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Protein

Abelson tyrosine-protein kinase 2

Gene

Abl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.PROSITE-ProRule annotation1 Publication

Cofactori

Mg2+1 Publication, Mn2+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 – 3171ATPPROSITE-ProRule annotation1 Publication
Active sitei409 – 4091Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 3029ATPPROSITE-ProRule annotationBy similarity
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: GO_Central
  5. protein tyrosine kinase activity Source: UniProtKB
  6. receptor binding Source: GO_Central

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. actin filament bundle assembly Source: MGI
  3. actin filament organization Source: MGI
  4. alpha-beta T cell differentiation Source: MGI
  5. Bergmann glial cell differentiation Source: MGI
  6. cell migration Source: GO_Central
  7. cellular protein localization Source: MGI
  8. cellular response to retinoic acid Source: MGI
  9. cerebellum morphogenesis Source: MGI
  10. dendrite morphogenesis Source: MGI
  11. dendritic spine maintenance Source: MGI
  12. epidermal growth factor receptor signaling pathway Source: MGI
  13. exploration behavior Source: MGI
  14. innate immune response Source: GO_Central
  15. learning Source: MGI
  16. negative regulation of cell-cell adhesion Source: MGI
  17. negative regulation of endothelial cell apoptotic process Source: MGI
  18. negative regulation of Rho protein signal transduction Source: MGI
  19. neuromuscular process controlling balance Source: MGI
  20. neuron remodeling Source: MGI
  21. peptidyl-tyrosine autophosphorylation Source: GO_Central
  22. peptidyl-tyrosine phosphorylation Source: UniProtKB
  23. phagocytosis Source: MGI
  24. platelet-derived growth factor receptor signaling pathway Source: MGI
  25. positive regulation of cytosolic calcium ion concentration Source: MGI
  26. positive regulation of ERK1 and ERK2 cascade Source: MGI
  27. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  28. positive regulation of interferon-gamma secretion Source: MGI
  29. positive regulation of interleukin-2 secretion Source: MGI
  30. positive regulation of neuron projection development Source: MGI
  31. positive regulation of oxidoreductase activity Source: MGI
  32. positive regulation of phospholipase C activity Source: MGI
  33. positive regulation of protein binding Source: MGI
  34. positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: MGI
  35. protein phosphorylation Source: UniProtKB
  36. regulation of apoptotic process Source: GO_Central
  37. regulation of cell proliferation Source: GO_Central
  38. regulation of extracellular matrix organization Source: MGI
  39. substrate-dependent cell migration, cell extension Source: MGI
  40. visual learning Source: MGI
Complete GO annotation...

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
  3. dendritic spine Source: MGI
  4. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  5. lamellipodium Source: MGI
  6. phagocytic cup Source: MGI
Complete GO annotation...

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 – 11Removed
Chaini2 – 11821181Abelson tyrosine-protein kinase 2PRO_0000258019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei116 – 1161PhosphotyrosineBy similarity
Modified residuei161 – 1611PhosphotyrosineBy similarity
Modified residuei174 – 1741PhosphotyrosineBy similarity
Modified residuei185 – 1851PhosphotyrosineBy similarity
Modified residuei218 – 2181PhosphotyrosineBy similarity
Modified residuei231 – 2311PhosphotyrosineBy similarity
Modified residuei261 – 2611Phosphotyrosine; by ABL1 and autocatalysisBy similarity
Modified residuei272 – 2721Phosphotyrosine; by autocatalysis1 Publication
Modified residuei275 – 2751PhosphoserineBy similarity
Modified residuei299 – 2991PhosphotyrosineBy similarity
Modified residuei303 – 3031PhosphotyrosineBy similarity
Modified residuei310 – 3101PhosphotyrosineBy similarity
Modified residuei438 – 4381PhosphothreonineBy similarity
Modified residuei439 – 4391Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinasesBy similarity
Modified residuei440 – 4401PhosphothreonineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity
Modified residuei515 – 5151PhosphotyrosineBy similarity
Modified residuei568 – 5681Phosphotyrosine; by autocatalysis1 Publication
Modified residuei621 – 6211Phosphoserine1 Publication
Modified residuei632 – 6321Phosphoserine1 Publication
Modified residuei634 – 6341PhosphoserineBy similarity
Modified residuei656 – 6561PhosphoserineBy similarity
Modified residuei665 – 6651PhosphothreonineBy similarity
Modified residuei670 – 6701PhosphoserineBy similarity
Modified residuei671 – 6711PhosphoserineBy similarity
Modified residuei672 – 6721PhosphoserineBy similarity
Modified residuei684 – 6841Phosphotyrosine; by autocatalysis1 Publication
Modified residuei719 – 7191PhosphotyrosineBy similarity
Modified residuei778 – 7781N6-acetyllysineBy similarity
Modified residuei785 – 7851PhosphoserineBy similarity
Modified residuei802 – 8021PhosphothreonineBy similarity
Modified residuei819 – 8191PhosphoserineBy similarity
Modified residuei822 – 8221PhosphoserineBy similarity
Modified residuei876 – 8761PhosphoserineBy similarity
Modified residuei915 – 9151PhosphoserineBy similarity
Modified residuei936 – 9361Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress (By similarity). Phosphorylated by PDGFRB.By similarity2 Publications
Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, 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

        10         20         30         40         50
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT
60 70 80 90 100
QHDHFASCVE DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN
110 120 130 140 150
LLGATESDPN LFVALYDFVA SGDNTLSITK GEKLRVLGYN QNGEWSEVRS
160 170 180 190 200
KNGQGWVPSN YITPVNSLEK HSWYHGPVSR SAAEYLLSSL INGSFLVRES
210 220 230 240 250
ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST LAELVHHHST
260 270 280 290 300
VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG
310 320 330 340 350
EVYVGVWKKY SLTVAVKTFK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV
360 370 380 390 400
CTLEPPFYIV TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL
410 420 430 440 450
EKKNFIHRDL AARNCLVGEN HVVKVADFGL SRLMTGDTYT AHAGAKFPIK
460 470 480 490 500
WTAPESLAYN TFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYDLLEK
510 520 530 540 550
GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE TMFHDSSISE
560 570 580 590 600
EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE
610 620 630 640 650
SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK
660 670 680 690 700
GGFFSSFMKK RNAPTPPKRS SSFREMENQP HKKYELTGNF SPVASLQNAD
710 720 730 740 750
GFSVAPSQQE PNLVPAKCYG GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI
760 770 780 790 800
TGFFTPRLIK KTLGLRAGKP TASDDTSKPF PRSNSTSSMS SGLPEQDRMA
810 820 830 840 850
MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE EGAAPARERP
860 870 880 890 900
KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG
910 920 930 940 950
VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG
960 970 980 990 1000
TDSQGNKFKL LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS
1010 1020 1030 1040 1050
DPEEEPTAPP AGQHTPETQE GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT
1060 1070 1080 1090 1100
SSISPAKMAN GTAGTKVALR KTKQAAEKIS ADKISKEALL ECADLLSSAI
1110 1120 1130 1140 1150
TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV SKLELSLQEL
1160 1170 1180
QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR
Length:1,182
Mass (Da):128,196
Last modified:August 2, 2005 - v1
Checksum:i08507298A9081228
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ084361 mRNA. Translation: AAY86039.1.
CCDSiCCDS15393.1.
UniGeneiMm.329515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ084361 mRNA. Translation: AAY86039.1.
CCDSiCCDS15393.1.
UniGeneiMm.329515.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiQ4JIM5.
ChEMBLiCHEMBL5222.

PTM databases

PhosphoSiteiQ4JIM5.

Proteomic databases

MaxQBiQ4JIM5.
PaxDbiQ4JIM5.
PRIDEiQ4JIM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:87860. Abl2.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000231988.
HOVERGENiHBG004162.
InParanoidiQ4JIM5.
PhylomeDBiQ4JIM5.

Miscellaneous databases

ChiTaRSiAbl2. mouse.
PROiQ4JIM5.
SOURCEiSearch...

Gene expression databases

GenevestigatoriQ4JIM5.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 90 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.