ABI2_HUMAN
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 03-AUG-2022, entry version 189.
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 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; 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; 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; Q5BKX5-3: C19orf54; NbExp=5; IntAct=EBI-11096309, EBI-11976299;
CC Q9NYB9-2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-11096309, EBI-8643161;
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; 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; A8MTA8-2: FAM166B; NbExp=3; IntAct=EBI-11096309, EBI-12160437;
CC Q9NYB9-2; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-11096309, EBI-745689;
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}.
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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 PDBsum; 2ED0; -.
DR PDBsum; 3P8C; -.
DR PDBsum; 4N78; -.
DR AlphaFoldDB; Q9NYB9; -.
DR BMRB; Q9NYB9; -.
DR SMR; Q9NYB9; -.
DR BioGRID; 115454; 285.
DR DIP; DIP-37566N; -.
DR IntAct; Q9NYB9; 241.
DR MINT; Q9NYB9; -.
DR STRING; 9606.ENSP00000295851; -.
DR MoonDB; Q9NYB9; Predicted.
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 PeptideAtlas; Q9NYB9; -.
DR PRIDE; Q9NYB9; -.
DR ProteomicsDB; 83209; -. [Q9NYB9-1]
DR ProteomicsDB; 83210; -. [Q9NYB9-2]
DR ProteomicsDB; 83211; -. [Q9NYB9-3]
DR ProteomicsDB; 83212; -. [Q9NYB9-4]
DR Antibodypedia; 34165; 231 antibodies from 30 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 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; 1478981at2759; -.
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 1081 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 192 other tissues.
DR ExpressionAtlas; Q9NYB9; baseline and differential.
DR Genevisible; Q9NYB9; HS.
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:BHF-UCL.
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 InterPro; IPR028457; ABI.
DR InterPro; IPR036993; ABI2.
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; PTHR10460; 2.
DR PANTHER; PTHR10460:SF26; PTHR10460:SF26; 2.
DR Pfam; PF07815; Abi_HHR; 1.
DR Pfam; PF14604; SH3_9; 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 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 (probable disease-associated variant found
FT in a consanguineous family with intellectual disability)"
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
