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O43602 (DCX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal migration protein doublecortin
Alternative name(s):
Doublin
Lissencephalin-X
Short name=Lis-X
Gene names
Name:DCX
Synonyms:DBCN, LISX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration. Ref.8

Subunit structure

Interacts with tubulin.

Subcellular location

Cytoplasm. Cell projection By similarity. Note: Localizes at neurite tips By similarity.

Tissue specificity

Highly expressed in neuronal cells of fetal brain (in the majority of cells of the cortical plate, intermediate zone and ventricular zone), but not expressed in other fetal tissues. In the adult, highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas.

Post-translational modification

Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules By similarity.

Phosphorylation at Ser-346 and Ser-378 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 By similarity.

Involvement in disease

Lissencephaly, X-linked 1 (LISX1) [MIM:300067]: A classic lissencephaly characterized by mental retardation and seizures that are more severe in male patients. Affected boys show an abnormally thick cortex with absent or severely reduced gyri. Clinical manifestations include feeding problems, abnormal muscular tone, seizures and severe to profound psychomotor retardation. Female patients display a less severe phenotype referred to as 'doublecortex'.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.10 Ref.11 Ref.19 Ref.22

Subcortical band heterotopia X-linked (SBHX) [MIM:300067]: SBHX is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20

A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).

Sequence similarities

Contains 2 doublecortin domains.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell projection
Cytoplasm
Microtubule
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseDisease mutation
Epilepsy
Lissencephaly
   DomainRepeat
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon extension

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement Ref.1. Source: ProtInc

central nervous system projection neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

nervous system development

Traceable author statement Ref.1. Source: ProtInc

neuron migration

Inferred from direct assay PubMed 14741102. Source: UniProtKB

   Cellular_componentcytoskeleton

Traceable author statement PubMed 11001923. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Traceable author statement PubMed 11001923. Source: ProtInc

neuron projection

Inferred from direct assay PubMed 14741102. Source: UniProtKB

   Molecular_functionmicrotubule binding

Inferred from direct assay PubMed 14741102. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 14741102. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoform LIS-XA possesses an alternative exon in 5' and is then translated from an upstream initiation codon. Isoform LIS-XB, isoform LIS-XC and isoform LIS-XD translation starts at the downstream initiation codon, leading to the absence of the 81 first amino acids. Isoform LIS-XC and isoform LIS-XD differ from isoform LIS-XB by a five amino acids and a one amino acid-insertion respectively.
Isoform 1 (identifier: O43602-1)

Also known as: LIS-XA;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43602-2)

Also known as: LIS-XB;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Isoform 3 (identifier: O43602-3)

Also known as: LIS-XC;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     391-391: S → SGNDQD
Isoform 4 (identifier: O43602-4)

Also known as: LIS-XD;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     405-405: S → SV
Isoform 5 (identifier: O43602-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     391-391: S → SGN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Neuronal migration protein doublecortin
PRO_0000079833

Regions

Domain134 – 22087Doublecortin 1
Domain261 – 34484Doublecortin 2
Compositional bias368 – 41851Pro/Ser-rich

Amino acid modifications

Modified residue951Phosphothreonine; by PKC Potential
Modified residue1091Phosphoserine; by CDK5 By similarity
Modified residue1281Phosphoserine; by MARK1 and PKA By similarity
Modified residue1511Phosphotyrosine; by ABL Potential
Modified residue1551Phosphoserine; by PKC Potential
Modified residue1711Phosphoserine; by CK2 Potential
Modified residue1911Phosphoserine; by PKC Potential
Modified residue1961Phosphoserine; by CK2, MARK1 and PKA By similarity
Modified residue3461Phosphoserine; by CK2 By similarity
Modified residue3681Phosphoserine; by CDK5 By similarity
Modified residue3701Phosphothreonine; by CDK5 By similarity
Modified residue3751Phosphoserine; by PKC Potential
Modified residue3781Phosphoserine; by CDK5 By similarity
Modified residue3871Phosphoserine; by CK2; alternate Potential
Modified residue3871Phosphoserine; by DYRK2; alternate Ref.8
Modified residue4021Phosphothreonine; by CDK5; alternate By similarity
Modified residue4021Phosphothreonine; by PKC and MAPK; alternate Potential
Modified residue4081Phosphoserine; by CDK5; alternate By similarity
Modified residue4081Phosphoserine; by MAPK; alternate Potential
Modified residue4121Phosphothreonine; by MAPK Potential
Modified residue4151Phosphoserine; by CDK5; alternate By similarity
Modified residue4151Phosphoserine; by MAPK; alternate Potential
Modified residue4181Phosphoserine; by PKC Potential
Modified residue4301Phosphoserine; by CK2 Potential
Modified residue4361Phosphoserine; by CK2 Potential

Natural variations

Alternative sequence1 – 8181Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_004186
Alternative sequence3911S → SGNDQD in isoform 3.
VSP_004187
Alternative sequence3911S → SGN in isoform 5.
VSP_026375
Alternative sequence4051S → SV in isoform 4.
VSP_004188
Natural variant1231T → I in LISX1. Ref.22
VAR_026022
Natural variant1241L → S in LISX1. Ref.11
VAR_007819
Natural variant1281S → R in LISX1 and SBHX. Ref.2 Ref.18
VAR_007820
Natural variant1311K → N in SBHX. Ref.17
VAR_026023
Natural variant1401R → H in SBHX. Ref.18
VAR_007822
Natural variant1401R → L in LISX1 and SBHX. Ref.2
VAR_007821
Natural variant1411N → D in LISX1. Ref.22
VAR_026024
Natural variant1431D → N in LISX1 and SBHX. Ref.1
VAR_007823
Natural variant1481G → E in SBHX. Ref.20
VAR_026025
Natural variant1521A → S in LISX1. Ref.22
VAR_026026
Natural variant1591R → H in SBH. Ref.15
VAR_010202
Natural variant1591R → L in SBHX. Ref.10 Ref.18
VAR_007824
Natural variant1671D → H in SBHX. Ref.18
VAR_007825
Natural variant1701R → G in SBHX; mild. Ref.15 Ref.18
VAR_010536
Natural variant1781L → R in SBHX. Ref.18
VAR_026027
Natural variant1811G → A in LISX1 and SBHX. Ref.10 Ref.18
VAR_007826
Natural variant1831R → S in LISX1. Ref.11
VAR_007827
Natural variant1851I → T in SBHX. Ref.18
VAR_026028
Natural variant2061Y → D in SBHX. Ref.12
VAR_007829
Natural variant2061Y → H in LISX1 and SBHX. Ref.1
VAR_007828
Natural variant2591R → C in SBHX. Ref.20
VAR_026029
Natural variant2591R → L in SBHX.
VAR_007830
Natural variant2671R → C in SBHX. Ref.10 Ref.14 Ref.18
VAR_007831
Natural variant2721P → L in SBHX.
VAR_026030
Natural variant2721P → R in SBHX.
VAR_007832
Natural variant2731R → W in LISX1 and SBHX. Ref.1 Ref.18
VAR_007833
Natural variant2771R → H in LISX1. Ref.18 Ref.19
Corresponds to variant rs56030372 [ dbSNP | Ensembl ].
VAR_026031
Natural variant2771R → S in epilepsy; resistant partial seizures; related to 'cryptogenic' epilepsy. Ref.21
VAR_026032
Natural variant2811N → I in SBHX. Ref.18
VAR_026033
Natural variant2811N → K in SBHX. Ref.10 Ref.18
VAR_007834
Natural variant2841T → A in SBHX. Ref.18
VAR_026034
Natural variant2841T → R in LISX1 and SBHX. Ref.2 Ref.18
VAR_007835
Natural variant2951I → T in SBHX. Ref.18
VAR_007836
Natural variant3031T → I in SBHX.
VAR_007837
Natural variant3041G → E in SBHX. Ref.12
VAR_007838
Natural variant3041G → V in SBHX. Ref.18
VAR_026035
Natural variant3171V → I in SBHX.
VAR_007839
Natural variant3241F → L in LISX1. Ref.22
VAR_026036
Natural variant3311I → N in SBHX.
VAR_007840
Natural variant3311I → T in SBHX. Ref.12
VAR_007841
Natural variant3321A → S in SBHX. Ref.18
VAR_026037
Natural variant3321A → V in SBHX. Ref.16
VAR_026038
Natural variant3341G → D in SBHX.
VAR_007842

Secondary structure

..................... 441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LIS-XA) [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 945988E263F261CD

FASTA44149,318
        10         20         30         40         50         60 
MKTLPLHSHC TEMQRLLPKL EMLTLGSSFC SLQGEFCQAM DSFTTVSHVG MCEETDASFN 

        70         80         90        100        110        120 
VFSPKFQFDR SHCQSLRFHQ NMELDFGHFD ERDKTSRNMR GSRMNGLPSP THSAHCSFYR 

       130        140        150        160        170        180 
TRTLQALSNE KKAKKVRFYR NGDRYFKGIV YAVSSDRFRS FDALLADLTR SLSDNINLPQ 

       190        200        210        220        230        240 
GVRYIYTIDG SRKIGSMDEL EEGESYVCSS DNFFKKVEYT KNVNPNWSVN VKTSANMKAP 

       250        260        270        280        290        300 
QSLASSNSAQ ARENKDFVRP KLVTIIRSGV KPRKAVRVLL NKKTAHSFEQ VLTDITEAIK 

       310        320        330        340        350        360 
LETGVVKKLY TLDGKQVTCL HDFFGDDDVF IACGPEKFRY AQDDFSLDEN ECRVMKGNPS 

       370        380        390        400        410        420 
ATAGPKASPT PQKTSAKSPG PMRRSKSPAD SANGTSSSQL STPKSKQSPI STPTSPGSLR 

       430        440 
KHKDLYLPLS LDDSDSLGDS M 

« Hide

Isoform 2 (LIS-XB) [UniParc].

Checksum: 91D0D89433AF52A0
Show »

FASTA36040,044
Isoform 3 (LIS-XC) [UniParc].

Checksum: 1E859F2114CC3BB1
Show »

FASTA36540,574
Isoform 4 (LIS-XD) [UniParc].

Checksum: 8DE5D9AE42D08AAF
Show »

FASTA36140,143
Isoform 5 [UniParc].

Checksum: 1E144731B8671F4B
Show »

FASTA36240,215

References

« Hide 'large scale' references
[1]"A novel CNS gene required for neuronal migration and involved in X-linked subcortical laminar heterotopia and lissencephaly syndrome."
Des Portes V., Pinard J.-M., Billuart P., Vinet M.-C., Koulakoff A., Carrie A., Gelot A., Dupuis E., Motte J., Berwald-Netter Y., Catala M., Kahn A., Beldjord C., Chelly J.
Cell 92:51-61(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 4), VARIANTS LISX1 ASN-143; HIS-206 AND TRP-273.
Tissue: Fetal brain.
[2]"Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein."
Gleeson J.G., Allen K.M., Fox J.W., Lamperti E.D., Berkovic S., Scheffer I., Cooper E.C., Dobyns W.B., Minnerath S.R., Ross M.E., Walsh C.A.
Cell 92:63-72(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS LISX1 ARG-128; LEU-140 AND ARG-284.
Tissue: Brain.
[3]"X-linked neuronal migration disorder (lissencephaly/subcortical band heterotopia) is caused by mutation in a novel brain-specific protein, lissencephalin-X."
Sossey-Alaoui K., Srivastava A.K.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fetal brain.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Dyrk kinases regulate phosphorylation of doublecortin, cytoskeletal organization, and neuronal morphology."
Slepak T.I., Salay L.D., Lemmon V.P., Bixby J.L.
Cytoskeleton 69:514-527(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-387.
[9]"The DCX-domain tandems of doublecortin and doublecortin-like kinase."
Kim M.H., Cierpicki T., Derewenda U., Krowarsch D., Feng Y., Devedjiev Y., Dauter Z., Walsh C.A., Otlewski J., Bushweller J.H., Derewenda Z.S.
Nat. Struct. Biol. 10:324-333(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 126-231.
[10]"Human doublecortin (DCX) and the homologous gene in mouse encode a putative Ca2+-dependent signaling protein which is mutated in human X-linked neuronal migration defects."
Sossey-Alaoui K., Hartung A.J., Guerrini R., Manchester D.K., Posar A., Puche-Mira A., Andermann E., Dobyns W.B., Srivastava A.K.
Hum. Mol. Genet. 7:1327-1332(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LISX1/SBHX LEU-159; ALA-181; CYS-267 AND LYS-281.
[11]"LIS1 and XLIS (DCX) mutations cause most classical lissencephaly, but different patterns of malformation."
Pilz D.T., Matsumoto N., Minnerath S.R., Mills P., Gleeson J.G., Allen K.M., Walsh C.A., Barkovich A.J., Dobyns W.B., Ledbetter D.H., Ross M.E.
Hum. Mol. Genet. 7:2029-2037(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LISX1 SER-124 AND SER-183.
[12]"Doublecortin is the major gene causing X-linked subcortical laminar heterotopia (SCLH)."
Des Portes V., Francis F., Pinard J.-M., Desguerre I., Moutard M.-L., Snoeck I., Meiners L.C., Capron F., Cusmai R., Ricci S., Motte J., Echenne B., Ponsot G., Dulac O., Chelly J., Beldjord C.
Hum. Mol. Genet. 7:1063-1070(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SBHX ASP-206; GLU-304 AND THR-331.
[13]"Characterization of mutations in the gene doublecortin in patients with double cortex syndrome."
Gleeson J.G., Minnerath S.R., Fox J.W., Allen K.M., Luo R.F., Hong S.E., Berg M.J., Kuzniecky R., Reitnauer P.J., Borgatti R., Puche-Mira A., Guerrini R., Holmes G.L., Rooney C.M., Berkovic S., Scheffer I., Cooper E.C., Ricci S. expand/collapse author list , Cusmai R., Crawford T.O., Leroy R., Andermann E., Wheless J.W., Dobyns W.B., Ross M.E., Walsh C.A.
Ann. Neurol. 45:146-153(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SBHX.
[14]"A novel mutation of the doublecortin gene in Japanese patients with X-linked lissencephaly and subcortical band heterotopia."
Kato M., Kimura T., Lin C., Ito A., Kodama S., Morikawa T., Soga T., Hayasaka K.
Hum. Genet. 104:341-344(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SBHX CYS-267.
[15]"Subcortical band heterotopia in rare affected males can be caused by missense mutations in DCX (XLIS) or LIS1."
Pilz D.T., Kuc J., Matsumoto N., Bodurtha J., Bernadi B., Tassinari C.A., Dobyns W.B., Ledbetter D.H.
Hum. Mol. Genet. 8:1757-1760(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SBHX HIS-159 AND GLY-170.
[16]"Genetic alteration of the DCX gene in Japanese patients with subcortical laminar heterotopia or isolated lissencephaly sequence."
Sakamoto M., Ono J., Okada S., Nakamura Y., Kurahashi H.
J. Hum. Genet. 45:167-170(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SBHX VAL-332.
[17]"Mutation of the doublecortin gene in male patients with double cortex syndrome: somatic mosaicism detected by hair root analysis."
Kato M., Kanai M., Soma O., Takusa Y., Kimura T., Numakura C., Matsuki T., Nakamura S., Hayasaka K.
Ann. Neurol. 50:547-551(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SBHX ASN-131.
[18]"Mutation analysis of the DCX gene and genotype/phenotype correlation in subcortical band heterotopia."
Matsumoto N., Leventer R.J., Kuc J.A., Mewborn S.K., Dudlicek L.L., Ramocki M.B., Pilz D.T., Mills P.L., Das S., Ross M.E., Ledbetter D.H., Dobyns W.B.
Eur. J. Hum. Genet. 9:5-12(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SBHX ARG-128; HIS-140; LEU-159; HIS-167; GLY-170; ARG-178; ALA-181; THR-185; CYS-267; TRP-273; HIS-277; ILE-281; LYS-281; ALA-284; ARG-284; THR-295; VAL-304 AND SER-332.
[19]"Incomplete penetrance with normal MRI in a woman with germline mutation of the DCX gene."
Demelas L., Serra G., Conti M., Achene A., Mastropaolo C., Matsumoto N., Dudlicek L.L., Mills P.L., Dobyns W.B., Ledbetter D.H., Das S.
Neurology 57:327-330(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LISX1 HIS-277.
[20]"Subcortical band heterotopia (SBH) in males: clinical, imaging and genetic findings in comparison with females."
D'Agostino M.D., Bernasconi A., Das S., Bastos A., Valerio R.M., Palmini A., Costa da Costa J., Scheffer I.E., Berkovic S., Guerrini R., Dravet C., Ono J., Gigli G., Federico A., Booth F., Bernardi B., Volpi L., Tassinari C.A. expand/collapse author list , Guggenheim M.A., Ledbetter D.H., Gleeson J.G., Lopes-Cendes I., Vossler D.G., Malaspina E., Franzoni E., Sartori R.J., Mitchell M.H., Mercho S., Dubeau F., Andermann F., Dobyns W.B., Andermann E.
Brain 125:2507-2522(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SBHX GLU-148 AND CYS-259.
[21]"So-called 'cryptogenic' partial seizures resulting from a subtle cortical dysgenesis due to a doublecortin gene mutation."
des Portes V., Abaoub L., Joannard A., Souville I., Francis F., Pinard J.-M., Chelly J., Beldjord C., Jouk P.S.
Seizure 11:273-277(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPILEPSY SER-277.
[22]"Somatic mosaicism and variable penetrance in doublecortin-associated migration disorders."
Aigner L., Uyanik G., Couillard-Despres S., Ploetz S., Wolff G., Morris-Rosendahl D., Martin P., Eckel U., Spranger S., Otte J., Woerle H., Holthausen H., Apheshiotis N., Fluegel D., Winkler J.
Neurology 60:329-332(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LISX1 ILE-123; ASP-141; SER-152 AND LEU-324.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ003112 mRNA. Translation: CAA05867.1.
AJ005592 expand/collapse EMBL AC list , AJ005593, AJ005594, AJ005595, AJ005596, AJ005597 Genomic DNA. Translation: CAA06617.1.
AF034634 mRNA. Translation: AAC52037.1.
AF040254 mRNA. Translation: AAC31797.1.
AF040255 mRNA. Translation: AAC31696.1.
AL031117 Genomic DNA. Translation: CAA19966.3.
AL450490, AL031117 Genomic DNA. Translation: CAI39488.2.
AL450490, AL031117 Genomic DNA. Translation: CAI39489.1.
AL031117, AL450490 Genomic DNA. Translation: CAI43156.1.
CH471120 Genomic DNA. Translation: EAX02644.1.
CH471120 Genomic DNA. Translation: EAX02645.1.
CH471120 Genomic DNA. Translation: EAX02642.1.
CH471120 Genomic DNA. Translation: EAX02643.1.
CH471120 Genomic DNA. Translation: EAX02646.1.
CH471120 Genomic DNA. Translation: EAX02647.1.
CH471120 Genomic DNA. Translation: EAX02649.1.
BC027925 mRNA. Translation: AAH27925.1.
RefSeqNP_000546.2. NM_000555.3.
NP_835364.1. NM_178151.2.
NP_835365.1. NM_178152.2.
NP_835366.1. NM_178153.2.
UniGeneHs.34780.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MJDNMR-A126-231[»]
2BQQX-ray2.20A126-231[»]
2XRPelectron microscopy8.20I127-221[»]
4ATUelectron microscopy8.30I83-441[»]
ProteinModelPortalO43602.
SMRO43602. Positions 132-237, 248-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108008. 12 interactions.
IntActO43602. 2 interactions.
STRING9606.ENSP00000337697.

PTM databases

PhosphoSiteO43602.

Proteomic databases

PaxDbO43602.
PRIDEO43602.

Protocols and materials databases

DNASU1641.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338081; ENSP00000337697; ENSG00000077279. [O43602-1]
ENST00000356220; ENSP00000348553; ENSG00000077279. [O43602-3]
ENST00000356915; ENSP00000349385; ENSG00000077279. [O43602-3]
ENST00000371993; ENSP00000361061; ENSG00000077279. [O43602-2]
ENST00000488120; ENSP00000419861; ENSG00000077279. [O43602-2]
GeneID1641.
KEGGhsa:1641.
UCSCuc004epd.3. human. [O43602-1]

Organism-specific databases

CTD1641.
GeneCardsGC0XM110537.
HGNCHGNC:2714. DCX.
HPACAB012243.
MIM300067. phenotype.
300121. gene.
neXtProtNX_O43602.
Orphanet2148. Lissencephaly type 1 due to doublecortin gene mutation.
99796. Subcortical band heterotopia.
PharmGKBPA27184.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238212.
HOVERGENHBG003790.
KOK16579.
OMAVKASASQ.
PhylomeDBO43602.
TreeFamTF318770.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressO43602.
BgeeO43602.
CleanExHS_DCX.
GenevestigatorO43602.

Family and domain databases

Gene3D3.10.20.230. 2 hits.
InterProIPR017302. Doublecortin_chordata.
IPR003533. Doublecortin_dom.
[Graphical view]
PfamPF03607. DCX. 2 hits.
[Graphical view]
PIRSFPIRSF037870. Doublin. 1 hit.
SMARTSM00537. DCX. 2 hits.
[Graphical view]
PROSITEPS50309. DC. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCX. human.
EvolutionaryTraceO43602.
GeneWikiDoublecortin.
GenomeRNAi1641.
NextBio6740.
PROO43602.
SOURCESearch...

Entry information

Entry nameDCX_HUMAN
AccessionPrimary (citable) accession number: O43602
Secondary accession number(s): A6NFY6 expand/collapse secondary AC list , A9Z1V8, D3DUY8, D3DUY9, D3DUZ0, O43911, Q5JYZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM