ID DAB1_MOUSE Reviewed; 588 AA. AC P97318; A2A963; A2A964; A2A965; A2A966; A2A967; A2A970; P97316; AC P97317; Q9DAP9; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 16-SEP-2015, entry version 130. DE RecName: Full=Disabled homolog 1; GN Name=Dab1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT mouse 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; 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., RA 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, RP AND 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., RA Cooper J.A.; RT "Activation of a Dab1/CrkL/C3G/Rap1 pathway in Reelin-stimulated RT 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 RT and 2."; RL J. Biol. Chem. 278:36572-36581(2003). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-174, AND INTERACTION WITH RP LRP8 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 RT by 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. CC Interacts (phosphorylated on tyrosine residues) with CRK and CRKL CC (via respective SH2 domain). Interacts with DAB2IP, SIAH1, LRP1, CC LRP8 and VLDLR. Interacts with APLP1 (via NPXY motif). CC {ECO:0000269|PubMed:12646221, ECO:0000269|PubMed:12737822, CC ECO:0000269|PubMed:12826668, ECO:0000269|PubMed:15062102, CC ECO:0000269|PubMed:9009273}. CC -!- INTERACTION: CC Q03157:Aplp1; NbExp=4; IntAct=EBI-81680, EBI-399929; CC P12023:App; NbExp=3; IntAct=EBI-81680, EBI-78814; CC Q3UHC7:Dab2ip; NbExp=3; IntAct=EBI-81680, EBI-6306507; CC Q91ZX7:Lrp1; NbExp=2; IntAct=EBI-81680, EBI-300955; CC A2ARV4:Lrp2; NbExp=2; IntAct=EBI-81680, EBI-300875; CC Q8VHR0:Pcdh18; NbExp=2; IntAct=EBI-81680, EBI-399910; CC 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 Note=No experimental confirmation available.; CC Name=DAB197; CC IsoId=P97318-4; Sequence=VSP_026205, VSP_003841, VSP_003842; CC Note=No experimental confirmation available.; CC Name=DAB204; CC IsoId=P97318-5; Sequence=VSP_026208, VSP_026209; CC Note=No experimental confirmation available.; 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 Note=No experimental confirmation available.; 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- CC Tyr(P) motif found in many tyrosine-phosphorylated proteins. CC -!- PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction CC in embryonic neurons (PubMed:11279201). Also found phosphorylated CC on Tyr-232 upon reelin induction (PubMed:15062102). Also CC phosphorylated on Ser-524 independently of reelin signaling. CC {ECO:0000269|PubMed:10959835, ECO:0000269|PubMed:11279201, CC ECO:0000269|PubMed:12077184, ECO:0000269|PubMed:15062102}. CC -!- SIMILARITY: Contains 1 PID domain. {ECO:0000255|PROSITE- CC ProRule:PRU00148}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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_011240429.1. [P97318-2] DR UniGene; Mm.289682; -. 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 ProteinModelPortal; P97318; -. DR SMR; P97318; 23-174. DR BioGrid; 199042; 13. DR DIP; DIP-30902N; -. DR IntAct; P97318; 16. DR MINT; MINT-258594; -. DR PhosphoSite; P97318; -. DR MaxQB; P97318; -. DR PRIDE; P97318; -. 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 eggNOG; NOG313182; -. DR GeneTree; ENSGT00520000055585; -. DR HOVERGEN; HBG018945; -. DR InParanoid; P97318; -. DR OMA; FQMAQPP; -. DR OrthoDB; EOG7HQN7R; -. DR PhylomeDB; P97318; -. DR TreeFam; TF316724; -. DR ChiTaRS; Dab1; mouse. DR EvolutionaryTrace; P97318; -. DR NextBio; 283176; -. DR PRO; PR:P97318; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; P97318; -. DR CleanEx; MM_DAB1; -. DR ExpressionAtlas; P97318; baseline and differential. DR Genevisible; P97318; MM. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005622; C:intracellular; TAS:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. 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: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:0035556; P:intracellular signal transduction; TAS:UniProtKB. DR GO; GO:0097477; P:lateral motor column neuron migration; IMP:UniProtKB. DR GO; GO:0007494; P:midgut development; IEA:Ensembl. 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 JAK-STAT cascade; IMP:MGI. DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB. 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:0042493; P:response to drug; IEA:Ensembl. 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/PTB_dom. 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; Complete proteome; KW Developmental protein; Differentiation; Neurogenesis; Phosphoprotein; KW Reference proteome. FT CHAIN 1 588 Disabled homolog 1. FT /FTId=PRO_0000079769. FT DOMAIN 36 189 PID. {ECO:0000255|PROSITE- FT ProRule:PRU00148}. FT MOD_RES 198 198 Phosphotyrosine. FT {ECO:0000269|PubMed:10959835, FT ECO:0000269|PubMed:11279201}. FT MOD_RES 220 220 Phosphotyrosine. FT {ECO:0000269|PubMed:11279201, FT ECO:0000269|PubMed:15062102}. FT MOD_RES 232 232 Phosphotyrosine. FT {ECO:0000269|PubMed:10959835, FT ECO:0000269|PubMed:15062102}. FT MOD_RES 524 524 Phosphoserine; by CDK5. FT {ECO:0000269|PubMed:12077184}. FT VAR_SEQ 2 23 STETELQVAVKTSAKKDSRKKG -> LC (in isoform FT DAB197). {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_026205. FT VAR_SEQ 187 221 Missing (in isoform DAB553). FT {ECO:0000305}. FT /FTId=VSP_026206. FT VAR_SEQ 200 217 YIVFEAGHEPIRDPETEE -> VISEPRQGFACSCEGSFD FT (in isoform DAB197 and isoform DAB217). FT {ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9009273}. FT /FTId=VSP_003841. FT VAR_SEQ 200 204 YIVFE -> NLQKN (in isoform DAB204). FT {ECO:0000305}. FT /FTId=VSP_026208. FT VAR_SEQ 205 588 Missing (in isoform DAB204). FT {ECO:0000305}. FT /FTId=VSP_026209. FT VAR_SEQ 218 588 Missing (in isoform DAB197 and isoform FT DAB217). {ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9009273}. FT /FTId=VSP_003842. FT VAR_SEQ 240 272 Missing (in isoform DAB555 and isoform FT DAB271). {ECO:0000303|PubMed:9009273}. FT /FTId=VSP_003843. FT VAR_SEQ 275 304 AVTQLELFGDMSTPPDITSPPTPATPGDAF -> SLVQSPA FT AERAEAESRTGPAEPGSILRPLG (in isoform FT DAB271). {ECO:0000303|PubMed:9009273}. FT /FTId=VSP_003844. FT VAR_SEQ 305 588 Missing (in isoform DAB271). FT {ECO:0000303|PubMed:9009273}. FT /FTId=VSP_003845. FT MUTAGEN 45 45 K->A: Impairs binding to PtdIns(4,5)P2. FT {ECO:0000269|PubMed:12826668}. FT MUTAGEN 82 82 K->A: Abolishes binding to PtdIns(4,5)P2. FT {ECO:0000269|PubMed:12826668}. FT MUTAGEN 114 114 S->T: Abolishes interaction with APLP1. FT {ECO:0000269|PubMed:12826668}. FT MUTAGEN 136 136 H->R: Greatly impairs interaction with FT APLP1. {ECO:0000269|PubMed:12826668}. FT MUTAGEN 158 158 F->V: Abolishes interaction with APLP1. FT {ECO:0000269|PubMed:12826668}. FT MUTAGEN 185 185 Y->F: Reduces phosphorylation by SRC or FT downstream kinase; when associated with FT F-198 and F-200. Abolishes FT phosphorylation by SRC or downstream FT kinase; when associated with F-198; F- FT 200; F-220 and F-232. FT {ECO:0000269|PubMed:10959835}. FT MUTAGEN 198 198 Y->F: Reduces phosphorylation by SRC or FT downstream kinase; when associated with FT F-185 and F-200. Abolishes FT phosphorylation by SRC or downstream FT kinase; when associated with F-185; F- FT 200; F-220 and F-232. FT {ECO:0000269|PubMed:10959835}. FT MUTAGEN 200 200 Y->F: Reduces phosphorylation by SRC or FT downstream kinase; when associated with FT F-185 and F-198. Abolishes FT phosphorylation by SRC or downstream FT kinase; when associated with F-185; F- FT 198; F-220 and F-232. FT {ECO:0000269|PubMed:10959835}. FT MUTAGEN 220 220 Y->F: Reduces phosphorylation by SRC or FT downstream kinase; when associated with FT F-232. Abolishes phosphorylation by SRC FT or downstream kinase; when associated FT with F-185; F-198; F-200 and F-232. FT Abolishes interaction with CRKL SH2 FT domain; when associated with F-232. FT {ECO:0000269|PubMed:10959835, FT ECO:0000269|PubMed:15062102}. FT MUTAGEN 232 232 Y->F: Reduces phosphorylation by SRC or FT downstream kinase; when associated with FT F-220. Abolishes phosphorylation by SRC FT or downstream kinase; when associated FT with F-185; F-198; F-200 and F-220. FT Abolishes interaction with CRKL SH2 FT domain; when associated with F-220. FT {ECO:0000269|PubMed:10959835, FT ECO:0000269|PubMed:15062102}. FT CONFLICT 29 29 A -> R (in Ref. 2; BAB24163). FT {ECO:0000305}. FT CONFLICT 239 239 P -> PVS (in Ref. 3; CAM17685/CAM26758). FT {ECO:0000305}. FT CONFLICT 248 248 E -> D (in Ref. 3; CAM17685/CAM26758). FT {ECO:0000305}. FT HELIX 28 35 {ECO:0000244|PDB:1NTV}. FT STRAND 40 51 {ECO:0000244|PDB:1NTV}. FT STRAND 53 55 {ECO:0000244|PDB:1NTV}. FT HELIX 58 76 {ECO:0000244|PDB:1NTV}. FT TURN 77 79 {ECO:0000244|PDB:1NTV}. FT STRAND 83 90 {ECO:0000244|PDB:1NTV}. FT STRAND 93 98 {ECO:0000244|PDB:1NTV}. FT TURN 99 101 {ECO:0000244|PDB:1NTV}. FT STRAND 104 108 {ECO:0000244|PDB:1NTV}. FT HELIX 110 112 {ECO:0000244|PDB:1NTV}. FT STRAND 113 118 {ECO:0000244|PDB:1NTV}. FT STRAND 125 132 {ECO:0000244|PDB:1NTV}. FT STRAND 137 145 {ECO:0000244|PDB:1NTV}. FT HELIX 148 166 {ECO:0000244|PDB:1NTV}. FT HELIX 170 173 {ECO:0000244|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 //