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Abl interactor 1 (Abelson interactor 1) (Abi-1) (Eps8 SH3 domain-binding protein) (Eps8-binding protein) (e3B1)

 ABI1_RAT                Reviewed;         476 AA.
Q9QZM5;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 128.
RecName: Full=Abl interactor 1;
AltName: Full=Abelson interactor 1;
Short=Abi-1;
AltName: Full=Eps8 SH3 domain-binding protein;
Short=Eps8-binding protein;
AltName: Full=e3B1;
Name=Abi1 {ECO:0000312|RGD:621008};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Nicolas G., Galand C., Lecomte M.C.;
"cDNA sequence of the rat eps8 binding protein (e3B1).";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[2]
SUBCELLULAR LOCATION.
PubMed=10995551; DOI=10.1006/mcne.2000.0865;
Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S.,
Pendergast A.M.;
"Localization and phosphorylation of Abl-interactor proteins, Abi-1
and Abi-2, in the developing nervous system.";
Mol. Cell. Neurosci. 16:244-257(2000).
[3]
FUNCTION IN NEUROGENESIS, INTERACTION WITH EPS8; MYC; MAX; SHANK2;
SHANK3 AND WASF1, PHOSPHORYLATION AT TYR-53, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-53.
PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
"Abelson interacting protein 1 (Abi-1) is essential for dendrite
morphogenesis and synapse formation.";
EMBO J. 26:1397-1409(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-434, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
{ECO:0000269|PubMed:17304222}.
-!- 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). {ECO:0000250|UniProtKB:Q8IZP0,
ECO:0000269|PubMed:17304222}.
-!- INTERACTION:
P52164:Max; NbExp=2; IntAct=EBI-920097, EBI-1184963;
Q9JLU4:Shank3; NbExp=7; IntAct=EBI-920097, EBI-6271152;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:17304222}. Cell projection, lamellipodium
{ECO:0000269|PubMed:17304222}. Cell projection, filopodium
{ECO:0000269|PubMed:17304222}. Cell projection, growth cone
{ECO:0000269|PubMed:10995551}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:17304222}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17304222}.
Note=Localized to protruding lamellipodia and filopodia tips. May
shuttle from the postsynaptic densities to the nucleus.
{ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:17304222}.
-!- TISSUE SPECIFICITY: Widely expressed in brain, high levels
detected in cortex, hippocampus and cerebellum (at protein level).
{ECO:0000269|PubMed:17304222}.
-!- DEVELOPMENTAL STAGE: Low protein levels at birth that increase
progressively at least until 14 days after birth.
{ECO:0000269|PubMed:17304222}.
-!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
sufficient for interaction with STX1A. {ECO:0000250}.
-!- PTM: 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.
{ECO:0000269|PubMed:17304222}.
-!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF176784; AAD55263.1; -; mRNA.
RefSeq; XP_006254416.1; XM_006254354.3.
UniGene; Rn.43675; -.
ProteinModelPortal; Q9QZM5; -.
SMR; Q9QZM5; -.
DIP; DIP-36968N; -.
IntAct; Q9QZM5; 8.
MINT; Q9QZM5; -.
STRING; 10116.ENSRNOP00000054381; -.
iPTMnet; Q9QZM5; -.
PhosphoSitePlus; Q9QZM5; -.
PaxDb; Q9QZM5; -.
PRIDE; Q9QZM5; -.
Ensembl; ENSRNOT00000091023; ENSRNOP00000071079; ENSRNOG00000031325.
GeneID; 79249; -.
UCSC; RGD:621008; rat.
CTD; 10006; -.
RGD; 621008; Abi1.
eggNOG; KOG2546; Eukaryota.
eggNOG; ENOG410Y0MH; LUCA.
GeneTree; ENSGT00390000003756; -.
HOGENOM; HOG000293213; -.
HOVERGEN; HBG050446; -.
InParanoid; Q9QZM5; -.
OrthoDB; EOG091G0AN8; -.
PhylomeDB; Q9QZM5; -.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
PRO; PR:Q9QZM5; -.
Proteomes; UP000002494; Chromosome 17.
Bgee; ENSRNOG00000031325; Expressed in 9 organ(s), highest expression level in Ammon's horn.
ExpressionAtlas; Q9QZM5; baseline and differential.
Genevisible; Q9QZM5; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:InterPro.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
CDD; cd11971; SH3_Abi1; 1.
InterPro; IPR028457; ABI.
InterPro; IPR028456; ABI1.
InterPro; IPR035725; Abi1_SH3.
InterPro; IPR012849; Abl-interactor_HHR_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR000727; T_SNARE_dom.
PANTHER; PTHR10460; PTHR10460; 1.
PANTHER; PTHR10460:SF2; PTHR10460:SF2; 1.
Pfam; PF07815; Abi_HHR; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
Acetylation; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; SH3 domain; Synapse.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8IZP0}.
CHAIN 2 476 Abl interactor 1.
/FTId=PRO_0000191789.
DOMAIN 45 107 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 414 473 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 332 386 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000269|PubMed:17304222}.
MOD_RES 169 169 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 173 173 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 208 208 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 210 210 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8CBW3}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MOD_RES 423 423 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8CBW3}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 475 475 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZP0}.
MUTAGEN 53 53 Y->A: Not phosphorylated and perinuclear
upon NMDA treatment.
{ECO:0000269|PubMed:17304222}.
SEQUENCE 476 AA; 51705 MW; A2B8CC377090BEA6 CRC64;
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKHGNNQP ARTGTLSRTN PPTQKPPSPP
VSGRGTLGRN TPYKTLEPVK PPTVPNDYMT SPARLGSQHS PGRTASLNQR PRTHSGSSGG
SGSRENSGSS SIGIPIAVPT PSPPTAGPAA PGAAPGSQYG TMTRQISRHN STTSSTSSGG
YRRTPSVTAQ FSAQPHVNGG PLYSQNSISI APPPPPMPQL TPQIPLTGFV ARVQENIADS
PTPPPPPPPD DIPMFDDSPP PPPPPPVDYE DEEAAVVQYS DPYADGDPAW APKNYIEKVV
AIYDYTKDKD DELSFKEGAI IYVIKKNDDG WFEGVCNRVT GLFPGNYVES IMHYTD


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