||||
Coiled coil | 162-206 | |||||
Sequence: KEKMLQDTEDKRKEKRRQKEQKRIDGTTREVKKVRKARNRRQEWN | ||||||
Compositional bias | 169-193 | Basic and acidic residues | ||||
Sequence: TEDKRKEKRRQKEQKRIDGTTREVK | ||||||
Region | 169-210 | Disordered | ||||
Sequence: TEDKRKEKRRQKEQKRIDGTTREVKKVRKARNRRQEWNMMAY | ||||||
Compositional bias | 223-262 | Polar residues | ||||
Sequence: SVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQP | ||||||
Region | 223-443 | Disordered | ||||
Sequence: SVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQPVTPSYAAGDVPPHGPASQAAEHEYRPPSASARHMALNRPQQPPPPPPPQAPEGSQASAPMAPADYGMLPAQIIEYYNPSGPPPPPPPPVIPSAQTAFVSPLQMPMQPPFPASASSTHAAPPHPPSTGLLVTAPPPPGPPPPPPGPPGPGSSLSSSPMHGPPVAEAKRQEPAQPPISDARSD | ||||||
Compositional bias | 300-315 | Pro residues | ||||
Sequence: RPQQPPPPPPPQAPEG | ||||||
Compositional bias | 338-355 | Pro residues | ||||
Sequence: YNPSGPPPPPPPPVIPSA | ||||||
Compositional bias | 388-412 | Pro residues | ||||
Sequence: TGLLVTAPPPPGPPPPPPGPPGPGS | ||||||
Domain | 440-457 | WH2 | ||||
Sequence: ARSDLLAAIRMGIQLKKV |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length502
- Mass (Da)55,293
- Last updated2005-02-01 v2
- ChecksumC0655CE181BD3C57
Q9UPY6-2
- Name2
- Differences from canonical
- 181-239: EQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTR → REKHKLNPNRNQQVNVRKVRTRKEEWERRKMGIEFMSDAKKLEQAGSAKEDRVPSG
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A590UJ74 | A0A590UJ74_HUMAN | WASF3 | 359 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 169-193 | Basic and acidic residues | ||||
Sequence: TEDKRKEKRRQKEQKRIDGTTREVK | ||||||
Alternative sequence | VSP_054517 | 181-239 | in isoform 2 | |||
Sequence: EQKRIDGTTREVKKVRKARNRRQEWNMMAYDKELRPDNRLSQSVYHGASSEGSLSPDTR → REKHKLNPNRNQQVNVRKVRTRKEEWERRKMGIEFMSDAKKLEQAGSAKEDRVPSG | ||||||
Compositional bias | 223-262 | Polar residues | ||||
Sequence: SVYHGASSEGSLSPDTRSHASDVTDYSYPATPNHSLHPQP | ||||||
Compositional bias | 300-315 | Pro residues | ||||
Sequence: RPQQPPPPPPPQAPEG | ||||||
Sequence conflict | 307-308 | in Ref. 1 and 2 | ||||
Sequence: PP → RR | ||||||
Compositional bias | 338-355 | Pro residues | ||||
Sequence: YNPSGPPPPPPPPVIPSA | ||||||
Compositional bias | 388-412 | Pro residues | ||||
Sequence: TGLLVTAPPPPGPPPPPPGPPGPGS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |