Q8CBW3 · ABI1_MOUSE
- ProteinAbl interactor 1
- GeneAbi1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. In vitro, at least isoform 2 and isoform 4 suppress the transforming activity of Abelson murine leukemia virus (v-Abl) after overexpression in fibroblasts. May play a role in regulation EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons.
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 | actin-based cell projection | |
Cellular Component | cell leading edge | |
Cellular Component | cytoskeleton | |
Cellular Component | filopodium tip | |
Cellular Component | glutamatergic synapse | |
Cellular Component | growth cone | |
Cellular Component | lamellipodium | |
Cellular Component | neuron projection | |
Cellular Component | nucleus | |
Cellular Component | postsynaptic density | |
Cellular Component | SCAR complex | |
Molecular Function | protein tyrosine kinase activator activity | |
Molecular Function | SH3 domain binding | |
Molecular Function | signaling adaptor activity | |
Biological Process | dendrite morphogenesis | |
Biological Process | lamellipodium morphogenesis | |
Biological Process | megakaryocyte development | |
Biological Process | neuron migration | |
Biological Process | postsynapse to nucleus signaling pathway | |
Biological Process | somitogenesis |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAbl interactor 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8CBW3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes. May shuttle from the postsynaptic densities to the nucleus (By similarity).
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-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000191788 | 2-481 | Abl interactor 1 | |||
Sequence: AELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANMERPVRYIRKPIDYTVLDDVGHGVKWLKAKHGNNQPARTGTLSRTNPPTQKPPSPPVSGRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTAGPAAPGAAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVAAQFSAQPHVNGGPLYSQNSISVAPPPPPMPQLTPQIPLTGFVARVQENIADSPTPPPPPPPDDIPMFDDSPPPPPPPPVDYEDEEAAVVQYSDPYADGDPAWAPKNYIEKVVAIYDYTKDKDDELSFKEGAIIYVIKKNDDGWFEGVCNRVTGLFPGNYVESIMHYTD | ||||||
Modified residue | 53 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 174 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 178 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 183 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 187 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 213 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 215 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 216 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 222 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 225 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 292 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 296 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 428 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 439 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 480 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1, required for nuclear but not for synaptic localization (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed with highest levels in bone marrow, spleen, brain, testes, and embryonic brain. In adult brain prominently expressed in the neocortex, hippocampus and dentate gyrus.
Developmental stage
Detected at 10 dpc and 12 dpc in developing brain, but does not appear more prominent in the neuroepithelium compared to the surrounding tissue.
Gene expression databases
Interaction
Subunit
Interacts with ENAH, Abelson murine leukemia virus V-ABL, ABL1, STX1A, SNAP25, VAMP2, and through its N-terminus with WASF1. Part of a complex consisting of ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with EPS8, SOS1, SOS2, GRB2, SPTA1, and the first SH3 domain of NCK1 (By similarity).
Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2. Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the interaction is direct. Interacts with the heterodimer MYC:MAX; the interaction may enhance MYC:MAX transcriptional activity. Interacts with FNBP1L (via the SH3 domain), WASF2, and CDC42, but only in the presence of FNBP1L (By similarity).
Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2. Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the interaction is direct. Interacts with the heterodimer MYC:MAX; the interaction may enhance MYC:MAX transcriptional activity. Interacts with FNBP1L (via the SH3 domain), WASF2, and CDC42, but only in the presence of FNBP1L (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8CBW3 | Diaph3 Q9Z207 | 2 | EBI-375511, EBI-6550123 | |
BINARY | Q8CBW3 | Eps8 Q08509 | 3 | EBI-375511, EBI-375596 | |
BINARY | Q8CBW3 | Sos2 Q02384 | 2 | EBI-375511, EBI-395573 | |
BINARY | Q8CBW3 | Wasf2 Q8BH43 | 2 | EBI-375511, EBI-643162 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-79 | Required for binding to WASF1 | ||||
Sequence: ALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQ | ||||||
Domain | 45-107 | t-SNARE coiled-coil homology | ||||
Sequence: KALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARR | ||||||
Region | 158-285 | Disordered | ||||
Sequence: AKHGNNQPARTGTLSRTNPPTQKPPSPPVSGRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTAGPAAPGAAPGSQYG | ||||||
Compositional bias | 215-261 | Polar residues | ||||
Sequence: TSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPI | ||||||
Compositional bias | 318-332 | Polar residues | ||||
Sequence: AQPHVNGGPLYSQNS | ||||||
Region | 318-348 | Disordered | ||||
Sequence: AQPHVNGGPLYSQNSISVAPPPPPMPQLTPQ | ||||||
Compositional bias | 333-347 | Pro residues | ||||
Sequence: ISVAPPPPPMPQLTP | ||||||
Region | 361-392 | Disordered | ||||
Sequence: NIADSPTPPPPPPPDDIPMFDDSPPPPPPPPV | ||||||
Compositional bias | 364-392 | Pro residues | ||||
Sequence: DSPTPPPPPPPDDIPMFDDSPPPPPPPPV | ||||||
Domain | 419-478 | SH3 | ||||
Sequence: NYIEKVVAIYDYTKDKDDELSFKEGAIIYVIKKNDDGWFEGVCNRVTGLFPGNYVESIMH |
Domain
The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A.
Sequence similarities
Belongs to the ABI family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q8CBW3-1
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
- Length481
- Mass (Da)52,288
- Last updated2007-01-23 v3
- Checksum1654A1E89438BC1D
Q8CBW3-2
- Name2
- Synonymsshort
Q8CBW3-3
- Name3
- Differences from canonical
- 154-158: Missing
Q8CBW3-4
- Name4
- Synonymslong
Q8CBW3-5
- Name5
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_010756 | 154-158 | in isoform 2, isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 215-261 | Polar residues | ||||
Sequence: TSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPI | ||||||
Alternative sequence | VSP_010757 | 274 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022636 | 274-362 | in isoform 5 | |||
Sequence: AAPGAAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVAAQFSAQPHVNGGPLYSQNSISVAPPPPPMPQLTPQIPLTGFVARVQENI → V | ||||||
Sequence conflict | 313 | in Ref. 4; AAH04657 | ||||
Sequence: A → T | ||||||
Compositional bias | 318-332 | Polar residues | ||||
Sequence: AQPHVNGGPLYSQNS | ||||||
Compositional bias | 333-347 | Pro residues | ||||
Sequence: ISVAPPPPPMPQLTP | ||||||
Alternative sequence | VSP_010758 | 333-361 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 364-392 | Pro residues | ||||
Sequence: DSPTPPPPPPPDDIPMFDDSPPPPPPPPV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF420251 EMBL· GenBank· DDBJ | AAL16036.1 EMBL· GenBank· DDBJ | mRNA | ||
AY033645 EMBL· GenBank· DDBJ | AAK59381.1 EMBL· GenBank· DDBJ | mRNA | ||
AK034476 EMBL· GenBank· DDBJ | BAC28722.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152061 EMBL· GenBank· DDBJ | BAE30917.1 EMBL· GenBank· DDBJ | mRNA | ||
AK152184 EMBL· GenBank· DDBJ | BAE31015.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151026 EMBL· GenBank· DDBJ | BAE30044.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004657 EMBL· GenBank· DDBJ | AAH04657.1 EMBL· GenBank· DDBJ | mRNA | ||
U17698 EMBL· GenBank· DDBJ | AAB00373.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |