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Q4JIM5

- ABL2_MOUSE

UniProt

Q4JIM5 - ABL2_MOUSE

Protein

Abelson tyrosine-protein kinase 2

Gene

Abl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (02 Aug 2005)
      Previous versions | rss
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    Functioni

    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, ABI1.7 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Cofactori

    Magnesium or manganese.1 Publication

    Enzyme regulationi

    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.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei317 – 3171ATP1 PublicationPROSITE-ProRule annotation
    Active sitei409 – 4091Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi294 – 3029ATPBy similarityPROSITE-ProRule annotation
    Nucleotide bindingi362 – 3687ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: UniProtKB
    3. manganese ion binding Source: UniProtKB
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    5. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. actin filament bundle assembly Source: MGI
    3. actin filament organization Source: MGI
    4. cell adhesion Source: UniProtKB-KW
    5. peptidyl-tyrosine phosphorylation Source: UniProtKB
    6. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Abelson tyrosine-protein kinase 2 (EC:2.7.10.2)
    Alternative name(s):
    Abelson murine leukemia viral oncogene homolog 2
    Abelson-related gene protein
    Tyrosine-protein kinase ARG
    Gene namesi
    Name:Abl2Imported
    Synonyms:Arg
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:87860. Abl2.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication

    GO - Cellular componenti

    1. actin cytoskeleton Source: MGI
    2. cytoplasmic membrane-bounded vesicle Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Disruption phenotypei

    Leads to defects in neuronal function.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi272 – 2721Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication
    Mutagenesisi317 – 3171K → M: Loss of kinase activity. 1 Publication
    Mutagenesisi439 – 4391Y → F: Partial reduction in ability to autophosphorylate. 1 Publication
    Mutagenesisi568 – 5681Y → F: No reduction in ability to autophosphorylate. 1 Publication
    Mutagenesisi684 – 6841Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 11821181Abelson tyrosine-protein kinase 2PRO_0000258019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei261 – 2611Phosphotyrosine; by ABL1 and autocatalysisBy similarity
    Modified residuei272 – 2721Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei275 – 2751PhosphoserineBy similarity
    Modified residuei439 – 4391Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinasesBy similarity
    Modified residuei568 – 5681Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei621 – 6211Phosphoserine2 Publications
    Modified residuei632 – 6321Phosphoserine2 Publications
    Modified residuei634 – 6341PhosphoserineBy similarity
    Modified residuei656 – 6561PhosphoserineBy similarity
    Modified residuei684 – 6841Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei719 – 7191PhosphotyrosineBy similarity
    Modified residuei819 – 8191PhosphoserineBy similarity
    Modified residuei822 – 8221PhosphoserineBy similarity
    Modified residuei915 – 9151PhosphoserineBy similarity
    Modified residuei936 – 9361Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress By similarity. Phosphorylated by PDGFRB.By similarity3 Publications
    Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ4JIM5.
    PaxDbiQ4JIM5.
    PRIDEiQ4JIM5.

    PTM databases

    PhosphoSiteiQ4JIM5.

    Expressioni

    Tissue specificityi

    Most abundant in adult mouse brain, especially in synapse-rich regions.1 Publication

    Gene expression databases

    GenevestigatoriQ4JIM5.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    DIPiDIP-60989N.
    IntActiQ4JIM5. 2 interactions.
    STRINGi10090.ENSMUSP00000027888.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4JIM5.
    SMRiQ4JIM5. Positions 108-558, 1058-1182.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini107 – 16761SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 26391SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini288 – 539252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 106105CAPAdd
    BLAST
    Regioni695 – 930236F-actin-bindingAdd
    BLAST
    Regioni1020 – 1182163F-actin-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi427 – 45125Kinase activation loopBy similarityAdd
    BLAST
    Motifi659 – 6613Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi561 – 5644Poly-Ser
    Compositional biasi735 – 7417Poly-Gly
    Compositional biasi984 – 9885Poly-Pro

    Domaini

    Contains two distinct classes of F-actin-binding domains. Although both can each bind F-actin, the 2 are required to bundle actin filaments.2 Publications

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231988.
    HOVERGENiHBG004162.
    InParanoidiQ4JIM5.
    PhylomeDBiQ4JIM5.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR015015. F-actin_binding.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF08919. F_actin_bind. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00808. FABD. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q4JIM5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT     50
    QHDHFASCVE DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN 100
    LLGATESDPN LFVALYDFVA SGDNTLSITK GEKLRVLGYN QNGEWSEVRS 150
    KNGQGWVPSN YITPVNSLEK HSWYHGPVSR SAAEYLLSSL INGSFLVRES 200
    ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST LAELVHHHST 250
    VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG 300
    EVYVGVWKKY SLTVAVKTFK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV 350
    CTLEPPFYIV TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL 400
    EKKNFIHRDL AARNCLVGEN HVVKVADFGL SRLMTGDTYT AHAGAKFPIK 450
    WTAPESLAYN TFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYDLLEK 500
    GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE TMFHDSSISE 550
    EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE 600
    SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK 650
    GGFFSSFMKK RNAPTPPKRS SSFREMENQP HKKYELTGNF SPVASLQNAD 700
    GFSVAPSQQE PNLVPAKCYG GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI 750
    TGFFTPRLIK KTLGLRAGKP TASDDTSKPF PRSNSTSSMS SGLPEQDRMA 800
    MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE EGAAPARERP 850
    KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG 900
    VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG 950
    TDSQGNKFKL LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS 1000
    DPEEEPTAPP AGQHTPETQE GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT 1050
    SSISPAKMAN GTAGTKVALR KTKQAAEKIS ADKISKEALL ECADLLSSAI 1100
    TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV SKLELSLQEL 1150
    QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR 1182
    Length:1,182
    Mass (Da):128,196
    Last modified:August 2, 2005 - v1
    Checksum:i08507298A9081228
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ084361 mRNA. Translation: AAY86039.1.
    CCDSiCCDS15393.1.
    UniGeneiMm.329515.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ084361 mRNA. Translation: AAY86039.1 .
    CCDSi CCDS15393.1.
    UniGenei Mm.329515.

    3D structure databases

    ProteinModelPortali Q4JIM5.
    SMRi Q4JIM5. Positions 108-558, 1058-1182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60989N.
    IntActi Q4JIM5. 2 interactions.
    STRINGi 10090.ENSMUSP00000027888.

    Chemistry

    ChEMBLi CHEMBL5222.

    PTM databases

    PhosphoSitei Q4JIM5.

    Proteomic databases

    MaxQBi Q4JIM5.
    PaxDbi Q4JIM5.
    PRIDEi Q4JIM5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:87860. Abl2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231988.
    HOVERGENi HBG004162.
    InParanoidi Q4JIM5.
    PhylomeDBi Q4JIM5.

    Miscellaneous databases

    ChiTaRSi ABL2. mouse.
    PROi Q4JIM5.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q4JIM5.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR015015. F-actin_binding.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF08919. F_actin_bind. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00808. FABD. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin."
      Wang Y., Miller A.L., Mooseker M.S., Koleske A.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:14865-14870(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, SUBCELLULAR LOCATION, ACTIN-BINDING.
      Strain: 129/SvJImported.
    2. "Two distinct phosphorylation pathways have additive effects on Abl family kinase activation."
      Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.
      Mol. Cell. Biol. 23:3884-3896(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CAP DOMAIN, FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-684, MUTAGENESIS OF TYR-272; LYS-317; TYR-439; TYR-568 AND TYR-684.
      Strain: 129/SvJImported.
    3. "Essential roles for the Abl and Arg tyrosine kinases in neurulation."
      Koleske A.J., Gifford A.M., Scott M.L., Nee M., Bronson R.T., Miczek K.A., Baltimore D.
      Neuron 21:1259-1272(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, FUNCTION.
    4. "Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes."
      Kain K.H., Klemke R.L.
      J. Biol. Chem. 276:16185-16192(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases."
      Woodring P.J., Hunter T., Wang J.Y.
      J. Cell Sci. 116:2613-2626(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    6. "Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor."
      Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.
      Mol. Cell. Biol. 24:2573-2583(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION.
    7. "How do Abl family kinases regulate cell shape and movement?"
      Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.
      Trends Cell Biol. 14:36-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    8. "Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane."
      Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J.
      Mol. Biol. Cell 17:4827-4836(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Use of a chemical genetic technique to identify myosin IIb as a substrate of the Abl-related gene (Arg) tyrosine kinase."
      Boyle S.N., Koleske A.J.
      Biochemistry 46:11614-11620(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Emerging roles of Abl family tyrosine kinases in microbial pathogenesis."
      Backert S., Feller S.M., Wessler S.
      Trends Biochem. Sci. 33:80-90(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    11. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-632 AND SER-936, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "ABL tyrosine kinases: evolution of function, regulation, and specificity."
      Colicelli J.
      Sci. Signal. 3:RE6-RE6(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, DOMAIN.

    Entry informationi

    Entry nameiABL2_MOUSE
    AccessioniPrimary (citable) accession number: Q4JIM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: August 2, 2005
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3