Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Non-specific protein-tyrosine kinase

Gene

Abl2

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.SAAS annotation

GO - Molecular functioni

GO - Biological processi

  • actin filament bundle assembly Source: MGI
  • actin filament organization Source: MGI
  • alpha-beta T cell differentiation Source: MGI
  • Bergmann glial cell differentiation Source: MGI
  • cell migration Source: GO_Central
  • 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: MGI
  • 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
  • regulation of cell proliferation Source: GO_Central
  • 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 kinaseSAAS annotation

Keywords - Ligandi

ATP-bindingSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_271985. Role of Abl in Robo-Slit signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific protein-tyrosine kinaseSAAS annotation (EC:2.7.10.2SAAS annotation)
Gene namesi
Name:Abl2Imported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:87860. Abl2.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • cytoplasmic membrane-bounded vesicle Source: MGI
  • cytosol Source: GOC
  • 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...

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027888.

Family & Domainsi

Sequence similaritiesi

Contains 1 SH3 domain.UniRule annotation
Contains SH2 domain.SAAS annotation
Contains protein kinase domain.SAAS annotation

Keywords - Domaini

SH3 domainUniRule annotationSAAS annotation

Phylogenomic databases

GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
KOiK08887.
OrthoDBiEOG7GTT2V.

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.

B2RQ57-1 [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 SLTVAVKTLK 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 HKKYELTGLP EQDRMAMTLP
710 720 730 740 750
RNCQRSKLQL ERTVSTSSQP EENVDRANDM LPKKSEEGAA PARERPKAKL
760 770 780 790 800
LPRGATALPL RAPDPAITES DSPGVGVAGV AAAPKGKERN GGTRLGVAGV
810 820 830 840 850
PEDGEQLGWS SPAKAVAVLP TTHNHKVPVL ISPTLKHTPA DVQLIGTDSQ
860 870 880 890 900
GNKFKLLSEH QVTSSGDKDR PRRVKPKCAP PPPPVMRLLQ HPSTCSDPEE
910 920 930 940 950
EPTAPPAGQH TPETQEGGKK AAPGPMPSSG KPGRPVMPPP QVPLPTSSIS
960 970 980 990 1000
PAKMANGTAG TKVALRKTKQ AAEKISADKI SKEALLECAD LLSSAITEPV
1010 1020 1030 1040 1050
PNSQLVDTGH QLLDYCSGYV DSIPQTRNKF AFREAVSKLE LSLQELQVSS
1060 1070
TAAGVPGTNP VLNNLLSCVQ EISDVVQR
Length:1,078
Mass (Da):117,766
Last modified:July 1, 2008 - v1
Checksum:i7CF6AA48C100E1F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114588 Genomic DNA. No translation available.
AC145078 Genomic DNA. No translation available.
BC137771 mRNA. Translation: AAI37772.1.
RefSeqiNP_001129576.1. NM_001136104.1.
NP_033725.2. NM_009595.3.
UniGeneiMm.329515.

Genome annotation databases

EnsembliENSMUST00000166172; ENSMUSP00000126181; ENSMUSG00000026596.
GeneIDi11352.
KEGGimmu:11352.
UCSCiuc011wuf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114588 Genomic DNA. No translation available.
AC145078 Genomic DNA. No translation available.
BC137771 mRNA. Translation: AAI37772.1.
RefSeqiNP_001129576.1. NM_001136104.1.
NP_033725.2. NM_009595.3.
UniGeneiMm.329515.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027888.

Protocols and materials databases

DNASUi11352.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000166172; ENSMUSP00000126181; ENSMUSG00000026596.
GeneIDi11352.
KEGGimmu:11352.
UCSCiuc011wuf.1. mouse.

Organism-specific databases

CTDi27.
MGIiMGI:87860. Abl2.

Phylogenomic databases

GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
KOiK08887.
OrthoDBiEOG7GTT2V.

Enzyme and pathway databases

ReactomeiREACT_271985. Role of Abl in Robo-Slit signaling.

Miscellaneous databases

ChiTaRSiAbl2. mouse.
NextBioi278624.
SOURCEiSearch...

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: C57BL/6JImported.

Entry informationi

Entry nameiB2RQ57_MOUSE
AccessioniPrimary (citable) accession number: B2RQ57
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: June 24, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

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 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.