ID DAB1_HUMAN Reviewed; 588 AA. AC O75553; A4FU90; B3KTG3; Q4LE59; Q5T6M6; Q5T6M9; Q5T835; Q5T836; Q5T837; AC Q6NWS9; Q6NWT0; Q6NWT1; Q9NYA8; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 3. DT 24-JAN-2024, entry version 184. DE RecName: Full=Disabled homolog 1; GN Name=DAB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 SPLICING. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., 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., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., 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., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 project: RT 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., Peltan I.D., RA 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 endocytosis and RT association with adaptor molecules."; RL J. Biol. Chem. 279:40536-40544(2004). RN [8] RP INVOLVEMENT IN SCA37, AND TISSUE SPECIFICITY. RX PubMed=28686858; DOI=10.1016/j.ajhg.2017.06.007; RA Seixas A.I., Loureiro J.R., Costa C., Ordonez-Ugalde A., Marcelino H., RA Oliveira C.L., Loureiro J.L., Dhingra A., Brandao E., Cruz V.T., RA Timoteo A., Quintans B., Rouleau G.A., Rizzu P., Carracedo A., Bessa J., RA Heutink P., Sequeiros J., Sobrido M.J., Coutinho P., Silveira I.; RT "A pentanucleotide ATTTC repeat insertion in the non-coding region of DAB1, RT mapping to SCA37, causes spinocerebellar ataxia."; RL Am. J. Hum. Genet. 101:87-103(2017). CC -!- FUNCTION: Adapter molecule functioning in neural development. May CC regulate SIAH1 activity. {ECO:0000250|UniProtKB:P97318}. CC -!- SUBUNIT: Associates with the SH2 domains of SRC, FYN and ABL (By CC similarity). Interacts (phosphorylated on tyrosine residues) with CRK CC and CRKL (via respective SH2 domain) (By similarity). Interacts with CC SIAH1, LRP8 and VLDLR (By similarity). Interacts with LRP1 CC (PubMed:15272003). Interacts with APLP1 (via NPXY motif) (By CC similarity). Interacts with DAB2IP (By similarity). CC {ECO:0000250|UniProtKB:P97318, ECO:0000250|UniProtKB:Q8CJH2, CC ECO:0000269|PubMed:15272003}. CC -!- INTERACTION: CC O75553; O14503: BHLHE40; NbExp=3; IntAct=EBI-7875264, EBI-711810; CC O75553; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-7875264, EBI-946029; CC O75553; Q8N365: CIART; NbExp=3; IntAct=EBI-7875264, EBI-10265133; CC O75553; Q15038: DAZAP2; NbExp=3; IntAct=EBI-7875264, EBI-724310; CC O75553; Q92567: FAM168A; NbExp=3; IntAct=EBI-7875264, EBI-7957930; CC O75553; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-7875264, EBI-10188461; CC O75553; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-7875264, EBI-2549423; CC O75553; Q8WVV9: HNRNPLL; NbExp=3; IntAct=EBI-7875264, EBI-535849; CC O75553; O43820: HYAL3; NbExp=3; IntAct=EBI-7875264, EBI-3913399; CC O75553; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-7875264, EBI-1048945; CC O75553; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-7875264, EBI-10241353; CC O75553; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-7875264, EBI-10261141; CC O75553; Q3B8N2: LGALS9B; NbExp=3; IntAct=EBI-7875264, EBI-10240775; CC O75553; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-7875264, EBI-9088829; CC O75553; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-7875264, EBI-739832; CC O75553; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-7875264, EBI-716006; CC O75553; Q86VM6: MBNL1; NbExp=3; IntAct=EBI-7875264, EBI-10225084; CC O75553; Q9NR56: MBNL1; NbExp=4; IntAct=EBI-7875264, EBI-2805004; CC O75553; Q9NUK0: MBNL3; NbExp=3; IntAct=EBI-7875264, EBI-6661142; CC O75553; Q96HR8: NAF1; NbExp=3; IntAct=EBI-7875264, EBI-2515597; CC O75553; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-7875264, EBI-741158; CC O75553; Q13526: PIN1; NbExp=3; IntAct=EBI-7875264, EBI-714158; CC O75553; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-7875264, EBI-1389308; CC O75553; Q13427: PPIG; NbExp=3; IntAct=EBI-7875264, EBI-396072; CC O75553; P86479: PRR20C; NbExp=3; IntAct=EBI-7875264, EBI-10172814; CC O75553; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-7875264, EBI-744023; CC O75553; O43251: RBFOX2; NbExp=3; IntAct=EBI-7875264, EBI-746056; CC O75553; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-7875264, EBI-372094; CC O75553; A1L4F5: ROR2; NbExp=3; IntAct=EBI-7875264, EBI-10172778; CC O75553; O00241-2: SIRPB1; NbExp=3; IntAct=EBI-7875264, EBI-10179231; CC O75553; Q8WU79: SMAP2; NbExp=3; IntAct=EBI-7875264, EBI-2822515; CC O75553; P14678-2: SNRPB; NbExp=3; IntAct=EBI-7875264, EBI-372475; CC O75553; Q96SI9: STRBP; NbExp=3; IntAct=EBI-7875264, EBI-740355; CC O75553; Q15560: TCEA2; NbExp=3; IntAct=EBI-7875264, EBI-710310; CC O75553; Q86VL0: TCEA2; NbExp=3; IntAct=EBI-7875264, EBI-10259904; CC O75553; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-7875264, EBI-954696; CC O75553; Q6ZXV5: TMTC3; NbExp=3; IntAct=EBI-7875264, EBI-10188441; CC O75553; Q6FIE9: TOLLIP; NbExp=3; IntAct=EBI-7875264, EBI-10249783; CC O75553; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-7875264, EBI-74615; CC O75553; O95231: VENTX; NbExp=4; IntAct=EBI-7875264, EBI-10191303; CC O75553; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-7875264, EBI-10188476; CC O75553; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-7875264, EBI-742550; CC O75553; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-7875264, EBI-597063; CC O75553; Q96MN9: ZNF488; NbExp=3; IntAct=EBI-7875264, EBI-948288; CC O75553; Q9H9I0; NbExp=3; IntAct=EBI-7875264, EBI-10309771; CC O75553-4; P05067: APP; NbExp=3; IntAct=EBI-21246842, EBI-77613; CC O75553-5; Q13526: PIN1; NbExp=3; IntAct=EBI-12133006, EBI-714158; CC O75553-5; P04271: S100B; NbExp=3; IntAct=EBI-12133006, EBI-458391; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=DAB588; CC IsoId=O75553-1; Sequence=Displayed; CC Name=DAB213; CC IsoId=O75553-2; Sequence=VSP_026168, VSP_026169; CC Name=DAB469; CC IsoId=O75553-3; Sequence=VSP_026166; CC Name=DAB537; CC IsoId=O75553-4; Sequence=VSP_026167, VSP_026171; CC Name=DAB553; CC IsoId=O75553-5; Sequence=VSP_026167; CC Name=DAB555; CC IsoId=O75553-6; Sequence=VSP_026170; CC -!- TISSUE SPECIFICITY: Mainly expressed in brain. CC {ECO:0000269|PubMed:28686858}. 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. Also phosphorylated on Ser-524 independently of CC reelin signaling. {ECO:0000250|UniProtKB:P97318}. CC -!- DISEASE: Spinocerebellar ataxia 37 (SCA37) [MIM:615945]: A form of CC spinocerebellar ataxia, a clinically and genetically heterogeneous CC group of cerebellar disorders. Patients show progressive incoordination CC of gait and often poor coordination of hands, speech and eye movements, CC due to degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. SCA37 is an autosomal dominant form CC characterized by adult-onset of slowly progressive gait instability, CC frequent falls, and dysarthria associated with cerebellar atrophy on CC brain imaging. {ECO:0000269|PubMed:28686858}. Note=The disease is CC caused by variants affecting the gene represented in this entry. 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; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL161740; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL354883; -; NOT_ANNOTATED_CDS; 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 AlphaFoldDB; O75553; -. DR SMR; O75553; -. DR BioGRID; 107970; 84. DR ELM; O75553; -. DR IntAct; O75553; 58. DR MINT; O75553; -. DR STRING; 9606.ENSP00000360280; -. DR GlyGen; O75553; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75553; -. DR PhosphoSitePlus; O75553; -. DR BioMuta; DAB1; -. DR EPD; O75553; -. DR MassIVE; O75553; -. DR PaxDb; 9606-ENSP00000360280; -. DR PeptideAtlas; O75553; -. DR ProteomicsDB; 50077; -. [O75553-1] DR ProteomicsDB; 50078; -. [O75553-2] DR ProteomicsDB; 50079; -. [O75553-3] DR ProteomicsDB; 50080; -. [O75553-4] DR ProteomicsDB; 50081; -. [O75553-5] DR ProteomicsDB; 50082; -. [O75553-6] DR Pumba; O75553; -. DR Antibodypedia; 19377; 608 antibodies from 35 providers. DR DNASU; 1600; -. DR Ensembl; ENST00000371230.1; ENSP00000360274.1; ENSG00000173406.16. [O75553-2] DR Ensembl; ENST00000371231.5; ENSP00000360275.1; ENSG00000173406.16. [O75553-1] DR Ensembl; ENST00000371236.7; ENSP00000360280.1; ENSG00000173406.16. [O75553-6] DR Ensembl; ENST00000414851.6; ENSP00000387581.3; ENSG00000173406.16. [O75553-6] DR Ensembl; ENST00000420954.6; ENSP00000395296.2; ENSG00000173406.16. [O75553-5] DR GeneID; 1600; -. DR KEGG; hsa:1600; -. DR MANE-Select; ENST00000371236.7; ENSP00000360280.1; NM_001365792.1; NP_001352721.1. [O75553-6] DR UCSC; uc001cyq.2; human. [O75553-1] DR AGR; HGNC:2661; -. DR CTD; 1600; -. DR DisGeNET; 1600; -. DR GeneCards; DAB1; -. DR GeneReviews; DAB1; -. DR HGNC; HGNC:2661; DAB1. DR HPA; ENSG00000173406; Tissue enhanced (brain, intestine, seminal vesicle). DR MalaCards; DAB1; -. DR MIM; 603448; gene. DR MIM; 615945; phenotype. DR neXtProt; NX_O75553; -. DR OpenTargets; ENSG00000173406; -. DR Orphanet; 363710; Spinocerebellar ataxia type 37. DR PharmGKB; PA27131; -. DR VEuPathDB; HostDB:ENSG00000173406; -. DR eggNOG; KOG3535; Eukaryota. DR GeneTree; ENSGT00940000158038; -. DR HOGENOM; CLU_020747_2_0_1; -. DR InParanoid; O75553; -. DR OMA; FDEKTGX; -. DR OrthoDB; 2913989at2759; -. DR PhylomeDB; O75553; -. DR TreeFam; TF316724; -. DR PathwayCommons; O75553; -. DR Reactome; R-HSA-8866376; Reelin signalling pathway. DR SignaLink; O75553; -. DR SIGNOR; O75553; -. DR BioGRID-ORCS; 1600; 7 hits in 1138 CRISPR screens. DR ChiTaRS; DAB1; human. DR GeneWiki; DAB1; -. DR GenomeRNAi; 1600; -. DR Pharos; O75553; Tbio. DR PRO; PR:O75553; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O75553; Protein. DR Bgee; ENSG00000173406; Expressed in cortical plate and 129 other cell types or tissues. DR ExpressionAtlas; O75553; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl. DR GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl. DR GO; GO:0007409; P:axonogenesis; 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:0016358; P:dendrite development; IEA:Ensembl. DR GO; GO:0051645; P:Golgi localization; IEA:Ensembl. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0097477; P:lateral motor column neuron migration; IBA:GO_Central. 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 receptor signaling pathway via JAK-STAT; IEA:Ensembl. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IEA:Ensembl. DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IEA:Ensembl. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl. DR GO; GO:0021517; P:ventral spinal cord development; IBA:GO_Central. DR CDD; cd01215; PTB_Dab; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR048559; DAB1/2_SBM. DR InterPro; IPR048561; Dab_PTB. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR006020; PTB/PI_dom. DR PANTHER; PTHR47695:SF4; DISABLED HOMOLOG 1; 1. DR PANTHER; PTHR47695; PID DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF21792; DAB2_SBM; 1. DR Pfam; PF00640; PID; 1. DR SMART; SM00462; PTB; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS01179; PID; 1. DR Genevisible; O75553; HS. PE 1: Evidence at protein level; KW Alternative splicing; Developmental protein; Differentiation; KW Neurodegeneration; Neurogenesis; Phosphoprotein; Reference proteome; KW Spinocerebellar ataxia. FT CHAIN 1..588 FT /note="Disabled homolog 1" FT /id="PRO_0000079767" 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 417..443 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:0000250|UniProtKB:P97318" FT MOD_RES 220 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P97318" FT MOD_RES 232 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P97318" FT MOD_RES 524 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P97318" FT VAR_SEQ 103..221 FT /note="Missing (in isoform DAB469)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026166" FT VAR_SEQ 185..219 FT /note="Missing (in isoform DAB553 and isoform DAB537)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026167" FT VAR_SEQ 200..213 FT /note="YIVFEAGHEPIRDP -> VISETSRGFRFKSD (in isoform FT DAB213)" FT /evidence="ECO:0000305" FT /id="VSP_026168" FT VAR_SEQ 214..588 FT /note="Missing (in isoform DAB213)" FT /evidence="ECO:0000305" FT /id="VSP_026169" FT VAR_SEQ 242..274 FT /note="Missing (in isoform DAB555)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9790777, ECO:0000303|Ref.2" FT /id="VSP_026170" FT VAR_SEQ 259..274 FT /note="Missing (in isoform DAB537)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026171" FT VARIANT 71 FT /note="V -> I (in dbSNP:rs1855377)" FT /id="VAR_056857" FT CONFLICT 15 FT /note="A -> T (in Ref. 6; AAI12939)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="K -> M (in Ref. 6; AAH67447)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="F -> L (in Ref. 2; AAF73058)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="P -> S (in Ref. 6; AAH67447)" FT /evidence="ECO:0000305" FT CONFLICT 324 FT /note="F -> L (in Ref. 1; AAC70068)" FT /evidence="ECO:0000305" FT CONFLICT 331 FT /note="S -> P (in Ref. 1; AAC70068)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="Q -> H (in Ref. 1; AAC70068)" FT /evidence="ECO:0000305" FT CONFLICT 368 FT /note="G -> R (in Ref. 2; AAF73058)" FT /evidence="ECO:0000305" FT CONFLICT 412 FT /note="M -> V (in Ref. 2; AAF73058)" FT /evidence="ECO:0000305" FT CONFLICT 586 FT /note="A -> D (in Ref. 1; AAC70068)" FT /evidence="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 //