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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)DescriptionActionsGraphical viewLength
Binding sitei317ATPPROSITE-ProRule annotation1 Publication1
Active sitei409Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi294 – 302ATPPROSITE-ProRule annotationBy similarity9
Nucleotide bindingi362 – 368ATPPROSITE-ProRule annotation7

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament bundle assembly Source: MGI
  • actin filament organization Source: MGI
  • alpha-beta T cell differentiation Source: MGI
  • Bergmann glial cell differentiation Source: MGI
  • cellular protein localization Source: MGI
  • cellular response to retinoic acid Source: MGI
  • cerebellum morphogenesis Source: MGI
  • dendrite morphogenesis Source: MGI
  • dendritic spine maintenance Source: MGI
  • epidermal growth factor receptor signaling pathway Source: MGI
  • exploration behavior Source: MGI
  • innate immune response Source: GO_Central
  • learning Source: MGI
  • negative regulation of cell-cell adhesion Source: MGI
  • negative regulation of endothelial cell apoptotic process Source: MGI
  • negative regulation of Rho protein signal transduction Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • neuron remodeling Source: MGI
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phagocytosis Source: MGI
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • positive regulation of cytosolic calcium ion concentration Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of interferon-gamma secretion Source: MGI
  • positive regulation of interleukin-2 secretion Source: MGI
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of oxidoreductase activity Source: MGI
  • positive regulation of phospholipase C activity Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: MGI
  • protein phosphorylation Source: UniProtKB
  • regulation of autophagy Source: InterPro
  • regulation of cell proliferation Source: GO_Central
  • regulation of endocytosis Source: InterPro
  • regulation of extracellular matrix organization Source: MGI
  • substrate-dependent cell migration, cell extension Source: MGI
  • 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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:87860. Abl2.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • cytoplasmic, membrane-bounded vesicle Source: MGI
  • dendritic spine Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • lamellipodium Source: MGI
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi272Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi317K → M: Loss of kinase activity. 1 Publication1
Mutagenesisi439Y → F: Partial reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi568Y → F: No reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi684Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5222.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002580192 – 1182Abelson tyrosine-protein kinase 2Add BLAST1181

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei97PhosphoserineBy similarity1
Modified residuei116PhosphotyrosineBy similarity1
Modified residuei161PhosphotyrosineBy similarity1
Modified residuei174PhosphotyrosineBy similarity1
Modified residuei185PhosphotyrosineBy similarity1
Modified residuei218PhosphotyrosineBy similarity1
Modified residuei231PhosphotyrosineBy similarity1
Modified residuei261Phosphotyrosine; by ABL1 and autocatalysisBy similarity1
Modified residuei272Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei275PhosphoserineBy similarity1
Modified residuei299PhosphotyrosineBy similarity1
Modified residuei303PhosphotyrosineBy similarity1
Modified residuei439Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinasesBy similarity1
Modified residuei459PhosphotyrosineBy similarity1
Modified residuei492PhosphoserineBy similarity1
Modified residuei568Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei606PhosphoserineBy similarity1
Modified residuei621PhosphoserineCombined sources1
Modified residuei632PhosphoserineCombined sources1
Modified residuei634PhosphoserineBy similarity1
Modified residuei656PhosphoserineBy similarity1
Modified residuei670PhosphoserineBy similarity1
Modified residuei671PhosphoserineBy similarity1
Modified residuei672PhosphoserineBy similarity1
Modified residuei684Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei719PhosphotyrosineBy similarity1
Modified residuei778N6-acetyllysineBy similarity1
Modified residuei785PhosphoserineBy similarity1
Modified residuei802PhosphothreonineBy similarity1
Modified residuei819PhosphoserineBy similarity1
Modified residuei822PhosphoserineCombined sources1
Modified residuei915PhosphoserineBy similarity1
Modified residuei936PhosphoserineCombined sources1

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

EPDiQ4JIM5.
MaxQBiQ4JIM5.
PaxDbiQ4JIM5.
PeptideAtlasiQ4JIM5.
PRIDEiQ4JIM5.

PTM databases

iPTMnetiQ4JIM5.
PhosphoSitePlusiQ4JIM5.

Expressioni

Tissue specificityi

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

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 interactors.
STRINGi10090.ENSMUSP00000027888.

Chemistry databases

BindingDBiQ4JIM5.

Structurei

Secondary structure

11182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi285 – 287Combined sources3
Beta strandi288 – 295Combined sources8
Beta strandi302 – 307Combined sources6
Helixi308 – 310Combined sources3
Beta strandi312 – 319Combined sources8
Helixi327 – 337Combined sources11
Beta strandi347 – 351Combined sources5
Beta strandi353 – 362Combined sources10
Helixi369 – 375Combined sources7
Turni378 – 380Combined sources3
Helixi383 – 402Combined sources20
Helixi412 – 414Combined sources3
Beta strandi415 – 417Combined sources3
Helixi419 – 421Combined sources3
Beta strandi423 – 425Combined sources3
Beta strandi435 – 437Combined sources3
Helixi449 – 451Combined sources3
Helixi454 – 459Combined sources6
Helixi464 – 479Combined sources16
Helixi491 – 493Combined sources3
Helixi494 – 499Combined sources6
Helixi512 – 521Combined sources10
Helixi526 – 528Combined sources3
Helixi532 – 545Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XLIX-ray2.50A/B279-546[»]
ProteinModelPortaliQ4JIM5.
SMRiQ4JIM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini107 – 167SH3PROSITE-ProRule annotationAdd BLAST61
Domaini173 – 263SH2PROSITE-ProRule annotationAdd BLAST91
Domaini288 – 539Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 106CAPAdd BLAST105
Regioni695 – 930F-actin-bindingAdd BLAST236
Regioni1020 – 1182F-actin-bindingAdd BLAST163

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi427 – 451Kinase activation loopBy similarityAdd BLAST25
Motifi659 – 661Nuclear localization signalSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi561 – 564Poly-Ser4
Compositional biasi735 – 741Poly-Gly7
Compositional biasi984 – 988Poly-Pro5

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000231988.
HOVERGENiHBG004162.
InParanoidiQ4JIM5.
PhylomeDBiQ4JIM5.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033217. ABL2.
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]
PANTHERiPTHR24418:SF87. PTHR24418:SF87. 1 hit.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XLIX-ray2.50A/B279-546[»]
ProteinModelPortaliQ4JIM5.
SMRiQ4JIM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiQ4JIM5.
ChEMBLiCHEMBL5222.

PTM databases

iPTMnetiQ4JIM5.
PhosphoSitePlusiQ4JIM5.

Proteomic databases

EPDiQ4JIM5.
MaxQBiQ4JIM5.
PaxDbiQ4JIM5.
PeptideAtlasiQ4JIM5.
PRIDEiQ4JIM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:87860. Abl2.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000231988.
HOVERGENiHBG004162.
InParanoidiQ4JIM5.
PhylomeDBiQ4JIM5.

Miscellaneous databases

ChiTaRSiAbl2. mouse.
PROiQ4JIM5.
SOURCEiSearch...

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033217. ABL2.
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]
PANTHERiPTHR24418:SF87. PTHR24418:SF87. 1 hit.
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...

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: November 2, 2016
This is version 101 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

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.