Q95107 · WASL_BOVIN
- ProteinActin nucleation-promoting factor WASL
- GeneWASL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids505 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex (PubMed:17609109).
Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity).
Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity).
Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity).
Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | nucleus | |
Molecular Function | actin binding | |
Molecular Function | identical protein binding | |
Molecular Function | microtubule binding | |
Biological Process | actin filament polymerization | |
Biological Process | cell division | |
Biological Process | dendritic spine morphogenesis | |
Biological Process | positive regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActin nucleation-promoting factor WASL
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ95107
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated. Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000188999 | 2-505 | Actin nucleation-promoting factor WASL | |||
Sequence: SSGQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQINNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVGAPPPPPNRMYPPPLPALPSSAPSGPPPPPPPLSVSGSVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTPAGSKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVTDAPESTPPAPAPTSGIVGALMEVMQKRSKAIHSSDEDEDEDDDEDFEDDDEWED | ||||||
Modified residue | 242 | Phosphoserine; by TNK2 | ||||
Sequence: S | ||||||
Modified residue | 256 | Phosphotyrosine; by FAK1 and TNK2 | ||||
Sequence: Y | ||||||
Modified residue | 307 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 484 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 485 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Binds actin and the Arp2/3 complex. Interacts with CDC42 (By similarity).
Interacts with FCHSD1. Interacts with FCHSD2 (By similarity).
Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP (By similarity).
Interacts with SNX9 (PubMed:17609109).
Interacts with the WW domains of PRPF40A/FBP11. Interacts with PTK2/FAK1. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity).
Interacts with NOSTRIN. Binds to TNK2. Interacts with SNX33. Interacts with NONO (via second RRM domain); the interaction is direct. Component of a multiprotein complex with NONO and SFPQ; associates with the complex via direct interaction with NONO (By similarity).
Interacts with FCHSD1. Interacts with FCHSD2 (By similarity).
Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP (By similarity).
Interacts with SNX9 (PubMed:17609109).
Interacts with the WW domains of PRPF40A/FBP11. Interacts with PTK2/FAK1. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity).
Interacts with NOSTRIN. Binds to TNK2. Interacts with SNX33. Interacts with NONO (via second RRM domain); the interaction is direct. Component of a multiprotein complex with NONO and SFPQ; associates with the complex via direct interaction with NONO (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q95107 | ACTR2 A7MB62 | 2 | EBI-6162776, EBI-6162748 | |
XENO | Q95107 | Cttn Q60598 | 2 | EBI-6162776, EBI-397955 | |
BINARY | Q95107 | WASL Q95107 | 3 | EBI-6162776, EBI-6162776 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-141 | WH1 | ||||
Sequence: LGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRR | ||||||
Region | 138-163 | Disordered | ||||
Sequence: LGRRQRKSEKRRDPPNGPNLPMATVD | ||||||
Region | 185-205 | Disordered | ||||
Sequence: TKEKKKGKAKKKRLTKADIGT | ||||||
Domain | 203-216 | CRIB | ||||
Sequence: IGTPSNFQHIGHVG | ||||||
Region | 266-406 | Disordered | ||||
Sequence: EAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVGAPPPPPNRMYPPPLPALPSSAPSGPPPPPPPLSVSGSVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTPAGSK | ||||||
Compositional bias | 274-395 | Pro residues | ||||
Sequence: RQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVGAPPPPPNRMYPPPLPALPSSAPSGPPPPPPPLSVSGSVAPPPPPPPPPPPGPPPPPGLPSDG | ||||||
Domain | 405-422 | WH2 1 | ||||
Sequence: SKAALLDQIREGAQLKKV | ||||||
Domain | 433-450 | WH2 2 | ||||
Sequence: GRDALLDQIRQGIQLKSV | ||||||
Region | 449-468 | Disordered | ||||
Sequence: SVTDAPESTPPAPAPTSGIV | ||||||
Region | 477-505 | Disordered | ||||
Sequence: KRSKAIHSSDEDEDEDDDEDFEDDDEWED | ||||||
Compositional bias | 486-505 | Acidic residues | ||||
Sequence: DEDEDEDDDEDFEDDDEWED |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length505
- Mass (Da)54,672
- Last updated1997-02-01 v1
- Checksum54B83B48F1CDB3B8
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q1M352 | A0A3Q1M352_BOVIN | WASL | 511 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 274-395 | Pro residues | ||||
Sequence: RQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVGAPPPPPNRMYPPPLPALPSSAPSGPPPPPPPLSVSGSVAPPPPPPPPPPPGPPPPPGLPSDG | ||||||
Compositional bias | 486-505 | Acidic residues | ||||
Sequence: DEDEDEDDDEDFEDDDEWED |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D67066 EMBL· GenBank· DDBJ | BAA11082.1 EMBL· GenBank· DDBJ | mRNA |