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Q9QZM5 (ABI1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Abl interactor 1
Alternative name(s):
Abelson interactor 1
Short name=Abi-1
Eps8 SH3 domain-binding protein
Short name=Eps8-binding protein
e3B1
Gene names
Name:Abi1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3

Subunit structure

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 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. Ref.3

Subcellular location

Cytoplasm By similarity. Nucleus. Cell projectionlamellipodium. Cell projectionfilopodium. Cell projectiongrowth cone. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cytoplasmcytoskeleton. Note: Localized to protruding lamellipodia and filopodia tips. May shuttle from the postsynaptic densities to the nucleus. Ref.2 Ref.3

Tissue specificity

Widely expressed in brain, high levels detected in cortex, hippocampus and cerebellum (at protein level). Ref.3

Developmental stage

Low protein levels at birth that increase progressively at least until 14 days after birth. Ref.3

Domain

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

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. Ref.3

Sequence similarities

Belongs to the ABI family.

Contains 1 SH3 domain.

Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
Postsynaptic cell membrane
Synapse
   DomainCoiled coil
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular component movement

Inferred from electronic annotation. Source: Ensembl

lamellipodium morphogenesis

Inferred from electronic annotation. Source: Ensembl

megakaryocyte development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

somitogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotein binding

Inferred from physical interaction Ref.3. Source: IntAct

protein tyrosine kinase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 476475Abl interactor 1
PRO_0000191789

Regions

Domain45 – 10763t-SNARE coiled-coil homology
Domain414 – 47360SH3
Compositional bias332 – 38655Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue531Phosphotyrosine Ref.3
Modified residue1781Phosphoserine By similarity
Modified residue2081Phosphotyrosine By similarity
Modified residue2111Phosphoserine By similarity
Modified residue2171Phosphoserine By similarity
Modified residue2201Phosphoserine By similarity
Modified residue2911Phosphoserine By similarity
Modified residue4231Phosphotyrosine By similarity
Modified residue4751Phosphothreonine By similarity

Experimental info

Mutagenesis531Y → A: Not phosphorylated and perinuclear upon NMDA treatment. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9QZM5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A2B8CC377090BEA6

FASTA47651,705
        10         20         30         40         50         60 
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS 

        70         80         90        100        110        120 
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 

       130        140        150        160        170        180 
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP 

       190        200        210        220        230        240 
VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG 

       250        260        270        280        290        300 
SGSRENSGSS SIGIPIAVPT PSPPTAGPAA PGAAPGSQYG TMTRQISRHN STTSSTSSGG 

       310        320        330        340        350        360 
YRRTPSVTAQ FSAQPHVNGG PLYSQNSISI APPPPPMPQL TPQIPLTGFV ARVQENIADS 

       370        380        390        400        410        420 
PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYS DPYADGDPAW APKNYIEKVV 

       430        440        450        460        470 
AIYDYTKDKD DELSFKEGAI IYVIKKNDDG WFEGVCNRVT GLFPGNYVES IMHYTD 

« Hide

References

[1]"cDNA sequence of the rat eps8 binding protein (e3B1)."
Nicolas G., Galand C., Lecomte M.C.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]"Localization and phosphorylation of Abl-interactor proteins, Abi-1 and Abi-2, in the developing nervous system."
Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S., Pendergast A.M.
Mol. Cell. Neurosci. 16:244-257(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation."
Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J., Kreutz M.R., Gundelfinger E.D., Boeckers T.M.
EMBO J. 26:1397-1409(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEUROGENESIS, INTERACTION WITH EPS8; MYC; MAX; SHANK2; SHANK3 AND WASF1, PHOSPHORYLATION AT TYR-53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF TYR-53.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF176784 mRNA. Translation: AAD55263.1.
RefSeqXP_006254416.1. XM_006254354.1.
UniGeneRn.43675.

3D structure databases

ProteinModelPortalQ9QZM5.
SMRQ9QZM5. Positions 404-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36968N.
IntActQ9QZM5. 9 interactions.
MINTMINT-4508312.

PTM databases

PhosphoSiteQ9QZM5.

Proteomic databases

PaxDbQ9QZM5.
PRIDEQ9QZM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000057572; ENSRNOP00000054381; ENSRNOG00000031325.
GeneID79249.
KEGGrno:79249.
UCSCRGD:621008. rat.

Organism-specific databases

CTD10006.
RGD621008. Abi1.

Phylogenomic databases

eggNOGNOG262939.
GeneTreeENSGT00390000003756.
HOGENOMHOG000293213.
HOVERGENHBG050446.
OMAMPMFDDS.
OrthoDBEOG7J17ZT.
PhylomeDBQ9QZM5.

Gene expression databases

GenevestigatorQ9QZM5.

Family and domain databases

InterProIPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
PfamPF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9QZM5.

Entry information

Entry nameABI1_RAT
AccessionPrimary (citable) accession number: Q9QZM5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families