Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Abl interactor 1

Gene

Abi1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. protein tyrosine kinase activator activity Source: Ensembl

GO - Biological processi

  1. lamellipodium morphogenesis Source: Ensembl
  2. megakaryocyte development Source: Ensembl
  3. peptidyl-tyrosine phosphorylation Source: Ensembl
  4. somitogenesis Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_285615. Regulation of actin dynamics for phagocytic cup formation.
REACT_301330. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Abi1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi621008. Abi1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: Ensembl
  4. filopodium Source: UniProtKB-SubCell
  5. growth cone Source: UniProtKB-SubCell
  6. lamellipodium Source: UniProtKB-SubCell
  7. nucleus Source: UniProtKB-SubCell
  8. postsynaptic density Source: UniProtKB-SubCell
  9. postsynaptic membrane Source: UniProtKB-KW
  10. SCAR complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531Y → A: Not phosphorylated and perinuclear upon NMDA treatment. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 476475Abl interactor 1PRO_0000191789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei53 – 531Phosphotyrosine1 Publication
Modified residuei169 – 1691PhosphothreonineBy similarity
Modified residuei173 – 1731PhosphothreonineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei208 – 2081PhosphotyrosineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei217 – 2171PhosphoserineBy similarity
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei423 – 4231PhosphotyrosineBy similarity
Modified residuei475 – 4751PhosphothreonineBy similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9QZM5.
PRIDEiQ9QZM5.

PTM databases

PhosphoSiteiQ9QZM5.

Expressioni

Tissue specificityi

Widely expressed in brain, high levels detected in cortex, hippocampus and cerebellum (at protein level).1 Publication

Developmental stagei

Low protein levels at birth that increase progressively at least until 14 days after birth.1 Publication

Gene expression databases

ExpressionAtlasiQ9QZM5. baseline and differential.
GenevestigatoriQ9QZM5.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MaxP521642EBI-920097,EBI-1184963
Shank3Q9JLU47EBI-920097,EBI-6271152

Protein-protein interaction databases

DIPiDIP-36968N.
IntActiQ9QZM5. 9 interactions.
MINTiMINT-4508312.

Structurei

3D structure databases

ProteinModelPortaliQ9QZM5.
SMRiQ9QZM5. Positions 404-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 10763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST
Domaini414 – 47360SH3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi332 – 38655Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ABI family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG262939.
GeneTreeiENSGT00390000003756.
HOGENOMiHOG000293213.
HOVERGENiHBG050446.
InParanoidiQ9QZM5.
OMAiMPMFDDS.
OrthoDBiEOG7J17ZT.
PhylomeDBiQ9QZM5.

Family and domain databases

InterProiIPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
PfamiPF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QZM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET
60 70 80 90 100
KAYTTQSLAS VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH
110 120 130 140 150
KEKVARREIG ILTTNKNTSR THKIIAPANM ERPVRYIRKP IDYTVLDDVG
160 170 180 190 200
HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP VSGRGTLGRN TPYKTLEPVK
210 220 230 240 250
PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG SGSRENSGSS
260 270 280 290 300
SIGIPIAVPT PSPPTAGPAA PGAAPGSQYG TMTRQISRHN STTSSTSSGG
310 320 330 340 350
YRRTPSVTAQ FSAQPHVNGG PLYSQNSISI APPPPPMPQL TPQIPLTGFV
360 370 380 390 400
ARVQENIADS PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYS
410 420 430 440 450
DPYADGDPAW APKNYIEKVV AIYDYTKDKD DELSFKEGAI IYVIKKNDDG
460 470
WFEGVCNRVT GLFPGNYVES IMHYTD
Length:476
Mass (Da):51,705
Last modified:January 23, 2007 - v3
Checksum:iA2B8CC377090BEA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176784 mRNA. Translation: AAD55263.1.
RefSeqiXP_006254416.1. XM_006254354.2.
UniGeneiRn.43675.

Genome annotation databases

EnsembliENSRNOT00000057572; ENSRNOP00000054381; ENSRNOG00000031325.
GeneIDi79249.
KEGGirno:79249.
UCSCiRGD:621008. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176784 mRNA. Translation: AAD55263.1.
RefSeqiXP_006254416.1. XM_006254354.2.
UniGeneiRn.43675.

3D structure databases

ProteinModelPortaliQ9QZM5.
SMRiQ9QZM5. Positions 404-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36968N.
IntActiQ9QZM5. 9 interactions.
MINTiMINT-4508312.

PTM databases

PhosphoSiteiQ9QZM5.

Proteomic databases

PaxDbiQ9QZM5.
PRIDEiQ9QZM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000057572; ENSRNOP00000054381; ENSRNOG00000031325.
GeneIDi79249.
KEGGirno:79249.
UCSCiRGD:621008. rat.

Organism-specific databases

CTDi10006.
RGDi621008. Abi1.

Phylogenomic databases

eggNOGiNOG262939.
GeneTreeiENSGT00390000003756.
HOGENOMiHOG000293213.
HOVERGENiHBG050446.
InParanoidiQ9QZM5.
OMAiMPMFDDS.
OrthoDBiEOG7J17ZT.
PhylomeDBiQ9QZM5.

Enzyme and pathway databases

ReactomeiREACT_285615. Regulation of actin dynamics for phagocytic cup formation.
REACT_301330. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

PROiQ9QZM5.

Gene expression databases

ExpressionAtlasiQ9QZM5. baseline and differential.
GenevestigatoriQ9QZM5.

Family and domain databases

InterProiIPR028457. ABI.
IPR028456. ABI1.
IPR012849. Abl-interactor_HHR_dom.
IPR001452. SH3_domain.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR10460. PTHR10460. 1 hit.
PTHR10460:SF2. PTHR10460:SF2. 1 hit.
PfamiPF07815. Abi_HHR. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA sequence of the rat eps8 binding protein (e3B1)."
    Nicolas G., Galand C., Lecomte M.C.
    Submitted (JUL-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(1999) [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(2006) [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.

Entry informationi

Entry nameiABI1_RAT
AccessioniPrimary (citable) accession number: Q9QZM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.