ID DAB1_HUMAN Reviewed; 588 AA. AC O75553; A4FU90; B3KTG3; Q4LE59; Q5T6M6; Q5T6M9; Q5T835; Q5T836; AC Q5T837; Q6NWS9; Q6NWT0; Q6NWT1; Q9NYA8; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 3. DT 29-APR-2015, entry version 118. DE RecName: Full=Disabled homolog 1; GN Name=DAB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DAB555). RX PubMed=9790777; DOI=10.1006/geno.1998.5523; RA Lambert de Rouvroit C., Goffinet A.M.; RT "Cloning of human DAB1 and mapping to chromosome 1p31-p32."; RL Genomics 53:246-247(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DAB555). RA Fazili Z., Sun W., Xu X.-X.; RT "Aberrant disabled-1 expression in tumors."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE RP SPLICING. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DAB555). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS DAB469; DAB537 AND RP DAB553). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH LRP1. RX PubMed=15272003; DOI=10.1074/jbc.M407592200; RA Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., RA Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.; RT "Serine and threonine phosphorylation of the low density lipoprotein RT receptor-related protein by protein kinase Calpha regulates RT endocytosis and association with adaptor molecules."; RL J. Biol. Chem. 279:40536-40544(2004). CC -!- FUNCTION: Adapter molecule functioning in neural development. May CC regulate SIAH1 activity (By similarity). {ECO:0000250}. 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. {ECO:0000269|PubMed:15272003}. CC -!- INTERACTION: CC Q9H9I0:-; NbExp=3; IntAct=EBI-7875264, EBI-10309771; CC C9J1Q0:ARID5A; NbExp=3; IntAct=EBI-7875264, EBI-10176351; CC O14503:BHLHE40; NbExp=3; IntAct=EBI-7875264, EBI-711810; CC Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-7875264, EBI-946029; CC Q8N365:CIART; NbExp=3; IntAct=EBI-7875264, EBI-10265133; CC Q15038:DAZAP2; NbExp=3; IntAct=EBI-7875264, EBI-724310; CC Q9BTL3:FAM103A1; NbExp=3; IntAct=EBI-7875264, EBI-744023; CC Q92567:FAM168A; NbExp=3; IntAct=EBI-7875264, EBI-7957930; CC Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-7875264, EBI-2549423; CC Q8WVV9:HNRNPLL; NbExp=3; IntAct=EBI-7875264, EBI-535849; CC O43820:HYAL3; NbExp=3; IntAct=EBI-7875264, EBI-3913399; CC Q3LI72:KRTAP19-5; NbExp=3; IntAct=EBI-7875264, EBI-1048945; CC Q3SYF9:KRTAP19-7; NbExp=3; IntAct=EBI-7875264, EBI-10241353; CC Q8IUC2:KRTAP8-1; NbExp=3; IntAct=EBI-7875264, EBI-10261141; CC Q3B8N2:LGALS9B; NbExp=3; IntAct=EBI-7875264, EBI-10240775; CC Q6DKI2:LGALS9C; NbExp=3; IntAct=EBI-7875264, EBI-9088829; CC Q8TBB1:LNX1; NbExp=3; IntAct=EBI-7875264, EBI-739832; CC Q9Y5V3:MAGED1; NbExp=3; IntAct=EBI-7875264, EBI-716006; CC Q86VM6:MBNL1; NbExp=3; IntAct=EBI-7875264, EBI-10225084; CC Q9NR56:MBNL1; NbExp=3; IntAct=EBI-7875264, EBI-2805004; CC Q9NUK0:MBNL3; NbExp=3; IntAct=EBI-7875264, EBI-6661142; CC Q96HR8:NAF1; NbExp=3; IntAct=EBI-7875264, EBI-2515597; CC Q13526:PIN1; NbExp=3; IntAct=EBI-7875264, EBI-714158; CC Q7Z3K3:POGZ; NbExp=3; IntAct=EBI-7875264, EBI-1389308; CC Q13427:PPIG; NbExp=3; IntAct=EBI-7875264, EBI-396072; CC P86479:PRR20C; NbExp=3; IntAct=EBI-7875264, EBI-10172814; CC O43251:RBFOX2; NbExp=3; IntAct=EBI-7875264, EBI-746056; CC Q9BQY4:RHOXF2; NbExp=3; IntAct=EBI-7875264, EBI-372094; CC A1L4F5:ROR2; NbExp=3; IntAct=EBI-7875264, EBI-10172778; CC O00241-2:SIRPB1; NbExp=3; IntAct=EBI-7875264, EBI-10179231; CC Q8WU79:SMAP2; NbExp=3; IntAct=EBI-7875264, EBI-2822515; CC P14678-2:SNRPB; NbExp=3; IntAct=EBI-7875264, EBI-372475; CC Q96SI9:STRBP; NbExp=3; IntAct=EBI-7875264, EBI-740355; CC Q15560:TCEA2; NbExp=3; IntAct=EBI-7875264, EBI-710310; CC Q86VL0:TCEA2; NbExp=3; IntAct=EBI-7875264, EBI-10259904; CC Q8N8B7:TCEANC; NbExp=3; IntAct=EBI-7875264, EBI-954696; CC Q6ZXV5:TMTC3; NbExp=3; IntAct=EBI-7875264, EBI-10188441; CC Q6FIE9:TOLLIP; NbExp=3; IntAct=EBI-7875264, EBI-10249783; CC Q9H0E2:TOLLIP; NbExp=3; IntAct=EBI-7875264, EBI-74615; CC O95231:VENTX; NbExp=3; IntAct=EBI-7875264, EBI-10191303; CC Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-7875264, EBI-741158; CC Q96K80:ZC3H10; NbExp=3; IntAct=EBI-7875264, EBI-742550; CC Q8TBK6:ZCCHC10; NbExp=3; IntAct=EBI-7875264, EBI-597063; CC Q96MN9:ZNF488; NbExp=3; IntAct=EBI-7875264, EBI-948288; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=DAB588; CC IsoId=O75553-1; Sequence=Displayed; CC Note=No experimental confirmation available.; CC Name=DAB213; CC IsoId=O75553-2; Sequence=VSP_026168, VSP_026169; CC Note=No experimental confirmation available.; CC Name=DAB469; CC IsoId=O75553-3; Sequence=VSP_026166; CC Note=No experimental confirmation available.; CC Name=DAB537; CC IsoId=O75553-4; Sequence=VSP_026167, VSP_026171; CC Note=No experimental confirmation available.; CC Name=DAB553; CC IsoId=O75553-5; Sequence=VSP_026167; CC Note=No experimental confirmation available.; CC Name=DAB555; CC IsoId=O75553-6; Sequence=VSP_026170; 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. Also phosphorylated on Ser-524 independently CC of reelin signaling. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 PID domain. {ECO:0000255|PROSITE- CC ProRule:PRU00148}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE06094.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF071062; AAC70068.1; -; mRNA. DR EMBL; AF263547; AAF73058.1; -; mRNA. DR EMBL; AL139219; CAI19217.1; -; Genomic_DNA. DR EMBL; AL354883; CAI19217.1; JOINED; Genomic_DNA. DR EMBL; AL139219; CAI19218.1; -; Genomic_DNA. DR EMBL; AL161740; CAI19218.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI19218.1; JOINED; Genomic_DNA. DR EMBL; AL139219; CAI19219.1; -; Genomic_DNA. DR EMBL; AL161740; CAI19219.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI19219.1; JOINED; Genomic_DNA. DR EMBL; AL139219; CAI19220.1; -; Genomic_DNA. DR EMBL; AL354883; CAI19220.1; JOINED; Genomic_DNA. DR EMBL; AL139219; CAI19221.1; -; Genomic_DNA. DR EMBL; AL161740; CAI19221.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI19221.1; JOINED; Genomic_DNA. DR EMBL; AL161740; CAI18815.1; -; Genomic_DNA. DR EMBL; AL139219; CAI18815.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI18815.1; JOINED; Genomic_DNA. DR EMBL; AL161740; CAI18816.1; -; Genomic_DNA. DR EMBL; AL139219; CAI18816.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI18816.1; JOINED; Genomic_DNA. DR EMBL; AL161740; CAI18817.1; -; Genomic_DNA. DR EMBL; AL139219; CAI18817.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI18817.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI22360.1; -; Genomic_DNA. DR EMBL; AL139219; CAI22360.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI22361.1; -; Genomic_DNA. DR EMBL; AL139219; CAI22361.1; JOINED; Genomic_DNA. DR EMBL; AL161740; CAI22361.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI22362.1; -; Genomic_DNA. DR EMBL; AL139219; CAI22362.1; JOINED; Genomic_DNA. DR EMBL; AL161740; CAI22362.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI22363.1; -; Genomic_DNA. DR EMBL; AL139219; CAI22363.1; JOINED; Genomic_DNA. DR EMBL; AL354883; CAI22364.1; -; Genomic_DNA. DR EMBL; AL139219; CAI22364.1; JOINED; Genomic_DNA. DR EMBL; AL161740; CAI22364.1; JOINED; Genomic_DNA. DR EMBL; AK095513; BAG53075.1; -; mRNA. DR EMBL; AB210012; BAE06094.1; ALT_INIT; mRNA. DR EMBL; CH471059; EAX06637.1; -; Genomic_DNA. DR EMBL; BC067445; AAH67445.1; -; mRNA. DR EMBL; BC067446; AAH67446.1; -; mRNA. DR EMBL; BC067447; AAH67447.1; -; mRNA. DR EMBL; BC112938; AAI12939.1; -; mRNA. DR CCDS; CCDS607.1; -. [O75553-6] DR RefSeq; NP_066566.3; NM_021080.3. [O75553-6] DR UniGene; Hs.477370; -. DR ProteinModelPortal; O75553; -. DR SMR; O75553; 23-174. DR BioGrid; 107970; 63. DR IntAct; O75553; 46. DR MINT; MINT-156038; -. DR PhosphoSite; O75553; -. DR BioMuta; DAB1; -. DR PaxDb; O75553; -. DR PRIDE; O75553; -. DR Ensembl; ENST00000371230; ENSP00000360274; ENSG00000173406. [O75553-2] DR Ensembl; ENST00000371231; ENSP00000360275; ENSG00000173406. [O75553-1] DR Ensembl; ENST00000371236; ENSP00000360280; ENSG00000173406. [O75553-6] DR Ensembl; ENST00000414851; ENSP00000387581; ENSG00000173406. [O75553-6] DR Ensembl; ENST00000420954; ENSP00000395296; ENSG00000173406. [O75553-5] DR GeneID; 1600; -. DR KEGG; hsa:1600; -. DR UCSC; uc001cyq.1; human. [O75553-5] DR UCSC; uc001cyr.1; human. [O75553-3] DR UCSC; uc001cys.1; human. [O75553-6] DR UCSC; uc001cyt.1; human. [O75553-1] DR UCSC; uc009vzw.1; human. [O75553-4] DR CTD; 1600; -. DR GeneCards; GC01M057460; -. DR HGNC; HGNC:2661; DAB1. DR HPA; CAB032329; -. DR HPA; HPA052033; -. DR MIM; 603448; gene. DR neXtProt; NX_O75553; -. DR PharmGKB; PA27131; -. DR eggNOG; NOG313182; -. DR GeneTree; ENSGT00520000055585; -. DR HOVERGEN; HBG018945; -. DR InParanoid; O75553; -. DR OMA; FQMAQPP; -. DR OrthoDB; EOG7HQN7R; -. DR PhylomeDB; O75553; -. DR TreeFam; TF316724; -. DR SignaLink; O75553; -. DR ChiTaRS; DAB1; human. DR GeneWiki; DAB1; -. DR GenomeRNAi; 1600; -. DR NextBio; 6562; -. DR PRO; PR:O75553; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; O75553; -. DR ExpressionAtlas; O75553; baseline and differential. DR Genevestigator; O75553; -. 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: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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl. DR GO; GO:0021813; P:cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration; IEA:Ensembl. DR GO; GO:0021589; P:cerebellum structural organization; IEA:Ensembl. DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl. DR GO; GO:0016358; P:dendrite development; IEA:Ensembl. DR GO; GO:0051645; P:Golgi localization; IEA:Ensembl. DR GO; GO:0097477; P:lateral motor column neuron migration; IEA:Ensembl. DR GO; GO:0007494; P:midgut development; IEA:Ensembl. DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl. DR GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl. DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl. DR GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IEA:Ensembl. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl. DR GO; GO:0021517; P:ventral spinal cord development; IEA:Ensembl. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR011993; PH_like_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 Alternative splicing; Complete proteome; Developmental protein; KW Differentiation; Neurogenesis; Phosphoprotein; Polymorphism; KW Reference proteome. FT CHAIN 1 588 Disabled homolog 1. FT /FTId=PRO_0000079767. FT DOMAIN 36 189 PID. {ECO:0000255|PROSITE- FT ProRule:PRU00148}. FT MOD_RES 198 198 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P97318}. FT MOD_RES 220 220 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P97318}. FT MOD_RES 232 232 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P97318}. FT MOD_RES 524 524 Phosphoserine; by CDK5. {ECO:0000250}. FT VAR_SEQ 103 221 Missing (in isoform DAB469). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_026166. FT VAR_SEQ 185 219 Missing (in isoform DAB553 and isoform FT DAB537). {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_026167. FT VAR_SEQ 200 213 YIVFEAGHEPIRDP -> VISETSRGFRFKSD (in FT isoform DAB213). {ECO:0000305}. FT /FTId=VSP_026168. FT VAR_SEQ 214 588 Missing (in isoform DAB213). FT {ECO:0000305}. FT /FTId=VSP_026169. FT VAR_SEQ 242 274 Missing (in isoform DAB555). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9790777, FT ECO:0000303|Ref.2}. FT /FTId=VSP_026170. FT VAR_SEQ 259 274 Missing (in isoform DAB537). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_026171. FT VARIANT 71 71 V -> I (in dbSNP:rs1855377). FT /FTId=VAR_056857. FT CONFLICT 15 15 A -> T (in Ref. 6; AAI12939). FT {ECO:0000305}. FT CONFLICT 59 59 K -> M (in Ref. 6; AAH67447). FT {ECO:0000305}. FT CONFLICT 86 86 F -> L (in Ref. 2; AAF73058). FT {ECO:0000305}. FT CONFLICT 295 295 P -> S (in Ref. 6; AAH67447). FT {ECO:0000305}. FT CONFLICT 324 324 F -> L (in Ref. 1; AAC70068). FT {ECO:0000305}. FT CONFLICT 331 331 S -> P (in Ref. 1; AAC70068). FT {ECO:0000305}. FT CONFLICT 359 359 Q -> H (in Ref. 1; AAC70068). FT {ECO:0000305}. FT CONFLICT 368 368 G -> R (in Ref. 2; AAF73058). FT {ECO:0000305}. FT CONFLICT 412 412 M -> V (in Ref. 2; AAF73058). FT {ECO:0000305}. FT CONFLICT 586 586 A -> D (in Ref. 1; AAC70068). FT {ECO:0000305}. SQ SEQUENCE 588 AA; 63775 MW; DAD4024364113AC5 CRC64; MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDI TDHRAFGYVC GKEGNHRFVA IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC EQAVYQTILE EDVEDPVYQY IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPV SNGYSFEDFE ERFAAATPNR NLPTDFDEIF EATKAVTQLE LFGDMSTPPD ITSPPTPATP GDAFIPSSSQ TLPASADVFS SVPFGTAAVP SGYVAMGAVL PSFWGQQPLV QQQMVMGAQP PVAQVMPGAQ PIAWGQPGLF PATQQPWPTV AGQFPPAAFM PTQTVMPLPA AMFQGPLTPL ATVPGTSDST RSSPQTDKPR QKMGKETFKD FQMAQPPPVP SRKPDQPSLT CTSEAFSSYF NKVGVAQDTD DCDDFDISQL NLTPVTSTTP STNSPPTPAP RQSSPSKSSA SHASDPTTDD IFEEGFESPS KSEEQEAPDG SQASSNSDPF GEPSGEPSGD NISPQAGS //