[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH EPS8 AND ABL1.
DOI=10.1038/sj.onc.1200822; PubMed=9010225 [NCBI, ExPASy, EBI, Israel, Japan]
Biesova Z.,
Piccoli C.,
Wong W.T.;
"Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth.";
Oncogene 14:233-241(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 3; 7; 8 AND 9), AND INTERACTION WITH SPTA1.
DOI=10.1074/jbc.273.22.13681; PubMed=9593709 [NCBI, ExPASy, EBI, Israel, Japan]
Ziemnicka-Kotula D.,
Xu J.,
Gu H.,
Potempska A.,
Kim K.S.,
Jenkins E.C.,
Trenkner E.,
Kotula L.;
"Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton.";
J. Biol. Chem. 273:13681-13692(1998).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND INTERACTION WITH ABL1; NAP1 AND NCK1.
DOI=10.1016/S0378-1119(01)00521-2; PubMed=11418237 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto A.,
Suzuki T.,
Sakaki Y.;
"Isolation of hNap1BP which interacts with human Nap 1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease.";
Gene 271:159-169(2001).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH NCF1.
TISSUE=Umbilical vein endothelial cell;
DOI=10.1016/S0014-5793(03)00262-X; PubMed=12681507 [NCBI, ExPASy, EBI, Israel, Japan]
Gu Y.,
Souza R.F.,
Wu R.F.,
Xu Y.C.,
Terada L.S.;
"Induction of colonic epithelial cell apoptosis by p47-dependent oxidants(1).";
FEBS Lett. 540:195-200(2003).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=T-cell;
Wilson L.A.,
Fields D.,
Cruz L.,
Friesen J.,
Siminovitch K.A.;
"A new member of the Abl interactor protein family, AblBP4.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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[6]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chikri M.M.,
Boutin M.P.,
Vaxillaire M.M.,
Froguel M.P.;
"In silico cloning of the human SSH3BP1/e3B1 gene.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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[7]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Quackenbush R.C.,
Pendergast A.M.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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[8]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P.,
Earthrowl M.E.,
Grafham D.V.,
Rubenfield M.,
French L.,
Steward C.A.,
Sims S.K.,
Jones M.C.,
Searle S.,
Scott C.,
Howe K.,
Hunt S.E.,
Andrews T.D.,
Gilbert J.G.R.,
Swarbreck D.,
Ashurst J.L.,
Taylor A.,
Battles J.,
Bird C.P., ![]()
Ainscough R.,
Almeida J.P.,
Ashwell R.I.S.,
Ambrose K.D.,
Babbage A.K.,
Bagguley C.L.,
Bailey J.,
Banerjee R.,
Bates K.,
Beasley H.,
Bray-Allen S.,
Brown A.J.,
Brown J.Y.,
Burford D.C.,
Burrill W.,
Burton J.,
Cahill P.,
Camire D.,
Carter N.P.,
Chapman J.C.,
Clark S.Y.,
Clarke G.,
Clee C.M.,
Clegg S.,
Corby N.,
Coulson A.,
Dhami P.,
Dutta I.,
Dunn M.,
Faulkner L.,
Frankish A.,
Frankland J.A.,
Garner P.,
Garnett J.,
Gribble S.,
Griffiths C.,
Grocock R.,
Gustafson E.,
Hammond S.,
Harley J.L.,
Hart E.,
Heath P.D.,
Ho T.P.,
Hopkins B.,
Horne J.,
Howden P.J.,
Huckle E.,
Hynds C.,
Johnson C.,
Johnson D.,
Kana A.,
Kay M.,
Kimberley A.M.,
Kershaw J.K.,
Kokkinaki M.,
Laird G.K.,
Lawlor S.,
Lee H.M.,
Leongamornlert D.A.,
Laird G.,
Lloyd C.,
Lloyd D.M.,
Loveland J.,
Lovell J.,
McLaren S.,
McLay K.E.,
McMurray A.,
Mashreghi-Mohammadi M.,
Matthews L.,
Milne S.,
Nickerson T.,
Nguyen M.,
Overton-Larty E.,
Palmer S.A.,
Pearce A.V.,
Peck A.I.,
Pelan S.,
Phillimore B.,
Porter K.,
Rice C.M.,
Rogosin A.,
Ross M.T.,
Sarafidou T.,
Sehra H.K.,
Shownkeen R.,
Skuce C.D.,
Smith M.,
Standring L.,
Sycamore N.,
Tester J.,
Thorpe A.,
Torcasso W.,
Tracey A.,
Tromans A.,
Tsolas J.,
Wall M.,
Walsh J.,
Wang H.,
Weinstock K.,
West A.P.,
Willey D.L.,
Whitehead S.L.,
Wilming L.,
Wray P.W.,
Young L.,
Chen Y.,
Lovering R.C.,
Moschonas N.K.,
Siebert R.,
Fechtel K.,
Bentley D.,
Durbin R.M.,
Hubbard T.,
Doucette-Stamm L.,
Beck S.,
Smith D.R.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
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[9]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[10]
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PROTEIN SEQUENCE OF 2-17.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K.,
Goethals M.,
Martens L.,
Van Damme J.,
Staes A.,
Thomas G.R.,
Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
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[11]
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PROTEIN SEQUENCE OF 2-17; 139-154; 229-237 AND 451-477, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V.,
Boldt K.,
von Kriegsheim A.F.,
Kolch W.;
Submitted (JUL-2007) to UniProtKB.
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[12]
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FUNCTION, AND INTERACTION WITH SOS1; SOS2 AND GRB2.
DOI=10.1128/MCB.20.20.7591-7601.2000; PubMed=11003655 [NCBI, ExPASy, EBI, Israel, Japan]
Fan P.-D.,
Goff S.P.;
"Abl interactor 1 binds to sos and inhibits epidermal growth factor- and v-Abl-induced activation of extracellular signal-regulated kinases.";
Mol. Cell. Biol. 20:7591-7601(2000).
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[13]
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ALTERNATIVE SPLICING (ISOFORMS 2 AND 10), AND CHROMOSOMAL TRANSLOCATION WITH MLL.
PubMed=9694699 [NCBI, ExPASy, EBI, Israel, Japan]
Taki T.,
Shibuya N.,
Taniwaki M.,
Hanada R.,
Morishita K.,
Bessho F.,
Yanagisawa M.,
Hayashi Y.;
"ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23).";
Blood 92:1125-1130(1998).
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[14]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-333, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan]
Salomon A.R.,
Ficarro S.B.,
Brill L.M.,
Brinker A.,
Phung Q.T.,
Ericson C.,
Sauer K.,
Brock A.,
Horn D.M.,
Schultz P.G.,
Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
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[15]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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[16]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K.,
Guo A.,
Zeng Q.,
Possemato A.,
Yu J.,
Haack H.,
Nardone J.,
Lee K.,
Reeves C.,
Li Y.,
Hu Y.,
Tan Z.,
Stokes M.,
Sullivan L.,
Mitchell J.,
Wetzel R.,
Macneill J.,
Ren J.M.,
Yuan J., ![]()
Bakalarski C.E.,
Villen J.,
Kornhauser J.M.,
Smith B.,
Li D.,
Zhou X.,
Gygi S.P.,
Gu T.-L.,
Polakiewicz R.D.,
Rush J.,
Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
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[17]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K.,
Sugiyama N.,
Kyono Y.,
Tomita M.,
Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
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[18]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P.,
Lewandrowski U.,
Wiesner J.,
Wortelkamp S.,
Moebius J.,
Schuetz C.,
Walter U.,
Gambaryan S.,
Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
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- 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 MENA. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level (By similarity).
- SUBUNIT: Interacts with ABL1, MENA, STX1A, SNAP25, VAMP2, EPS8, 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 (By similarity). Interacts with SOS1, SOS2, GRB2, SPTA1 and the first SH3 domain of NCK1. Isoform 6 does not interact with NCK1. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2.
- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-375446, EBI-375543;
Q9UQB8:BAIAP2; NbExp=1; IntAct=EBI-375446, EBI-525456;
Q08509:Eps8 (xeno); NbExp=2; IntAct=EBI-375446, EBI-375596;
P14598:NCF1; NbExp=4; IntAct=EBI-375446, EBI-395044;
P16333:NCK1; NbExp=1; IntAct=EBI-375446, EBI-389883;
Q9Y2A7:NCKAP1; NbExp=2; IntAct=EBI-375446, EBI-389845;
P02549:SPTA1; NbExp=1; IntAct=EBI-375446, EBI-375617;
- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity). Cell projection, lamellipodium (By similarity). Cell projection, filopodium (By similarity). Cell projection, growth cone (By similarity). Cell junction, synapse, synaptosome (By similarity). Cytoplasm, cytoskeleton (By similarity). Note=Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes (By similarity).
- ALTERNATIVE PRODUCTS:
10 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
| | | | | | | |
| Name | 9 |
| Synonyms | 2 |
| Isoform ID | Q8IZP0-9 |
| Features which should be applied to build the isoform sequence: VSP_010750. |
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- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and sufficient for interaction with STX1A (By similarity).
- PTM: In vitro substrate for v-Abl (By similarity). Phosphorylated on tyrosine residues after serum stimulation or induction by v-Abl.
- DISEASE: A chromosomal aberration involving ABI1 is a cause of acute leukemias. Translocation t(10;11)(p11.2;q23) with MLL. ABI1 isoform 2 was found to be present in acute leukemia MLL-ABI1 fusion transcript.
- SIMILARITY: Belongs to the ABI family.
- SIMILARITY: Contains 1 SH3 domain.
- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/ABI1ID233.html";.
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