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Protein

Tyrosine-protein kinase

Gene

Abl2

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinaseUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-428890. Role of Abl in Robo-Slit signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinaseUniRule annotation (EC:2.7.10.2UniRule annotation)
Gene namesi
Name:Abl2Imported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:87860. Abl2.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 16761SH3InterPro annotationAdd
BLAST
Domaini173 – 26391SH2InterPro annotationAdd
BLAST
Domaini288 – 539252Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.UniRule annotationSAAS annotation
Contains 1 SH2 domain.UniRule annotation
Contains 1 SH3 domain.UniRule annotation
Contains 1 protein kinase domain.UniRule annotation

Keywords - Domaini

SH3 domainUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
KOiK08887.
OrthoDBiEOG7GTT2V.

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.

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
KOiK08887.
OrthoDBiEOG7GTT2V.

Enzyme and pathway databases

ReactomeiR-MMU-428890. Role of Abl in Robo-Slit signaling.

Miscellaneous databases

ChiTaRSiAbl2. mouse.
NextBioi278624.
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...

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: May 11, 2016
This is version 76 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

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.