DAB1_MOUSE
ID DAB1_MOUSE Reviewed; 588 AA.
AC P97318; A2A963; A2A964; A2A965; A2A966; A2A967; A2A970; P97316; P97317;
AC Q9DAP9;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Disabled homolog 1;
GN Name=Dab1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS DAB217; DAB271 AND
RP DAB555), FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=9009273; DOI=10.1093/emboj/16.1.121;
RA Howell B.W., Gertler F.B., Cooper J.A.;
RT "Mouse disabled (mDab1): a Src binding protein implicated in neuronal
RT development.";
RL EMBO J. 16:121-132(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DAB197).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION AT TYR-198 AND TYR-232, AND MUTAGENESIS OF TYR-185;
RP TYR-198; TYR-200; TYR-220 AND TYR-232.
RX PubMed=10959835; DOI=10.1016/s0960-9822(00)00608-4;
RA Howell B.W., Herrick T.M., Hildebrand J.D., Zhang Y., Cooper J.A.;
RT "Dab1 tyrosine phosphorylation sites relay positional signals during mouse
RT brain development.";
RL Curr. Biol. 10:877-885(2000).
RN [5]
RP PHOSPHORYLATION AT TYR-198 AND TYR-220.
RX PubMed=11279201; DOI=10.1074/jbc.m101422200;
RA Keshvara L., Benhayon D., Magdaleno S., Curran T.;
RT "Identification of reelin-induced sites of tyrosyl phosphorylation on
RT disabled 1.";
RL J. Biol. Chem. 276:16008-16014(2001).
RN [6]
RP PHOSPHORYLATION AT SER-524.
RX PubMed=12077184; DOI=10.1523/jneurosci.22-12-04869.2002;
RA Keshvara L., Magdaleno S., Benhayon D., Curran T.;
RT "Cyclin-dependent kinase 5 phosphorylates disabled 1 independently of
RT reelin signaling.";
RL J. Neurosci. 22:4869-4877(2002).
RN [7]
RP INTERACTION WITH SIAH1.
RX PubMed=12646221; DOI=10.1016/s0006-291x(03)00247-x;
RA Park T.-J., Hamanaka H., Ohshima T., Watanabe N., Mikoshiba K., Nukina N.;
RT "Inhibition of ubiquitin ligase Siah-1A by disabled-1.";
RL Biochem. Biophys. Res. Commun. 302:671-678(2003).
RN [8]
RP PHOSPHORYLATION AT TYR-220 AND TYR-232, INTERACTION WITH CRK AND CRKL, AND
RP MUTAGENESIS OF TYR-220 AND TYR-232.
RX PubMed=15062102; DOI=10.1016/j.cub.2004.03.038;
RA Ballif B.A., Arnaud L., Arthur W.T., Guris D., Imamoto A., Cooper J.A.;
RT "Activation of a Dab1/CrkL/C3G/Rap1 pathway in Reelin-stimulated neurons.";
RL Curr. Biol. 14:606-610(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-183, INTERACTION WITH
RP PHOSPHATIDYLINOSITIDES AND APLP1, AND MUTAGENESIS OF LYS-45; LYS-82;
RP SER-114; HIS-136 AND PHE-158.
RX PubMed=12826668; DOI=10.1074/jbc.m304384200;
RA Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J.,
RA Rock C.O., Curran T., Park H.W.;
RT "Crystal structures of the Dab homology domains of mouse disabled 1 and
RT 2.";
RL J. Biol. Chem. 278:36572-36581(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-174, AND INTERACTION WITH LRP8
RP AND VLDLR.
RX PubMed=12737822; DOI=10.1016/s0969-2126(03)00068-6;
RA Stolt P.C., Jeon H., Song H.K., Herz J., Eck M.J., Blacklow S.C.;
RT "Origins of peptide selectivity and phosphoinositide binding revealed by
RT structures of disabled-1 PTB domain complexes.";
RL Structure 11:569-579(2003).
CC -!- FUNCTION: Adapter molecule functioning in neural development. May
CC regulate SIAH1 activity. {ECO:0000269|PubMed:9009273}.
CC -!- SUBUNIT: Associates with the SH2 domains of SRC, FYN and ABL. Interacts
CC (phosphorylated on tyrosine residues) with CRK and CRKL (via respective
CC SH2 domain) (PubMed:15062102). Interacts with SIAH1, LRP8 and VLDLR
CC (PubMed:12646221, PubMed:12737822). Interacts with LRP1 (By
CC similarity). Interacts with APLP1 (via NPXY motif) (PubMed:12826668).
CC Interacts with DAB2IP (By similarity). {ECO:0000250|UniProtKB:O75553,
CC ECO:0000250|UniProtKB:Q8CJH2, ECO:0000269|PubMed:12646221,
CC ECO:0000269|PubMed:12737822, ECO:0000269|PubMed:12826668,
CC ECO:0000269|PubMed:15062102, ECO:0000269|PubMed:9009273}.
CC -!- INTERACTION:
CC P97318; Q03157: Aplp1; NbExp=4; IntAct=EBI-81680, EBI-399929;
CC P97318; P12023: App; NbExp=3; IntAct=EBI-81680, EBI-78814;
CC P97318; Q3UHC7: Dab2ip; NbExp=3; IntAct=EBI-81680, EBI-6306507;
CC P97318; Q91ZX7: Lrp1; NbExp=2; IntAct=EBI-81680, EBI-300955;
CC P97318; A2ARV4: Lrp2; NbExp=2; IntAct=EBI-81680, EBI-300875;
CC P97318; Q8VHR0: Pcdh18; NbExp=2; IntAct=EBI-81680, EBI-399910;
CC P97318; P61092: Siah1a; NbExp=3; IntAct=EBI-81680, EBI-446761;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=DAB588;
CC IsoId=P97318-1; Sequence=Displayed;
CC Name=DAB197;
CC IsoId=P97318-4; Sequence=VSP_026205, VSP_003841, VSP_003842;
CC Name=DAB204;
CC IsoId=P97318-5; Sequence=VSP_026208, VSP_026209;
CC Name=DAB217;
CC IsoId=P97318-6; Sequence=VSP_003841, VSP_003842;
CC Name=DAB271;
CC IsoId=P97318-3; Sequence=VSP_003843, VSP_003844, VSP_003845;
CC Name=DAB553;
CC IsoId=P97318-8; Sequence=VSP_026206;
CC Name=DAB555;
CC IsoId=P97318-2; Sequence=VSP_003843;
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain.
CC {ECO:0000269|PubMed:9009273}.
CC -!- DOMAIN: The PID domain specifically binds to the Asn-Pro-Xaa-Tyr(P)
CC motif found in many tyrosine-phosphorylated proteins.
CC -!- PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in
CC embryonic neurons (PubMed:11279201). Also found phosphorylated on Tyr-
CC 232 upon reelin induction (PubMed:15062102). Also phosphorylated on
CC Ser-524 independently of reelin signaling.
CC {ECO:0000269|PubMed:10959835, ECO:0000269|PubMed:11279201,
CC ECO:0000269|PubMed:12077184, ECO:0000269|PubMed:15062102}.
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DR EMBL; Y08380; CAA69663.1; -; mRNA.
DR EMBL; Y08379; CAA69662.1; -; mRNA.
DR EMBL; Y08381; CAA69664.1; -; mRNA.
DR EMBL; Y08383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK005640; BAB24163.1; -; mRNA.
DR EMBL; AL627134; CAM26758.1; -; Genomic_DNA.
DR EMBL; AL645483; CAM26758.1; JOINED; Genomic_DNA.
DR EMBL; AL627134; CAM26759.1; -; Genomic_DNA.
DR EMBL; AL645483; CAM26759.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM26759.1; JOINED; Genomic_DNA.
DR EMBL; AL627134; CAM26760.1; -; Genomic_DNA.
DR EMBL; AL645483; CAM26760.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM26760.1; JOINED; Genomic_DNA.
DR EMBL; AL627134; CAM26762.1; -; Genomic_DNA.
DR EMBL; AL645483; CAM26762.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM26762.1; JOINED; Genomic_DNA.
DR EMBL; AL627134; CAM26765.1; -; Genomic_DNA.
DR EMBL; AL645483; CAM26765.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM26765.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM17685.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM17685.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM17686.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM17686.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM17686.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM17687.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM17687.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM17687.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM17689.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM17689.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM17689.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM17690.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM17690.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM17690.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM19059.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM19059.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM19059.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM19060.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM19060.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM19060.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM19062.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM19062.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM19062.1; JOINED; Genomic_DNA.
DR EMBL; AL669938; CAM19063.1; -; Genomic_DNA.
DR EMBL; AL627134; CAM19063.1; JOINED; Genomic_DNA.
DR EMBL; AL645483; CAM19063.1; JOINED; Genomic_DNA.
DR CCDS; CCDS18413.1; -. [P97318-2]
DR CCDS; CCDS89790.1; -. [P97318-5]
DR RefSeq; NP_034144.1; NM_010014.3. [P97318-6]
DR RefSeq; NP_796233.2; NM_177259.4. [P97318-2]
DR RefSeq; XP_011238731.1; XM_011240429.2.
DR PDB; 1NTV; X-ray; 1.50 A; A=23-174.
DR PDB; 1NU2; X-ray; 1.90 A; A=23-174.
DR PDB; 1OQN; X-ray; 2.30 A; A/B=25-183.
DR PDBsum; 1NTV; -.
DR PDBsum; 1NU2; -.
DR PDBsum; 1OQN; -.
DR AlphaFoldDB; P97318; -.
DR SMR; P97318; -.
DR BioGRID; 199042; 30.
DR DIP; DIP-30902N; -.
DR ELM; P97318; -.
DR IntAct; P97318; 18.
DR MINT; P97318; -.
DR STRING; 10090.ENSMUSP00000102443; -.
DR iPTMnet; P97318; -.
DR PhosphoSitePlus; P97318; -.
DR MaxQB; P97318; -.
DR PRIDE; P97318; -.
DR ProteomicsDB; 279264; -. [P97318-1]
DR ProteomicsDB; 279265; -. [P97318-4]
DR ProteomicsDB; 279266; -. [P97318-5]
DR ProteomicsDB; 279267; -. [P97318-6]
DR ProteomicsDB; 279268; -. [P97318-3]
DR ProteomicsDB; 279269; -. [P97318-8]
DR ProteomicsDB; 279270; -. [P97318-2]
DR Antibodypedia; 19377; 524 antibodies from 35 providers.
DR DNASU; 13131; -.
DR Ensembl; ENSMUST00000106826; ENSMUSP00000102439; ENSMUSG00000028519. [P97318-4]
DR Ensembl; ENSMUST00000106827; ENSMUSP00000102440; ENSMUSG00000028519. [P97318-5]
DR Ensembl; ENSMUST00000106830; ENSMUSP00000102443; ENSMUSG00000028519. [P97318-2]
DR GeneID; 13131; -.
DR KEGG; mmu:13131; -.
DR UCSC; uc008txu.1; mouse. [P97318-5]
DR UCSC; uc008txv.2; mouse. [P97318-6]
DR CTD; 1600; -.
DR MGI; MGI:108554; Dab1.
DR VEuPathDB; HostDB:ENSMUSG00000028519; -.
DR eggNOG; KOG3535; Eukaryota.
DR GeneTree; ENSGT00940000158038; -.
DR HOGENOM; CLU_020747_2_0_1; -.
DR InParanoid; P97318; -.
DR OMA; FDEKTGX; -.
DR PhylomeDB; P97318; -.
DR TreeFam; TF316724; -.
DR Reactome; R-MMU-8866376; Reelin signalling pathway.
DR BioGRID-ORCS; 13131; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dab1; mouse.
DR EvolutionaryTrace; P97318; -.
DR PRO; PR:P97318; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P97318; protein.
DR Bgee; ENSMUSG00000028519; Expressed in cortical plate and 216 other tissues.
DR ExpressionAtlas; P97318; baseline and differential.
DR Genevisible; P97318; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IGI:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; TAS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; TAS:UniProtKB.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0021813; P:cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration; IMP:MGI.
DR GO; GO:0007417; P:central nervous system development; TAS:UniProtKB.
DR GO; GO:0021589; P:cerebellum structural organization; IMP:MGI.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0051645; P:Golgi localization; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:UniProtKB.
DR GO; GO:0097477; P:lateral motor column neuron migration; IMP:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; IMP:MGI.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:MGI.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IMP:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IMP:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IMP:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..588
FT /note="Disabled homolog 1"
FT /id="PRO_0000079769"
FT DOMAIN 36..189
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10959835,
FT ECO:0000269|PubMed:11279201"
FT MOD_RES 220
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11279201,
FT ECO:0000269|PubMed:15062102"
FT MOD_RES 232
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10959835,
FT ECO:0000269|PubMed:15062102"
FT MOD_RES 524
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:12077184"
FT VAR_SEQ 2..23
FT /note="STETELQVAVKTSAKKDSRKKG -> LC (in isoform DAB197)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026205"
FT VAR_SEQ 187..221
FT /note="Missing (in isoform DAB553)"
FT /evidence="ECO:0000305"
FT /id="VSP_026206"
FT VAR_SEQ 200..217
FT /note="YIVFEAGHEPIRDPETEE -> VISEPRQGFACSCEGSFD (in isoform
FT DAB197 and isoform DAB217)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9009273"
FT /id="VSP_003841"
FT VAR_SEQ 200..204
FT /note="YIVFE -> NLQKN (in isoform DAB204)"
FT /evidence="ECO:0000305"
FT /id="VSP_026208"
FT VAR_SEQ 205..588
FT /note="Missing (in isoform DAB204)"
FT /evidence="ECO:0000305"
FT /id="VSP_026209"
FT VAR_SEQ 218..588
FT /note="Missing (in isoform DAB197 and isoform DAB217)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9009273"
FT /id="VSP_003842"
FT VAR_SEQ 240..272
FT /note="Missing (in isoform DAB555 and isoform DAB271)"
FT /evidence="ECO:0000303|PubMed:9009273"
FT /id="VSP_003843"
FT VAR_SEQ 275..304
FT /note="AVTQLELFGDMSTPPDITSPPTPATPGDAF -> SLVQSPAAERAEAESRTG
FT PAEPGSILRPLG (in isoform DAB271)"
FT /evidence="ECO:0000303|PubMed:9009273"
FT /id="VSP_003844"
FT VAR_SEQ 305..588
FT /note="Missing (in isoform DAB271)"
FT /evidence="ECO:0000303|PubMed:9009273"
FT /id="VSP_003845"
FT MUTAGEN 45
FT /note="K->A: Impairs binding to PtdIns(4,5)P2."
FT /evidence="ECO:0000269|PubMed:12826668"
FT MUTAGEN 82
FT /note="K->A: Abolishes binding to PtdIns(4,5)P2."
FT /evidence="ECO:0000269|PubMed:12826668"
FT MUTAGEN 114
FT /note="S->T: Abolishes interaction with APLP1."
FT /evidence="ECO:0000269|PubMed:12826668"
FT MUTAGEN 136
FT /note="H->R: Greatly impairs interaction with APLP1."
FT /evidence="ECO:0000269|PubMed:12826668"
FT MUTAGEN 158
FT /note="F->V: Abolishes interaction with APLP1."
FT /evidence="ECO:0000269|PubMed:12826668"
FT MUTAGEN 185
FT /note="Y->F: Reduces phosphorylation by SRC or downstream
FT kinase; when associated with F-198 and F-200. Abolishes
FT phosphorylation by SRC or downstream kinase; when
FT associated with F-198; F-200; F-220 and F-232."
FT /evidence="ECO:0000269|PubMed:10959835"
FT MUTAGEN 198
FT /note="Y->F: Reduces phosphorylation by SRC or downstream
FT kinase; when associated with F-185 and F-200. Abolishes
FT phosphorylation by SRC or downstream kinase; when
FT associated with F-185; F-200; F-220 and F-232."
FT /evidence="ECO:0000269|PubMed:10959835"
FT MUTAGEN 200
FT /note="Y->F: Reduces phosphorylation by SRC or downstream
FT kinase; when associated with F-185 and F-198. Abolishes
FT phosphorylation by SRC or downstream kinase; when
FT associated with F-185; F-198; F-220 and F-232."
FT /evidence="ECO:0000269|PubMed:10959835"
FT MUTAGEN 220
FT /note="Y->F: Reduces phosphorylation by SRC or downstream
FT kinase; when associated with F-232. Abolishes
FT phosphorylation by SRC or downstream kinase; when
FT associated with F-185; F-198; F-200 and F-232. Abolishes
FT interaction with CRKL SH2 domain; when associated with F-
FT 232."
FT /evidence="ECO:0000269|PubMed:10959835,
FT ECO:0000269|PubMed:15062102"
FT MUTAGEN 232
FT /note="Y->F: Reduces phosphorylation by SRC or downstream
FT kinase; when associated with F-220. Abolishes
FT phosphorylation by SRC or downstream kinase; when
FT associated with F-185; F-198; F-200 and F-220. Abolishes
FT interaction with CRKL SH2 domain; when associated with F-
FT 220."
FT /evidence="ECO:0000269|PubMed:10959835,
FT ECO:0000269|PubMed:15062102"
FT CONFLICT 29
FT /note="A -> R (in Ref. 2; BAB24163)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="P -> PVS (in Ref. 3; CAM17685/CAM26758)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="E -> D (in Ref. 3; CAM17685/CAM26758)"
FT /evidence="ECO:0000305"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1NTV"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:1NTV"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1NTV"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1NTV"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1NTV"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:1NTV"
FT HELIX 148..166
FT /evidence="ECO:0007829|PDB:1NTV"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1NTV"
SQ SEQUENCE 588 AA; 63578 MW; 08404220792B1DB4 CRC64;
MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL
CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDI
TDHRAFGYVC GKEGNHRFVA IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC
EQAVYQTILE EDVEDPVYQY IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPN
SQPLEDFESR FAAATPNRNL SMDFDELLEA TKVSAVTQLE LFGDMSTPPD ITSPPTPATP
GDAFLPSSSQ TLPGSADVFG SMSFGTAAVP SGYVAMGAVL PSFWGQQPLV QQQIAMGAQP
PVAQVIPGAQ PIAWGQPGLF PATQQAWPTV AGQFPPAAFM PTQTVMPLAA AMFQGPLTPL
ATVPGTNDSA RSSPQSDKPR QKMGKESFKD FQMVQPPPVP SRKPDQPSLT CTSEAFSSYF
NKVGVAQDTD DCDDFDISQL NLTPVTSTTP STNSPPTPAP RQSSPSKSSA SHVSDPTADD
IFEEGFESPS KSEEQEAPDG SQASSTSDPF GEPSGEPSGD NISPQDGS
