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Tyrosine-protein kinase abl-1 (EC 2.7.10.2)

 ABL1_CAEEL              Reviewed;        1224 AA.
P03949; Q9U3A2; Q9U3A3;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
17-JAN-2003, sequence version 4.
23-MAY-2018, entry version 168.
RecName: Full=Tyrosine-protein kinase abl-1;
EC=2.7.10.2;
Name=abl-1; ORFNames=M79.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-706.
PubMed=3457381; DOI=10.1073/pnas.83.7.2172;
Goddard J.M., Weiland J.J., Capecchi M.R.;
"Isolation and characterization of Caenorhabditis elegans DNA
sequences homologous to the v-abl oncogene.";
Proc. Natl. Acad. Sci. U.S.A. 83:2172-2176(1986).
[3]
FUNCTION.
PubMed=16729024; DOI=10.1038/sj.cdd.4401976;
Salinas L.S., Maldonado E., Navarro R.E.;
"Stress-induced germ cell apoptosis by a p53 independent pathway in
Caenorhabditis elegans.";
Cell Death Differ. 13:2129-2139(2006).
[4]
FUNCTION, INTERACTION WITH MIG-13 AND SOEM-1, AND SUBCELLULAR
LOCATION.
PubMed=27780040; DOI=10.1016/j.devcel.2016.09.029;
Zhu Z., Chai Y., Jiang Y., Li W., Hu H., Li W., Wu J.W., Wang Z.X.,
Huang S., Ou G.;
"Functional coordination of WAVE and WASP in C. elegans neuroblast
migration.";
Dev. Cell 39:224-238(2016).
-!- FUNCTION: Functions downstream of migratory protein mig-13 and is
involved in Q neuroblast migration during larval development
(PubMed:27780040). Recruited by mig-13 to the leading edge of Q
neuroblasts and their descendents to signal downstream, likely to
the wve-1 pathway, and direct migration along the anteroposterior
body axis (PubMed:27780040). Promotes germline cell apoptosis in
response to oxidative, osmotic and heat shock stresses
(PubMed:16729024). {ECO:0000269|PubMed:16729024,
ECO:0000269|PubMed:27780040}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Interacts (via SH2 and SH3 domains) with mig-13; the
interaction is direct. May interact with soem-1.
{ECO:0000269|PubMed:27780040}.
-!- INTERACTION:
G5EEL1:alp-1; NbExp=4; IntAct=EBI-2315883, EBI-2315902;
Q11181:C05D10.4; NbExp=6; IntAct=EBI-2315883, EBI-2316016;
G5ED33:eps-8; NbExp=6; IntAct=EBI-2315883, EBI-2315916;
Q9TYX9:M57.1; NbExp=4; IntAct=EBI-2315883, EBI-2315745;
Q22227:mig-5; NbExp=3; IntAct=EBI-2315883, EBI-316403;
Q95QA6:pat-12; NbExp=3; IntAct=EBI-2315883, EBI-327642;
Q18953:secs-1; NbExp=7; IntAct=EBI-2315883, EBI-318539;
G5EF87:swsn-1; NbExp=5; IntAct=EBI-2315883, EBI-311928;
Q18320:szy-4; NbExp=3; IntAct=EBI-2315883, EBI-327120;
G5EDS1:vab-3; NbExp=4; IntAct=EBI-2315883, EBI-319610;
O02174:zfp-3; NbExp=5; IntAct=EBI-2315883, EBI-2315779;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27780040}.
Cytoplasm {ECO:0000269|PubMed:27780040}. Note=Enriched at the
leading edge compared to cytoplasm. Targeted to the leading edge
of Q neuroblasts by mig-13. {ECO:0000269|PubMed:27780040}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=a;
IsoId=P03949-1; Sequence=Displayed;
Name=b;
IsoId=P03949-2; Sequence=VSP_004963;
Name=c;
IsoId=P03949-3; Sequence=VSP_004962;
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. ABL subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; Z50806; CAA90691.2; -; Genomic_DNA.
EMBL; Z50806; CAB60296.2; -; Genomic_DNA.
EMBL; Z50806; CAB60297.2; -; Genomic_DNA.
EMBL; M13235; AAA28129.1; -; Genomic_DNA.
PIR; T23832; T23832.
RefSeq; NP_509777.2; NM_077376.6. [P03949-2]
RefSeq; NP_509778.2; NM_077377.4. [P03949-1]
RefSeq; NP_509779.2; NM_077378.2. [P03949-3]
UniGene; Cel.19997; -.
ProteinModelPortal; P03949; -.
SMR; P03949; -.
BioGrid; 46173; 18.
DIP; DIP-48409N; -.
IntAct; P03949; 45.
STRING; 6239.M79.1a; -.
iPTMnet; P03949; -.
EPD; P03949; -.
PaxDb; P03949; -.
PRIDE; P03949; -.
EnsemblMetazoa; M79.1a; M79.1a; WBGene00000018. [P03949-1]
GeneID; 181261; -.
KEGG; cel:CELE_M79.1; -.
UCSC; M79.1b; c. elegans. [P03949-1]
CTD; 181261; -.
WormBase; M79.1a; CE31570; WBGene00000018; abl-1. [P03949-1]
WormBase; M79.1b; CE31571; WBGene00000018; abl-1. [P03949-2]
WormBase; M79.1c; CE31572; WBGene00000018; abl-1. [P03949-3]
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000017506; -.
InParanoid; P03949; -.
KO; K06619; -.
OMA; LQHHRPF; -.
OrthoDB; EOG091G0D46; -.
BRENDA; 2.7.10.2; 1045.
Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-CEL-428890; Role of ABL in ROBO-SLIT signaling.
Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
SignaLink; P03949; -.
PRO; PR:P03949; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00000018; -.
GO; GO:0005737; C:cytoplasm; ISS:WormBase.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:WormBase.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0050832; P:defense response to fungus; IMP:WormBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:WormBase.
GO; GO:0000077; P:DNA damage checkpoint; IGI:WormBase.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:WormBase.
GO; GO:0030336; P:negative regulation of cell migration; IGI:WormBase.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:WormBase.
GO; GO:1901075; P:negative regulation of engulfment of apoptotic cell; IGI:WormBase.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0010212; P:response to ionizing radiation; IMP:WormBase.
GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd09935; SH2_ABL; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR033221; ABL1.
InterPro; IPR035837; ABL_SH2.
InterPro; IPR015015; F-actin_binding.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
PANTHER; PTHR24418:SF88; PTHR24418:SF88; 1.
Pfam; PF08919; F_actin_bind; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00808; FABD; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Cytoplasm; Kinase; Membrane; Nucleotide-binding; Reference proteome;
SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
CHAIN 1 1224 Tyrosine-protein kinase abl-1.
/FTId=PRO_0000088055.
DOMAIN 115 188 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 194 284 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 311 562 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 317 325 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 385 391 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 450 474 Kinase activation loop. {ECO:0000250}.
ACT_SITE 432 432 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 340 340 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VAR_SEQ 1 88 MGHSHSTGKEINDNELFTCEDPVFDQPVASPKSEISSKLAE
EIERSKSPLILEVSPRTPDSVQMFRPTFDTFRPPNSDSSTF
RGSQSR -> MIMNPCFRERSQKRTKKRAKNRAKSRSTMYL
SKVGDSSLAMSRSLPSVALPMHYLHHKLAESICFITATIDS
L (in isoform c). {ECO:0000305}.
/FTId=VSP_004962.
VAR_SEQ 54 63 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_004963.
SEQUENCE 1224 AA; 138326 MW; 56D8513DD2061071 CRC64;
MGHSHSTGKE INDNELFTCE DPVFDQPVAS PKSEISSKLA EEIERSKSPL ILEVSPRTPD
SVQMFRPTFD TFRPPNSDSS TFRGSQSRED LVACSSMNSV NNVHDMNTVS SSSSSSAPLF
VALYDFHGVG EEQLSLRKGD QVRILGYNKN NEWCEARLYS TRKNDASNQR RLGEIGWVPS
NFIAPYNSLD KYTWYHGKIS RSDSEAILGS GITGSFLVRE SETSIGQYTI SVRHDGRVFH
YRINVDNTEK MFITQEVKFR TLGELVHHHS VHADGLICLL MYPASKKDKG RGLFSLSPNA
PDEWELDRSE IIMHNKLGGG QYGDVYEGYW KRHDCTIAVK ALKEDAMPLH EFLAEAAIMK
DLHHKNLVRL LGVCTHEAPF YIITEFMCNG NLLEYLRRTD KSLLPPIILV QMASQIASGM
SYLEARHFIH RDLAARNCLV SEHNIVKIAD FGLARFMKED TYTAHAGAKF PIKWTAPEGL
AFNTFSSKSD VWAFGVLLWE IATYGMAPYP GVELSNVYGL LENGFRMDGP QGCPPSVYRL
MLQCWNWSPS DRPRFRDIHF NLENLISSNS LNDEVQKQLK KNNDKKLESD KRRSNVRERS
DSKSRHSSHH DRDRDRESLH SRNSNPEIPN RSFIRTDDSV SFFNPSTTSK VTSFRAQGPP
FPPPPQQNTK PKLLKSVLNS NARHASEEFE RNEQDDVVPL AEKNVRKAVT RLGGTMPKGQ
RIDAYLDSMR RVDSWKESTD ADNEGAGSSS LSRTVSNDSL DTLPLPDSMN SSTYVKMHPA
SGENVFLRQI RSKLKKRSET PELDHIDSDT ADETTKSEKS PFGSLNKSSI KYPIKNAPEF
SENHSRVSPV PVPPSRNASV SVRPDSKAED SSDETTKDVG MWGPKHAVTR KIEIVKNDSY
PNVEGELKAK IRNLRHVPKE ESNTSSQEDL PLDATDNTND SIIVIPRDEK AKVRQLVTQK
VSPLQHHRPF SLQCPNNSTS SAISHSEHAD SSETSSLSGV YEERMKPELP RKRSNGDTKV
VPVTWIINGE KEPNGMARTK SLRDITSKFE QLGTASTIES KIEEAVPYRE HALEKKGTSK
RFSMLEGSNE LKHVVPPRKN RNQDESGSID EEPVSKDMIV SLLKVIQKEF VNLFNLASSE
ITDEKLQQFV IMADNVQKLH STCSVYAEQI SPHSKFRFKE LLSQLEIYNR QIKFSHNPRA
KPVDDKLKMA FQDCFDQIMR LVDR


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