Q9QZM5 · ABI1_RAT

Function

function

May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of 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 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 Componentactin-based cell projection
Cellular Componentcell leading edge
Cellular Componentcytoskeleton
Cellular Componentfilopodium tip
Cellular Componentglutamatergic synapse
Cellular Componentgrowth cone
Cellular Componentlamellipodium
Cellular Componentneuron projection
Cellular Componentnucleus
Cellular Componentpostsynaptic density
Cellular ComponentSCAR complex
Molecular Functionprotein tyrosine kinase activator activity
Molecular FunctionSH3 domain binding
Molecular Functionsignaling adaptor activity
Biological Processdendrite morphogenesis
Biological Processlamellipodium morphogenesis
Biological Processmegakaryocyte development
Biological Processneuron migration
Biological Processpostsynapse to nucleus signaling pathway
Biological Processsomitogenesis

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Abl interactor 1
  • Alternative names
    • Abelson interactor 1 (Abi-1)
    • Eps8 SH3 domain-binding protein (Eps8-binding protein)
    • e3B1

Gene names

    • Name
      Abi1

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9QZM5

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Postsynaptic density
Note: Localized to protruding lamellipodia and filopodia tips. May shuttle from the postsynaptic densities to the nucleus.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis53Not phosphorylated and perinuclear upon NMDA treatment.

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001917892-476Abl interactor 1
Modified residue53Phosphotyrosine
Modified residue169Phosphothreonine
Modified residue173Phosphothreonine
Modified residue178Phosphoserine
Modified residue182Phosphoserine
Modified residue208Phosphotyrosine
Modified residue210Phosphothreonine
Modified residue211Phosphoserine
Modified residue217Phosphoserine
Modified residue220Phosphoserine
Modified residue287Phosphoserine
Modified residue291Phosphoserine
Modified residue423Phosphotyrosine
Modified residue434Phosphoserine
Modified residue475Phosphothreonine

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.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed in brain, high levels detected in cortex, hippocampus and cerebellum (at protein level).

Developmental stage

Low protein levels at birth that increase progressively at least until 14 days after birth.

Gene expression databases

Interaction

Subunit

Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8, SOS1, SOS2, GRB2, SPTA1, NCKAP1/NAP1, the first SH3 domain of NCK1 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. 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

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9QZM5Max P521642EBI-920097, EBI-1184963
BINARY Q9QZM5Shank3 Q9JLU47EBI-920097, EBI-6271152

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain45-107t-SNARE coiled-coil homology
Region150-280Disordered
Compositional bias210-256Polar residues
Compositional bias312-327Polar residues
Region312-343Disordered
Compositional bias328-342Pro residues
Region356-387Disordered
Compositional bias359-387Pro residues
Domain414-473SH3

Domain

The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A.

Sequence similarities

Belongs to the ABI family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    476
  • Mass (Da)
    51,705
  • Last updated
    2007-01-23 v3
  • Checksum
    A2B8CC377090BEA6
MAELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANMERPVRYIRKPIDYTVLDDVGHGVKHGNNQPARTGTLSRTNPPTQKPPSPPVSGRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTAGPAAPGAAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVTAQFSAQPHVNGGPLYSQNSISIAPPPPPMPQLTPQIPLTGFVARVQENIADSPTPPPPPPPDDIPMFDDSPPPPPPPPVDYEDEEAAVVQYSDPYADGDPAWAPKNYIEKVVAIYDYTKDKDDELSFKEGAIIYVIKKNDDGWFEGVCNRVTGLFPGNYVESIMHYTD

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6AGM2A0A8I6AGM2_RATAbi1447
A0A8I6A0X0A0A8I6A0X0_RATAbi1422
A2VD09A2VD09_RATAbi1481
A0A8I5ZQS1A0A8I5ZQS1_RATAbi1393
A0A8L2UQ93A0A8L2UQ93_RATAbi1475

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias210-256Polar residues
Compositional bias312-327Polar residues
Compositional bias328-342Pro residues
Compositional bias359-387Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF176784
EMBL· GenBank· DDBJ
AAD55263.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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