ABL1_MOUSE
ID ABL1_MOUSE Reviewed; 1123 AA.
AC P00520; P97896; Q61252; Q61253; Q61254; Q61255; Q61256; Q61257; Q61258;
AC Q61259; Q61260; Q61261; Q6PCM5; Q8C1X4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 255.
DE RecName: Full=Tyrosine-protein kinase ABL1;
DE EC=2.7.10.2 {ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:20072125};
DE AltName: Full=Abelson murine leukemia viral oncogene homolog 1;
DE AltName: Full=Abelson tyrosine-protein kinase 1;
DE AltName: Full=Proto-oncogene c-Abl;
DE AltName: Full=p150;
GN Name=Abl1; Synonyms=Abl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
RC TISSUE=Testis;
RX PubMed=3317402; DOI=10.1073/pnas.84.23.8200;
RA Oppi C., Shore S.K., Reddy E.P.;
RT "Nucleotide sequence of testis-derived c-abl cDNAs: implications for
RT testis-specific transcription and abl oncogene activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=ICR; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187 (ISOFORMS I; II; III AND IV).
RX PubMed=7665185; DOI=10.1006/geno.1995.1008;
RA Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D.,
RA Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y.,
RA McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G.,
RA Heisterkamp N., Groffen J., Roe B.A.;
RT "Sequence and analysis of the human ABL gene, the BCR gene, and regions
RT involved in the Philadelphia chromosomal translocation.";
RL Genomics 27:67-82(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-182.
RX PubMed=6319018; DOI=10.1016/0092-8674(84)90228-9;
RA Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.;
RT "The mouse c-abl locus: molecular cloning and characterization.";
RL Cell 36:349-356(1984).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=3283651;
RA Bernards A., Paskind M., Baltimore D.;
RT "Four murine c-abl mRNAs arise by usage of two transcriptional promoters
RT and alternative splicing.";
RL Oncogene 2:297-304(1988).
RN [7]
RP PHOSPHORYLATION AT THR-547 AND SER-569.
RX PubMed=2183353; DOI=10.1126/science.2183353;
RA Kipreos E.T., Wang J.Y.;
RT "Differential phosphorylation of c-Abl in cell cycle determined by cdc2
RT kinase and phosphatase activity.";
RL Science 248:217-220(1990).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=2065352; DOI=10.1016/0092-8674(91)90011-m;
RA Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T., Mulligan R.C.;
RT "Neonatal lethality and lymphopenia in mice with a homozygous disruption of
RT the c-abl proto-oncogene.";
RL Cell 65:1153-1163(1991).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=2065353; DOI=10.1016/0092-8674(91)90012-n;
RA Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T.,
RA Boast S., Harbison M.L., Robertson E.J., Goff S.P.;
RT "Mice homozygous for the ablm1 mutation show poor viability and depletion
RT of selected B and T cell populations.";
RL Cell 65:1165-1175(1991).
RN [10]
RP DNA-BINDING, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=1566087; DOI=10.1126/science.256.5055.382;
RA Kipreos E.T., Wang J.Y.;
RT "Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA.";
RL Science 256:382-385(1992).
RN [11]
RP FUNCTION.
RX PubMed=8194526; DOI=10.1002/j.1460-2075.1994.tb06518.x;
RA Feller S.M., Knudsen B., Hanafusa H.;
RT "c-Abl kinase regulates the protein binding activity of c-Crk.";
RL EMBO J. 13:2341-2351(1994).
RN [12]
RP FUNCTION.
RX PubMed=7780740; DOI=10.1016/s0960-9822(95)00060-1;
RA Mayer B.J., Hirai H., Sakai R.;
RT "Evidence that SH2 domains promote processive phosphorylation by protein-
RT tyrosine kinases.";
RL Curr. Biol. 5:296-305(1995).
RN [13]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-446, AND MUTAGENESIS OF SER-446.
RX PubMed=9109492; DOI=10.1038/386732a0;
RA Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M.,
RA Weichselbaum R., Weaver D., Kufe D.;
RT "Functional interaction between DNA-PK and c-Abl in response to DNA
RT damage.";
RL Nature 386:732-735(1997).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=9636171; DOI=10.1073/pnas.95.13.7457;
RA Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K.,
RA Wang J.Y., Hope T.J.;
RT "Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998).
RN [15]
RP IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, AND
RP INTERACTION WITH CABLES1.
RC TISSUE=Brain;
RX PubMed=10896159; DOI=10.1016/s0896-6273(00)81200-3;
RA Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L.,
RA Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.;
RT "Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation,
RT kinase upregulation, and neurite outgrowth.";
RL Neuron 26:633-646(2000).
RN [16]
RP INTERACTION WITH PSTPIP1.
RX PubMed=11163214; DOI=10.1016/s1097-2765(00)00138-6;
RA Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A.,
RA Goff S.P.;
RT "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine
RT phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.";
RL Mol. Cell 6:1413-1423(2000).
RN [17]
RP REVIEW ON FUNCTION.
RX PubMed=11114745; DOI=10.1038/sj.onc.1203878;
RA Wang J.Y.;
RT "Regulation of cell death by the Abl tyrosine kinase.";
RL Oncogene 19:5643-5650(2000).
RN [18]
RP INTERACTION WITH CRK, AND FUNCTION.
RX PubMed=11279004; DOI=10.1074/jbc.m100095200;
RA Kain K.H., Klemke R.L.;
RT "Inhibition of cell migration by Abl family tyrosine kinases through
RT uncoupling of Crk-CAS complexes.";
RL J. Biol. Chem. 276:16185-16192(2001).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11350980; DOI=10.1074/jbc.m101414200;
RA Kumar S., Bharti A., Mishra N.C., Raina D., Kharbanda S., Saxena S.,
RA Kufe D.;
RT "Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic
RT cell death response to oxidative stress.";
RL J. Biol. Chem. 276:17281-17285(2001).
RN [20]
RP FUNCTION.
RX PubMed=11279131; DOI=10.1074/jbc.m100792200;
RA Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C.,
RA Schettini G., Sudol M., Russo T.;
RT "The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells
RT expressing a constitutively active form of the Abl protoncogene.";
RL J. Biol. Chem. 276:19787-19792(2001).
RN [21]
RP INTERACTION WITH ZDHHC16.
RX PubMed=12021275; DOI=10.1074/jbc.m202388200;
RA Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.;
RT "Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-
RT apoptotic activity.";
RL J. Biol. Chem. 277:28870-28876(2002).
RN [22]
RP FUNCTION.
RX PubMed=12107171; DOI=10.1074/jbc.m204416200;
RA Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.;
RT "Interaction between UV-damaged DNA binding activity proteins and the c-Abl
RT tyrosine kinase.";
RL J. Biol. Chem. 277:34870-34878(2002).
RN [23]
RP REVIEW ON FUNCTION.
RX PubMed=12775773; DOI=10.1242/jcs.00622;
RA Woodring P.J., Hunter T., Wang J.Y.;
RT "Regulation of F-actin-dependent processes by the Abl family of tyrosine
RT kinases.";
RL J. Cell Sci. 116:2613-2626(2003).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, INTERACTION
RP WITH CRK, PHOSPHORYLATION AT TYR-226 AND TYR-393, AND MUTAGENESIS OF
RP TYR-226; LYS-271 AND TYR-393.
RX PubMed=12748290; DOI=10.1128/mcb.23.11.3884-3896.2003;
RA Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
RT "Two distinct phosphorylation pathways have additive effects on Abl family
RT kinase activation.";
RL Mol. Cell. Biol. 23:3884-3896(2003).
RN [25]
RP FUNCTION, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=14993293; DOI=10.1128/mcb.24.6.2573-2583.2004;
RA Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
RT "Bidirectional signaling links the Abelson kinases to the platelet-derived
RT growth factor receptor.";
RL Mol. Cell. Biol. 24:2573-2583(2004).
RN [26]
RP REVIEW ON FUNCTION.
RX PubMed=15686624; DOI=10.1038/sj.cr.7290261;
RA Shaul Y., Ben-Yehoyada M.;
RT "Role of c-Abl in the DNA damage stress response.";
RL Cell Res. 15:33-35(2005).
RN [27]
RP FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION, AND INTERACTION
RP WITH ITGB1; HCK AND FGR.
RX PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
RA Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
RA Berton G.;
RT "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
RT migration.";
RL FEBS Lett. 584:15-21(2010).
RN [28]
RP REVIEW ON FUNCTION, AND DOMAIN.
RX PubMed=20841568; DOI=10.1126/scisignal.3139re6;
RA Colicelli J.;
RT "ABL tyrosine kinases: evolution of function, regulation, and
RT specificity.";
RL Sci. Signal. 3:RE6-RE6(2010).
RN [29]
RP FUNCTION, AND INTERACTION WITH TBX21.
RX PubMed=21690296; DOI=10.1128/mcb.05383-11;
RA Chen A., Lee S.M., Gao B., Shannon S., Zhu Z., Fang D.;
RT "c-Abl-mediated tyrosine phosphorylation of the T-bet DNA-binding domain
RT regulates CD4+ T-cell differentiation and allergic lung inflammation.";
RL Mol. Cell. Biol. 31:3445-3456(2011).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
RX PubMed=7664083; DOI=10.1038/nsb0894-546;
RA Musacchio A., Saraste M., Wilmanns M.;
RT "High-resolution crystal structures of tyrosine kinase SH3 domains
RT complexed with proline-rich peptides.";
RL Nat. Struct. Biol. 1:546-551(1994).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515 IN COMPLEX WITH INHIBITOR
RP STI-571, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT
RP TYR-393, AND ACTIVATION LOOP.
RX PubMed=10988075; DOI=10.1126/science.289.5486.1938;
RA Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B.,
RA Kuriyan J.;
RT "Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase.";
RL Science 289:1938-1942(2000).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-515, MYRISTOYLATION AT GLY-2
RP (ISOFORM IV), AND ACTIVITY REGULATION.
RX PubMed=12654251; DOI=10.1016/s0092-8674(03)00194-6;
RA Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D., Bornmann W.,
RA Clarkson B., Superti-Furga G., Kuriyan J.;
RT "Structural basis for the autoinhibition of c-Abl tyrosine kinase.";
RL Cell 112:859-871(2003).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 229-515 OF WILD-TYPE AND MUTANT
RP ILE-315 IN COMPLEX WITH INHIBITOR PPY-A.
RX PubMed=17718712; DOI=10.1111/j.1747-0285.2007.00556.x;
RA Zhou T., Parillon L., Li F., Wang Y., Keats J., Lamore S., Xu Q.,
RA Shakespeare W., Dalgarno D., Zhu X.;
RT "Crystal structure of the T315I mutant of AbI kinase.";
RL Chem. Biol. Drug Des. 70:171-181(2007).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 229-515 OF MUTANT ILE-315 IN
RP COMPLEX WITH INHIBITOR AP24534, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=19878872; DOI=10.1016/j.ccr.2009.09.028;
RA O'Hare T., Shakespeare W.C., Zhu X., Eide C.A., Rivera V.M., Wang F.,
RA Adrian L.T., Zhou T., Huang W.S., Xu Q., Metcalf C.A. III, Tyner J.W.,
RA Loriaux M.M., Corbin A.S., Wardwell S., Ning Y., Keats J.A., Wang Y.,
RA Sundaramoorthi R., Thomas M., Zhou D., Snodgrass J., Commodore L.,
RA Sawyer T.K., Dalgarno D.C., Deininger M.W., Druker B.J., Clackson T.;
RT "AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently
RT inhibits the T315I mutant and overcomes mutation-based resistance.";
RL Cancer Cell 16:401-412(2009).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 115-401 IN COMPLEXES WITH
RP INHIBITORS AP24283 AND AP24163.
RX PubMed=19895503; DOI=10.1111/j.1747-0285.2009.00905.x;
RA Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K., Shakespeare W.C.,
RA Clackson T., Zhu X., Dalgarno D.C.;
RT "Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors sharing
RT a common vinyl purine template.";
RL Chem. Biol. Drug Des. 75:18-28(2010).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 115-401 IN COMPLEX WITH
RP INHIBITORS IMATINIB AND GNF-2, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF PRO-112; TYR-128; TYR-139; SER-229;
RP THR-315; CYS-464; PRO-465; PHE-497; GLU-505 AND VAL-506.
RX PubMed=20072125; DOI=10.1038/nature08675;
RA Zhang J., Adrian F.J., Jahnke W., Cowan-Jacob S.W., Li A.G., Iacob R.E.,
RA Sim T., Powers J., Dierks C., Sun F., Guo G.R., Ding Q., Okram B., Choi Y.,
RA Wojciechowski A., Deng X., Liu G., Fendrich G., Strauss A., Vajpai N.,
RA Grzesiek S., Tuntland T., Liu Y., Bursulaya B., Azam M., Manley P.W.,
RA Engen J.R., Daley G.Q., Warmuth M., Gray N.S.;
RT "Targeting Bcr-Abl by combining allosteric with ATP-binding-site
RT inhibitors.";
RL Nature 463:501-506(2010).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in
CC many key processes linked to cell growth and survival such as
CC cytoskeleton remodeling in response to extracellular stimuli, cell
CC motility and adhesion, receptor endocytosis, autophagy, DNA damage
CC response and apoptosis. Coordinates actin remodeling through tyrosine
CC phosphorylation of proteins controlling cytoskeleton dynamics like
CC WASF3 (involved in branch formation); ANXA1 (involved in membrane
CC anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling);
CC or MAPT and PXN (microtubule-binding proteins). Phosphorylation of
CC WASF3 is critical for the stimulation of lamellipodia formation and
CC cell migration. Involved in the regulation of cell adhesion and
CC motility through phosphorylation of key regulators of these processes
CC such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple
CC receptor tyrosine kinases and more particularly promotes endocytosis of
CC EGFR, facilitates the formation of neuromuscular synapses through MUSK,
CC inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of
CC activated B-cell receptor complexes. Other substrates which are
CC involved in endocytosis regulation are the caveolin (CAV1) and RIN1.
CC Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive
CC receptor down-regulation and actin remodeling. Phosphorylation of CBL
CC leads to increased EGFR stability. Involved in late-stage autophagy by
CC regulating positively the trafficking and function of lysosomal
CC components. ABL1 targets to mitochondria in response to oxidative
CC stress and thereby mediates mitochondrial dysfunction and cell death.
CC In response to oxidative stress, phosphorylates serine/threonine kinase
CC PRKD2 at 'Tyr-717' (By similarity). ABL1 is also translocated in the
CC nucleus where it has DNA-binding activity and is involved in DNA-damage
CC response and apoptosis. Many substrates are known mediators of DNA
CC repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates
CC the proapoptotic pathway when the DNA damage is too severe to be
CC repaired. Phosphorylates TP73, a primary regulator for this type of
CC damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191'
CC and regulates its processing in the apoptotic response to DNA damage.
CC Phosphorylates PSMA7 that leads to an inhibition of proteasomal
CC activity and cell cycle transition blocks. Regulates T-cell
CC differentiation in a TBX21-dependent manner (PubMed:21690296).
CC Phosphorylates TBX21 on tyrosine residues leading to an enhancement of
CC its transcriptional activator activity (PubMed:21690296).
CC {ECO:0000250|UniProtKB:P00519, ECO:0000269|PubMed:11279004,
CC ECO:0000269|PubMed:11279131, ECO:0000269|PubMed:11350980,
CC ECO:0000269|PubMed:12107171, ECO:0000269|PubMed:12748290,
CC ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:19878872,
CC ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21690296,
CC ECO:0000269|PubMed:7780740, ECO:0000269|PubMed:8194526,
CC ECO:0000269|PubMed:9109492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290,
CC ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:20072125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12748290};
CC Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but
CC Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Stabilized in the inactive form by an association
CC between the SH3 domain and the SH2-TK linker region, interactions of
CC the N-terminal cap, and contributions from an N-terminal myristoyl
CC group and phospholipids. Activated by autophosphorylation as well as by
CC SRC-family kinase-mediated phosphorylation (By similarity). Activated
CC by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell
CC death inducers and DNA-damage (By similarity). Phosphatidylinositol
CC 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to
CC regulate cytoskeletal and membrane proteins, inhibits also the tyrosine
CC kinase activity. Inhibited by imatinib mesylate (Gleevec).
CC {ECO:0000250, ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12654251,
CC ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293,
CC ECO:0000269|PubMed:20072125, ECO:0000269|PubMed:9109492}.
CC -!- SUBUNIT: Interacts with INPPL1/SHIP2. Interacts with SORBS1 following
CC insulin stimulation. Found in a trimolecular complex containing CDK5
CC and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with
CC ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG,
CC YWHAH, SFN AND YWHAZ; the interaction with 14-3-3 proteins requires
CC phosphorylation on Thr-734 and sequesters ABL1 into the cytoplasm.
CC Interacts (via SH3 domain) with CASP9; the interaction is direct and
CC increases in the response of cells to genotoxic stress and ABL1/c-Abl
CC activation (By similarity). Interacts with ABI1, ABI2, BCR, CRK, FYN,
CC LYN, PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1,
CC CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement
CC critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell
CC (EC) barrier enhancement. Interacts with STX17; probably phosphorylates
CC STX17 (By similarity). Interacts with ITGB1, HCK and FGR. Found in a
CC complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of
CC CRK phosphorylation by ABL kinases (By similarity). Interacts with
CC TBX21 (PubMed:21690296). {ECO:0000250|UniProtKB:P00519,
CC ECO:0000269|PubMed:10896159, ECO:0000269|PubMed:11163214,
CC ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:12021275,
CC ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:19903482,
CC ECO:0000269|PubMed:21690296}.
CC -!- INTERACTION:
CC P00520; Q32MD9: Cdon; NbExp=2; IntAct=EBI-914519, EBI-7017034;
CC P00520; P97465: Dok1; NbExp=4; IntAct=EBI-914519, EBI-914917;
CC P00520; Q99M51: Nck1; NbExp=2; IntAct=EBI-914519, EBI-642202;
CC P00520; P97814: Pstpip1; NbExp=5; IntAct=EBI-914519, EBI-7484574;
CC P00520; O55042: Snca; NbExp=2; IntAct=EBI-914519, EBI-2310271;
CC P00520; P46527: CDKN1B; Xeno; NbExp=2; IntAct=EBI-914519, EBI-519280;
CC P00520; P28693: EPHB2; Xeno; NbExp=5; IntAct=EBI-914519, EBI-6725885;
CC P00520; P70602: Ptpn18; Xeno; NbExp=2; IntAct=EBI-914519, EBI-7484661;
CC P00520-4; Q8IZP0-4: ABI1; Xeno; NbExp=5; IntAct=EBI-8593082, EBI-8593095;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion.
CC Note=The myristoylated c-ABL protein is reported to be nuclear.
CC Sequestered into the cytoplasm through interaction with 14-3-3 proteins
CC (By similarity). Localizes to mitochondria in response to oxidative
CC stress. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=I;
CC IsoId=P00520-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P00520-2; Sequence=VSP_004959;
CC Name=III;
CC IsoId=P00520-3; Sequence=VSP_004958;
CC Name=IV;
CC IsoId=P00520-4; Sequence=VSP_004960;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: Acetylated at Lys-710 by EP300 which promotes the cytoplasmic
CC translocation. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases
CC disrupts SH3 domain-based autoinhibitory interactions and
CC intermolecular associations, such as that with ABI1, and also enhances
CC kinase activity (By similarity). Phosphorylation at Tyr-226 and Tyr-393
CC correlate with increased activity (By similarity). DNA damage-induced
CC activation of ABL1 requires the function of ATM and Ser-446
CC phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been
CC attributed to a CDC2-associated kinase and is coupled to cell division.
CC Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK
CC and reduces binding to ABI1 (By similarity). Phosphorylation on Thr-734
CC is required for binding 14-3-3 proteins for cytoplasmic translocation
CC (By similarity). Phosphorylated by PDGFRB and PRKDC. {ECO:0000250,
CC ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290,
CC ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:1566087,
CC ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:2183353,
CC ECO:0000269|PubMed:9109492}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Isoform IV is myristoylated on Gly-2.
CC {ECO:0000269|PubMed:12654251}.
CC -!- DISRUPTION PHENOTYPE: Mutants are born with the expected Mendelian
CC frequency, but fail to thrive and most die within three weeks after
CC birth. Most mutants are runted, and have atrophied thymuses with severe
CC thymocyte deficiency. Mutants that survive to weaning age are most
CC often runted, and about half of them show lymphopenia. They display a
CC major reduction in the number of pre-B and immature B-cell classes in
CC bone marrow with a wide variation between individuals, but essentially
CC normal mature B-cell levels. Mutants are highly susceptible to
CC infections. {ECO:0000269|PubMed:2065352, ECO:0000269|PubMed:2065353}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; J02995; AAA88241.1; -; mRNA.
DR EMBL; AK090095; BAC41088.1; -; mRNA.
DR EMBL; BC059260; AAH59260.1; -; mRNA.
DR EMBL; U14721; AAB60451.1; -; Genomic_DNA.
DR EMBL; U14720; AAB60451.1; JOINED; Genomic_DNA.
DR EMBL; U14721; AAB60450.1; -; Genomic_DNA.
DR EMBL; U14720; AAB60450.1; JOINED; Genomic_DNA.
DR EMBL; U14721; AAB60448.1; -; Genomic_DNA.
DR EMBL; U13835; AAB60448.1; JOINED; Genomic_DNA.
DR EMBL; U14721; AAB60449.1; -; Genomic_DNA.
DR EMBL; U13835; AAB60449.1; JOINED; Genomic_DNA.
DR EMBL; X07539; CAA30411.1; -; Genomic_DNA.
DR EMBL; X07539; CAA30412.1; -; Genomic_DNA.
DR EMBL; X07540; CAA30413.1; -; Genomic_DNA.
DR EMBL; X07541; CAA30414.1; -; Genomic_DNA.
DR EMBL; M12263; AAA37136.1; -; mRNA.
DR EMBL; M12264; AAA37137.1; -; mRNA.
DR EMBL; M12265; AAA37138.1; -; mRNA.
DR EMBL; M12266; AAA37134.1; -; Genomic_DNA.
DR EMBL; K03228; AAA37135.1; -; mRNA.
DR CCDS; CCDS15901.1; -. [P00520-1]
DR CCDS; CCDS50563.1; -. [P00520-4]
DR PIR; A39962; A39962.
DR PIR; S00774; S00774.
DR RefSeq; NP_001106174.1; NM_001112703.2. [P00520-4]
DR RefSeq; NP_001269974.1; NM_001283045.1. [P00520-3]
DR RefSeq; NP_001269975.1; NM_001283046.1. [P00520-2]
DR RefSeq; NP_033724.2; NM_009594.4. [P00520-1]
DR PDB; 1ABO; X-ray; 2.00 A; A/B=61-121.
DR PDB; 1ABQ; X-ray; 2.80 A; A=61-121.
DR PDB; 1FPU; X-ray; 2.40 A; A/B=229-515.
DR PDB; 1IEP; X-ray; 2.10 A; A/B=229-515.
DR PDB; 1M52; X-ray; 2.60 A; A/B=229-515.
DR PDB; 1OPJ; X-ray; 1.75 A; A/B=229-515.
DR PDB; 1OPK; X-ray; 1.80 A; A=27-515.
DR PDB; 2HZN; X-ray; 2.70 A; A=229-515.
DR PDB; 2QOH; X-ray; 1.95 A; A/B=229-515.
DR PDB; 2Z60; X-ray; 1.95 A; A=229-515.
DR PDB; 3DK3; X-ray; 2.02 A; A/B=233-514.
DR PDB; 3DK6; X-ray; 2.02 A; A/B=233-514.
DR PDB; 3DK7; X-ray; 2.01 A; A/B=233-505.
DR PDB; 3IK3; X-ray; 1.90 A; A/B=229-513.
DR PDB; 3K5V; X-ray; 1.74 A; A/B=229-515.
DR PDB; 3KF4; X-ray; 1.90 A; A/B=229-515.
DR PDB; 3KFA; X-ray; 1.22 A; A/B=229-515.
DR PDB; 3MS9; X-ray; 1.80 A; A/B=229-515.
DR PDB; 3MSS; X-ray; 1.95 A; A/B/C/D=229-515.
DR PDB; 3OXZ; X-ray; 2.20 A; A=229-511.
DR PDB; 3OY3; X-ray; 1.95 A; A/B=229-511.
DR PDB; 5IH2; X-ray; 1.80 A; M/N=757-765.
DR PDB; 6HD4; X-ray; 2.03 A; A/B=229-515.
DR PDB; 6HD6; X-ray; 2.30 A; A/B=229-515.
DR PDBsum; 1ABO; -.
DR PDBsum; 1ABQ; -.
DR PDBsum; 1FPU; -.
DR PDBsum; 1IEP; -.
DR PDBsum; 1M52; -.
DR PDBsum; 1OPJ; -.
DR PDBsum; 1OPK; -.
DR PDBsum; 2HZN; -.
DR PDBsum; 2QOH; -.
DR PDBsum; 2Z60; -.
DR PDBsum; 3DK3; -.
DR PDBsum; 3DK6; -.
DR PDBsum; 3DK7; -.
DR PDBsum; 3IK3; -.
DR PDBsum; 3K5V; -.
DR PDBsum; 3KF4; -.
DR PDBsum; 3KFA; -.
DR PDBsum; 3MS9; -.
DR PDBsum; 3MSS; -.
DR PDBsum; 3OXZ; -.
DR PDBsum; 3OY3; -.
DR PDBsum; 5IH2; -.
DR PDBsum; 6HD4; -.
DR PDBsum; 6HD6; -.
DR AlphaFoldDB; P00520; -.
DR BMRB; P00520; -.
DR SMR; P00520; -.
DR BioGRID; 197906; 21.
DR CORUM; P00520; -.
DR ELM; P00520; -.
DR IntAct; P00520; 24.
DR MINT; P00520; -.
DR STRING; 10090.ENSMUSP00000075167; -.
DR BindingDB; P00520; -.
DR ChEMBL; CHEMBL3099; -.
DR DrugCentral; P00520; -.
DR iPTMnet; P00520; -.
DR PhosphoSitePlus; P00520; -.
DR jPOST; P00520; -.
DR MaxQB; P00520; -.
DR PaxDb; P00520; -.
DR PeptideAtlas; P00520; -.
DR PRIDE; P00520; -.
DR ProteomicsDB; 285962; -. [P00520-1]
DR ProteomicsDB; 285963; -. [P00520-2]
DR ProteomicsDB; 285964; -. [P00520-3]
DR ProteomicsDB; 285965; -. [P00520-4]
DR Antibodypedia; 3637; 2229 antibodies from 44 providers.
DR DNASU; 11350; -.
DR Ensembl; ENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842. [P00520-1]
DR Ensembl; ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842. [P00520-4]
DR GeneID; 11350; -.
DR KEGG; mmu:11350; -.
DR UCSC; uc008jdz.3; mouse. [P00520-1]
DR UCSC; uc033hmk.1; mouse. [P00520-2]
DR UCSC; uc033hml.1; mouse. [P00520-3]
DR CTD; 25; -.
DR MGI; MGI:87859; Abl1.
DR VEuPathDB; HostDB:ENSMUSG00000026842; -.
DR eggNOG; KOG4278; Eukaryota.
DR GeneTree; ENSGT00940000153838; -.
DR HOGENOM; CLU_002795_0_0_1; -.
DR InParanoid; P00520; -.
DR OMA; CPAFLGK; -.
DR TreeFam; TF105081; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-MMU-525793; Myogenesis.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR BioGRID-ORCS; 11350; 8 hits in 114 CRISPR screens.
DR ChiTaRS; Abl1; mouse.
DR EvolutionaryTrace; P00520; -.
DR PRO; PR:P00520; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P00520; protein.
DR Bgee; ENSMUSG00000026842; Expressed in external carotid artery and 263 other tissues.
DR ExpressionAtlas; P00520; baseline and differential.
DR Genevisible; P00520; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000405; F:bubble DNA binding; ISO:MGI.
DR GO; GO:0070097; F:delta-catenin binding; ISO:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:ARUK-UCL.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR GO; GO:1990051; P:activation of protein kinase C activity; ISO:MGI.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IGI:MGI.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:MGI.
DR GO; GO:0001922; P:B-1 B cell homeostasis; IMP:MGI.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IGI:MGI.
DR GO; GO:0021587; P:cerebellum morphogenesis; IGI:MGI.
DR GO; GO:0072359; P:circulatory system development; IGI:MGI.
DR GO; GO:1904157; P:DN4 thymocyte differentiation; IGI:MGI.
DR GO; GO:0071103; P:DNA conformation change; ISO:MGI.
DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0030035; P:microspike assembly; IDA:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IGI:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IGI:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IGI:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:MGI.
DR GO; GO:1900275; P:negative regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IGI:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0070997; P:neuron death; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0038189; P:neuropilin signaling pathway; ISO:MGI.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
DR GO; GO:1903210; P:podocyte apoptotic process; ISO:MGI.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:1904531; P:positive regulation of actin filament binding; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:1905555; P:positive regulation of blood vessel branching; IMP:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IMP:UniProtKB.
DR GO; GO:1903055; P:positive regulation of extracellular matrix organization; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IGI:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IGI:MGI.
DR GO; GO:1904528; P:positive regulation of microtubule binding; ISO:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IGI:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:MGI.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:MGI.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:2000406; P:positive regulation of T cell migration; IMP:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
DR GO; GO:0009791; P:post-embryonic development; IGI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:1904518; P:protein localization to cytoplasmic microtubule plus-end; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:2000772; P:regulation of cellular senescence; IGI:MGI.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IGI:MGI.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; IGI:ARUK-UCL.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0002333; P:transitional one stage B cell differentiation; IMP:MGI.
DR CDD; cd09935; SH2_ABL; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID50269; -.
DR InterPro; IPR033221; ABL1.
DR InterPro; IPR035837; ABL_SH2.
DR InterPro; IPR015015; F-actin-binding.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF162; PTHR24418:SF162; 1.
DR Pfam; PF08919; F_actin_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00808; FABD; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding;
KW Autophagy; Cell adhesion; Chromosomal rearrangement; Cytoplasm;
KW Cytoskeleton; DNA damage; DNA repair; DNA-binding; Endocytosis; Kinase;
KW Lipoprotein; Magnesium; Manganese; Metal-binding; Mitochondrion; Myristate;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase; Ubl conjugation.
FT CHAIN 1..1123
FT /note="Tyrosine-protein kinase ABL1"
FT /id="PRO_0000088051"
FT DOMAIN 61..121
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 127..217
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 242..493
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..60
FT /note="CAP"
FT REGION 504..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..961
FT /note="DNA-binding"
FT REGION 945..1123
FT /note="F-actin-binding"
FT /evidence="ECO:0000250"
FT MOTIF 381..405
FT /note="Kinase activation loop"
FT MOTIF 605..609
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255"
FT MOTIF 708..714
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255"
FT MOTIF 761..768
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255"
FT MOTIF 1083..1093
FT /note="Nuclear export signal"
FT COMPBIAS 533..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 248..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 316..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 70
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 115
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 128
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 172
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 215
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 226
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 257
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 393
FT /note="Phosphotyrosine; by autocatalysis and SRC-type Tyr-
FT kinases"
FT /evidence="ECO:0000269|PubMed:10988075,
FT ECO:0000269|PubMed:12748290"
FT MOD_RES 413
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9109492"
FT MOD_RES 547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:2183353"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2183353"
FT MOD_RES 618
FT /note="Phosphoserine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 619
FT /note="Phosphoserine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 710
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 750
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 812
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 821
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT VAR_SEQ 1..26
FT /note="MLEICLKLVGCKSKKGLSSSSSCYLE -> MISFDLLSDELHLKLLVLDV
FT (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_004959"
FT VAR_SEQ 1..26
FT /note="MLEICLKLVGCKSKKGLSSSSSCYLE -> MSQRWTYTKCRVQRDPALPFM
FT (in isoform III)"
FT /evidence="ECO:0000305"
FT /id="VSP_004958"
FT VAR_SEQ 1..26
FT /note="MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGDQRRPSLPALHF
FT IKGAGKRDSSRHGGPHCNVFVEH (in isoform IV)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004960"
FT MUTAGEN 112
FT /note="P->S: Strongly reduced inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 128
FT /note="Y->D: Strongly reduced inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 139
FT /note="Y->C: Strongly reduced inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 226
FT /note="Y->F: Minimal reduction in ability to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 229
FT /note="S->P: Strongly reduced inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 271
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 315
FT /note="T->I: Loss of inhibition by imatinib. Loss of
FT inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 393
FT /note="Y->F: Minimal reduction in ability to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 446
FT /note="S->A: No effect on basal activity, but abolishes
FT ionizing radiation-induced activation."
FT /evidence="ECO:0000269|PubMed:9109492"
FT MUTAGEN 464
FT /note="C->Y: Loss of inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 465
FT /note="P->S: Loss of inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 497
FT /note="F->L: Strongly reduced inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 505
FT /note="E->K: Loss of inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 506
FT /note="V->L: Strongly reduced inhibition by GNF-2."
FT /evidence="ECO:0000269|PubMed:20072125"
FT MUTAGEN 1083
FT /note="L->A: Loss of nuclear export."
FT CONFLICT 184..187
FT /note="LYVS -> VGDW (in Ref. 4; AAB60451/AAB60450)"
FT /evidence="ECO:0000305"
FT CONFLICT 782..786
FT /note="PPRLV -> LPGWL (in Ref. 1; AAA88241)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="D -> G (in Ref. 2; BAC41088)"
FT /evidence="ECO:0000305"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1ABQ"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1OPK"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1OPK"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 307..316
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:3KFA"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 337..357
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1M52"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 408..413
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 418..433
FT /evidence="ECO:0007829|PDB:3KFA"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:2HZN"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 466..475
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3KFA"
FT HELIX 486..509
FT /evidence="ECO:0007829|PDB:3KFA"
FT INIT_MET P00520-4:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID P00520-4:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12654251"
SQ SEQUENCE 1123 AA; 122673 MW; BD48ADE8557AE95C CRC64;
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE
NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN
SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS
DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT
DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA MEYLEKKNFI
HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS
DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP
SDRPSFAEIH QAFETMFQES SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE
QKDAPDTPEL LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS DAAEPTKSPK
ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA EEESGMSSSK RFLRSCSASC
MPHGARDTEW RSVTLPRDLP SAGKQFDSST FGGHKSEKPA LPRKRTSESR SEQVAKSTAM
PPPRLVKKNE EAAEEGFKDT ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS
GMGTPATAEP APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP VPPSVPKPQS
TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS TRVSLRKTRQ PPERIASGTI
TKGVVLDSTE ALCLAISRNS EQMASHSAVL EAGKNLYTFC VSYVDSIQQM RNKFAFREAI
NKLESNLREL QICPATASSG PAATQDFSKL LSSVKEISDI VRR
