ABI1_HUMAN
ID ABI1_HUMAN Reviewed; 508 AA.
AC Q8IZP0; A9Z1Y6; B3KX62; B4DQ58; H7BXI6; O15147; O76049; O95060; Q5T2R3;
AC Q5T2R4; Q5T2R6; Q5T2R7; Q5T2R9; Q5W070; Q5W072; Q8TB63; Q96S81; Q9NXZ9;
AC Q9NYB8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Abl interactor 1;
DE AltName: Full=Abelson interactor 1;
DE Short=Abi-1;
DE AltName: Full=Abl-binding protein 4;
DE Short=AblBP4;
DE AltName: Full=Eps8 SH3 domain-binding protein;
DE Short=Eps8-binding protein;
DE AltName: Full=Nap1-binding protein;
DE Short=Nap1BP;
DE AltName: Full=Spectrin SH3 domain-binding protein 1;
DE AltName: Full=e3B1;
GN Name=ABI1 {ECO:0000312|HGNC:HGNC:11320}; Synonyms=SSH3BP1;
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 6), PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH EPS8 AND ABL1.
RX PubMed=9010225; DOI=10.1038/sj.onc.1200822;
RA Biesova Z., Piccoli C., Wong W.T.;
RT "Isolation and characterization of e3B1, an eps8 binding protein that
RT regulates cell growth.";
RL Oncogene 14:233-241(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 3;
RP 7; 8 AND 9), AND INTERACTION WITH SPTA1.
RX PubMed=9593709; DOI=10.1074/jbc.273.22.13681;
RA Ziemnicka-Kotula D., Xu J., Gu H., Potempska A., Kim K.S., Jenkins E.C.,
RA Trenkner E., Kotula L.;
RT "Identification of a candidate human spectrin Src homology 3 domain-binding
RT protein suggests a general mechanism of association of tyrosine kinases
RT with the spectrin-based membrane skeleton.";
RL J. Biol. Chem. 273:13681-13692(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND INTERACTION
RP WITH ABL1; NAP1 AND NCK1.
RX PubMed=11418237; DOI=10.1016/s0378-1119(01)00521-2;
RA Yamamoto A., Suzuki T., Sakaki Y.;
RT "Isolation of hNap1BP which interacts with human Nap 1 (NCKAP1) whose
RT expression is down-regulated in Alzheimer's disease.";
RL Gene 271:159-169(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH NCF1.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=12681507; DOI=10.1016/s0014-5793(03)00262-x;
RA Gu Y., Souza R.F., Wu R.F., Xu Y.C., Terada L.S.;
RT "Induction of colonic epithelial cell apoptosis by p47-dependent
RT oxidants(1).";
RL FEBS Lett. 540:195-200(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=T-cell;
RA Wilson L.A., Fields D., Cruz L., Friesen J., Siminovitch K.A.;
RT "A new member of the Abl interactor protein family, AblBP4.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chikri M.M., Boutin M.P., Vaxillaire M.M., Froguel M.P.;
RT "In silico cloning of the human SSH3BP1/e3B1 gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Quackenbush R.C., Pendergast A.M.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 11 AND 12).
RC TISSUE=Cerebellum;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Muscle;
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 [12]
RP PROTEIN SEQUENCE OF 2-17.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [13]
RP PROTEIN SEQUENCE OF 2-17; 139-154; 229-237 AND 451-477, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [14]
RP FUNCTION, AND INTERACTION WITH SOS1; SOS2 AND GRB2.
RX PubMed=11003655; DOI=10.1128/mcb.20.20.7591-7601.2000;
RA Fan P.-D., Goff S.P.;
RT "Abl interactor 1 binds to sos and inhibits epidermal growth factor- and v-
RT Abl-induced activation of extracellular signal-regulated kinases.";
RL Mol. Cell. Biol. 20:7591-7601(2000).
RN [15]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 10), AND CHROMOSOMAL TRANSLOCATION
RP WITH KMT2A.
RX PubMed=9694699;
RA Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F.,
RA Yanagisawa M., Hayashi Y.;
RT "ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in
RT acute myeloid leukemia with t(10;11)(p11.2;q23).";
RL Blood 92:1125-1130(1998).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP IDENTIFICATION IN THE WAVE2 COMPLEX.
RX PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
RA Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M., Yaffe M.B.,
RA Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
RT "Hem-1 complexes are essential for Rac activation, actin polymerization,
RT and myosin regulation during neutrophil chemotaxis.";
RL PLoS Biol. 4:E38-E38(2006).
RN [18]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-213.
RX PubMed=18328268; DOI=10.1016/j.bbamcr.2008.01.028;
RA Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X.,
RA Debnath A.K., Cowburn D., Kotula L.;
RT "Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by
RT phosphopeptides derived from Abi1/Hssh3bp1.";
RL Biochim. Biophys. Acta 1783:737-747(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-216, AND
RP IDENTIFICATION BY 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 [22]
RP INTERACTION WITH FNBP1L; WASF2 AND CDC42.
RX PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
RA Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A., Malabarba M.G.,
RA Disanza A., Stradal T.B., Cassata G., Confalonieri S., Hardin J.D.,
RA Soto M.C., Grant B.D., Scita G.;
RT "Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and
RT membrane trafficking during Caenorhabditis elegans oocyte growth and
RT embryonic epidermal morphogenesis.";
RL PLoS Genet. 5:E1000675-E1000675(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND THR-507, 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-225 AND SER-323, AND
RP IDENTIFICATION BY 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 [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; TYR-213; SER-225;
RP SER-319 AND SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; THR-178; SER-183;
RP SER-187; SER-222 AND SER-225, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May act in negative regulation of cell growth and
CC transformation by interacting with nonreceptor tyrosine kinases ABL1
CC and/or ABL2. May play a role in regulation of EGF-induced Erk pathway
CC activation. Involved in cytoskeletal reorganization and EGFR signaling.
CC Together with EPS8 participates in transduction of signals from Ras to
CC Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac
CC specific guanine nucleotide exchange factor (GEF) activity and ABI1
CC seems to act as an adapter in the complex. Regulates ABL1/c-Abl-
CC mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and
CC there seems to regulate WASF1 protein level. In brain, seems to
CC regulate the dendritic outgrowth and branching as well as to determine
CC the shape and number of synaptic contacts of developing neurons.
CC {ECO:0000269|PubMed:11003655, ECO:0000269|PubMed:18328268}.
CC -!- SUBUNIT: Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8, and
CC through its N-terminus with WASF1. Part of a complex consisting of
CC ABI1, STX1A and SNAP25. Part of a complex consisting of ABI1, EPS8 and
CC SOS1 (By similarity). Interacts with SOS1, SOS2, GRB2, SPTA1 and the
CC first SH3 domain of NCK1. Isoform 6 does not interact with NCK1.
CC Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1,
CC NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells) and WASF2/WAVE2
CC (PubMed:16417406). Interacts (via SH3 domain) with SHANK2 and SHANK3,
CC but not SHANK1; the interaction is direct. Interacts with the
CC heterodimer MYC:MAX; the interaction may enhance MYC:MAX
CC transcriptional activity. Interacts with FNBP1L (via the SH3 domain),
CC WASF2, and CDC42, but only in the presence of FNBP1L (PubMed:19798448).
CC {ECO:0000250, ECO:0000269|PubMed:11003655, ECO:0000269|PubMed:11418237,
CC ECO:0000269|PubMed:12681507, ECO:0000269|PubMed:16417406,
CC ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:9010225,
CC ECO:0000269|PubMed:9593709}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 protein UL135. {ECO:0000269|PubMed:25121749}.
CC -!- INTERACTION:
CC Q8IZP0; P00519: ABL1; NbExp=11; IntAct=EBI-375446, EBI-375543;
CC Q8IZP0; P42684: ABL2; NbExp=2; IntAct=EBI-375446, EBI-1102694;
CC Q8IZP0; O00555: CACNA1A; NbExp=2; IntAct=EBI-375446, EBI-766279;
CC Q8IZP0; Q13191: CBLB; NbExp=2; IntAct=EBI-375446, EBI-744027;
CC Q8IZP0; P14598: NCF1; NbExp=5; IntAct=EBI-375446, EBI-395044;
CC Q8IZP0; Q9Y2A7: NCKAP1; NbExp=5; IntAct=EBI-375446, EBI-389845;
CC Q8IZP0; P27986: PIK3R1; NbExp=8; IntAct=EBI-375446, EBI-79464;
CC Q8IZP0; Q92569: PIK3R3; NbExp=2; IntAct=EBI-375446, EBI-79893;
CC Q8IZP0; P20936: RASA1; NbExp=2; IntAct=EBI-375446, EBI-1026476;
CC Q8IZP0; O14512: SOCS7; NbExp=2; IntAct=EBI-375446, EBI-1539606;
CC Q8IZP0; P02549: SPTA1; NbExp=2; IntAct=EBI-375446, EBI-375617;
CC Q8IZP0; P15498: VAV1; NbExp=2; IntAct=EBI-375446, EBI-625518;
CC Q8IZP0; P52735: VAV2; NbExp=2; IntAct=EBI-375446, EBI-297549;
CC Q8IZP0; Q08509: Eps8; Xeno; NbExp=2; IntAct=EBI-375446, EBI-375596;
CC Q8IZP0; P26450: Pik3r1; Xeno; NbExp=3; IntAct=EBI-375446, EBI-641764;
CC Q8IZP0-2; P22681: CBL; NbExp=3; IntAct=EBI-7358775, EBI-518228;
CC Q8IZP0-2; P13612: ITGA4; NbExp=2; IntAct=EBI-7358775, EBI-703044;
CC Q8IZP0-4; P00520-4: Abl1; Xeno; NbExp=5; IntAct=EBI-8593095, EBI-8593082;
CC Q8IZP0-5; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11743294, EBI-11096309;
CC Q8IZP0-5; Q8WYQ4-2: C22orf15; NbExp=3; IntAct=EBI-11743294, EBI-12030460;
CC Q8IZP0-5; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-11743294, EBI-10961624;
CC Q8IZP0-5; Q8TD31-3: CCHCR1; NbExp=5; IntAct=EBI-11743294, EBI-10175300;
CC Q8IZP0-5; O60941-5: DTNB; NbExp=3; IntAct=EBI-11743294, EBI-11984733;
CC Q8IZP0-5; O15372: EIF3H; NbExp=3; IntAct=EBI-11743294, EBI-709735;
CC Q8IZP0-5; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-11743294, EBI-744099;
CC Q8IZP0-5; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-11743294, EBI-11986315;
CC Q8IZP0-5; Q6PCT2-2: FBXL19; NbExp=3; IntAct=EBI-11743294, EBI-11959077;
CC Q8IZP0-5; Q14192: FHL2; NbExp=3; IntAct=EBI-11743294, EBI-701903;
CC Q8IZP0-5; Q03014: HHEX; NbExp=3; IntAct=EBI-11743294, EBI-747421;
CC Q8IZP0-5; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-11743294, EBI-7060731;
CC Q8IZP0-5; Q86YM7: HOMER1; NbExp=3; IntAct=EBI-11743294, EBI-746815;
CC Q8IZP0-5; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11743294, EBI-748420;
CC Q8IZP0-5; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-11743294, EBI-10188326;
CC Q8IZP0-5; P25800: LMO1; NbExp=3; IntAct=EBI-11743294, EBI-8639312;
CC Q8IZP0-5; Q9Y586: MAB21L2; NbExp=3; IntAct=EBI-11743294, EBI-6659161;
CC Q8IZP0-5; O94856-3: NFASC; NbExp=3; IntAct=EBI-11743294, EBI-12035911;
CC Q8IZP0-5; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-11743294, EBI-2859639;
CC Q8IZP0-5; P54646: PRKAA2; NbExp=3; IntAct=EBI-11743294, EBI-1383852;
CC Q8IZP0-5; Q96T37-3: RBM15; NbExp=3; IntAct=EBI-11743294, EBI-12041043;
CC Q8IZP0-5; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-11743294, EBI-1504830;
CC Q8IZP0-5; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-11743294, EBI-358489;
CC Q8IZP0-5; O94875-10: SORBS2; NbExp=3; IntAct=EBI-11743294, EBI-12037893;
CC Q8IZP0-5; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-11743294, EBI-6550597;
CC Q8IZP0-5; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-11743294, EBI-9090990;
CC Q8IZP0-5; Q5ST30: VARS2; NbExp=3; IntAct=EBI-11743294, EBI-2116622;
CC Q8IZP0-5; P50552: VASP; NbExp=3; IntAct=EBI-11743294, EBI-748201;
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=12;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q8IZP0-1; Sequence=Displayed;
CC Name=2; Synonyms=long, B48;
CC IsoId=Q8IZP0-2; Sequence=VSP_010749, VSP_010750, VSP_010751,
CC VSP_010752;
CC Name=3;
CC IsoId=Q8IZP0-3; Sequence=VSP_010750, VSP_010752;
CC Name=4;
CC IsoId=Q8IZP0-4; Sequence=VSP_010750, VSP_010751, VSP_010752;
CC Name=5;
CC IsoId=Q8IZP0-5; Sequence=VSP_010749, VSP_010750;
CC Name=6;
CC IsoId=Q8IZP0-6; Sequence=VSP_010750, VSP_010751;
CC Name=7; Synonyms=4;
CC IsoId=Q8IZP0-7; Sequence=VSP_010750, VSP_010751, VSP_010754,
CC VSP_010755;
CC Name=8; Synonyms=5;
CC IsoId=Q8IZP0-8; Sequence=VSP_010750, VSP_010751, VSP_010754,
CC VSP_010752;
CC Name=9; Synonyms=2;
CC IsoId=Q8IZP0-9; Sequence=VSP_010750;
CC Name=10; Synonyms=B30;
CC IsoId=Q8IZP0-10; Sequence=VSP_010749, VSP_010750, VSP_010751,
CC VSP_010754, VSP_010752, VSP_010753;
CC Name=11;
CC IsoId=Q8IZP0-11; Sequence=VSP_043403, VSP_010750, VSP_010751,
CC VSP_010754, VSP_010752, VSP_010753;
CC Name=12;
CC IsoId=Q8IZP0-12; Sequence=VSP_044604, VSP_010752;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
CC {ECO:0000269|PubMed:11418237}.
CC -!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and
CC sufficient for interaction with STX1A. {ECO:0000250}.
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.
CC {ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:9010225}.
CC -!- DISEASE: Note=A chromosomal aberration involving ABI1 is a cause of
CC acute leukemias. Translocation t(10;11)(p11.2;q23) with KMT2A/MLL1.
CC ABI1 isoform 2 was found to be present in acute leukemia KMT2A/MLL1-
CC ABI1 fusion transcript. {ECO:0000269|PubMed:9694699}.
CC -!- SIMILARITY: Belongs to the ABI family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ABI1ID233.html";
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DR EMBL; AF006516; AAB62569.1; -; mRNA.
DR EMBL; U87166; AAC39757.1; -; mRNA.
DR EMBL; AB040151; BAB55675.1; -; mRNA.
DR EMBL; AF540955; AAN28379.1; -; mRNA.
DR EMBL; AF001628; AAD00897.1; -; mRNA.
DR EMBL; AJ277065; CAB88006.1; -; Genomic_DNA.
DR EMBL; AJ277066; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277067; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277068; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277069; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277070; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277071; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277072; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277073; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AJ277074; CAB88006.1; JOINED; Genomic_DNA.
DR EMBL; AF260262; AAF70309.1; -; mRNA.
DR EMBL; AK126803; BAG54374.1; -; mRNA.
DR EMBL; AK298646; BAG60820.1; -; mRNA.
DR EMBL; AK291823; BAF84512.1; -; mRNA.
DR EMBL; AL139404; CAH73112.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73112.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73113.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73113.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73114.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73114.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73115.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73115.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73116.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73116.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73117.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73117.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73118.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73118.1; JOINED; Genomic_DNA.
DR EMBL; AL139404; CAH73119.1; -; Genomic_DNA.
DR EMBL; AL390961; CAH73119.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17272.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17272.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17273.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17273.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17274.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17274.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17275.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17275.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17276.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17276.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17277.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17277.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17278.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17278.1; JOINED; Genomic_DNA.
DR EMBL; AL390961; CAI17279.1; -; Genomic_DNA.
DR EMBL; AL139404; CAI17279.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW86079.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86080.1; -; Genomic_DNA.
DR EMBL; BC024254; AAH24254.1; -; mRNA.
DR CCDS; CCDS31169.1; -. [Q8IZP0-5]
DR CCDS; CCDS31170.1; -. [Q8IZP0-3]
DR CCDS; CCDS31171.1; -. [Q8IZP0-9]
DR CCDS; CCDS53497.1; -. [Q8IZP0-11]
DR CCDS; CCDS53498.1; -. [Q8IZP0-2]
DR CCDS; CCDS53499.1; -. [Q8IZP0-4]
DR CCDS; CCDS53500.1; -. [Q8IZP0-6]
DR CCDS; CCDS53501.1; -. [Q8IZP0-12]
DR CCDS; CCDS7150.1; -. [Q8IZP0-1]
DR CCDS; CCDS73077.1; -. [Q8IZP0-8]
DR CCDS; CCDS73078.1; -. [Q8IZP0-7]
DR RefSeq; NP_001012768.1; NM_001012750.2. [Q8IZP0-9]
DR RefSeq; NP_001012769.1; NM_001012751.2. [Q8IZP0-3]
DR RefSeq; NP_001012770.1; NM_001012752.2. [Q8IZP0-5]
DR RefSeq; NP_001171587.1; NM_001178116.1. [Q8IZP0-12]
DR RefSeq; NP_001171590.1; NM_001178119.1. [Q8IZP0-6]
DR RefSeq; NP_001171591.1; NM_001178120.1. [Q8IZP0-4]
DR RefSeq; NP_001171592.1; NM_001178121.1. [Q8IZP0-2]
DR RefSeq; NP_001171593.1; NM_001178122.1. [Q8IZP0-7]
DR RefSeq; NP_001171594.1; NM_001178123.1.
DR RefSeq; NP_001171595.1; NM_001178124.1. [Q8IZP0-10]
DR RefSeq; NP_001171596.1; NM_001178125.1. [Q8IZP0-11]
DR RefSeq; NP_005461.2; NM_005470.3. [Q8IZP0-1]
DR AlphaFoldDB; Q8IZP0; -.
DR SMR; Q8IZP0; -.
DR BioGRID; 115324; 189.
DR CORUM; Q8IZP0; -.
DR DIP; DIP-31118N; -.
DR ELM; Q8IZP0; -.
DR IntAct; Q8IZP0; 160.
DR MINT; Q8IZP0; -.
DR STRING; 9606.ENSP00000365312; -.
DR GlyGen; Q8IZP0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZP0; -.
DR PhosphoSitePlus; Q8IZP0; -.
DR BioMuta; ABI1; -.
DR DMDM; 50400546; -.
DR EPD; Q8IZP0; -.
DR jPOST; Q8IZP0; -.
DR MassIVE; Q8IZP0; -.
DR MaxQB; Q8IZP0; -.
DR PaxDb; Q8IZP0; -.
DR PeptideAtlas; Q8IZP0; -.
DR PRIDE; Q8IZP0; -.
DR ProteomicsDB; 43294; -.
DR ProteomicsDB; 71380; -. [Q8IZP0-1]
DR ProteomicsDB; 71381; -. [Q8IZP0-10]
DR ProteomicsDB; 71382; -. [Q8IZP0-11]
DR ProteomicsDB; 71383; -. [Q8IZP0-2]
DR ProteomicsDB; 71384; -. [Q8IZP0-3]
DR ProteomicsDB; 71385; -. [Q8IZP0-4]
DR ProteomicsDB; 71386; -. [Q8IZP0-5]
DR ProteomicsDB; 71387; -. [Q8IZP0-6]
DR ProteomicsDB; 71388; -. [Q8IZP0-7]
DR ProteomicsDB; 71389; -. [Q8IZP0-8]
DR ProteomicsDB; 71390; -. [Q8IZP0-9]
DR Antibodypedia; 3646; 363 antibodies from 40 providers.
DR DNASU; 10006; -.
DR Ensembl; ENST00000346832.10; ENSP00000279599.8; ENSG00000136754.18. [Q8IZP0-12]
DR Ensembl; ENST00000359188.8; ENSP00000352114.4; ENSG00000136754.18. [Q8IZP0-6]
DR Ensembl; ENST00000376137.8; ENSP00000365307.5; ENSG00000136754.18. [Q8IZP0-7]
DR Ensembl; ENST00000376138.7; ENSP00000365308.3; ENSG00000136754.18. [Q8IZP0-3]
DR Ensembl; ENST00000376139.6; ENSP00000365309.2; ENSG00000136754.18. [Q8IZP0-5]
DR Ensembl; ENST00000376140.4; ENSP00000365310.3; ENSG00000136754.18. [Q8IZP0-9]
DR Ensembl; ENST00000376142.6; ENSP00000365312.2; ENSG00000136754.18. [Q8IZP0-1]
DR Ensembl; ENST00000376166.5; ENSP00000365336.1; ENSG00000136754.18. [Q8IZP0-2]
DR Ensembl; ENST00000376170.8; ENSP00000365340.4; ENSG00000136754.18. [Q8IZP0-4]
DR Ensembl; ENST00000490841.6; ENSP00000440101.1; ENSG00000136754.18. [Q8IZP0-11]
DR GeneID; 10006; -.
DR KEGG; hsa:10006; -.
DR MANE-Select; ENST00000376140.4; ENSP00000365310.3; NM_001012750.3; NP_001012768.1. [Q8IZP0-9]
DR UCSC; uc001isx.4; human. [Q8IZP0-1]
DR CTD; 10006; -.
DR DisGeNET; 10006; -.
DR GeneCards; ABI1; -.
DR HGNC; HGNC:11320; ABI1.
DR HPA; ENSG00000136754; Low tissue specificity.
DR MIM; 603050; gene.
DR neXtProt; NX_Q8IZP0; -.
DR OpenTargets; ENSG00000136754; -.
DR PharmGKB; PA36144; -.
DR VEuPathDB; HostDB:ENSG00000136754; -.
DR eggNOG; KOG2546; Eukaryota.
DR GeneTree; ENSGT00940000154811; -.
DR InParanoid; Q8IZP0; -.
DR OMA; VGHGVKE; -.
DR OrthoDB; 1478981at2759; -.
DR PhylomeDB; Q8IZP0; -.
DR TreeFam; TF314303; -.
DR PathwayCommons; Q8IZP0; -.
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; Q8IZP0; -.
DR SIGNOR; Q8IZP0; -.
DR BioGRID-ORCS; 10006; 36 hits in 1085 CRISPR screens.
DR ChiTaRS; ABI1; human.
DR GeneWiki; ABI1; -.
DR GenomeRNAi; 10006; -.
DR Pharos; Q8IZP0; Tbio.
DR PRO; PR:Q8IZP0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IZP0; protein.
DR Bgee; ENSG00000136754; Expressed in epithelium of nasopharynx and 204 other tissues.
DR ExpressionAtlas; Q8IZP0; baseline and differential.
DR Genevisible; Q8IZP0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISS:ARUK-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:ARUK-UCL.
DR GO; GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR CDD; cd11971; SH3_Abi1; 1.
DR InterPro; IPR028457; ABI.
DR InterPro; IPR028456; ABI1.
DR InterPro; IPR035725; Abi1_SH3.
DR InterPro; IPR012849; Abl-interactor_HHR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR10460; PTHR10460; 1.
DR PANTHER; PTHR10460:SF2; PTHR10460:SF2; 1.
DR Pfam; PF07815; Abi_HHR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection;
KW Chromosomal rearrangement; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.13,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..508
FT /note="Abl interactor 1"
FT /id="PRO_0000191787"
FT DOMAIN 45..107
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 446..505
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 18..79
FT /note="Required for binding to WASF1"
FT /evidence="ECO:0000250"
FT REGION 159..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..421
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 262..290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 95..96
FT /note="Breakpoint for translocation to form KMT2A/MLL1-
FT ABI1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZM5"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 213
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:18328268,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBW3"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBW3"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZM5"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 38
FT /note="I -> IQRHGFAVLLCLLSNSWP (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044604"
FT VAR_SEQ 96..159
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043403"
FT VAR_SEQ 154..158
FT /note="Missing (in isoform 2, isoform 5 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:12681507,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.7"
FT /id="VSP_010749"
FT VAR_SEQ 274..300
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10
FT and isoform 11)"
FT /evidence="ECO:0000303|PubMed:11418237,
FT ECO:0000303|PubMed:12681507, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9010225,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.7"
FT /id="VSP_010750"
FT VAR_SEQ 301
FT /note="Missing (in isoform 2, isoform 4, isoform 6, isoform
FT 7, isoform 8, isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:12681507,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9010225, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.7"
FT /id="VSP_010751"
FT VAR_SEQ 302..359
FT /note="Missing (in isoform 7, isoform 8, isoform 10 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:12681507,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.5"
FT /id="VSP_010754"
FT VAR_SEQ 360..388
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 8, isoform 10, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:11418237,
FT ECO:0000303|PubMed:12681507, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.7"
FT /id="VSP_010752"
FT VAR_SEQ 360
FT /note="I -> V (in isoform 7)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_010755"
FT VAR_SEQ 389
FT /note="I -> V (in isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010753"
FT VARIANT 331
FT /note="G -> A (in dbSNP:rs2306236)"
FT /id="VAR_048159"
FT CONFLICT 177
FT /note="P -> L (in Ref. 2; AAC39757)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="S -> F (in Ref. 2; AAC39757 and 4; AAN28379)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="D -> G (in Ref. 8; BAG54374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 55081 MW; 2D76F305934127CB CRC64;
MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK
PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS
GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPENISVPP PSGAPPAPPL APLLPVSTVI
AAPGSAPGSQ YGTMTRQISR HNSTTSSTSS GGYRRTPSVT AQFSAQPHVN GGPLYSQNSI
SIAPPPPPMP QLTPQIPLTG FVARVQENIA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD
YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFMEG AIIYVIKKND
DGWYEGVCNR VTGLFPGNYV ESIMHYTD
