ABI1_MOUSE
ID ABI1_MOUSE Reviewed; 481 AA.
AC Q8CBW3; Q3U8V0; Q60747; Q91ZM5; Q923I9; Q99KH4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Abl interactor 1;
DE AltName: Full=Abelson interactor 1;
DE Short=Abi-1;
DE AltName: Full=Ablphilin-1;
DE AltName: Full=Eps8 SH3 domain-binding protein;
DE Short=Eps8-binding protein;
DE AltName: Full=Spectrin SH3 domain-binding protein 1;
DE AltName: Full=e3B1;
GN Name=Abi1 {ECO:0000312|MGI:MGI:104913}; Synonyms=Ssh3bp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORM 2),
RP AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=11526477; DOI=10.1038/sj.onc.1204502;
RA Ikeguchi A., Yang H.-Y., Gao G., Goff S.P.;
RT "Inhibition of v-Abl transformation in 3T3 cells overexpressing different
RT forms of the Abelson interactor protein Abi-1.";
RL Oncogene 20:4926-4934(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11477655; DOI=10.1002/gcc.1160;
RA Shibuya N., Taki T., Mugishima H., Chin M., Tsuchida M., Sako M., Kawa K.,
RA Ishii E., Miura I., Yanagisawa M., Hayashi Y.;
RT "t(10;11)-acute leukemias with MLL-AF10 and MLL-ABI1 chimeric transcripts:
RT specific expression patterns of ABI1 gene in leukemia and solid tumor cell
RT lines.";
RL Genes Chromosomes Cancer 32:1-10(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-360 (ISOFORM 4), FUNCTION,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, AND INTERACTION WITH ABL1 AND V-ABL.
RX PubMed=7590237; DOI=10.1101/gad.9.21.2583;
RA Shi Y., Alin K., Goff S.P.;
RT "Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal
RT portion of the Abl protein, suppresses v-abl transforming activity.";
RL Genes Dev. 9:2583-2597(1995).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH EPS8 AND SOS1.
RX PubMed=10499589; DOI=10.1038/45822;
RA Scita G., Nordstrom J., Carbone R., Tenca P., Giardina G., Gutkind S.,
RA Bjarnegard M., Betsholtz C., Di Fiore P.P.;
RT "EPS8 and E3B1 transduce signals from Ras to Rac.";
RL Nature 401:290-293(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH ENAH.
RX PubMed=12672821; DOI=10.1074/jbc.m301447200;
RA Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,
RA Shishido T.;
RT "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
RT enabled (Mena) by c-Abl kinase.";
RL J. Biol. Chem. 278:21685-21692(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STX1A; SNAP25; VAMP2
RP AND WASF1.
RX PubMed=15143189; DOI=10.1128/mcb.24.11.4979-4993.2004;
RA Echarri A., Lai M.J., Robinson M.R., Pendergast A.M.;
RT "Abl interactor 1 (Abi-1) wave-binding and SNARE domains regulate its
RT nucleocytoplasmic shuttling, lamellipodium localization, and wave-1
RT levels.";
RL Mol. Cell. Biol. 24:4979-4993(2004).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10995551; DOI=10.1006/mcne.2000.0865;
RA Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S.,
RA Pendergast A.M.;
RT "Localization and phosphorylation of Abl-interactor proteins, Abi-1 and
RT Abi-2, in the developing nervous system.";
RL Mol. Cell. Neurosci. 16:244-257(2000).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11516653; DOI=10.1016/s0960-9822(01)00239-1;
RA Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V.,
RA Pendergast A.M.;
RT "The Abl interactor proteins localize to sites of actin polymerization at
RT the tips of lamellipodia and filopodia.";
RL Curr. Biol. 11:891-895(2001).
RN [11]
RP COMPONENT OF WAVE2 COMPLEX.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=14765121; DOI=10.1038/sj.emboj.7600084;
RA Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J.,
RA Stradal T.E.B.;
RT "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia
RT formation.";
RL EMBO J. 23:749-759(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH EPS8.
RX PubMed=15558031; DOI=10.1038/ncb1199;
RA Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E.,
RA Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G.;
RT "Eps8 controls actin-based motility by capping the barbed ends of actin
RT filaments.";
RL Nat. Cell Biol. 6:1180-1188(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND TYR-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May act in negative regulation of cell growth and
CC transformation by interacting with nonreceptor tyrosine kinases ABL1
CC and/or ABL2. In vitro, at least isoform 2 and isoform 4 suppress the
CC transforming activity of Abelson murine leukemia virus (v-Abl) after
CC overexpression in fibroblasts. May play a role in regulation EGF-
CC induced Erk pathway activation. Involved in cytoskeletal reorganization
CC and EGFR signaling. Together with EPS8 participates in transduction of
CC signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and
CC SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF)
CC activity and ABI1 seems to act as an adapter in the complex. Regulates
CC ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to
CC lamellipodia and there seems to regulate WASF1 protein level. In brain,
CC seems to regulate the dendritic outgrowth and branching as well as to
CC determine the shape and number of synaptic contacts of developing
CC neurons. {ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:11526477,
CC ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15143189,
CC ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:7590237}.
CC -!- SUBUNIT: Interacts with ENAH, Abelson murine leukemia virus V-ABL,
CC ABL1, STX1A, SNAP25, VAMP2, and through its N-terminus with WASF1. Part
CC of a complex consisting of ABI1, STX1A and SNAP25. Part of a complex
CC consisting of ABI1, EPS8 and SOS1. Interacts with EPS8, SOS1, SOS2,
CC GRB2, SPTA1, and the first SH3 domain of NCK1 (By similarity).
CC Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2.
CC Interacts (via SH3 domain) with SHANK2 and SHANK3, but not SHANK1; the
CC interaction is direct. Interacts with the heterodimer MYC:MAX; the
CC interaction may enhance MYC:MAX transcriptional activity. Interacts
CC with FNBP1L (via the SH3 domain), WASF2, and CDC42, but only in the
CC presence of FNBP1L (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8IZP0, ECO:0000269|PubMed:10499589,
CC ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15143189,
CC ECO:0000269|PubMed:15558031, ECO:0000269|PubMed:7590237}.
CC -!- INTERACTION:
CC Q8CBW3; Q9Z207: Diaph3; NbExp=2; IntAct=EBI-375511, EBI-6550123;
CC Q8CBW3; Q08509: Eps8; NbExp=3; IntAct=EBI-375511, EBI-375596;
CC Q8CBW3; Q02384: Sos2; NbExp=2; IntAct=EBI-375511, EBI-395573;
CC Q8CBW3; Q8BH43: Wasf2; NbExp=2; IntAct=EBI-375511, EBI-643162;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cell projection, lamellipodium {ECO:0000250}. Cell projection,
CC filopodium {ECO:0000250}. Cell projection, growth cone {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Localized to protruding lamellipodia and filopodia
CC tips. Also localized to neuronal growth cones and synaptosomes. May
CC shuttle from the postsynaptic densities to the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CBW3-1; Sequence=Displayed;
CC Name=2; Synonyms=short;
CC IsoId=Q8CBW3-2; Sequence=VSP_010756, VSP_010757, VSP_010758;
CC Name=3;
CC IsoId=Q8CBW3-3; Sequence=VSP_010756;
CC Name=4; Synonyms=long;
CC IsoId=Q8CBW3-4; Sequence=VSP_010756, VSP_010757;
CC Name=5;
CC IsoId=Q8CBW3-5; Sequence=VSP_010756, VSP_022636;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in bone
CC marrow, spleen, brain, testes, and embryonic brain. In adult brain
CC prominently expressed in the neocortex, hippocampus and dentate gyrus.
CC {ECO:0000269|PubMed:10995551, ECO:0000269|PubMed:7590237}.
CC -!- DEVELOPMENTAL STAGE: Detected at 10 dpc and 12 dpc in developing brain,
CC but does not appear more prominent in the neuroepithelium compared to
CC the surrounding tissue. {ECO:0000269|PubMed:10995551}.
CC -!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
CC sufficient for interaction with STX1A.
CC -!- PTM: Phosphorylated on tyrosine residues after serum stimulation or
CC induction by v-Abl. Seems to be phosphorylated at Tyr-53 by ABL1,
CC required for nuclear but not for synaptic localization (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
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DR EMBL; AF420251; AAL16036.1; -; mRNA.
DR EMBL; AY033645; AAK59381.1; -; mRNA.
DR EMBL; AK034476; BAC28722.1; -; mRNA.
DR EMBL; AK152061; BAE30917.1; -; mRNA.
DR EMBL; AK152184; BAE31015.1; -; mRNA.
DR EMBL; AK151026; BAE30044.1; -; mRNA.
DR EMBL; BC004657; AAH04657.1; -; mRNA.
DR EMBL; U17698; AAB00373.1; ALT_SEQ; mRNA.
DR CCDS; CCDS38058.1; -. [Q8CBW3-5]
DR CCDS; CCDS38059.1; -. [Q8CBW3-3]
DR CCDS; CCDS38060.1; -. [Q8CBW3-2]
DR CCDS; CCDS38061.1; -. [Q8CBW3-1]
DR CCDS; CCDS50513.1; -. [Q8CBW3-4]
DR RefSeq; NP_001070658.1; NM_001077190.3. [Q8CBW3-1]
DR RefSeq; NP_001070660.1; NM_001077192.3. [Q8CBW3-2]
DR RefSeq; NP_001070661.1; NM_001077193.3. [Q8CBW3-5]
DR RefSeq; NP_031406.2; NM_007380.4. [Q8CBW3-4]
DR AlphaFoldDB; Q8CBW3; -.
DR SMR; Q8CBW3; -.
DR BioGRID; 197905; 28.
DR CORUM; Q8CBW3; -.
DR DIP; DIP-29534N; -.
DR IntAct; Q8CBW3; 34.
DR MINT; Q8CBW3; -.
DR STRING; 10090.ENSMUSP00000118491; -.
DR iPTMnet; Q8CBW3; -.
DR PhosphoSitePlus; Q8CBW3; -.
DR EPD; Q8CBW3; -.
DR jPOST; Q8CBW3; -.
DR MaxQB; Q8CBW3; -.
DR PaxDb; Q8CBW3; -.
DR PRIDE; Q8CBW3; -.
DR ProteomicsDB; 286057; -. [Q8CBW3-1]
DR ProteomicsDB; 286058; -. [Q8CBW3-2]
DR ProteomicsDB; 286059; -. [Q8CBW3-3]
DR ProteomicsDB; 286060; -. [Q8CBW3-4]
DR ProteomicsDB; 286061; -. [Q8CBW3-5]
DR Antibodypedia; 3646; 363 antibodies from 40 providers.
DR DNASU; 11308; -.
DR Ensembl; ENSMUST00000114544; ENSMUSP00000110191; ENSMUSG00000058835. [Q8CBW3-5]
DR Ensembl; ENSMUST00000123948; ENSMUSP00000118491; ENSMUSG00000058835. [Q8CBW3-1]
DR Ensembl; ENSMUST00000126112; ENSMUSP00000117335; ENSMUSG00000058835. [Q8CBW3-3]
DR Ensembl; ENSMUST00000140164; ENSMUSP00000120462; ENSMUSG00000058835. [Q8CBW3-4]
DR Ensembl; ENSMUST00000149719; ENSMUSP00000120621; ENSMUSG00000058835. [Q8CBW3-2]
DR GeneID; 11308; -.
DR KEGG; mmu:11308; -.
DR UCSC; uc008ins.2; mouse. [Q8CBW3-1]
DR UCSC; uc008inw.2; mouse. [Q8CBW3-5]
DR CTD; 10006; -.
DR MGI; MGI:104913; Abi1.
DR VEuPathDB; HostDB:ENSMUSG00000058835; -.
DR eggNOG; KOG2546; Eukaryota.
DR GeneTree; ENSGT00940000154811; -.
DR HOGENOM; CLU_035421_0_0_1; -.
DR InParanoid; Q8CBW3; -.
DR OMA; VGHGVKE; -.
DR PhylomeDB; Q8CBW3; -.
DR TreeFam; TF314303; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 11308; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Abi1; mouse.
DR PRO; PR:Q8CBW3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CBW3; protein.
DR Bgee; ENSMUSG00000058835; Expressed in mesenteric lymph node and 242 other tissues.
DR ExpressionAtlas; Q8CBW3; baseline and differential.
DR Genevisible; Q8CBW3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0032433; C:filopodium tip; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0031209; C:SCAR complex; IDA:ARUK-UCL.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:ARUK-UCL.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0048813; P:dendrite morphogenesis; IDA:MGI.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR CDD; cd11971; SH3_Abi1; 1.
DR InterPro; IPR028457; ABI.
DR InterPro; IPR028456; ABI1.
DR InterPro; IPR035725; Abi1_SH3.
DR InterPro; IPR012849; Abl-interactor_HHR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR10460; PTHR10460; 1.
DR PANTHER; PTHR10460:SF2; PTHR10460:SF2; 1.
DR Pfam; PF07815; Abi_HHR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome; SH3 domain;
KW Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT CHAIN 2..481
FT /note="Abl interactor 1"
FT /id="PRO_0000191788"
FT DOMAIN 45..107
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 419..478
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 18..79
FT /note="Required for binding to WASF1"
FT REGION 158..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZM5"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 213
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT MOD_RES 428
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZM5"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZP0"
FT VAR_SEQ 154..158
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11477655,
FT ECO:0000303|PubMed:11526477, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7590237"
FT /id="VSP_010756"
FT VAR_SEQ 274..362
FT /note="AAPGAAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVAAQFSAQPHVNGG
FT PLYSQNSISVAPPPPPMPQLTPQIPLTGFVARVQENI -> V (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022636"
FT VAR_SEQ 274
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11477655,
FT ECO:0000303|PubMed:11526477, ECO:0000303|PubMed:7590237"
FT /id="VSP_010757"
FT VAR_SEQ 333..361
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11477655"
FT /id="VSP_010758"
FT CONFLICT 313
FT /note="A -> T (in Ref. 4; AAH04657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52288 MW; 1654A1E89438BC1D CRC64;
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK
PPSPPVSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS
GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT AGPAAPGAAP GSQYGTMTRQ ISRHNSTTSS
TSSGGYRRTP SVAAQFSAQP HVNGGPLYSQ NSISVAPPPP PMPQLTPQIP LTGFVARVQE
NIADSPTPPP PPPPDDIPMF DDSPPPPPPP PVDYEDEEAA VVQYSDPYAD GDPAWAPKNY
IEKVVAIYDY TKDKDDELSF KEGAIIYVIK KNDDGWFEGV CNRVTGLFPG NYVESIMHYT
D
