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 24-JAN-2024, entry version 190. 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, RC and 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 33. DR CORUM; Q8CBW3; -. DR DIP; DIP-29534N; -. DR IntAct; Q8CBW3; 34. DR MINT; Q8CBW3; -. DR STRING; 10090.ENSMUSP00000118491; -. DR GlyGen; Q8CBW3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8CBW3; -. DR PhosphoSitePlus; Q8CBW3; -. DR EPD; Q8CBW3; -. DR jPOST; Q8CBW3; -. DR MaxQB; Q8CBW3; -. DR PaxDb; 10090-ENSMUSP00000118491; -. 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 Pumba; Q8CBW3; -. DR Antibodypedia; 3646; 402 antibodies from 40 providers. DR DNASU; 11308; -. DR Ensembl; ENSMUST00000114544.10; ENSMUSP00000110191.4; ENSMUSG00000058835.15. [Q8CBW3-5] DR Ensembl; ENSMUST00000123948.8; ENSMUSP00000118491.2; ENSMUSG00000058835.15. [Q8CBW3-1] DR Ensembl; ENSMUST00000126112.8; ENSMUSP00000117335.2; ENSMUSG00000058835.15. [Q8CBW3-3] DR Ensembl; ENSMUST00000140164.8; ENSMUSP00000120462.2; ENSMUSG00000058835.15. [Q8CBW3-4] DR Ensembl; ENSMUST00000149719.8; ENSMUSP00000120621.2; ENSMUSG00000058835.15. [Q8CBW3-2] DR GeneID; 11308; -. DR KEGG; mmu:11308; -. DR UCSC; uc008ins.2; mouse. [Q8CBW3-1] DR UCSC; uc008inw.2; mouse. [Q8CBW3-5] DR AGR; MGI:104913; -. 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 OrthoDB; 3028771at2759; -. 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; 4 hits in 78 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 245 other cell types or tissues. DR ExpressionAtlas; Q8CBW3; baseline and differential. 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: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:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI. DR GO; GO:0001756; P:somitogenesis; IMP:MGI. DR CDD; cd11971; SH3_Abi1; 1. DR Gene3D; 6.10.140.1620; -; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR028457; ABI. 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:SF2; ABL INTERACTOR 1; 1. DR PANTHER; PTHR10460; ABL INTERACTOR FAMILY MEMBER; 1. DR Pfam; PF07815; Abi_HHR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50192; T_SNARE; 1. DR Genevisible; Q8CBW3; MM. 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 //