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Abelson tyrosine-protein kinase 2 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 2) (Abelson-related gene protein) (Tyrosine-protein kinase ARG)

 ABL2_MOUSE              Reviewed;        1182 AA.
Q4JIM5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
02-AUG-2005, sequence version 1.
22-NOV-2017, entry version 110.
RecName: Full=Abelson tyrosine-protein kinase 2;
EC=2.7.10.2;
AltName: Full=Abelson murine leukemia viral oncogene homolog 2;
AltName: Full=Abelson-related gene protein;
AltName: Full=Tyrosine-protein kinase ARG;
Name=Abl2 {ECO:0000312|EMBL:AAY86039.1, ECO:0000312|MGI:MGI:87860};
Synonyms=Arg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAY86039.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, SUBCELLULAR LOCATION,
AND ACTIN-BINDING.
STRAIN=129/SvJ {ECO:0000312|EMBL:AAY86039.1};
PubMed=11752434; DOI=10.1073/pnas.251249298;
Wang Y., Miller A.L., Mooseker M.S., Koleske A.J.;
"The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-
actin-binding domains to bundle F-actin.";
Proc. Natl. Acad. Sci. U.S.A. 98:14865-14870(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:AAY86039.1}
NUCLEOTIDE SEQUENCE [MRNA], CAP DOMAIN, FUNCTION, ENZYME REGULATION,
INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND
TYR-684, AND MUTAGENESIS OF TYR-272; LYS-317; TYR-439; TYR-568 AND
TYR-684.
STRAIN=129/SvJ {ECO:0000312|EMBL:AAY86039.1};
PubMed=12748290; DOI=10.1128/MCB.23.11.3884-3896.2003;
Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
"Two distinct phosphorylation pathways have additive effects on Abl
family kinase activation.";
Mol. Cell. Biol. 23:3884-3896(2003).
[3]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=9883720; DOI=10.1016/S0896-6273(00)80646-7;
Koleske A.J., Gifford A.M., Scott M.L., Nee M., Bronson R.T.,
Miczek K.A., Baltimore D.;
"Essential roles for the Abl and Arg tyrosine kinases in
neurulation.";
Neuron 21:1259-1272(1998).
[4]
FUNCTION.
PubMed=11279004; DOI=10.1074/jbc.M100095200;
Kain K.H., Klemke R.L.;
"Inhibition of cell migration by Abl family tyrosine kinases through
uncoupling of Crk-CAS complexes.";
J. Biol. Chem. 276:16185-16192(2001).
[5]
REVIEW ON FUNCTION.
PubMed=12775773; DOI=10.1242/jcs.00622;
Woodring P.J., Hunter T., Wang J.Y.;
"Regulation of F-actin-dependent processes by the Abl family of
tyrosine kinases.";
J. Cell Sci. 116:2613-2626(2003).
[6]
FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION.
PubMed=14993293; DOI=10.1128/MCB.24.6.2573-2583.2004;
Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
"Bidirectional signaling links the Abelson kinases to the platelet-
derived growth factor receptor.";
Mol. Cell. Biol. 24:2573-2583(2004).
[7]
REVIEW ON FUNCTION.
PubMed=14729179; DOI=10.1016/j.tcb.2003.11.003;
Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.;
"How do Abl family kinases regulate cell shape and movement?";
Trends Cell Biol. 14:36-44(2004).
[8]
FUNCTION.
PubMed=16971514; DOI=10.1091/mbc.E06-02-0132;
Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J.;
"Integrin signaling through Arg activates p190RhoGAP by promoting its
binding to p120RasGAP and recruitment to the membrane.";
Mol. Biol. Cell 17:4827-4836(2006).
[9]
FUNCTION.
PubMed=17892306; DOI=10.1021/bi701119s;
Boyle S.N., Koleske A.J.;
"Use of a chemical genetic technique to identify myosin IIb as a
substrate of the Abl-related gene (Arg) tyrosine kinase.";
Biochemistry 46:11614-11620(2007).
[10]
REVIEW ON FUNCTION.
PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006;
Backert S., Feller S.M., Wessler S.;
"Emerging roles of Abl family tyrosine kinases in microbial
pathogenesis.";
Trends Biochem. Sci. 33:80-90(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-632 AND
SER-936, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-632 AND
SER-822, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
REVIEW ON FUNCTION, AND DOMAIN.
PubMed=20841568; DOI=10.1126/scisignal.3139re6;
Colicelli J.;
"ABL tyrosine kinases: evolution of function, regulation, and
specificity.";
Sci. Signal. 3:RE6-RE6(2010).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-
overlapping role in key processes linked to cell growth and
survival such as cytoskeleton remodeling in response to
extracellular stimuli, cell motility and adhesion, receptor
endocytosis, autophagy, DNA damage response and apoptosis.
Coordinates actin remodeling through tyrosine phosphorylation of
proteins controlling cytoskeleton dynamics like MYH10 (involved in
movement); CTTN (involved in signaling); or TUBA1 and TUBB
(microtubule subunits). Binds directly F-actin and regulates actin
cytoskeletal structure through its F-actin-bundling activity.
Involved in the regulation of cell adhesion and motility through
phosphorylation of key regulators of these processes such as CRK,
CRKL or DOK1. Required for adhesion-dependent phosphorylation of
ARHGAP35 which promotes its association with RASA1, resulting in
recruitment of ARHGAP35 to the cell periphery where it inhibits
RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB
and other substrates which are involved in endocytosis regulation
such as RIN1. In brain, may regulate neurotransmission by
phosphorylating proteins at the synapse. Finally, functions as its
own regulator through autocatalytic activity as well as through
phosphorylation of its inhibitor, ABI1.
{ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11752434,
ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293,
ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:17892306,
ECO:0000269|PubMed:9883720}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:12748290}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12748290};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:12748290};
-!- ENZYME REGULATION: Stabilized in the inactive form by an
association between the SH3 domain and the SH2-TK linker region,
interactions of the N-terminal cap, and contributions from an N-
terminal myristoyl group and phospholipids. Activated by
autophosphorylation as well as by SRC-family kinase-mediated
phosphorylation. Activated by RIN1 binding to the SH2 and SH3
domains (By similarity). Inhibited by imatinib mesylate (Gleevec).
Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant
phosphoinositide known to regulate cytoskeletal and membrane
proteins, inhibits the tyrosine kinase activity. {ECO:0000250,
ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.
-!- SUBUNIT: Interacts with PSMA7. Interacts with CTTN (By
similarity). Found in a complex with ABL1, ABL2, CRK and UNC119;
leading to the inhibition of CRK phosphorylation by ABL kinases
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11752434}.
-!- TISSUE SPECIFICITY: Most abundant in adult mouse brain, especially
in synapse-rich regions. {ECO:0000269|PubMed:9883720}.
-!- DOMAIN: Contains two distinct classes of F-actin-binding domains.
Although both can each bind F-actin, the 2 are required to bundle
actin filaments. {ECO:0000269|PubMed:11752434,
ECO:0000269|PubMed:20841568}.
-!- PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative
stress (By similarity). Phosphorylated by PDGFRB. {ECO:0000250,
ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.
-!- PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to
degradation (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Leads to defects in neuronal function.
{ECO:0000269|PubMed:9883720}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. ABL subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; DQ084361; AAY86039.1; -; mRNA.
CCDS; CCDS15393.1; -.
UniGene; Mm.329515; -.
PDB; 4XLI; X-ray; 2.50 A; A/B=279-546.
PDBsum; 4XLI; -.
ProteinModelPortal; Q4JIM5; -.
SMR; Q4JIM5; -.
DIP; DIP-60989N; -.
IntAct; Q4JIM5; 4.
STRING; 10090.ENSMUSP00000027888; -.
ChEMBL; CHEMBL5222; -.
iPTMnet; Q4JIM5; -.
PhosphoSitePlus; Q4JIM5; -.
EPD; Q4JIM5; -.
MaxQB; Q4JIM5; -.
PaxDb; Q4JIM5; -.
PeptideAtlas; Q4JIM5; -.
PRIDE; Q4JIM5; -.
MGI; MGI:87860; Abl2.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000231988; -.
HOVERGEN; HBG004162; -.
InParanoid; Q4JIM5; -.
PhylomeDB; Q4JIM5; -.
ChiTaRS; Abl2; mouse.
PRO; PR:Q4JIM5; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; TAS:MGI.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0001891; C:phagocytic cup; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
GO; GO:0007015; P:actin filament organization; IDA:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0002118; P:aggressive behavior; IMP:MGI.
GO; GO:0046632; P:alpha-beta T cell differentiation; IGI:MGI.
GO; GO:0031223; P:auditory behavior; IMP:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
GO; GO:0072358; P:cardiovascular system development; IGI:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0034613; P:cellular protein localization; IMP:MGI.
GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
GO; GO:0021587; P:cerebellum morphogenesis; IGI:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0097062; P:dendritic spine maintenance; IMP:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0035640; P:exploration behavior; IGI:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007612; P:learning; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IGI:MGI.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IGI:MGI.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
GO; GO:0060563; P:neuroepithelial cell differentiation; IGI:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IGI:MGI.
GO; GO:0016322; P:neuron remodeling; IMP:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IMP:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IGI:MGI.
GO; GO:1900042; P:positive regulation of interleukin-2 secretion; IGI:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:MGI.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IMP:MGI.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
GO; GO:0009791; P:post-embryonic development; IGI:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:1903053; P:regulation of extracellular matrix organization; IGI:MGI.
GO; GO:0022414; P:reproductive process; IMP:MGI.
GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IGI:MGI.
GO; GO:0008542; P:visual learning; IGI:MGI.
CDD; cd09935; SH2_ABL; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035837; ABL_SH2.
InterPro; IPR015015; F-actin_binding.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF08919; F_actin_bind; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00808; FABD; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell adhesion;
Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Lipoprotein;
Magnesium; Manganese; Metal-binding; Myristate; Nucleotide-binding;
Phosphoprotein; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 1182 Abelson tyrosine-protein kinase 2.
/FTId=PRO_0000258019.
DOMAIN 107 167 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 173 263 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 288 539 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 294 302 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
NP_BIND 362 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 106 CAP.
REGION 695 930 F-actin-binding.
REGION 1020 1182 F-actin-binding.
MOTIF 427 451 Kinase activation loop. {ECO:0000250}.
MOTIF 659 661 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 561 564 Poly-Ser.
COMPBIAS 735 741 Poly-Gly.
COMPBIAS 984 988 Poly-Pro.
ACT_SITE 409 409 Proton acceptor.
{ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028}.
BINDING 317 317 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:12748290}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 116 116 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 161 161 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 174 174 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 218 218 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 231 231 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 261 261 Phosphotyrosine; by ABL1 and
autocatalysis.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 272 272 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 299 299 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 303 303 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 439 439 Phosphotyrosine; by autocatalysis and
SRC-type Tyr-kinases.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 459 459 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000250|UniProtKB:P00520}.
MOD_RES 568 568 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 606 606 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 656 656 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 684 684 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 719 719 Phosphotyrosine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 778 778 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 802 802 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 915 915 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:P00519}.
MUTAGEN 272 272 Y->F: Minimal reduction in ability to
autophosphorylate.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 317 317 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 439 439 Y->F: Partial reduction in ability to
autophosphorylate.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 568 568 Y->F: No reduction in ability to
autophosphorylate.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 684 684 Y->F: Minimal reduction in ability to
autophosphorylate.
{ECO:0000269|PubMed:12748290}.
HELIX 285 287 {ECO:0000244|PDB:4XLI}.
STRAND 288 295 {ECO:0000244|PDB:4XLI}.
STRAND 302 307 {ECO:0000244|PDB:4XLI}.
HELIX 308 310 {ECO:0000244|PDB:4XLI}.
STRAND 312 319 {ECO:0000244|PDB:4XLI}.
HELIX 327 337 {ECO:0000244|PDB:4XLI}.
STRAND 347 351 {ECO:0000244|PDB:4XLI}.
STRAND 353 362 {ECO:0000244|PDB:4XLI}.
HELIX 369 375 {ECO:0000244|PDB:4XLI}.
TURN 378 380 {ECO:0000244|PDB:4XLI}.
HELIX 383 402 {ECO:0000244|PDB:4XLI}.
HELIX 412 414 {ECO:0000244|PDB:4XLI}.
STRAND 415 417 {ECO:0000244|PDB:4XLI}.
HELIX 419 421 {ECO:0000244|PDB:4XLI}.
STRAND 423 425 {ECO:0000244|PDB:4XLI}.
STRAND 435 437 {ECO:0000244|PDB:4XLI}.
HELIX 449 451 {ECO:0000244|PDB:4XLI}.
HELIX 454 459 {ECO:0000244|PDB:4XLI}.
HELIX 464 479 {ECO:0000244|PDB:4XLI}.
HELIX 491 493 {ECO:0000244|PDB:4XLI}.
HELIX 494 499 {ECO:0000244|PDB:4XLI}.
HELIX 512 521 {ECO:0000244|PDB:4XLI}.
HELIX 526 528 {ECO:0000244|PDB:4XLI}.
HELIX 532 545 {ECO:0000244|PDB:4XLI}.
SEQUENCE 1182 AA; 128196 MW; 08507298A9081228 CRC64;
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT QHDHFASCVE
DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA
SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR
SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST
LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG
EVYVGVWKKY SLTVAVKTFK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV
TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN
HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT
YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE
TMFHDSSISE EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE
SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK GGFFSSFMKK
RNAPTPPKRS SSFREMENQP HKKYELTGNF SPVASLQNAD GFSVAPSQQE PNLVPAKCYG
GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI TGFFTPRLIK KTLGLRAGKP TASDDTSKPF
PRSNSTSSMS SGLPEQDRMA MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE
EGAAPARERP KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG
VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL
LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS DPEEEPTAPP AGQHTPETQE
GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS
ADKISKEALL ECADLLSSAI TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV
SKLELSLQEL QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR


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