DCX_HUMAN
ID DCX_HUMAN Reviewed; 365 AA.
AC O43602; A6NFY6; A9Z1V8; D3DUY8; D3DUY9; D3DUZ0; O43911; Q5JYZ5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Neuronal migration protein doublecortin;
DE AltName: Full=Doublin;
DE AltName: Full=Lissencephalin-X;
DE Short=Lis-X;
GN Name=DCX; Synonyms=DBCN, LISX;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), ALTERNATIVE SPLICING,
RP AND VARIANTS LISX1 ASN-62; HIS-125 AND TRP-192.
RC TISSUE=Fetal brain;
RX PubMed=9489699; DOI=10.1016/s0092-8674(00)80898-3;
RA Des Portes V., Pinard J.-M., Billuart P., Vinet M.-C., Koulakoff A.,
RA Carrie A., Gelot A., Dupuis E., Motte J., Berwald-Netter Y., Catala M.,
RA Kahn A., Beldjord C., Chelly J.;
RT "A novel CNS gene required for neuronal migration and involved in X-linked
RT subcortical laminar heterotopia and lissencephaly syndrome.";
RL Cell 92:51-61(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS LISX1 ARG-47; LEU-59
RP AND ARG-203.
RC TISSUE=Brain;
RX PubMed=9489700; DOI=10.1016/s0092-8674(00)80899-5;
RA Gleeson J.G., Allen K.M., Fox J.W., Lamperti E.D., Berkovic S.,
RA Scheffer I., Cooper E.C., Dobyns W.B., Minnerath S.R., Ross M.E.,
RA Walsh C.A.;
RT "Doublecortin, a brain-specific gene mutated in human X-linked
RT lissencephaly and double cortex syndrome, encodes a putative signaling
RT protein.";
RL Cell 92:63-72(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RA Sossey-Alaoui K., Srivastava A.K.;
RT "X-linked neuronal migration disorder (lissencephaly/subcortical band
RT heterotopia) is caused by mutation in a novel brain-specific protein,
RT lissencephalin-X.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION AT SER-306.
RX PubMed=22359282; DOI=10.1002/cm.21021;
RA Slepak T.I., Salay L.D., Lemmon V.P., Bixby J.L.;
RT "Dyrk kinases regulate phosphorylation of doublecortin, cytoskeletal
RT organization, and neuronal morphology.";
RL Cytoskeleton 69:514-527(2012).
RN [9]
RP INTERACTION WITH USP9X.
RX PubMed=24607389; DOI=10.1016/j.ajhg.2014.02.004;
RA Homan C.C., Kumar R., Nguyen L.S., Haan E., Raymond F.L., Abidi F.,
RA Raynaud M., Schwartz C.E., Wood S.A., Gecz J., Jolly L.A.;
RT "Mutations in USP9X are associated with X-linked intellectual disability
RT and disrupt neuronal cell migration and growth.";
RL Am. J. Hum. Genet. 94:470-478(2014).
RN [10]
RP STRUCTURE BY NMR OF 45-150.
RX PubMed=12692530; DOI=10.1038/nsb918;
RA Kim M.H., Cierpicki T., Derewenda U., Krowarsch D., Feng Y., Devedjiev Y.,
RA Dauter Z., Walsh C.A., Otlewski J., Bushweller J.H., Derewenda Z.S.;
RT "The DCX-domain tandems of doublecortin and doublecortin-like kinase.";
RL Nat. Struct. Biol. 10:324-333(2003).
RN [11]
RP VARIANTS LISX1/SBHX LEU-78; ALA-100; CYS-186 AND LYS-200.
RX PubMed=9668176; DOI=10.1093/hmg/7.8.1327;
RA Sossey-Alaoui K., Hartung A.J., Guerrini R., Manchester D.K., Posar A.,
RA Puche-Mira A., Andermann E., Dobyns W.B., Srivastava A.K.;
RT "Human doublecortin (DCX) and the homologous gene in mouse encode a
RT putative Ca2+-dependent signaling protein which is mutated in human X-
RT linked neuronal migration defects.";
RL Hum. Mol. Genet. 7:1327-1332(1998).
RN [12]
RP VARIANTS LISX1 SER-43 AND SER-102.
RX PubMed=9817918; DOI=10.1093/hmg/7.13.2029;
RA Pilz D.T., Matsumoto N., Minnerath S.R., Mills P., Gleeson J.G.,
RA Allen K.M., Walsh C.A., Barkovich A.J., Dobyns W.B., Ledbetter D.H.,
RA Ross M.E.;
RT "LIS1 and XLIS (DCX) mutations cause most classical lissencephaly, but
RT different patterns of malformation.";
RL Hum. Mol. Genet. 7:2029-2037(1998).
RN [13]
RP VARIANTS SBHX ASP-125; GLU-223 AND THR-250.
RX PubMed=9618162; DOI=10.1093/hmg/7.7.1063;
RA Des Portes V., Francis F., Pinard J.-M., Desguerre I., Moutard M.-L.,
RA Snoeck I., Meiners L.C., Capron F., Cusmai R., Ricci S., Motte J.,
RA Echenne B., Ponsot G., Dulac O., Chelly J., Beldjord C.;
RT "Doublecortin is the major gene causing X-linked subcortical laminar
RT heterotopia (SCLH).";
RL Hum. Mol. Genet. 7:1063-1070(1998).
RN [14]
RP VARIANTS SBHX.
RX PubMed=9989615; DOI=10.1002/1531-8249(199902)45:2<146::aid-ana3>3.0.co;2-n;
RA Gleeson J.G., Minnerath S.R., Fox J.W., Allen K.M., Luo R.F., Hong S.E.,
RA Berg M.J., Kuzniecky R., Reitnauer P.J., Borgatti R., Puche-Mira A.,
RA Guerrini R., Holmes G.L., Rooney C.M., Berkovic S., Scheffer I.,
RA Cooper E.C., Ricci S., Cusmai R., Crawford T.O., Leroy R., Andermann E.,
RA Wheless J.W., Dobyns W.B., Ross M.E., Walsh C.A.;
RT "Characterization of mutations in the gene doublecortin in patients with
RT double cortex syndrome.";
RL Ann. Neurol. 45:146-153(1999).
RN [15]
RP VARIANT SBHX CYS-186.
RX PubMed=10369164; DOI=10.1007/s004390050963;
RA Kato M., Kimura T., Lin C., Ito A., Kodama S., Morikawa T., Soga T.,
RA Hayasaka K.;
RT "A novel mutation of the doublecortin gene in Japanese patients with X-
RT linked lissencephaly and subcortical band heterotopia.";
RL Hum. Genet. 104:341-344(1999).
RN [16]
RP VARIANTS SBHX HIS-78 AND GLY-89.
RX PubMed=10441340; DOI=10.1093/hmg/8.9.1757;
RA Pilz D.T., Kuc J., Matsumoto N., Bodurtha J., Bernadi B., Tassinari C.A.,
RA Dobyns W.B., Ledbetter D.H.;
RT "Subcortical band heterotopia in rare affected males can be caused by
RT missense mutations in DCX (XLIS) or LIS1.";
RL Hum. Mol. Genet. 8:1757-1760(1999).
RN [17]
RP VARIANT SBHX VAL-251.
RX PubMed=10807542; DOI=10.1007/s100380050204;
RA Sakamoto M., Ono J., Okada S., Nakamura Y., Kurahashi H.;
RT "Genetic alteration of the DCX gene in Japanese patients with subcortical
RT laminar heterotopia or isolated lissencephaly sequence.";
RL J. Hum. Genet. 45:167-170(2000).
RN [18]
RP VARIANT SBHX ASN-50.
RX PubMed=11601509; DOI=10.1002/ana.1231;
RA Kato M., Kanai M., Soma O., Takusa Y., Kimura T., Numakura C., Matsuki T.,
RA Nakamura S., Hayasaka K.;
RT "Mutation of the doublecortin gene in male patients with double cortex
RT syndrome: somatic mosaicism detected by hair root analysis.";
RL Ann. Neurol. 50:547-551(2001).
RN [19]
RP VARIANTS SBHX ARG-47; HIS-59; LEU-78; HIS-86; GLY-89; ARG-97; ALA-100;
RP THR-104; CYS-186; TRP-192; HIS-196; ILE-200; LYS-200; ALA-203; ARG-203;
RP THR-214; VAL-223 AND SER-251.
RX PubMed=11175293; DOI=10.1038/sj.ejhg.5200548;
RA Matsumoto N., Leventer R.J., Kuc J.A., Mewborn S.K., Dudlicek L.L.,
RA Ramocki M.B., Pilz D.T., Mills P.L., Das S., Ross M.E., Ledbetter D.H.,
RA Dobyns W.B.;
RT "Mutation analysis of the DCX gene and genotype/phenotype correlation in
RT subcortical band heterotopia.";
RL Eur. J. Hum. Genet. 9:5-12(2001).
RN [20]
RP VARIANT LISX1 HIS-196.
RX PubMed=11468322; DOI=10.1212/wnl.57.2.327;
RA Demelas L., Serra G., Conti M., Achene A., Mastropaolo C., Matsumoto N.,
RA Dudlicek L.L., Mills P.L., Dobyns W.B., Ledbetter D.H., Das S.;
RT "Incomplete penetrance with normal MRI in a woman with germline mutation of
RT the DCX gene.";
RL Neurology 57:327-330(2001).
RN [21]
RP VARIANTS SBHX GLU-67 AND CYS-178.
RX PubMed=12390976; DOI=10.1093/brain/awf248;
RA D'Agostino M.D., Bernasconi A., Das S., Bastos A., Valerio R.M.,
RA Palmini A., Costa da Costa J., Scheffer I.E., Berkovic S., Guerrini R.,
RA Dravet C., Ono J., Gigli G., Federico A., Booth F., Bernardi B., Volpi L.,
RA Tassinari C.A., Guggenheim M.A., Ledbetter D.H., Gleeson J.G.,
RA Lopes-Cendes I., Vossler D.G., Malaspina E., Franzoni E., Sartori R.J.,
RA Mitchell M.H., Mercho S., Dubeau F., Andermann F., Dobyns W.B.,
RA Andermann E.;
RT "Subcortical band heterotopia (SBH) in males: clinical, imaging and genetic
RT findings in comparison with females.";
RL Brain 125:2507-2522(2002).
RN [22]
RP VARIANT EPILEPSY SER-196.
RX PubMed=12027577; DOI=10.1053/seiz.2001.0607;
RA des Portes V., Abaoub L., Joannard A., Souville I., Francis F.,
RA Pinard J.-M., Chelly J., Beldjord C., Jouk P.S.;
RT "So-called 'cryptogenic' partial seizures resulting from a subtle cortical
RT dysgenesis due to a doublecortin gene mutation.";
RL Seizure 11:273-277(2002).
RN [23]
RP VARIANTS LISX1 ILE-42; ASP-60; SER-71 AND LEU-243.
RX PubMed=12552055; DOI=10.1212/01.wnl.0000042091.90361.d2;
RA Aigner L., Uyanik G., Couillard-Despres S., Ploetz S., Wolff G.,
RA Morris-Rosendahl D., Martin P., Eckel U., Spranger S., Otte J., Woerle H.,
RA Holthausen H., Apheshiotis N., Fluegel D., Winkler J.;
RT "Somatic mosaicism and variable penetrance in doublecortin-associated
RT migration disorders.";
RL Neurology 60:329-332(2003).
RN [24]
RP VARIANT LISX1 GLY-262, CHARACTERIZATION OF VARIANT LISX1 GLY-262, AND
RP SUBUNIT.
RX PubMed=27292316; DOI=10.1016/j.ejpn.2016.05.010;
RA Tsai M.H., Kuo P.W., Myers C.T., Li S.W., Lin W.C., Fu T.Y., Chang H.Y.,
RA Mefford H.C., Chang Y.C., Tsai J.W.;
RT "A novel DCX missense mutation in a family with X-linked lissencephaly and
RT subcortical band heterotopia syndrome inherited from a low-level somatic
RT mosaic mother: Genetic and functional studies.";
RL Eur. J. Paediatr. Neurol. 20:788-794(2016).
CC -!- FUNCTION: Microtubule-associated protein required for initial steps of
CC neuronal dispersion and cortex lamination during cerebral cortex
CC development. May act by competing with the putative neuronal protein
CC kinase DCLK1 in binding to a target protein. May in that way
CC participate in a signaling pathway that is crucial for neuronal
CC interaction before and during migration, possibly as part of a calcium
CC ion-dependent signal transduction pathway. May be part with
CC PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that
CC promote neuronal migration. {ECO:0000269|PubMed:22359282}.
CC -!- SUBUNIT: Interacts with tubulin (PubMed:27292316). Interacts with USP9X
CC (PubMed:24607389). {ECO:0000269|PubMed:24607389,
CC ECO:0000269|PubMed:27292316}.
CC -!- INTERACTION:
CC O43602; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-8646694, EBI-739580;
CC O43602; Q08379: GOLGA2; NbExp=4; IntAct=EBI-8646694, EBI-618309;
CC O43602; Q13422: IKZF1; NbExp=4; IntAct=EBI-8646694, EBI-745305;
CC O43602; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-8646694, EBI-2125614;
CC O43602; Q6A162: KRT40; NbExp=3; IntAct=EBI-8646694, EBI-10171697;
CC O43602; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8646694, EBI-10171774;
CC O43602; P50221: MEOX1; NbExp=3; IntAct=EBI-8646694, EBI-2864512;
CC O43602; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-8646694, EBI-10172526;
CC O43602; Q6NUQ1: RINT1; NbExp=4; IntAct=EBI-8646694, EBI-726876;
CC O43602; Q96R06: SPAG5; NbExp=3; IntAct=EBI-8646694, EBI-413317;
CC O43602; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-8646694, EBI-717399;
CC O43602; P36406: TRIM23; NbExp=3; IntAct=EBI-8646694, EBI-740098;
CC O43602; P14373: TRIM27; NbExp=3; IntAct=EBI-8646694, EBI-719493;
CC O43602; O15062: ZBTB5; NbExp=3; IntAct=EBI-8646694, EBI-722671;
CC O43602-2; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-14148644, EBI-11975051;
CC O43602-2; A1L4K1: FSD2; NbExp=3; IntAct=EBI-14148644, EBI-5661036;
CC O43602-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-14148644, EBI-618309;
CC O43602-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-14148644, EBI-10961706;
CC O43602-2; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-14148644, EBI-11522367;
CC O43602-2; P45984: MAPK9; NbExp=3; IntAct=EBI-14148644, EBI-713568;
CC O43602-2; P50221: MEOX1; NbExp=3; IntAct=EBI-14148644, EBI-2864512;
CC O43602-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-14148644, EBI-16439278;
CC O43602-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-14148644, EBI-10172526;
CC O43602-2; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-14148644, EBI-11522433;
CC O43602-2; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-14148644, EBI-2799833;
CC O43602-2; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-14148644, EBI-12017160;
CC O43602-2; O15062: ZBTB5; NbExp=3; IntAct=EBI-14148644, EBI-722671;
CC O43602-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-14148644, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:Q9ESI7}. Note=Localizes at neurite
CC tips. {ECO:0000250|UniProtKB:Q9ESI7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O43602-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43602-2; Sequence=VSP_058155;
CC -!- TISSUE SPECIFICITY: Highly expressed in neuronal cells of fetal brain
CC (in the majority of cells of the cortical plate, intermediate zone and
CC ventricular zone), but not expressed in other fetal tissues. In the
CC adult, highly expressed in the brain frontal lobe, but very low
CC expression in other regions of brain, and not detected in heart,
CC placenta, lung, liver, skeletal muscles, kidney and pancreas.
CC -!- PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability to
CC bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-
CC 297 seems to occur only in neonatal brain, the levels falling
CC precipitously by postnatal day 21 (By similarity).
CC {ECO:0000250|UniProtKB:O88809, ECO:0000250|UniProtKB:Q9ESI7}.
CC -!- PTM: Ubiquitinated by MDM2, leading to its degradation by the
CC proteasome. Ubiquitinated by MDM2 and subsequent degradation leads to
CC reduce the dendritic spine density of olfactory bulb granule cells.
CC {ECO:0000250|UniProtKB:O88809}.
CC -!- DISEASE: Lissencephaly, X-linked 1 (LISX1) [MIM:300067]: A classic
CC lissencephaly characterized by intellectual disability and seizures
CC that are more severe in male patients. Affected boys show an abnormally
CC thick cortex with absent or severely reduced gyri. Clinical
CC manifestations include feeding problems, abnormal muscular tone,
CC seizures and severe to profound psychomotor retardation. Female
CC patients display a less severe phenotype referred to as 'doublecortex'.
CC {ECO:0000269|PubMed:11468322, ECO:0000269|PubMed:12552055,
CC ECO:0000269|PubMed:27292316, ECO:0000269|PubMed:9489699,
CC ECO:0000269|PubMed:9489700, ECO:0000269|PubMed:9668176,
CC ECO:0000269|PubMed:9817918}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Subcortical band heterotopia X-linked (SBHX) [MIM:300067]:
CC SBHX is a mild brain malformation of the lissencephaly spectrum. It is
CC characterized by bilateral and symmetric plates or bands of gray matter
CC found in the central white matter between the cortex and cerebral
CC ventricles, cerebral convolutions usually appearing normal.
CC {ECO:0000269|PubMed:10369164, ECO:0000269|PubMed:10441340,
CC ECO:0000269|PubMed:10807542, ECO:0000269|PubMed:11175293,
CC ECO:0000269|PubMed:11601509, ECO:0000269|PubMed:12390976,
CC ECO:0000269|PubMed:9618162, ECO:0000269|PubMed:9989615}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=A chromosomal aberration involving DCX is found in
CC lissencephaly. Translocation t(X;2)(q22.3;p25.1).
CC -!- SEQUENCE CAUTION:
CC Sequence=EAX02642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAX02644.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAX02649.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ003112; CAA05867.1; -; mRNA.
DR EMBL; AJ005592; CAA06617.1; -; Genomic_DNA.
DR EMBL; AJ005593; CAA06617.1; JOINED; Genomic_DNA.
DR EMBL; AJ005594; CAA06617.1; JOINED; Genomic_DNA.
DR EMBL; AJ005595; CAA06617.1; JOINED; Genomic_DNA.
DR EMBL; AJ005596; CAA06617.1; JOINED; Genomic_DNA.
DR EMBL; AJ005597; CAA06617.1; JOINED; Genomic_DNA.
DR EMBL; AF034634; AAC52037.1; -; mRNA.
DR EMBL; AF040254; AAC31797.1; -; mRNA.
DR EMBL; AF040255; AAC31696.1; -; mRNA.
DR EMBL; AL031117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471120; EAX02644.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471120; EAX02645.1; -; Genomic_DNA.
DR EMBL; CH471120; EAX02642.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471120; EAX02643.1; -; Genomic_DNA.
DR EMBL; CH471120; EAX02646.1; -; Genomic_DNA.
DR EMBL; CH471120; EAX02647.1; -; Genomic_DNA.
DR EMBL; CH471120; EAX02649.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC027925; AAH27925.1; -; mRNA.
DR CCDS; CCDS14557.1; -. [O43602-2]
DR CCDS; CCDS14558.1; -. [O43602-1]
DR RefSeq; NP_000546.2; NM_000555.3.
DR RefSeq; NP_835364.1; NM_178151.2. [O43602-2]
DR RefSeq; NP_835365.1; NM_178152.2. [O43602-1]
DR RefSeq; NP_835366.1; NM_178153.2. [O43602-2]
DR PDB; 1MJD; NMR; -; A=45-150.
DR PDB; 2BQQ; X-ray; 2.20 A; A=45-150.
DR PDB; 2XRP; EM; 8.20 A; I=46-140.
DR PDB; 4ATU; EM; 8.30 A; I=2-365.
DR PDB; 5IKC; X-ray; 2.06 A; M/N=52-140.
DR PDB; 5IN7; X-ray; 2.48 A; A/B=46-150.
DR PDB; 5IO9; X-ray; 1.30 A; A/B=52-149.
DR PDB; 5IOI; X-ray; 2.40 A; A/B/C/D/E/F=52-150.
DR PDB; 5IP4; X-ray; 1.81 A; D/E=170-260.
DR PDB; 6FNZ; X-ray; 2.23 A; A/B/C/D=174-254.
DR PDB; 6REV; EM; 3.80 A; N=44-142.
DR PDB; 6RF2; EM; 4.20 A; C=178-264.
DR PDB; 6RF8; EM; 3.80 A; N=44-142.
DR PDB; 6RFD; EM; 3.90 A; N=44-142.
DR PDBsum; 1MJD; -.
DR PDBsum; 2BQQ; -.
DR PDBsum; 2XRP; -.
DR PDBsum; 4ATU; -.
DR PDBsum; 5IKC; -.
DR PDBsum; 5IN7; -.
DR PDBsum; 5IO9; -.
DR PDBsum; 5IOI; -.
DR PDBsum; 5IP4; -.
DR PDBsum; 6FNZ; -.
DR PDBsum; 6REV; -.
DR PDBsum; 6RF2; -.
DR PDBsum; 6RF8; -.
DR PDBsum; 6RFD; -.
DR AlphaFoldDB; O43602; -.
DR BMRB; O43602; -.
DR SMR; O43602; -.
DR BioGRID; 108008; 71.
DR IntAct; O43602; 41.
DR MINT; O43602; -.
DR STRING; 9606.ENSP00000337697; -.
DR iPTMnet; O43602; -.
DR PhosphoSitePlus; O43602; -.
DR BioMuta; DCX; -.
DR EPD; O43602; -.
DR jPOST; O43602; -.
DR MassIVE; O43602; -.
DR MaxQB; O43602; -.
DR PaxDb; O43602; -.
DR PeptideAtlas; O43602; -.
DR PRIDE; O43602; -.
DR ProteomicsDB; 49072; -. [O43602-1]
DR ProteomicsDB; 49073; -. [O43602-2]
DR ABCD; O43602; 2 sequenced antibodies.
DR Antibodypedia; 29535; 755 antibodies from 45 providers.
DR DNASU; 1641; -.
DR Ensembl; ENST00000358070.10; ENSP00000350776.5; ENSG00000077279.20. [O43602-2]
DR Ensembl; ENST00000488120.2; ENSP00000419861.1; ENSG00000077279.20. [O43602-2]
DR Ensembl; ENST00000496551.2; ENSP00000490448.1; ENSG00000077279.20. [O43602-1]
DR Ensembl; ENST00000635795.1; ENSP00000489635.1; ENSG00000077279.20. [O43602-1]
DR GeneID; 1641; -.
DR KEGG; hsa:1641; -.
DR UCSC; uc004epd.4; human. [O43602-1]
DR CTD; 1641; -.
DR DisGeNET; 1641; -.
DR GeneCards; DCX; -.
DR GeneReviews; DCX; -.
DR HGNC; HGNC:2714; DCX.
DR HPA; ENSG00000077279; Tissue enhanced (brain, endometrium, retina).
DR MalaCards; DCX; -.
DR MIM; 300067; phenotype.
DR MIM; 300121; gene.
DR neXtProt; NX_O43602; -.
DR OpenTargets; ENSG00000077279; -.
DR Orphanet; 2148; Lissencephaly type 1 due to doublecortin gene mutation.
DR Orphanet; 99796; Subcortical band heterotopia.
DR PharmGKB; PA27184; -.
DR VEuPathDB; HostDB:ENSG00000077279; -.
DR eggNOG; KOG3757; Eukaryota.
DR GeneTree; ENSGT00940000161570; -.
DR HOGENOM; CLU_035041_1_1_1; -.
DR InParanoid; O43602; -.
DR OrthoDB; 330091at2759; -.
DR TreeFam; TF318770; -.
DR PathwayCommons; O43602; -.
DR Reactome; R-HSA-447043; Neurofascin interactions.
DR SignaLink; O43602; -.
DR SIGNOR; O43602; -.
DR BioGRID-ORCS; 1641; 14 hits in 696 CRISPR screens.
DR EvolutionaryTrace; O43602; -.
DR GeneWiki; Doublecortin; -.
DR GenomeRNAi; 1641; -.
DR Pharos; O43602; Tbio.
DR PRO; PR:O43602; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O43602; protein.
DR Bgee; ENSG00000077279; Expressed in cortical plate and 79 other tissues.
DR ExpressionAtlas; O43602; baseline and differential.
DR Genevisible; O43602; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0001764; P:neuron migration; IDA:UniProtKB.
DR GO; GO:0042461; P:photoreceptor cell development; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR DisProt; DP02462; -.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR017302; Doublecortin_chordata.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR040163; RP1/RP1L1/DCX.
DR PANTHER; PTHR23005; PTHR23005; 1.
DR Pfam; PF03607; DCX; 2.
DR PIRSF; PIRSF037870; Doublin; 1.
DR SMART; SM00537; DCX; 2.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection;
KW Chromosomal rearrangement; Cytoplasm; Developmental protein;
KW Differentiation; Disease variant; Epilepsy; Lissencephaly; Microtubule;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..365
FT /note="Neuronal migration protein doublecortin"
FT /id="PRO_0000079833"
FT DOMAIN 53..139
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 180..263
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 11..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 28
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 47
FT /note="Phosphoserine; by MARK1 and PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9ESI7"
FT MOD_RES 70
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000255"
FT MOD_RES 74
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 90
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 110
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 115
FT /note="Phosphoserine; by CK2, MARK1 and PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9ESI7"
FT MOD_RES 265
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 287
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 289
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 294
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 297
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 306
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:O88809, ECO:0000255"
FT MOD_RES 306
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:22359282"
FT MOD_RES 326
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 326
FT /note="Phosphothreonine; by PKC and MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 332
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 332
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 336
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 339
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O88809"
FT MOD_RES 339
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000255"
FT MOD_RES 342
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 354
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 360
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT VAR_SEQ 310..315
FT /note="SGNDQD -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9489699, ECO:0000303|PubMed:9489700,
FT ECO:0000303|Ref.3"
FT /id="VSP_058155"
FT VARIANT 42
FT /note="T -> I (in LISX1)"
FT /evidence="ECO:0000269|PubMed:12552055"
FT /id="VAR_026022"
FT VARIANT 43
FT /note="L -> S (in LISX1; dbSNP:rs587783521)"
FT /evidence="ECO:0000269|PubMed:9817918"
FT /id="VAR_007819"
FT VARIANT 47
FT /note="S -> R (in LISX1 and SBHX; dbSNP:rs104894783)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:9489700"
FT /id="VAR_007820"
FT VARIANT 50
FT /note="K -> N (in SBHX; dbSNP:rs587783523)"
FT /evidence="ECO:0000269|PubMed:11601509"
FT /id="VAR_026023"
FT VARIANT 59
FT /note="R -> H (in SBHX; dbSNP:rs122457137)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_007822"
FT VARIANT 59
FT /note="R -> L (in LISX1 and SBHX; dbSNP:rs122457137)"
FT /evidence="ECO:0000269|PubMed:9489700"
FT /id="VAR_007821"
FT VARIANT 60
FT /note="N -> D (in LISX1)"
FT /evidence="ECO:0000269|PubMed:12552055"
FT /id="VAR_026024"
FT VARIANT 62
FT /note="D -> N (in LISX1 and SBHX; dbSNP:rs104894779)"
FT /evidence="ECO:0000269|PubMed:9489699"
FT /id="VAR_007823"
FT VARIANT 67
FT /note="G -> E (in SBHX)"
FT /evidence="ECO:0000269|PubMed:12390976"
FT /id="VAR_026025"
FT VARIANT 71
FT /note="A -> S (in LISX1; dbSNP:rs104894786)"
FT /evidence="ECO:0000269|PubMed:12552055"
FT /id="VAR_026026"
FT VARIANT 78
FT /note="R -> H (in SBH; dbSNP:rs104894784)"
FT /evidence="ECO:0000269|PubMed:10441340"
FT /id="VAR_010202"
FT VARIANT 78
FT /note="R -> L (in SBHX; dbSNP:rs104894784)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:9668176"
FT /id="VAR_007824"
FT VARIANT 86
FT /note="D -> H (in SBHX)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_007825"
FT VARIANT 89
FT /note="R -> G (in SBHX; mild; dbSNP:rs104894785)"
FT /evidence="ECO:0000269|PubMed:10441340,
FT ECO:0000269|PubMed:11175293"
FT /id="VAR_010536"
FT VARIANT 97
FT /note="L -> R (in SBHX; dbSNP:rs587783537)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_026027"
FT VARIANT 100
FT /note="G -> A (in LISX1 and SBHX)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:9668176"
FT /id="VAR_007826"
FT VARIANT 102
FT /note="R -> S (in LISX1)"
FT /evidence="ECO:0000269|PubMed:9817918"
FT /id="VAR_007827"
FT VARIANT 104
FT /note="I -> T (in SBHX)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_026028"
FT VARIANT 125
FT /note="Y -> D (in SBHX)"
FT /evidence="ECO:0000269|PubMed:9618162"
FT /id="VAR_007829"
FT VARIANT 125
FT /note="Y -> H (in LISX1 and SBHX; dbSNP:rs104894781)"
FT /evidence="ECO:0000269|PubMed:9489699"
FT /id="VAR_007828"
FT VARIANT 178
FT /note="R -> C (in SBHX; dbSNP:rs587783558)"
FT /evidence="ECO:0000269|PubMed:12390976"
FT /id="VAR_026029"
FT VARIANT 178
FT /note="R -> L (in SBHX; dbSNP:rs587783559)"
FT /id="VAR_007830"
FT VARIANT 186
FT /note="R -> C (in SBHX; dbSNP:rs587783562)"
FT /evidence="ECO:0000269|PubMed:10369164,
FT ECO:0000269|PubMed:11175293, ECO:0000269|PubMed:9668176"
FT /id="VAR_007831"
FT VARIANT 191
FT /note="P -> L (in SBHX)"
FT /id="VAR_026030"
FT VARIANT 191
FT /note="P -> R (in SBHX; dbSNP:rs587783566)"
FT /id="VAR_007832"
FT VARIANT 192
FT /note="R -> W (in LISX1 and SBHX; dbSNP:rs104894780)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:9489699"
FT /id="VAR_007833"
FT VARIANT 196
FT /note="R -> H (in LISX1; dbSNP:rs56030372)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:11468322"
FT /id="VAR_026031"
FT VARIANT 196
FT /note="R -> S (in epilepsy; resistant partial seizures;
FT related to 'cryptogenic' epilepsy; dbSNP:rs587783568)"
FT /evidence="ECO:0000269|PubMed:12027577"
FT /id="VAR_026032"
FT VARIANT 200
FT /note="N -> I (in SBHX)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_026033"
FT VARIANT 200
FT /note="N -> K (in SBHX)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:9668176"
FT /id="VAR_007834"
FT VARIANT 203
FT /note="T -> A (in SBHX; dbSNP:rs587783570)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_026034"
FT VARIANT 203
FT /note="T -> R (in LISX1 and SBHX; dbSNP:rs104894782)"
FT /evidence="ECO:0000269|PubMed:11175293,
FT ECO:0000269|PubMed:9489700"
FT /id="VAR_007835"
FT VARIANT 214
FT /note="I -> T (in SBHX; dbSNP:rs587783574)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_007836"
FT VARIANT 222
FT /note="T -> I (in SBHX)"
FT /id="VAR_007837"
FT VARIANT 223
FT /note="G -> E (in SBHX)"
FT /evidence="ECO:0000269|PubMed:9618162"
FT /id="VAR_007838"
FT VARIANT 223
FT /note="G -> V (in SBHX)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_026035"
FT VARIANT 236
FT /note="V -> I (in SBHX; dbSNP:rs1324159050)"
FT /id="VAR_007839"
FT VARIANT 243
FT /note="F -> L (in LISX1)"
FT /evidence="ECO:0000269|PubMed:12552055"
FT /id="VAR_026036"
FT VARIANT 250
FT /note="I -> N (in SBHX)"
FT /id="VAR_007840"
FT VARIANT 250
FT /note="I -> T (in SBHX)"
FT /evidence="ECO:0000269|PubMed:9618162"
FT /id="VAR_007841"
FT VARIANT 251
FT /note="A -> S (in SBHX; dbSNP:rs587783585)"
FT /evidence="ECO:0000269|PubMed:11175293"
FT /id="VAR_026037"
FT VARIANT 251
FT /note="A -> V (in SBHX)"
FT /evidence="ECO:0000269|PubMed:10807542"
FT /id="VAR_026038"
FT VARIANT 253
FT /note="G -> D (in SBHX)"
FT /id="VAR_007842"
FT VARIANT 262
FT /note="D -> G (in LISX1 and SBHX; decreased tubulin
FT binding; dbSNP:rs398124557)"
FT /evidence="ECO:0000269|PubMed:27292316"
FT /id="VAR_077482"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5IO9"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5IO9"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5IO9"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5IO9"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:5IO9"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5IO9"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5IO9"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1MJD"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5IO9"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:5IO9"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:5IO9"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:5IO9"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5IP4"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:5IP4"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5IP4"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:5IP4"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:5IP4"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5IP4"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:5IP4"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5IP4"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5IP4"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5IP4"
SQ SEQUENCE 365 AA; 40574 MW; 1E859F2114CC3BB1 CRC64;
MELDFGHFDE RDKTSRNMRG SRMNGLPSPT HSAHCSFYRT RTLQALSNEK KAKKVRFYRN
GDRYFKGIVY AVSSDRFRSF DALLADLTRS LSDNINLPQG VRYIYTIDGS RKIGSMDELE
EGESYVCSSD NFFKKVEYTK NVNPNWSVNV KTSANMKAPQ SLASSNSAQA RENKDFVRPK
LVTIIRSGVK PRKAVRVLLN KKTAHSFEQV LTDITEAIKL ETGVVKKLYT LDGKQVTCLH
DFFGDDDVFI ACGPEKFRYA QDDFSLDENE CRVMKGNPSA TAGPKASPTP QKTSAKSPGP
MRRSKSPADS GNDQDANGTS SSQLSTPKSK QSPISTPTSP GSLRKHKDLY LPLSLDDSDS
LGDSM
