Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00478
Entry Name
UniProt Accession
Theoretical PI
7.97
Molecular Weight
128196.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Abelson tyrosine-protein kinase 2
Protein Synonyms/Alias
2.7.10.2; Abelson murine leukemia viral oncogene homolog 2; Abelson-related gene protein; Tyrosine-protein kinase ARG;
Gene Name
Abl2
Gene Synonyms/Alias
Arg;
Created Date
31-OCT-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGQQVGRVG
[1]
N-Myristoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Resh MD. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta. 1999 Aug12;1451(1):1-16. Review.[PMID:10446384]
Functional Description
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.
Sequence Annotation
Domain: 107 167 SH3.
Domain: 173 263 SH2.
Domain: 288 539 Protein kinase.
Nucleotide-binding: 294 302 ATP.
Nucleotide-binding: 362 368 ATP.
Region: 2 106 CAP.
Region: 695 930 F-actin-binding.
Region: 1020 1182 F-actin-binding.
Motif: 427 451 Kinase activation loop.
Motif: 659 661 Nuclear localization signal.
Active site: 409 409 Proton acceptor.
Binding site: 317 317 ATP.
Modified residue: 261 261 Phosphotyrosine; by ABL1 andautocatalysis.
Modified residue: 272 272 Phosphotyrosine; by autocatalysis.
Modified residue: 275 275 Phosphoserine.
Modified residue: 439 439 Phosphotyrosine; by autocatalysis andSRC-type Tyr-kinases.
Modified residue: 568 568 Phosphotyrosine; by autocatalysis.
Modified residue: 621 621 Phosphoserine.
Modified residue: 632 632 Phosphoserine.
Modified residue: 634 634 Phosphoserine.
Modified residue: 656 656 Phosphoserine.
Modified residue: 684 684 Phosphotyrosine; by autocatalysis.
Modified residue: 719 719 Phosphotyrosine.
Modified residue: 819 819 Phosphoserine.
Modified residue: 822 822 Phosphoserine.
Modified residue: 915 915 Phosphoserine.
Modified residue: 936 936 Phosphoserine.
Protein Length
1182 AA.
Protein Sequence
(Canonical)
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT QHDHFASCVE  60
DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA  120
SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR  180
SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST  240
LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG  300
EVYVGVWKKY SLTVAVKTFK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV  360
TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN  420
HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT  480
YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE  540
TMFHDSSISE EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE  600
SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK GGFFSSFMKK  660
RNAPTPPKRS SSFREMENQP HKKYELTGNF SPVASLQNAD GFSVAPSQQE PNLVPAKCYG  720
GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI TGFFTPRLIK KTLGLRAGKP TASDDTSKPF  780
PRSNSTSSMS SGLPEQDRMA MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE  840
EGAAPARERP KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG  900
VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL  960
LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS DPEEEPTAPP AGQHTPETQE  1020
GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS  1080
ADKISKEALL ECADLLSSAI TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV  1140
SKLELSLQEL QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR                     1182
FASTA
(Canonical)
>LipidDB-10090-00478|Q4JIM5
MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTADAGFNVFTQHDHFASCVE
DGFEGDKTGGSSPEVLHRPFGCDAESQALNEAIRWSSKENLLGATESDPNLFVALYDFVA
SGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSR
SAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTTDSKVYVTAESRFST
LAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYG
EVYVGVWKKYSLTVAVKTFKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIV
TEYMPYGNLLDYLRECSREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGEN
HVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIAT
YGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFE
TMFHDSSISEEVAEELGRTASSSSVVPYLPRLPLLPSKTRTLRKQGENKENLDGGLDAAE
SLASSSAPAGFIRSTQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKK
RNAPTPPKRSSSFREMENQPHKKYELTGNFSPVASLQNADGFSVAPSQQEPNLVPAKCYG
GSFAQRNLCADDDSGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPF
PRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSE
EGAAPARERPKAKLLPRGATALPLRAPDPAITESDSPGVGVAGVAAAPKGKERNGGTRLG
VAGVPEDGEQLGWSSPAKAVAVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKL
LSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSTCSDPEEEPTAPPAGQHTPETQE
GGKKAAPGPVPSSGKPGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKIS
ADKISKEALLECADLLSSAITEPVPNSQLVDTGHQLLDYCSGYVDSIPQTRNKFAFREAV
SKLELSLQELQVSSTAAGVPGTNPVLNNLLSCVQEISDVVQR
Gene Ontology
GO:0015629; C:actin cytoskeleton; IDA:MGI
GO:0016023; C:cytoplasmic membrane-bounded vesicle; TAS:MGI
GO:0043197; C:dendritic spine; IDA:MGI
GO:0030027; C:lamellipodium; IDA:MGI
GO:0001891; C:phagocytic cup; IDA:MGI
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0000287; F:magnesium ion binding; IDA:UniProtKB
GO:0030145; F:manganese ion binding; IDA:UniProtKB
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC
GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB
GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB
GO:0051017; P:actin filament bundle assembly; IDA:MGI
GO:0007015; P:actin filament organization; IDA:MGI
GO:0046632; P:alpha-beta T cell differentiation; IGI:MGI
GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI
GO:0007155; P:cell adhesion; IEA:UniProtKB-KW
GO:0034613; P:cellular protein localization; IMP:MGI
GO:0021587; P:cerebellum morphogenesis; IGI:MGI
GO:0048813; P:dendrite morphogenesis; IMP:MGI
GO:0097062; P:dendritic spine maintenance; IMP:MGI
GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:MGI
GO:0035640; P:exploration behavior; IGI:MGI
GO:0007612; P:learning; IMP:MGI
GO:0022408; P:negative regulation of cell-cell adhesion; IGI:MGI
GO:2000352; P:negative regulation of endothelial cell apoptotic process; IGI:MGI
GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI
GO:0050885; P:neuromuscular process controlling balance; IGI:MGI
GO:0016322; P:neuron remodeling; IMP:MGI
GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB
GO:0006909; P:phagocytosis; IMP:MGI
GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IGI:MGI
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI
GO:1902715; P:positive regulation of interferon-gamma secretion; IGI:MGI
GO:1900042; P:positive regulation of interleukin-2 secretion; IGI:MGI
GO:0010976; P:positive regulation of neuron projection development; IGI:MGI
GO:0032092; P:positive regulation of protein binding; IMP:MGI
GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI
GO:0006468; P:protein phosphorylation; IDA:UniProtKB
GO:1903053; P:regulation of extracellular matrix organization; IGI:MGI
GO:0006930; P:substrate-dependent cell migration, cell extension; IGI:MGI
Interpro
InterPro; IPR015015; F-actin_binding
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR000980; SH2
InterPro; IPR001452; SH3_domain
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom
Pfam
Pfam; PF08919; F_actin_bind;
Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00017; SH2;
Pfam; PF00018; SH3_1;
SMART
SMART; SM00808; FABD;
SMART; SM00252; SH2;
SMART; SM00326; SH3;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS50001; SH2;
PROSITE; PS50002; SH3;
PRINTS
PRINTS; PR00401; SH2DOMAIN;
PRINTS; PR00109; TYRKINASE;