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Q4JIM5

- ABL2_MOUSE

UniProt

Q4JIM5 - ABL2_MOUSE

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Protein
Abelson tyrosine-protein kinase 2
Gene
Abl2, Arg
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 Publication

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei317 – 3171ATP1 Publication
Active sitei409 – 4091Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 3029ATP By similarityBy similarity
Nucleotide bindingi362 – 3687ATP By similarity

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
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:Abl2
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
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 By similarity
Chaini2 – 11821181Abelson tyrosine-protein kinase 2
PRO_0000258019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarityBy similarity
Modified residuei261 – 2611Phosphotyrosine; by ABL1 and autocatalysis By similarity
Modified residuei272 – 2721Phosphotyrosine; by autocatalysis1 Publication
Modified residuei275 – 2751Phosphoserine By similarity
Modified residuei439 – 4391Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases By similarity1 Publication
Modified residuei568 – 5681Phosphotyrosine; by autocatalysis1 Publication
Modified residuei621 – 6211Phosphoserine1 Publication
Modified residuei632 – 6321Phosphoserine1 Publication
Modified residuei634 – 6341Phosphoserine By similarity
Modified residuei656 – 6561Phosphoserine By similarity
Modified residuei684 – 6841Phosphotyrosine; by autocatalysis1 Publication
Modified residuei719 – 7191Phosphotyrosine By similarity
Modified residuei819 – 8191Phosphoserine By similarity
Modified residuei822 – 8221Phosphoserine By similarity
Modified residuei915 – 9151Phosphoserine By similarity
Modified residuei936 – 9361Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress By similarity. Phosphorylated by PDGFRB.2 Publications
Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation 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.1 Publication

Protein-protein interaction databases

IntActiQ4JIM5. 2 interactions.
STRINGi10090.ENSMUSP00000027888.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 16761SH3
Add
BLAST
Domaini173 – 26391SH2
Add
BLAST
Domaini288 – 539252Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 106105CAP
Add
BLAST
Regioni695 – 930236F-actin-binding
Add
BLAST
Regioni1020 – 1182163F-actin-binding
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi427 – 45125Kinase activation loop By similarity
Add
BLAST
Motifi659 – 6613Nuclear localization signal Reviewed prediction

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.3 Publications

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

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

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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

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

« 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/SvJ.
  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/SvJ.
  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: July 9, 2014
This is version 84 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

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