ID ABI2_HUMAN Reviewed; 513 AA. AC Q9NYB9; B4DSN1; Q13147; Q13249; Q13801; Q9BV70; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 197. DE RecName: Full=Abl interactor 2 {ECO:0000303|Ref.16}; DE AltName: Full=Abelson interactor 2 {ECO:0000303|Ref.16}; DE Short=Abi-2 {ECO:0000303|PubMed:7590236}; DE AltName: Full=Abl-binding protein 3; DE Short=AblBP3; DE AltName: Full=Arg-binding protein 1 {ECO:0000303|PubMed:8649853}; DE Short=ArgBP1 {ECO:0000303|PubMed:8649853}; GN Name=ABI2 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:24011}; GN Synonyms=ARGBPIA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, RP PHOSPHORYLATION, INTERACTION WITH ABL1, TISSUE SPECIFICITY, AND DOMAIN. RX PubMed=7590236; DOI=10.1101/gad.9.21.2569; RA Dai Z., Pendergast A.M.; RT "Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine RT kinase and modulates c-Abl transforming activity."; RL Genes Dev. 9:2569-2582(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Ren R.; RT "Cloning of a binding substrate of the Abl protein tyrosine kinase."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, RP INTERACTION WITH ABL2, AND DOMAIN. RC TISSUE=Brain; RX PubMed=8649853; RA Wang B., Mysliwiec T., Krainc D., Jensen R.A., Sonoda G., Testa J.R., RA Golemis E.A., Kruh G.D.; RT "Identification of ArgBP1, an Arg protein tyrosine kinase binding protein RT that is the human homologue of a CNS-specific Xenopus gene."; RL Oncogene 12:1921-1929(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [7] RP FUNCTION. RX PubMed=10498863; DOI=10.1038/sj.onc.1202911; RA Juang J.L., Hoffmann F.M.; RT "Drosophila abelson interacting protein (dAbi) is a positive regulator of RT abelson tyrosine kinase activity."; RL Oncogene 18:5138-5147(1999). RN [8] 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 [9] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=15572692; DOI=10.1128/mcb.24.24.10905-10922.2004; RA Grove M., Demyanenko G., Echarri A., Zipfel P.A., Quiroz M.E., RA Rodriguiz R.M., Playford M., Martensen S.A., Robinson M.R., Wetsel W.C., RA Maness P.F., Pendergast A.M.; RT "ABI2-deficient mice exhibit defective cell migration, aberrant dendritic RT spine morphogenesis, and deficits in learning and memory."; RL Mol. Cell. Biol. 24:10905-10922(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-368, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-227 AND SER-368, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135 (MICROBIAL INFECTION). RX PubMed=25121749; DOI=10.1016/j.chom.2014.07.005; RA Stanton R.J., Prod'homme V., Purbhoo M.A., Moore M., Aicheler R.J., RA Heinzmann M., Bailer S.M., Haas J., Antrobus R., Weekes M.P., Lehner P.J., RA Vojtesek B., Miners K.L., Man S., Wilkie G.S., Davison A.J., Wang E.C., RA Tomasec P., Wilkinson G.W.; RT "HCMV pUL135 remodels the actin cytoskeleton to impair immune recognition RT of infected cells."; RL Cell Host Microbe 16:201-214(2014). RN [16] RP STRUCTURE BY NMR OF 444-508. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of Abl interactor 2 (Abelson RT interactor 2)."; RL Submitted (FEB-2008) to the PDB data bank. RN [17] RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-164, SUBUNIT, AND FUNCTION. RX PubMed=21107423; DOI=10.1038/nature09623; RA Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M., RA Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.; RT "Structure and control of the actin regulatory WAVE complex."; RL Nature 468:533-538(2010). RN [18] RP VARIANT 132-ARG--GLU-513 DEL. RX PubMed=28397838; DOI=10.1038/mp.2017.60; RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K., RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M., RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M., RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R., RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M., RA Vincent J.B.; RT "Mapping autosomal recessive intellectual disability: combined microarray RT and exome sequencing identifies 26 novel candidate genes in 192 RT consanguineous families."; RL Mol. Psychiatry 23:973-984(2018). CC -!- FUNCTION: Regulator of actin cytoskeleton dynamics underlying cell CC motility and adhesion. Functions as a component of the WAVE complex, CC which activates actin nucleating machinery Arp2/3 to drive lamellipodia CC formation (PubMed:21107423). Acts as a regulator and substrate of CC nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked CC to cell growth and differentiation. Positively regulates ABL1-mediated CC phosphorylation of ENAH, which is required for proper polymerization of CC nucleated actin filaments at the leading edge (PubMed:7590236, CC PubMed:8649853, PubMed:10498863). Contributes to the regulation of CC actin assembly at the tips of neuron projections. In particular, CC controls dendritic spine morphogenesis and may promote dendritic spine CC specification toward large mushroom-type spines known as repositories CC of memory in the brain (By similarity). In hippocampal neurons, may CC mediate actin-dependent BDNF-NTRK2 early endocytic trafficking that CC triggers dendrite outgrowth (By similarity). Participates in ocular CC lens morphogenesis, likely by regulating lamellipodia-driven adherens CC junction formation at the epithelial cell-secondary lens fiber CC interface (By similarity). Also required for nascent adherens junction CC assembly in epithelial cells (PubMed:15572692). CC {ECO:0000250|UniProtKB:P62484, ECO:0000269|PubMed:10498863, CC ECO:0000269|PubMed:15572692, ECO:0000269|PubMed:21107423, CC ECO:0000269|PubMed:7590236, ECO:0000269|PubMed:8649853}. CC -!- SUBUNIT: Component of the WAVE complex composed of ABI2, CYFIP1 or CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by CC WAVE1, ABI2 and BRK1. CYFIP2 binds to activated RAC1 which causes the CC complex to dissociate, releasing activated WASF1 (PubMed:21107423). CC Interacts (via SH3 domain) with ABL1 and ABL2 (PubMed:7590236, CC PubMed:8649853). {ECO:0000269|PubMed:21107423, CC ECO:0000269|PubMed:7590236, ECO:0000269|PubMed:8649853}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC UL135. {ECO:0000269|PubMed:25121749}. CC -!- INTERACTION: CC Q9NYB9; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-743598, EBI-743598; CC Q9NYB9; P00519: ABL1; NbExp=2; IntAct=EBI-743598, EBI-375543; CC Q9NYB9; A7KAX9: ARHGAP32; NbExp=4; IntAct=EBI-743598, EBI-308663; CC Q9NYB9; Q9H6L4: ARMC7; NbExp=4; IntAct=EBI-743598, EBI-742909; CC Q9NYB9; Q9UL45: BLOC1S6; NbExp=5; IntAct=EBI-743598, EBI-465781; CC Q9NYB9; Q68D86: CCDC102B; NbExp=5; IntAct=EBI-743598, EBI-10171570; CC Q9NYB9; Q8TD31: CCHCR1; NbExp=3; IntAct=EBI-743598, EBI-949834; CC Q9NYB9; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-743598, EBI-10175300; CC Q9NYB9; O43186: CRX; NbExp=5; IntAct=EBI-743598, EBI-748171; CC Q9NYB9; O60941: DTNB; NbExp=6; IntAct=EBI-743598, EBI-740402; CC Q9NYB9; O43281: EFS; NbExp=6; IntAct=EBI-743598, EBI-718488; CC Q9NYB9; Q9H6Z9: EGLN3; NbExp=3; IntAct=EBI-743598, EBI-1175354; CC Q9NYB9; Q6IB98: EIF3S3; NbExp=3; IntAct=EBI-743598, EBI-10184995; CC Q9NYB9; Q96CN9: GCC1; NbExp=4; IntAct=EBI-743598, EBI-746252; CC Q9NYB9; O14964: HGS; NbExp=5; IntAct=EBI-743598, EBI-740220; CC Q9NYB9; P61978: HNRNPK; NbExp=6; IntAct=EBI-743598, EBI-304185; CC Q9NYB9; Q9NSC5: HOMER3; NbExp=7; IntAct=EBI-743598, EBI-748420; CC Q9NYB9; Q8IY31: IFT20; NbExp=6; IntAct=EBI-743598, EBI-744203; CC Q9NYB9; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-743598, EBI-8638439; CC Q9NYB9; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-743598, EBI-10188326; CC Q9NYB9; Q9BVG8: KIFC3; NbExp=5; IntAct=EBI-743598, EBI-2125614; CC Q9NYB9; A1A4E9: KRT13; NbExp=3; IntAct=EBI-743598, EBI-10171552; CC Q9NYB9; P19012: KRT15; NbExp=6; IntAct=EBI-743598, EBI-739566; CC Q9NYB9; P08727: KRT19; NbExp=3; IntAct=EBI-743598, EBI-742756; CC Q9NYB9; P35900: KRT20; NbExp=3; IntAct=EBI-743598, EBI-742094; CC Q9NYB9; Q15323: KRT31; NbExp=5; IntAct=EBI-743598, EBI-948001; CC Q9NYB9; Q14525: KRT33B; NbExp=3; IntAct=EBI-743598, EBI-1049638; CC Q9NYB9; P25791: LMO2; NbExp=5; IntAct=EBI-743598, EBI-739696; CC Q9NYB9; Q96HT8: MRFAP1L1; NbExp=7; IntAct=EBI-743598, EBI-748896; CC Q9NYB9; Q9H9J2: MRPL44; NbExp=3; IntAct=EBI-743598, EBI-713619; CC Q9NYB9; O43639: NCK2; NbExp=6; IntAct=EBI-743598, EBI-713635; CC Q9NYB9; P37198: NUP62; NbExp=6; IntAct=EBI-743598, EBI-347978; CC Q9NYB9; Q15154: PCM1; NbExp=3; IntAct=EBI-743598, EBI-741421; CC Q9NYB9; Q13526: PIN1; NbExp=5; IntAct=EBI-743598, EBI-714158; CC Q9NYB9; P30405: PPIF; NbExp=4; IntAct=EBI-743598, EBI-5544229; CC Q9NYB9; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-743598, EBI-2860740; CC Q9NYB9; Q13131: PRKAA1; NbExp=5; IntAct=EBI-743598, EBI-1181405; CC Q9NYB9; P54646: PRKAA2; NbExp=5; IntAct=EBI-743598, EBI-1383852; CC Q9NYB9; Q569H4: PRR16; NbExp=4; IntAct=EBI-743598, EBI-5564642; CC Q9NYB9; O00560: SDCBP; NbExp=5; IntAct=EBI-743598, EBI-727004; CC Q9NYB9; O75886: STAM2; NbExp=5; IntAct=EBI-743598, EBI-373258; CC Q9NYB9; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-743598, EBI-1105213; CC Q9NYB9; Q08117: TLE5; NbExp=5; IntAct=EBI-743598, EBI-717810; CC Q9NYB9; Q13049: TRIM32; NbExp=6; IntAct=EBI-743598, EBI-742790; CC Q9NYB9; Q15654: TRIP6; NbExp=5; IntAct=EBI-743598, EBI-742327; CC Q9NYB9; Q5ST30-4: VARS2; NbExp=3; IntAct=EBI-743598, EBI-10244997; CC Q9NYB9; P50552: VASP; NbExp=5; IntAct=EBI-743598, EBI-748201; CC Q9NYB9; P18206: VCL; NbExp=3; IntAct=EBI-743598, EBI-716775; CC Q9NYB9; Q9Y3C0: WASHC3; NbExp=4; IntAct=EBI-743598, EBI-712969; CC Q9NYB9; O43516: WIPF1; NbExp=4; IntAct=EBI-743598, EBI-346356; CC Q9NYB9; Q8VHK2: Caskin1; Xeno; NbExp=3; IntAct=EBI-743598, EBI-7049475; CC Q9NYB9-2; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-11096309, EBI-11743294; CC Q9NYB9-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11096309, EBI-11096309; CC Q9NYB9-2; Q9P2A4: ABI3; NbExp=5; IntAct=EBI-11096309, EBI-742038; CC Q9NYB9-2; P42684-3: ABL2; NbExp=3; IntAct=EBI-11096309, EBI-10693977; CC Q9NYB9-2; O94929-2: ABLIM3; NbExp=3; IntAct=EBI-11096309, EBI-11961672; CC Q9NYB9-2; Q5BKX5-3: ACTMAP; NbExp=5; IntAct=EBI-11096309, EBI-11976299; CC Q9NYB9-2; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-11096309, EBI-8643161; CC Q9NYB9-2; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11096309, EBI-357530; CC Q9NYB9-2; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-11096309, EBI-11745576; CC Q9NYB9-2; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-11096309, EBI-14493093; CC Q9NYB9-2; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-11096309, EBI-11954519; CC Q9NYB9-2; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-11096309, EBI-745689; CC Q9NYB9-2; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-11096309, EBI-12811889; CC Q9NYB9-2; O95429: BAG4; NbExp=5; IntAct=EBI-11096309, EBI-2949658; CC Q9NYB9-2; Q9NQY0: BIN3; NbExp=7; IntAct=EBI-11096309, EBI-2653038; CC Q9NYB9-2; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-11096309, EBI-465861; CC Q9NYB9-2; Q9UL45: BLOC1S6; NbExp=6; IntAct=EBI-11096309, EBI-465781; CC Q9NYB9-2; Q96GS4: BORCS6; NbExp=5; IntAct=EBI-11096309, EBI-10193358; CC Q9NYB9-2; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-11096309, EBI-747505; CC Q9NYB9-2; A1L168: C20orf202; NbExp=3; IntAct=EBI-11096309, EBI-18396958; CC Q9NYB9-2; Q53FE4: C4orf17; NbExp=3; IntAct=EBI-11096309, EBI-715110; CC Q9NYB9-2; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-11096309, EBI-10171570; CC Q9NYB9-2; Q96NT0: CCDC115; NbExp=5; IntAct=EBI-11096309, EBI-2810325; CC Q9NYB9-2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-11096309, EBI-10961624; CC Q9NYB9-2; Q96LY2-2: CCDC74B; NbExp=3; IntAct=EBI-11096309, EBI-17967022; CC Q9NYB9-2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-11096309, EBI-10175300; CC Q9NYB9-2; Q9H3R5: CENPH; NbExp=6; IntAct=EBI-11096309, EBI-1003700; CC Q9NYB9-2; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-11096309, EBI-2350265; CC Q9NYB9-2; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-11096309, EBI-744115; CC Q9NYB9-2; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-11096309, EBI-11752486; CC Q9NYB9-2; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-11096309, EBI-12160437; CC Q9NYB9-2; Q16740: CLPP; NbExp=3; IntAct=EBI-11096309, EBI-1056029; CC Q9NYB9-2; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-11096309, EBI-9091495; CC Q9NYB9-2; Q9NWM3: CUEDC1; NbExp=3; IntAct=EBI-11096309, EBI-5838167; CC Q9NYB9-2; Q13561: DCTN2; NbExp=3; IntAct=EBI-11096309, EBI-715074; CC Q9NYB9-2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-11096309, EBI-11988027; CC Q9NYB9-2; Q9P1A6-3: DLGAP2; NbExp=3; IntAct=EBI-11096309, EBI-12019838; CC Q9NYB9-2; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-11096309, EBI-12000556; CC Q9NYB9-2; Q6TDU7: DNAI7; NbExp=3; IntAct=EBI-11096309, EBI-5235378; CC Q9NYB9-2; O60941-5: DTNB; NbExp=5; IntAct=EBI-11096309, EBI-11984733; CC Q9NYB9-2; O43281-2: EFS; NbExp=5; IntAct=EBI-11096309, EBI-11525448; CC Q9NYB9-2; Q05215: EGR4; NbExp=3; IntAct=EBI-11096309, EBI-19949420; CC Q9NYB9-2; Q9H0I2: ENKD1; NbExp=6; IntAct=EBI-11096309, EBI-744099; CC Q9NYB9-2; Q8TE68-2: EPS8L1; NbExp=3; IntAct=EBI-11096309, EBI-12003490; CC Q9NYB9-2; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-11096309, EBI-7225287; CC Q9NYB9-2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-11096309, EBI-6658203; CC Q9NYB9-2; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-11096309, EBI-2870039; CC Q9NYB9-2; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-11096309, EBI-11959077; CC Q9NYB9-2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-11096309, EBI-750641; CC Q9NYB9-2; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-11096309, EBI-10226858; CC Q9NYB9-2; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-11096309, EBI-11320806; CC Q9NYB9-2; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-11096309, EBI-7960826; CC Q9NYB9-2; P14136: GFAP; NbExp=6; IntAct=EBI-11096309, EBI-744302; CC Q9NYB9-2; Q86UU5: GGN; NbExp=3; IntAct=EBI-11096309, EBI-10259069; CC Q9NYB9-2; O95872: GPANK1; NbExp=3; IntAct=EBI-11096309, EBI-751540; CC Q9NYB9-2; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-11096309, EBI-14103818; CC Q9NYB9-2; Q03014: HHEX; NbExp=3; IntAct=EBI-11096309, EBI-747421; CC Q9NYB9-2; P61978-2: HNRNPK; NbExp=6; IntAct=EBI-11096309, EBI-7060731; CC Q9NYB9-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11096309, EBI-748420; CC Q9NYB9-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-11096309, EBI-7116203; CC Q9NYB9-2; Q8IY31-3: IFT20; NbExp=7; IntAct=EBI-11096309, EBI-9091197; CC Q9NYB9-2; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-11096309, EBI-8638439; CC Q9NYB9-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-11096309, EBI-6509505; CC Q9NYB9-2; Q9C086: INO80B; NbExp=3; IntAct=EBI-11096309, EBI-715611; CC Q9NYB9-2; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-11096309, EBI-4311436; CC Q9NYB9-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11096309, EBI-1055254; CC Q9NYB9-2; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-11096309, EBI-10188326; CC Q9NYB9-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-11096309, EBI-14069005; CC Q9NYB9-2; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-11096309, EBI-373334; CC Q9NYB9-2; P02533: KRT14; NbExp=3; IntAct=EBI-11096309, EBI-702178; CC Q9NYB9-2; P19012: KRT15; NbExp=3; IntAct=EBI-11096309, EBI-739566; CC Q9NYB9-2; P08727: KRT19; NbExp=3; IntAct=EBI-11096309, EBI-742756; CC Q9NYB9-2; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-11096309, EBI-2952736; CC Q9NYB9-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-11096309, EBI-3044087; CC Q9NYB9-2; O76011: KRT34; NbExp=3; IntAct=EBI-11096309, EBI-1047093; CC Q9NYB9-2; O76013-2: KRT36; NbExp=3; IntAct=EBI-11096309, EBI-11958506; CC Q9NYB9-2; O95678: KRT75; NbExp=3; IntAct=EBI-11096309, EBI-2949715; CC Q9NYB9-2; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-11096309, EBI-726510; CC Q9NYB9-2; Q3B8N2: LGALS9B; NbExp=3; IntAct=EBI-11096309, EBI-10240775; CC Q9NYB9-2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-11096309, EBI-12039345; CC Q9NYB9-2; Q68G74: LHX8; NbExp=3; IntAct=EBI-11096309, EBI-8474075; CC Q9NYB9-2; P25800: LMO1; NbExp=8; IntAct=EBI-11096309, EBI-8639312; CC Q9NYB9-2; P25791-3: LMO2; NbExp=6; IntAct=EBI-11096309, EBI-11959475; CC Q9NYB9-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11096309, EBI-11742507; CC Q9NYB9-2; P61968: LMO4; NbExp=3; IntAct=EBI-11096309, EBI-2798728; CC Q9NYB9-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11096309, EBI-739832; CC Q9NYB9-2; Q96LR2: LURAP1; NbExp=3; IntAct=EBI-11096309, EBI-741355; CC Q9NYB9-2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-11096309, EBI-741037; CC Q9NYB9-2; P43355: MAGEA1; NbExp=3; IntAct=EBI-11096309, EBI-740978; CC Q9NYB9-2; Q9BTT4: MED10; NbExp=3; IntAct=EBI-11096309, EBI-394354; CC Q9NYB9-2; Q9P086: MED11; NbExp=3; IntAct=EBI-11096309, EBI-394704; CC Q9NYB9-2; Q9NX70: MED29; NbExp=3; IntAct=EBI-11096309, EBI-394656; CC Q9NYB9-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11096309, EBI-16439278; CC Q9NYB9-2; Q9Y605: MRFAP1; NbExp=5; IntAct=EBI-11096309, EBI-995714; CC Q9NYB9-2; Q13084: MRPL28; NbExp=3; IntAct=EBI-11096309, EBI-723426; CC Q9NYB9-2; P15173: MYOG; NbExp=3; IntAct=EBI-11096309, EBI-3906629; CC Q9NYB9-2; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-11096309, EBI-5662487; CC Q9NYB9-2; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-11096309, EBI-16429340; CC Q9NYB9-2; A0A0S2Z4E4: NCK1; NbExp=3; IntAct=EBI-11096309, EBI-16432934; CC Q9NYB9-2; O43639: NCK2; NbExp=10; IntAct=EBI-11096309, EBI-713635; CC Q9NYB9-2; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-11096309, EBI-10963850; CC Q9NYB9-2; O94856-3: NFASC; NbExp=3; IntAct=EBI-11096309, EBI-12035911; CC Q9NYB9-2; Q5HYW2: NHSL2; NbExp=9; IntAct=EBI-11096309, EBI-2859639; CC Q9NYB9-2; O00746: NME4; NbExp=3; IntAct=EBI-11096309, EBI-744871; CC Q9NYB9-2; O43482: OIP5; NbExp=3; IntAct=EBI-11096309, EBI-536879; CC Q9NYB9-2; A6NGQ2: OOEP; NbExp=3; IntAct=EBI-11096309, EBI-18583589; CC Q9NYB9-2; Q13177: PAK2; NbExp=3; IntAct=EBI-11096309, EBI-1045887; CC Q9NYB9-2; Q15154-3: PCM1; NbExp=3; IntAct=EBI-11096309, EBI-11742977; CC Q9NYB9-2; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-11096309, EBI-350517; CC Q9NYB9-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-11096309, EBI-357275; CC Q9NYB9-2; Q8N4B1-4: PHETA1; NbExp=8; IntAct=EBI-11096309, EBI-14131832; CC Q9NYB9-2; O43189: PHF1; NbExp=3; IntAct=EBI-11096309, EBI-530034; CC Q9NYB9-2; Q13526: PIN1; NbExp=3; IntAct=EBI-11096309, EBI-714158; CC Q9NYB9-2; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-11096309, EBI-12014286; CC Q9NYB9-2; P01189: POMC; NbExp=3; IntAct=EBI-11096309, EBI-12219503; CC Q9NYB9-2; P30405: PPIF; NbExp=3; IntAct=EBI-11096309, EBI-5544229; CC Q9NYB9-2; Q08209-2: PPP3CA; NbExp=3; IntAct=EBI-11096309, EBI-11959013; CC Q9NYB9-2; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-11096309, EBI-3957793; CC Q9NYB9-2; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11096309, EBI-11320284; CC Q9NYB9-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-11096309, EBI-1383852; CC Q9NYB9-2; Q569H4: PRR16; NbExp=8; IntAct=EBI-11096309, EBI-5564642; CC Q9NYB9-2; P86480: PRR20D; NbExp=3; IntAct=EBI-11096309, EBI-12754095; CC Q9NYB9-2; P25786: PSMA1; NbExp=3; IntAct=EBI-11096309, EBI-359352; CC Q9NYB9-2; Q6NUJ5: PWWP2B; NbExp=3; IntAct=EBI-11096309, EBI-10251192; CC Q9NYB9-2; Q15276: RABEP1; NbExp=3; IntAct=EBI-11096309, EBI-447043; CC Q9NYB9-2; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-11096309, EBI-14093916; CC Q9NYB9-2; Q9Y272: RASD1; NbExp=3; IntAct=EBI-11096309, EBI-740818; CC Q9NYB9-2; Q15287: RNPS1; NbExp=3; IntAct=EBI-11096309, EBI-395959; CC Q9NYB9-2; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-11096309, EBI-366570; CC Q9NYB9-2; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-11096309, EBI-748350; CC Q9NYB9-2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-11096309, EBI-6257312; CC Q9NYB9-2; O76038: SCGN; NbExp=3; IntAct=EBI-11096309, EBI-749420; CC Q9NYB9-2; Q9Y3L3: SH3BP1; NbExp=3; IntAct=EBI-11096309, EBI-346869; CC Q9NYB9-2; Q13239-3: SLA; NbExp=3; IntAct=EBI-11096309, EBI-17630587; CC Q9NYB9-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-11096309, EBI-358489; CC Q9NYB9-2; O60641-3: SNAP91; NbExp=3; IntAct=EBI-11096309, EBI-12854506; CC Q9NYB9-2; O95295: SNAPIN; NbExp=5; IntAct=EBI-11096309, EBI-296723; CC Q9NYB9-2; Q96RF0: SNX18; NbExp=3; IntAct=EBI-11096309, EBI-298169; CC Q9NYB9-2; Q9UNH6-3: SNX7; NbExp=3; IntAct=EBI-11096309, EBI-12424584; CC Q9NYB9-2; O60504: SORBS3; NbExp=3; IntAct=EBI-11096309, EBI-741237; CC Q9NYB9-2; O75886: STAM2; NbExp=3; IntAct=EBI-11096309, EBI-373258; CC Q9NYB9-2; Q8N4C7: STX19; NbExp=3; IntAct=EBI-11096309, EBI-8484990; CC Q9NYB9-2; Q12846: STX4; NbExp=3; IntAct=EBI-11096309, EBI-744942; CC Q9NYB9-2; Q08117-2: TLE5; NbExp=6; IntAct=EBI-11096309, EBI-11741437; CC Q9NYB9-2; P07951-2: TPM2; NbExp=3; IntAct=EBI-11096309, EBI-10977815; CC Q9NYB9-2; Q13049: TRIM32; NbExp=8; IntAct=EBI-11096309, EBI-742790; CC Q9NYB9-2; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-11096309, EBI-2341648; CC Q9NYB9-2; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-11096309, EBI-11059915; CC Q9NYB9-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11096309, EBI-947187; CC Q9NYB9-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11096309, EBI-739895; CC Q9NYB9-2; O75604: USP2; NbExp=3; IntAct=EBI-11096309, EBI-743272; CC Q9NYB9-2; Q5ST30: VARS2; NbExp=3; IntAct=EBI-11096309, EBI-2116622; CC Q9NYB9-2; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-11096309, EBI-12146727; CC Q9NYB9-2; Q9UPY6-2: WASF3; NbExp=3; IntAct=EBI-11096309, EBI-12026286; CC Q9NYB9-2; Q9Y3C0: WASHC3; NbExp=5; IntAct=EBI-11096309, EBI-712969; CC Q9NYB9-2; O00401: WASL; NbExp=5; IntAct=EBI-11096309, EBI-957615; CC Q9NYB9-2; O43516-4: WIPF1; NbExp=3; IntAct=EBI-11096309, EBI-12052927; CC Q9NYB9-2; Q9NZC7-5: WWOX; NbExp=5; IntAct=EBI-11096309, EBI-12040603; CC Q9NYB9-2; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-11096309, EBI-11419867; CC Q9NYB9-2; Q9H0C1: ZMYND12; NbExp=5; IntAct=EBI-11096309, EBI-12030590; CC Q9NYB9-2; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-11096309, EBI-17269964; CC Q9NYB9-2; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-11096309, EBI-16429014; CC Q9NYB9-2; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-11096309, EBI-4395732; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11516653, CC ECO:0000269|PubMed:7590236, ECO:0000269|PubMed:8649853}. Nucleus CC {ECO:0000269|PubMed:7590236}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell projection, lamellipodium CC {ECO:0000269|PubMed:11516653, ECO:0000269|PubMed:15572692}. Cell CC projection, filopodium {ECO:0000269|PubMed:11516653}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:15572692}. Cell junction, adherens CC junction {ECO:0000269|PubMed:15572692}. Note=Isoform 1 but not isoform CC 3 is localized to protruding lamellipodia and filopodia tips CC (PubMed:11516653, PubMed:15572692). Present at nascent adherens CC junctions, where it clusters adjacent to the tips of F-actin CC protrusions (PubMed:15572692). {ECO:0000269|PubMed:11516653, CC ECO:0000269|PubMed:15572692}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Abi-2b; CC IsoId=Q9NYB9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NYB9-2; Sequence=VSP_010761, VSP_010762, VSP_010763; CC Name=3; Synonyms=Abi-2a; CC IsoId=Q9NYB9-3; Sequence=VSP_010759, VSP_010760, VSP_010761, CC VSP_010762; CC Name=4; CC IsoId=Q9NYB9-4; Sequence=VSP_010761; CC -!- TISSUE SPECIFICITY: Widely expressed. Abundant in testes, ovary, CC thymus, and colon, with lower but detectable levels in prostate, CC peripheral blood leukocytes, and spleen. {ECO:0000269|PubMed:7590236}. CC -!- DOMAIN: The SH3 domain is critical for binding to ABL1 and ABL2. CC {ECO:0000269|PubMed:7590236, ECO:0000269|PubMed:8649853}. CC -!- PTM: Phosphorylated by ABL1. {ECO:0000269|PubMed:7590236}. 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; U23435; AAA92289.1; -; mRNA. DR EMBL; U31089; AAA75446.1; -; mRNA. DR EMBL; AF260261; AAF70308.1; -; mRNA. DR EMBL; X95632; CAA64885.1; -; mRNA. DR EMBL; BT009920; AAP88922.1; -; mRNA. DR EMBL; AK299824; BAG61693.1; -; mRNA. DR EMBL; BC001439; AAH01439.1; -; mRNA. DR CCDS; CCDS2358.1; -. [Q9NYB9-2] DR CCDS; CCDS63093.1; -. [Q9NYB9-1] DR CCDS; CCDS63094.1; -. [Q9NYB9-4] DR PIR; G01936; G01936. DR RefSeq; NP_001269854.1; NM_001282925.1. DR RefSeq; NP_001269855.1; NM_001282926.1. DR RefSeq; NP_001269856.1; NM_001282927.1. [Q9NYB9-3] DR RefSeq; NP_005750.4; NM_005759.5. [Q9NYB9-2] DR RefSeq; XP_006712248.1; XM_006712185.1. DR PDB; 2ED0; NMR; -; A=444-508. DR PDB; 3P8C; X-ray; 2.29 A; F=1-154. DR PDB; 4N78; X-ray; 2.43 A; F=1-513. DR PDB; 7USC; EM; 3.00 A; E=1-154. DR PDB; 7USD; EM; 3.00 A; E=1-154. DR PDB; 7USE; EM; 3.00 A; E=1-154. DR PDBsum; 2ED0; -. DR PDBsum; 3P8C; -. DR PDBsum; 4N78; -. DR PDBsum; 7USC; -. DR PDBsum; 7USD; -. DR PDBsum; 7USE; -. DR AlphaFoldDB; Q9NYB9; -. DR BMRB; Q9NYB9; -. DR SMR; Q9NYB9; -. DR BioGRID; 115454; 294. DR DIP; DIP-37566N; -. DR IntAct; Q9NYB9; 245. DR MINT; Q9NYB9; -. DR STRING; 9606.ENSP00000295851; -. DR MoonDB; Q9NYB9; Predicted. DR GlyGen; Q9NYB9; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; Q9NYB9; -. DR PhosphoSitePlus; Q9NYB9; -. DR BioMuta; ABI2; -. DR DMDM; 50400673; -. DR CPTAC; CPTAC-1593; -. DR EPD; Q9NYB9; -. DR jPOST; Q9NYB9; -. DR MassIVE; Q9NYB9; -. DR MaxQB; Q9NYB9; -. DR PaxDb; 9606-ENSP00000295851; -. DR PeptideAtlas; Q9NYB9; -. DR ProteomicsDB; 83209; -. [Q9NYB9-1] DR ProteomicsDB; 83210; -. [Q9NYB9-2] DR ProteomicsDB; 83211; -. [Q9NYB9-3] DR ProteomicsDB; 83212; -. [Q9NYB9-4] DR Pumba; Q9NYB9; -. DR Antibodypedia; 34165; 263 antibodies from 31 providers. DR DNASU; 10152; -. DR Ensembl; ENST00000261017.9; ENSP00000261017.5; ENSG00000138443.17. [Q9NYB9-2] DR GeneID; 10152; -. DR KEGG; hsa:10152; -. DR UCSC; uc002uzz.5; human. [Q9NYB9-1] DR AGR; HGNC:24011; -. DR CTD; 10152; -. DR DisGeNET; 10152; -. DR GeneCards; ABI2; -. DR HGNC; HGNC:24011; ABI2. DR HPA; ENSG00000138443; Low tissue specificity. DR MIM; 606442; gene. DR neXtProt; NX_Q9NYB9; -. DR OpenTargets; ENSG00000138443; -. DR PharmGKB; PA134977642; -. DR VEuPathDB; HostDB:ENSG00000138443; -. DR eggNOG; KOG2546; Eukaryota. DR GeneTree; ENSGT00940000156089; -. DR InParanoid; Q9NYB9; -. DR OrthoDB; 3028771at2759; -. DR PhylomeDB; Q9NYB9; -. DR TreeFam; TF314303; -. DR PathwayCommons; Q9NYB9; -. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis. DR SignaLink; Q9NYB9; -. DR SIGNOR; Q9NYB9; -. DR BioGRID-ORCS; 10152; 10 hits in 1158 CRISPR screens. DR ChiTaRS; ABI2; human. DR EvolutionaryTrace; Q9NYB9; -. DR GeneWiki; ABI2; -. DR GenomeRNAi; 10152; -. DR Pharos; Q9NYB9; Tbio. DR PRO; PR:Q9NYB9; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9NYB9; Protein. DR Bgee; ENSG00000138443; Expressed in Brodmann (1909) area 23 and 194 other cell types or tissues. DR ExpressionAtlas; Q9NYB9; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB. DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0031209; C:SCAR complex; IDA:UniProtKB. DR GO; GO:0008093; F:cytoskeletal anchor activity; TAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019900; F:kinase binding; NAS:UniProtKB. DR GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB. DR GO; GO:0035591; F:signaling adaptor activity; IDA:ARUK-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL. DR GO; GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB. DR GO; GO:0016477; P:cell migration; TAS:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB. DR GO; GO:0070309; P:lens fiber cell morphogenesis; ISS:UniProtKB. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB. DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:ARUK-UCL. DR GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProtKB. DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB. DR GO; GO:0045186; P:zonula adherens assembly; IMP:UniProtKB. DR CDD; cd11972; SH3_Abi2; 1. DR DisProt; DP02386; -. DR Gene3D; 6.10.140.1620; -; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR028457; ABI. DR InterPro; IPR035726; Abi2_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:SF26; ABL INTERACTOR 2; 1. DR PANTHER; PTHR10460; ABL INTERACTOR FAMILY MEMBER; 1. DR Pfam; PF07815; Abi_HHR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01217; PRICHEXTENSN. 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; Q9NYB9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell projection; KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; KW Host-virus interaction; Intellectual disability; Neurogenesis; Nucleus; KW Phosphoprotein; Reference proteome; SH3 domain. FT CHAIN 1..513 FT /note="Abl interactor 2" FT /id="PRO_0000191790" FT DOMAIN 45..107 FT /note="t-SNARE coiled-coil homology" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202" FT DOMAIN 451..510 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 167..431 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..265 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..290 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..396 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 397..420 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62484" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 361 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P62484" FT MOD_RES 368 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..45 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7590236" FT /id="VSP_010759" FT VAR_SEQ 46..95 FT /note="ALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRMESSINHISQ FT -> MSCRCWISRHPSYEGWNLQSIIFHKQIRGVDLESTFVTKFGNNCSLRLNE (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:7590236" FT /id="VSP_010760" FT VAR_SEQ 154..159 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7590236, FT ECO:0000303|PubMed:8649853, ECO:0000303|Ref.2, FT ECO:0000303|Ref.4" FT /id="VSP_010761" FT VAR_SEQ 284..344 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7590236, ECO:0000303|PubMed:8649853, FT ECO:0000303|Ref.2, ECO:0000303|Ref.4" FT /id="VSP_010762" FT VAR_SEQ 399 FT /note="S -> SLAPPPPSILQVTPQLPLMGFVARVQENIS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8649853, ECO:0000303|Ref.2, FT ECO:0000303|Ref.4" FT /id="VSP_010763" FT VARIANT 132..513 FT /note="Missing (found in a consanguineous family with FT intellectual disability; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:28397838" FT /id="VAR_080776" FT CONFLICT 22 FT /note="S -> R (in Ref. 3; CAA64885)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="A -> D (in Ref. 3; CAA64885)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="S -> T (in Ref. 2; AAA75446)" FT /evidence="ECO:0000305" FT CONFLICT 249 FT /note="G -> P (in Ref. 1; AAA92289)" FT /evidence="ECO:0000305" FT CONFLICT 317 FT /note="N -> D (in Ref. 5; BAG61693)" FT /evidence="ECO:0000305" FT CONFLICT 324..325 FT /note="PN -> QT (in Ref. 5; BAG61693)" FT /evidence="ECO:0000305" FT CONFLICT 432 FT /note="A -> V (in Ref. 2; AAA75446)" FT /evidence="ECO:0000305" FT CONFLICT 500 FT /note="F -> S (in Ref. 2; AAA75446)" FT /evidence="ECO:0000305" FT HELIX 1..9 FT /evidence="ECO:0007829|PDB:3P8C" FT HELIX 11..39 FT /evidence="ECO:0007829|PDB:3P8C" FT HELIX 43..110 FT /evidence="ECO:0007829|PDB:3P8C" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:3P8C" FT TURN 143..151 FT /evidence="ECO:0007829|PDB:3P8C" FT STRAND 453..458 FT /evidence="ECO:0007829|PDB:2ED0" FT STRAND 477..483 FT /evidence="ECO:0007829|PDB:2ED0" FT STRAND 485..493 FT /evidence="ECO:0007829|PDB:2ED0" FT STRAND 496..501 FT /evidence="ECO:0007829|PDB:2ED0" FT STRAND 504..507 FT /evidence="ECO:0007829|PDB:2ED0" SQ SEQUENCE 513 AA; 55663 MW; 822983A69E5EA512 CRC64; MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET KAYTTQSLAS VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK PPSPPMSGKG TLGRHSPYRT LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT YSSSGSSGGS HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF YSMNRPASRH TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD TPPPPPPVEE PVFDESPPPP PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV IKKNDDGWYE GVMNGVTGLF PGNYVESIMH YSE //