Tyrosine-protein kinase ABL2 - Mus musculus (Mouse)

Sequence

>sp|Q4JIM5|ABL2_MOUSE Tyrosine-protein kinase ABL2 OS=Mus musculus GN=Abl2 PE=1 SV=1 MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTADAGFNVFTQHDHFASCVE DGFEGDKTGGSSPEVLHRPFGCDAESQALNEAIRWSSKENLLGATESDPNLFVALYDFVA SGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSR SAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTTDSKVYVTAESRFST LAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYG EVYVGVWKKYSLTVAVKTFKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIV TEYMPYGNLLDYLRECSREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGEN HVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIAT YGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFE TMFHDSSISEEVAEELGRTASSSSVVPYLPRLPLLPSKTRTLRKQGENKENLDGGLDAAE SLASSSAPAGFIRSTQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKK RNAPTPPKRSSSFREMENQPHKKYELTGNFSPVASLQNADGFSVAPSQQEPNLVPAKCYG GSFAQRNLCADDDSGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPF PRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSE EGAAPARERPKAKLLPRGATALPLRAPDPAITESDSPGVGVAGVAAAPKGKERNGGTRLG VAGVPEDGEQLGWSSPAKAVAVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKL LSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSTCSDPEEEPTAPPAGQHTPETQE GGKKAAPGPVPSSGKPGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKIS ADKISKEALLECADLLSSAITEPVPNSQLVDTGHQLLDYCSGYVDSIPQTRNKFAFREAV SKLELSLQELQVSSTAAGVPGTNPVLNNLLSCVQEISDVVQR

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Reviewed, UniProtKB/Swiss-Prot Q4JIM5 (ABL2_MOUSE)

Last modified June 16, 2009. Version 39. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Tyrosine-protein kinase ABL2
    EC=2.7.10.2
Alternative name(s):
    Abelson murine leukemia viral oncogene homolog 2
    Abelson-related gene protein
    Tyrosine kinase ARG

Gene names

Name:	Abl2
Synonyms:	Arg

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	1182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Regulates cytoskeleton remodeling during cell differentiation, cell division and cell adhesion. Localizes to dynamic actin structures, and phosphorylates CRK and CRKL, DOK1, and other proteins controlling cytoskeleton dynamics. Ref.1 Ref.2
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.2
Cofactor	Magnesium or manganese. Ref.2
Enzyme regulation	Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the amino-terminal cap, and contributions from an amino-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. Inhibited by imatinib mesylate (Gleevec). Ref.2
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

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Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cytoplasm Cytoskeleton
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein
Gene Ontology (GO)
Biological process	actin filament bundle formation Ref.1 Inferred from direct assay. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine phosphorylation Ref.2 Inferred from direct assay. Source: UniProtKB
Cellular component	actin cytoskeleton Ref.1 Inferred from direct assay. Source: MGI cytoplasmic membrane-bounded vesicle Traceable author statement. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Ref.2 Inferred from direct assay. Source: UniProtKB manganese ion binding Ref.2 Inferred from direct assay. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 1182

1181

Tyrosine-protein kinase ABL2

PRO_0000258019

Regions

Domain

107 – 167

SH3

Domain

173 – 263

SH2

Domain

288 – 539

252

Protein kinase

Nucleotide binding

294 – 302

ATP By similarity UniProtKB P28523

Region

2 – 106

105

CAP

Motif

658 – 660

Nuclear localization signal Potential

Sites

Active site

409

Proton acceptor By similarity UniProtKB P28523

Binding site

317

ATP Ref.2

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

116

Phosphotyrosine By similarity

Modified residue

203

Phosphoserine By similarity

Modified residue

231

Phosphotyrosine By similarity UniProtKB P00519

Modified residue

272

Phosphotyrosine; by autocatalysis Ref.2

Modified residue

275

Phosphoserine By similarity

Modified residue

299

Phosphotyrosine By similarity UniProtKB P00519

Modified residue

303

Phosphotyrosine By similarity UniProtKB P00519

Modified residue

310

Phosphotyrosine By similarity UniProtKB P00519

Modified residue

439

Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.2 Ref.3

Modified residue

440

Phosphothreonine By similarity UniProtKB P00519

Modified residue

492

Phosphoserine By similarity UniProtKB P00519

Modified residue

515

Phosphotyrosine By similarity UniProtKB P00519

Modified residue

568

Phosphotyrosine; by autocatalysis Ref.2

Modified residue

621

Phosphoserine

Modified residue

632

Phosphoserine By similarity

Modified residue

634

Phosphoserine By similarity

Modified residue

656

Phosphoserine By similarity

Modified residue

672

Phosphoserine By similarity

Modified residue

684

Phosphotyrosine; by autocatalysis Ref.2

Modified residue

719

Phosphotyrosine By similarity

Modified residue

785

Phosphoserine By similarity

Modified residue

819

Phosphoserine By similarity

Modified residue

822

Phosphoserine By similarity

Modified residue

915

Phosphoserine By similarity

Modified residue

936

Phosphoserine By similarity

Lipidation

N-myristoyl glycine By similarity UniProtKB P00519

Experimental info

Mutagenesis

272

Y → F: Minimal reduction in ability to autophosphorylate. Ref.2

Mutagenesis

317

K → M: Loss of kinase activity. Ref.2

Mutagenesis

439

Y → F: Partial reduction in ability to autophosphorylate. Ref.2

Mutagenesis

568

Y → F: No reduction in ability to autophosphorylate. Ref.2

Mutagenesis

684

Y → F: Minimal reduction in ability to autophosphorylate. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q4JIM5-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 08507298A9081228
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FASTA

1,182

128,196

        10         20         30         40         50         60 
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT QHDHFASCVE 

        70         80         90        100        110        120 
DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA 

       130        140        150        160        170        180 
SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR 

       190        200        210        220        230        240 
SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST 

       250        260        270        280        290        300 
LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG 

       310        320        330        340        350        360 
EVYVGVWKKY SLTVAVKTFK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV 

       370        380        390        400        410        420 
TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN 

       430        440        450        460        470        480 
HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT 

       490        500        510        520        530        540 
YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE 

       550        560        570        580        590        600 
TMFHDSSISE EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE 

       610        620        630        640        650        660 
SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK GGFFSSFMKK 

       670        680        690        700        710        720 
RNAPTPPKRS SSFREMENQP HKKYELTGNF SPVASLQNAD GFSVAPSQQE PNLVPAKCYG 

       730        740        750        760        770        780 
GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI TGFFTPRLIK KTLGLRAGKP TASDDTSKPF 

       790        800        810        820        830        840 
PRSNSTSSMS SGLPEQDRMA MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE 

       850        860        870        880        890        900 
EGAAPARERP KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG 

       910        920        930        940        950        960 
VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL 

       970        980        990       1000       1010       1020 
LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS DPEEEPTAPP AGQHTPETQE 

      1030       1040       1050       1060       1070       1080 
GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS 

      1090       1100       1110       1120       1130       1140 
ADKISKEALL ECADLLSSAI TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV 

      1150       1160       1170       1180 
SKLELSLQEL QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11752434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. 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: 12748290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CAP DOMAIN, FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, AUTOPHOSPHORYLATION 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]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, MASS SPECTROMETRY. Tissue: Brain.
[4]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936, MASS SPECTROMETRY. Tissue: Brain cortex.
[5]	"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: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	DQ084361 mRNA. Translation: AAY86039.1.
IPI	IPI00117039.
UniGene	Mm.329515
3D structure databases
SMR	Q4JIM5. Positions 110-558.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000026596. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:87860. Abl2.
Phylogenomic databases
HOVERGEN	Q4JIM5.
Enzyme and pathway databases
BRENDA	2.7.10.2. 244.
Gene expression databases
ArrayExpress	Q4JIM5.
Bgee	Q4JIM5.
GermOnline	ENSMUSG00000026596. Mus musculus.
Family and domain databases
InterPro	IPR015015. F-actin_binding. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR000980. SH2. IPR001452. SH3_domain. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
Pfam	PF08919. F_actin_bind. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. PD000093. SH2. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00808. FABD. 1 hit. SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	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]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

ABL2_MOUSE

Accession

Primary (citable) accession number: Q4JIM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 2, 2005
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents