Abelson tyrosine-protein kinase 2

NameAbelson tyrosine-protein kinase 2
Synonyms2.7.10.2 Abelson murine leukemia viral oncogene homolog 2 Abelson-related gene protein ABLL ARG Tyrosine-protein kinase ARG
Gene NameABL2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0000867|Abelson tyrosine-protein kinase 2
MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQHDHFASCVE
DGFEGDKTGGSSPEALHRPYGCDVEPQALNEAIRWSSKENLLGATESDPNLFVALYDFVA
SGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSR
SAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTADGKVYVTAESRFST
LAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYG
EVYVGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIV
TEYMPYGNLLDYLRECNREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGEN
HVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIAT
YGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFE
TMFHDSSISEEVAEELGRAASSSSVVPYLPRLPILPSKTRTLKKQVENKENIEGAQDATE
NSASSLAPGFIRGAQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKR
NAPTPPKRSSSFREMENQPHKKYELTGNFSSVASLQHADGFSFTPAQQEANLVPPKCYGG
SFAQRNLCNDDGGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPR
SNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEES
AAPSRERPKAKLLPRGATALPLRTPSGDLAITEKDPPGVGVAGVAAAPKGKEKNGGARLG
MAGVPEDGEQPGWPSPAKAAPVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKL
LSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSICSDPTEEPTALTAGQSTSETQE
GGKKAALGAVPISGKAGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKIS
ADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAV
SKLELSLQELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR
Number of residues1182
Molecular Weight128341.935
Theoretical pI8.17
GO Classification
Functions
    non-membrane spanning protein tyrosine kinase activity
magnesium ion binding
actin filament binding
ATP binding
protein kinase activity
actin monomer binding
receptor binding
protein tyrosine kinase activity
manganese ion binding
Processes
    regulation of actin cytoskeleton reorganization
cell differentiation
cellular protein localization
regulation of autophagy
phagocytosis
cell migration
exploration behavior
regulation of cell proliferation
visual learning
cellular protein modification process
regulation of endocytosis
regulation of cell motility
positive regulation of neuron projection development
epidermal growth factor receptor signaling pathway
Bergmann glial cell differentiation
cellular response to retinoic acid
regulation of cell adhesion
innate immune response
neuron remodeling
positive regulation of Wnt signaling pathway, planar cell polarity pathway
dendrite morphogenesis
regulation of apoptotic process
alpha-beta T cell differentiation
peptidyl-tyrosine autophosphorylation
dendritic spine maintenance
positive regulation of interleukin-2 secretion
signal transduction
substrate-dependent cell migration, cell extension
negative regulation of Rho protein signal transduction
peptidyl-tyrosine phosphorylation
actin filament bundle assembly
cerebellum morphogenesis
positive regulation of ERK1 and ERK2 cascade
positive regulation of I-kappaB kinase/NF-kappaB signaling
platelet-derived growth factor receptor signaling pathway
negative regulation of cell-cell adhesion
positive regulation of phospholipase C activity
positive regulation of protein binding
positive regulation of cytosolic calcium ion concentration
regulation of extracellular matrix organization
negative regulation of endothelial cell apoptotic process
positive regulation of interferon-gamma secretion
positive regulation of oxidoreductase activity
neuromuscular process controlling balance
axon guidance
Components
    dendritic spine
actin cytoskeleton
phagocytic cup
cytosol
extrinsic component of cytoplasmic side of plasma membrane
lamellipodium
General FunctionReceptor binding
Specific FunctionNon-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 and receptor endocytosis. 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, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 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. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1.
Transmembrane Regions
GenBank Protein ID178993
UniProtKB IDP42684
UniProtKB Entry NameABL2_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0021263|Abelson tyrosine-protein kinase 2 (ABL2)
ATGGTCCTTGGGACAGTTCTCCTTCCACCTAATAGTTATGGCAGAGATCAGGACACTTCA
CTTTGCTGCCTGTGCACTGAGGCCTCAGAATCTGCTCTACCCGACTTAACAGATCACTTT
GCCAGCTGTGTGGAGGATGGATTTGAGGGAGACAAGACTGGAGGCAGTAGTCCAGAAGCT
TTGCATCGTCCCTATGGTTGTGATGTTGAACCCCAGGCACTAAATGAGGCTATCAGGTGG
AGCTCCAAGGAGAACTTGCTCGGAGCCACTGAGAGTGACCCTAATCTCTTCGTTGCACTT
TATGATTTTGTAGCAAGTGGTGATAACACACTCAGCATCACTAAAGGTGAAAAGCTACGA
GTCCTTGGTTACAACCAGAATGGTGAGTGGAGTGAAGTTCGCTCTAAGAATGGGCAGGGC
TGGGTGCCAAGCAACTACATCACCCCAGTGAACAGCCTGGAAAAACACTCCTGGTACCAT
GGACCTGTGTCACGCAGTGCAGCTGAGTATCTGCTCAGCAGTCTAATCAATGGCAGCTTC
CTGGTGCGAGAAAGTGAGAGTAGCCCTGGGCAGCTGTCCATCTCGCTCAGGTACGAGGGA
CGTGTGTATCACTACAGGATCAATACCACTGCAGATGGCAAGGTGTATGTGACTGCTGAG
AGCCGCTTCAGCACCTTGGCAGAGCTTGTACACCATCACTCCACAGTGGCTGATGGGCTG
GTGACAACATTACACTACCCAGCACCCAAGTGTAATAAGCCTACAGTCTATGGTGTGTCC
CCCATCCACGACAAATGGGAAATGGAGCGAACAGATATTACCATGAAGCACAAACTTGGG
GGCGGTCAGTATGGAGAGGTTTACGTTGGCGTCTGGAAGAAATACAGCCTTACAGTTGCT
GTGAAAACATTGAAGGAAGATACCATGGAGGTAGAAGAATTCCTGAAAGAAGCTGCAGTA
ATGAAGGAAATCAAGCATCCTAATCTGGTACAACTTTTAGGTGTGTGTACTTTGGAGCCA
CCATTTTACATTGTGACTGAATACATGCCATACGGGAATTTGCTGGATTACCTCCGAGAA
TGCAACCGAGAAGAGGTGACTGCAGTTGTGCTGCTCTACATGGCCACTCAGATTTCTTCT
GCAATGGAGTACTTAGAGAAGAAGAATTTCATCCATAGAGATCTTGCAGCTCGTAACTGC
CTAGTGGGAGAAAACCATGTGGTAAAAGTGGCTGACTTTGGCTTAAGTAGATTGATGACT
GGAGACACTTATACTGCTCATGCTGGAGCCAAATTTCCTATTAAGTGGACAGCACCAGAG
AGTCTTGCCTACAATACCTTCTCAATTAAATCTGACGTCTGGGCTTTTGGGGTATTGTTG
TGGGAAATTGCTACCTATGGAATGTCACCATATCCAGGTATTGACCTGTCTCAGGTCTAT
GACCTACTAGAAAAAGGATATCGAATGGAACAGCCTGAGGGATGCCCCCCTAAGGTTTAT
GAACTTATGAGAGCATGCTGGAAGTGGAGCCCTGCCGATAGGCCCTCTTTTGCTGAAACA
CACCAAGCTTTTGAAACCATGTTCCATGACTCCAGCATTTCTGAAGAGGTAGCTGAGGAG
CTTGGGAGAGCCGCCTCCTCGTCATCTGTTGTTCCATACCTGCCCCGGCTACCTATACTT
CCTTCCAAGACTCGGACACTGAAGAAACAGGTGGAGAACAAGGAGAACATTGAAGGGGCA
CAAGATGCCACAGAAAATTCTGCTTCCAGTTTAGCACCAGGGTTCATCAGAGGTGCACAG
GCCTCTAGTGGATCCCCAGCACTGCCTCGAAAGCAAAGAGACAAGTCACCCAGCAGCCTC
TTGGAAGATGCCAAAGAGACATGCTTCACCAGGGATAGGAAGGGGGGCTTCTTCAGCTCC
TTCATGAAGAAGAGAAATGCTCCTACACCCCCCAAACGCAGCAGCTCCTTCCGAGAAATG
GAGAATCAGCCCCATAAGAAATACGAACTCACGGGGCTTCCAGAGCAGGATAGGATGGCA
ATGACCCTTCCCAGGAACTGCCAGAGGTCCAAACTCCAGCTGGAAAGGACAGTGTCCACC
TCTTCTCAGCCAGAAGAGAATGTGGACAGGGCCAATGACATGCTTCCAAAAAAATCAGAG
GAAAGTGCTGCTCCAAGCAGGGAGAGACCAAAAGCCAAGTTATTGCCCAGAGGAGCCACA
GCTCTTCCTCTCAGAACACCCTCTGGGGATCTAGCCATTACAGAGAAGGACCCTCCAGGG
GTGGGAGTGGCTGGAGTGGCAGCTGCCCCCAAGGGTAAAGAGAAGAATGGTGGGGCACGA
CTTGGGATGGCTGGAGTTCCAGAGGATGGAGAGCAGCCGGGCTGGCCTTCTCCAGCCAAG
GCTGCCCCCGTCCTCCCAACCACTCACAACCACAAAGTGCCAGTCCTTATCTCACCCACT
CTGAAACACACTCCAGCTGACGTGCAGCTCATTGGCACAGACTCTCAGGGGAATAAATTC
AAGCTCTTATCTGAGCATCAGGTCACATCCTCTGGAGACAAGGACCGACCCCGACGGGTA
AAACCAAAGTGTGCCCCACCCCCACCACCAGTGATGAGACTACTGCAGCATCCGTCCATC
TGCTCAGACCCTACAGAAGAGCCAACTGCCCTAACTGCAGGACAGTCCACATCAGAAACA
CAGGAAGGAGGAAAGAAGGCAGCTCTGGGCGCAGTGCCCATCAGTGGGAAAGCTGGGAGG
CCAGTGATGCCTCCACCTCAAGTGCCTCTGCCCACATCTTCCATCTCGCCAGCCAAAATG
GCCAATGGCACAGCAGGTACTAAAGTGGCTCTGAGAAAAACCAAACAGGCCGCTGAGAAA
ATCTCAGCAGACAAAATCAGCAAAGAGGCCCTGCTGGAATGTGCTGACCTACTGTCCAGT
GCACTCACGGAACCTGTGCCCAACAGCCAGCTGGTAGACACTGGACACCAGCTGCTTGAC
TACTGCTCAGGCTATGTGGACTGCATCCCTCAAACTCGCAACAAATTTGCCTTCCGAGAG
GCTGTGAGCAAACTGGAACTCAGCCTGCAGGAGCTACAGGTTTCTTCAGCAGCTGCTGGT
GTGCCCGGGACAAACCCTGTCCTTAATAACTTATTGTCATGTGTACAGGAAATCAGTGAT
GTGGTGCAGAGGTAG
GenBank Gene IDM35296
GeneCard IDNone
GenAtlas IDABL2
HGNC IDHGNC:77
Chromosome Location1
Locus1q24-q25
References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21.[14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7.[15489334 ]
  3. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8.[17344846 ]
  4. Kruh GD, Perego R, Miki T, Aaronson SA: The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases. Proc Natl Acad Sci U S A. 1990 Aug;87(15):5802-6.[2198571 ]
  5. Bianchi C, Torsello B, Angeloni V, Bombelli S, Soldi M, Invernizzi L, Brambilla P, Perego RA: Eight full-length abelson related gene (Arg) isoforms are constitutively expressed in caki-1 cell line and cell distribution of two isoforms has been analyzed after transfection. J Cell Biochem. 2008 Dec 1;105(5):1219-27. doi: 10.1002/jcb.21922.[18810762 ]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399.[17974005 ]
  7. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21.[16710414 ]
  8. Liu W, MacGrath SM, Koleske AJ, Boggon TJ: Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):154-8. doi: 10.1107/S1744309111056132. Epub 2012 Jan 25.[22297987 ]
  9. Kruh GD, King CR, Kraus MH, Popescu NC, Amsbaugh SC, McBride WO, Aaronson SA: A novel human gene closely related to the abl proto-oncogene. Science. 1986 Dec 19;234(4783):1545-8.[3787260 ]
  10. Tanis KQ, Veach D, Duewel HS, Bornmann WG, Koleske AJ: Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol Cell Biol. 2003 Jun;23(11):3884-96.[12748290 ]
  11. Hu H, Bliss JM, Wang Y, Colicelli J: RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial-cell adhesion and migration. Curr Biol. 2005 May 10;15(9):815-23.[15886098 ]
  12. Cao C, Li Y, Leng Y, Li P, Ma Q, Kufe D: Ubiquitination and degradation of the Arg tyrosine kinase is regulated by oxidative stress. Oncogene. 2005 Apr 7;24(15):2433-40.[15735735 ]
  13. Liu X, Huang W, Li C, Li P, Yuan J, Li X, Qiu XB, Ma Q, Cao C: Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation. Mol Cell. 2006 May 5;22(3):317-27.[16678104 ]
  14. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10.[16964243 ]
  15. Boyle SN, Michaud GA, Schweitzer B, Predki PF, Koleske AJ: A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation. Curr Biol. 2007 Mar 6;17(5):445-51. Epub 2007 Feb 15.[17306540 ]
  16. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6.[17525332 ]
  17. Yogalingam G, Pendergast AM: Abl kinases regulate autophagy by promoting the trafficking and function of lysosomal components. J Biol Chem. 2008 Dec 19;283(51):35941-53. doi: 10.1074/jbc.M804543200. Epub 2008 Oct 21.[18945674 ]
  18. Woodring PJ, Hunter T, Wang JY: Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases. J Cell Sci. 2003 Jul 1;116(Pt 13):2613-26.[12775773 ]
  19. Hernandez SE, Krishnaswami M, Miller AL, Koleske AJ: How do Abl family kinases regulate cell shape and movement? Trends Cell Biol. 2004 Jan;14(1):36-44.[14729179 ]
  20. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007.[18691976 ]
  21. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31.[18669648 ]
  22. Backert S, Feller SM, Wessler S: Emerging roles of Abl family tyrosine kinases in microbial pathogenesis. Trends Biochem Sci. 2008 Feb;33(2):80-90. doi: 10.1016/j.tibs.2007.10.006. Epub 2008 Jan 7.[18182299 ]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309.[19413330 ]
  24. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15.[19369195 ]
  25. Vepachedu R, Karim Z, Patel O, Goplen N, Alam R: Unc119 protects from Shigella infection by inhibiting the Abl family kinases. PLoS One. 2009;4(4):e5211. doi: 10.1371/journal.pone.0005211. Epub 2009 Apr 17.[19381274 ]
  26. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007.[19690332 ]
  27. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475.[20068231 ]
  28. Colicelli J: ABL tyrosine kinases: evolution of function, regulation, and specificity. Sci Signal. 2010 Sep 14;3(139):re6. doi: 10.1126/scisignal.3139re6.[20841568 ]
  29. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570.[21406692 ]
  30. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22.[24275569 ]
  31. Salah E, Ugochukwu E, Barr AJ, von Delft F, Knapp S, Elkins JM: Crystal structures of ABL-related gene (ABL2) in complex with imatinib, tozasertib (VX-680), and a type I inhibitor of the triazole carbothioamide class. J Med Chem. 2011 Apr 14;54(7):2359-67. doi: 10.1021/jm101506n. Epub 2011 Mar 18.[21417343 ]

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