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Reviewed, UniProtKB/Swiss-Prot Q4JIM5 (ABL2_MOUSE)

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

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1182 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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

Cytoplasmcytoskeleton.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 11821181Tyrosine-protein kinase ABL2
PRO_0000258019

Regions

Domain107 – 16761SH3
Domain173 – 26391SH2
Domain288 – 539252Protein kinase
Nucleotide binding294 – 3029ATP By similarity UniProtKB P28523
Region2 – 106105CAP
Motif658 – 6603Nuclear localization signal Potential

Sites

Active site4091Proton acceptor By similarity UniProtKB P28523
Binding site3171ATP Ref.2

Amino acid modifications

Modified residue711Phosphoserine By similarity
Modified residue1161Phosphotyrosine By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2311Phosphotyrosine By similarity UniProtKB P00519
Modified residue2721Phosphotyrosine; by autocatalysis Ref.2
Modified residue2751Phosphoserine By similarity
Modified residue2991Phosphotyrosine By similarity UniProtKB P00519
Modified residue3031Phosphotyrosine By similarity UniProtKB P00519
Modified residue3101Phosphotyrosine By similarity UniProtKB P00519
Modified residue4391Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.2 Ref.3
Modified residue4401Phosphothreonine By similarity UniProtKB P00519
Modified residue4921Phosphoserine By similarity UniProtKB P00519
Modified residue5151Phosphotyrosine By similarity UniProtKB P00519
Modified residue5681Phosphotyrosine; by autocatalysis Ref.2
Modified residue6211Phosphoserine
Modified residue6321Phosphoserine By similarity
Modified residue6341Phosphoserine By similarity
Modified residue6561Phosphoserine By similarity
Modified residue6721Phosphoserine By similarity
Modified residue6841Phosphotyrosine; by autocatalysis Ref.2
Modified residue7191Phosphotyrosine By similarity
Modified residue7851Phosphoserine By similarity
Modified residue8191Phosphoserine By similarity
Modified residue8221Phosphoserine By similarity
Modified residue9151Phosphoserine By similarity
Modified residue9361Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity UniProtKB P00519

Experimental info

Mutagenesis2721Y → F: Minimal reduction in ability to autophosphorylate. Ref.2
Mutagenesis3171K → M: Loss of kinase activity. Ref.2
Mutagenesis4391Y → F: Partial reduction in ability to autophosphorylate. Ref.2
Mutagenesis5681Y → F: No reduction in ability to autophosphorylate. Ref.2
Mutagenesis6841Y → F: Minimal reduction in ability to autophosphorylate. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q4JIM5-1 [UniParc].

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

FASTA1,182128,196
        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 

« Hide

References

« Hide '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.

Cross-references

Sequence databases

DQ084361 mRNA. Translation: AAY86039.1.
IPIIPI00117039.
UniGeneMm.329515

3D structure databases

SMRQ4JIM5. Positions 110-558.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000026596. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:87860. Abl2.

Phylogenomic databases

HOVERGENQ4JIM5.

Enzyme and pathway databases

BRENDA2.7.10.2. 244.

Gene expression databases

ArrayExpressQ4JIM5.
BgeeQ4JIM5.
GermOnlineENSMUSG00000026596. Mus musculus.

Family and domain databases

InterProIPR015015. 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]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. 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]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameABL2_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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) · Sequences · References · Cross-references · Entry information · Relevant documents