SRC1_CAEEL
ID SRC1_CAEEL Reviewed; 533 AA.
AC G5EE56; W6RRW6; W6RTE9; W6SBD5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tyrosine protein-kinase src-1 {ECO:0000305};
DE EC=2.7.10.2 {ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548, ECO:0000269|PubMed:20226672};
DE AltName: Full=SRC oncogene related protein 1 {ECO:0000312|WormBase:Y92H12A.1a};
GN Name=src-1 {ECO:0000312|WormBase:Y92H12A.1a};
GN ORFNames=Y92H12A.1 {ECO:0000312|WormBase:Y92H12A.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RX PubMed=12110172; DOI=10.1016/s1534-5807(02)00185-5;
RA Bei Y., Hogan J., Berkowitz L.A., Soto M., Rocheleau C.E., Pang K.M.,
RA Collins J., Mello C.C.;
RT "SRC-1 and Wnt signaling act together to specify endoderm and to control
RT cleavage orientation in early C. elegans embryos.";
RL Dev. Cell 3:113-125(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, PHOSPHORYLATION AT TYR-528, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF TYR-528.
RX PubMed=12527374; DOI=10.1016/s0014-5793(02)03819-x;
RA Hirose T., Koga M., Ohshima Y., Okada M.;
RT "Distinct roles of the Src family kinases, SRC-1 and KIN-22, that are
RT negatively regulated by CSK-1 in C. elegans.";
RL FEBS Lett. 534:133-138(2003).
RN [3] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LYS-290.
RX PubMed=16251208; DOI=10.1242/dev.02103;
RA Itoh B., Hirose T., Takata N., Nishiwaki K., Koga M., Ohshima Y., Okada M.;
RT "SRC-1, a non-receptor type of protein tyrosine kinase, controls the
RT direction of cell and growth cone migration in C. elegans.";
RL Development 132:5161-5172(2005).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-5, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 108-TRP-TRP-109; ARG-165 AND LYS-290.
RX PubMed=16024786; DOI=10.1128/mcb.25.15.6485-6495.2005;
RA Lee J., Li W., Guan K.L.;
RT "SRC-1 mediates UNC-5 signaling in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 25:6485-6495(2005).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT
RP TYR-416, AND MUTAGENESIS OF TYR-416.
RX PubMed=19210548; DOI=10.1111/j.1365-2443.2008.01275.x;
RA Takata N., Itoh B., Misaki K., Hirose T., Yonemura S., Okada M.;
RT "Non-receptor tyrosine kinase CSK-1 controls pharyngeal muscle organization
RT in Caenorhabditis elegans.";
RL Genes Cells 14:381-393(2009).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, INTERACTION
RP WITH INA-1 AND CED-2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-416,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-416.
RX PubMed=20226672; DOI=10.1016/j.cub.2010.01.062;
RA Hsu T.Y., Wu Y.C.;
RT "Engulfment of apoptotic cells in C. elegans is mediated by integrin
RT alpha/SRC signaling.";
RL Curr. Biol. 20:477-486(2010).
RN [8]
RP FUNCTION.
RX PubMed=22293500; DOI=10.1016/j.febslet.2012.01.031;
RA Masuda H., Nakamura K., Takata N., Itoh B., Hirose T., Moribe H.,
RA Mekada E., Okada M.;
RT "MIG-13 controls anteroposterior cell migration by interacting with UNC-
RT 71/ADM-1 and SRC-1 in Caenorhabditis elegans.";
RL FEBS Lett. 586:740-746(2012).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase which plays a role in
CC endoderm development by controlling spindle orientation in EMS
CC blastomere, probably downstream of receptor mes-1. Also involved in
CC embryonic body morphogenesis, especially in the formation of the
CC pharynx and the intestine (PubMed:12110172, PubMed:12527374,
CC PubMed:19210548). May be dispensable for pharyngeal muscle organization
CC in the adult (PubMed:19210548). Probably phosphorylates netrin receptor
CC unc-5, to regulate distal tip cell (DTC) migration during gonad
CC development and in axon repulsion (PubMed:16024786, PubMed:16251208).
CC Plays a role in the migration of the QR neuroblast, a precursor of the
CC AVM neuron, and in the migration of the axon cone of AVM, ALM, CAN and
CC PVM neurons (PubMed:16251208, PubMed:22293500). May act downstream of
CC migratory protein mig-13 to control AVM neuron migration
CC (PubMed:22293500). Probably downstream of integrin ina-1/pat-3, plays a
CC role in the clearance of apoptotic cells during mid-embryogenesis
CC (PubMed:20226672). {ECO:0000269|PubMed:12110172,
CC ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:16024786,
CC ECO:0000269|PubMed:16251208, ECO:0000269|PubMed:19210548,
CC ECO:0000269|PubMed:20226672, ECO:0000269|PubMed:22293500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000269|PubMed:12527374, ECO:0000269|PubMed:19210548,
CC ECO:0000269|PubMed:20226672};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:20226672};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20226672};
CC -!- ACTIVITY REGULATION: May be activated by autophosphorylation
CC (PubMed:19210548, PubMed:20226672). May be inhibited by csk-1-mediated
CC phosphorylation (PubMed:12527374). {ECO:0000269|PubMed:12527374,
CC ECO:0000269|PubMed:20226672, ECO:0000305|PubMed:19210548}.
CC -!- SUBUNIT: Interacts (via SH2 domain and SH3 domain) with unc-5 (via
CC cytoplasmic domain); the interaction requires kinase activity
CC (PubMed:16024786). Interacts (when activated and phosphorylated at
CC 'Tyr-416') with ina-1 (via cytoplasmic domain) and with ced-2 (via SH2
CC domain) (PubMed:20226672). {ECO:0000269|PubMed:16024786,
CC ECO:0000269|PubMed:20226672}.
CC -!- INTERACTION:
CC G5EE56; Q9BIF4: ehs-1; NbExp=3; IntAct=EBI-6538807, EBI-11466207;
CC G5EE56; Q09442: sap-49; NbExp=3; IntAct=EBI-6538807, EBI-2316106;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20226672};
CC Lipid-anchor {ECO:0000255}; Cytoplasmic side
CC {ECO:0000269|PubMed:20226672}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:20226672}. Note=Co-localizes with ina-1 at the site
CC of the phagosomal cup formation during apoptotic cell engulfment.
CC {ECO:0000269|PubMed:20226672}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:Y92H12A.1a};
CC IsoId=G5EE56-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y92H12A.1b};
CC IsoId=G5EE56-2; Sequence=VSP_057939;
CC Name=c {ECO:0000312|WormBase:Y92H12A.1c};
CC IsoId=G5EE56-3; Sequence=VSP_057938;
CC Name=d {ECO:0000312|WormBase:Y92H12A.1d};
CC IsoId=G5EE56-4; Sequence=VSP_057937;
CC -!- TISSUE SPECIFICITY: Expressed in some neurons (ASE, ADF, AVA, AUA, RMDV
CC and BAG) in the head region, anchor cell, vulva, cells around anus,
CC body wall muscle, pharyngeal muscles in procorpus and metacorpus
CC (PubMed:12527374). Expressed in gonadal distal tip cells
CC (PubMed:12527374, PubMed:16251208). {ECO:0000269|PubMed:12527374,
CC ECO:0000269|PubMed:16251208}.
CC -!- PTM: May be phosphorylated on Tyr-528 by csk-1.
CC {ECO:0000269|PubMed:12527374}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a growth arrest
CC between gastrulation and the 2-fold stage and an increase in number of
CC apoptotic cell corpses at the comma and 1.5-fold stages
CC (PubMed:12527374, PubMed:16024786, PubMed:20226672). The few
CC hermaphrodite animals reaching adulthood have gonadal defects
CC characterized by the formation of a straight gonad resulting from
CC defects in distal tip cells migration during the first and second turns
CC (PubMed:16251208, PubMed:16024786). {ECO:0000269|PubMed:12527374,
CC ECO:0000269|PubMed:16024786, ECO:0000269|PubMed:16251208,
CC ECO:0000269|PubMed:20226672}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000305}.
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DR EMBL; AF475094; AAL84635.1; -; mRNA.
DR EMBL; AF419171; AAN31394.1; -; mRNA.
DR EMBL; BX284601; CCD71465.1; -; Genomic_DNA.
DR EMBL; BX284601; CDM63506.1; -; Genomic_DNA.
DR EMBL; BX284601; CDM63507.1; -; Genomic_DNA.
DR EMBL; BX284601; CDM63508.1; -; Genomic_DNA.
DR RefSeq; NP_001293420.1; NM_001306491.1.
DR RefSeq; NP_001293421.1; NM_001306492.1. [G5EE56-3]
DR RefSeq; NP_001293422.1; NM_001306493.1. [G5EE56-4]
DR RefSeq; NP_490866.4; NM_058465.5.
DR AlphaFoldDB; G5EE56; -.
DR SMR; G5EE56; -.
DR IntAct; G5EE56; 78.
DR STRING; 6239.Y92H12A.1; -.
DR iPTMnet; G5EE56; -.
DR EPD; G5EE56; -.
DR PaxDb; G5EE56; -.
DR PeptideAtlas; G5EE56; -.
DR EnsemblMetazoa; Y92H12A.1a.1; Y92H12A.1a.1; WBGene00005077. [G5EE56-1]
DR EnsemblMetazoa; Y92H12A.1b.1; Y92H12A.1b.1; WBGene00005077. [G5EE56-2]
DR EnsemblMetazoa; Y92H12A.1c.1; Y92H12A.1c.1; WBGene00005077. [G5EE56-3]
DR EnsemblMetazoa; Y92H12A.1d.1; Y92H12A.1d.1; WBGene00005077. [G5EE56-4]
DR GeneID; 171722; -.
DR CTD; 171722; -.
DR WormBase; Y92H12A.1a; CE39993; WBGene00005077; src-1. [G5EE56-1]
DR WormBase; Y92H12A.1b; CE49528; WBGene00005077; src-1. [G5EE56-2]
DR WormBase; Y92H12A.1c; CE49606; WBGene00005077; src-1. [G5EE56-3]
DR WormBase; Y92H12A.1d; CE49574; WBGene00005077; src-1. [G5EE56-4]
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000166089; -.
DR InParanoid; G5EE56; -.
DR OMA; HEMMMLC; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; G5EE56; -.
DR Reactome; R-CEL-1227986; Signaling by ERBB2.
DR Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-CEL-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-CEL-177929; Signaling by EGFR.
DR Reactome; R-CEL-180292; GAB1 signalosome.
DR Reactome; R-CEL-186763; Downstream signal transduction.
DR Reactome; R-CEL-210990; PECAM1 interactions.
DR Reactome; R-CEL-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-373753; Nephrin family interactions.
DR Reactome; R-CEL-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CEL-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-CEL-3928664; Ephrin signaling.
DR Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-CEL-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-CEL-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-CEL-399956; CRMPs in Sema3A signaling.
DR Reactome; R-CEL-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-418885; DCC mediated attractive signaling.
DR Reactome; R-CEL-430116; GP1b-IX-V activation signalling.
DR Reactome; R-CEL-432142; Platelet sensitization by LDL.
DR Reactome; R-CEL-437239; Recycling pathway of L1.
DR Reactome; R-CEL-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-CEL-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-8866376; Reelin signalling pathway.
DR Reactome; R-CEL-8874081; MET activates PTK2 signaling.
DR Reactome; R-CEL-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-912631; Regulation of signaling by CBL.
DR SignaLink; G5EE56; -.
DR PRO; PR:G5EE56; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00005077; Expressed in embryo and 3 other tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0043292; C:contractile fiber; IDA:WormBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0001891; C:phagocytic cup; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990890; F:netrin receptor binding; IPI:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:WormBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:WormBase.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071679; P:commissural neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IGI:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:WormBase.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IGI:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection; Kinase;
KW Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; SH2 domain;
KW SH3 domain; Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..533
FT /note="Tyrosine protein-kinase src-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434507"
FT DOMAIN 71..132
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 138..237
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 262..521
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 268..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 416
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19210548,
FT ECO:0000269|PubMed:20226672"
FT MOD_RES 528
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12527374"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..308
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057937"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057938"
FT VAR_SEQ 26
FT /note="R -> RYPRR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057939"
FT MUTAGEN 108..109
FT /note="WW->RR: Partial loss of interaction with unc-5."
FT /evidence="ECO:0000269|PubMed:16024786"
FT MUTAGEN 165
FT /note="R->A: Loss of interaction with unc-5."
FT /evidence="ECO:0000269|PubMed:16024786"
FT MUTAGEN 290
FT /note="K->M: Probable loss of kinase activity. Gonadal
FT defects characterized by the formation of a straight gonad
FT resulting from defects in the first and second turns during
FT development. Abnormal migration of AVM and abnormal
FT guidance of PVM neuron axon."
FT /evidence="ECO:0000269|PubMed:16024786,
FT ECO:0000269|PubMed:16251208"
FT MUTAGEN 416
FT /note="Y->F: Abolishes phosphorylation which results in
FT loss of kinase activity. Loss of interaction with ina-1 and
FT ced-2."
FT /evidence="ECO:0000269|PubMed:19210548,
FT ECO:0000269|PubMed:20226672"
FT MUTAGEN 528
FT /note="Y->F: Abolishes phosphorylation which results in
FT constitutive activation."
FT /evidence="ECO:0000269|PubMed:12527374"
SQ SEQUENCE 533 AA; 60661 MW; 803E6B7E35A14BF1 CRC64;
MGCLFSKERR SGGSDMGVSE RIDVSRFQTP QQQTVFHVNN GGNEGTISQL NGTSDGMMGN
GRGGGGGGGA QERETLVALY PYDSRADGDL SFQKGDAMYL LDHSNCDWWY VRHQRTGQTG
YVPRNFVAKQ QTIESEEWYA GKIPRNRAER LVLSSHLPKG TFLIREREAD TREFALTIRD
TDDQRNGGTV KHYKIKRLDH DQGYFITTRR TFRSLQELVR YYSDVPDGLC CQLTFPAPRL
APTRPDLSHD TQQNWEIPRN QLHLKRKLGD GNFGEVWYGK WRGIVEVAIK TMKPGTMSPE
AFLQEAQIMK QCDHPNLVKL YAVCTREEPF YIITEYMING SLLQYLRTDG STLGIQALVD
MAAQIANGMM YLEERKLVHR DLAARNVLVG DKISGVPVVK VADFGLARKL MEEDIYEART
GAKFPIKWTA PEAATCGNFT VKSDVWSYGI LLYEIMTKGQ VPYPGMHNRE VVEQVELGYR
MPMPRGCPEQ IYEEVLLKCW DKTPDRRPTF DTLYHFFDDY FVSTQPNYAP PSA
