DAB1_HUMAN
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 03-AUG-2022, entry version 176.
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};
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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; 80.
DR ELM; O75553; -.
DR IntAct; O75553; 58.
DR MINT; O75553; -.
DR STRING; 9606.ENSP00000360280; -.
DR iPTMnet; O75553; -.
DR PhosphoSitePlus; O75553; -.
DR BioMuta; DAB1; -.
DR EPD; O75553; -.
DR MassIVE; O75553; -.
DR PeptideAtlas; O75553; -.
DR PRIDE; 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 Antibodypedia; 19377; 524 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 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; 279276at2759; -.
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 1059 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 127 other tissues.
DR ExpressionAtlas; O75553; baseline and differential.
DR Genevisible; O75553; HS.
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: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: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 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 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
