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O43602

- DCX_HUMAN

UniProt

O43602 - DCX_HUMAN

Protein

Neuronal migration protein doublecortin

Gene

DCX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. microtubule binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. axon extension Source: Ensembl
    2. axon guidance Source: Reactome
    3. brain development Source: Ensembl
    4. central nervous system development Source: ProtInc
    5. central nervous system projection neuron axonogenesis Source: Ensembl
    6. dendrite morphogenesis Source: Ensembl
    7. intracellular signal transduction Source: InterPro
    8. nervous system development Source: ProtInc
    9. neuron migration Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_22312. Neurofascin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuronal migration protein doublecortin
    Alternative name(s):
    Doublin
    Lissencephalin-X
    Short name:
    Lis-X
    Gene namesi
    Name:DCX
    Synonyms:DBCN, LISX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2714. DCX.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoskeleton Source: ProtInc
    2. cytosol Source: Reactome
    3. microtubule Source: UniProtKB-KW
    4. microtubule associated complex Source: ProtInc
    5. neuron projection Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    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'.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231T → I in LISX1. 1 Publication
    VAR_026022
    Natural varianti124 – 1241L → S in LISX1. 1 Publication
    VAR_007819
    Natural varianti128 – 1281S → R in LISX1 and SBHX. 2 Publications
    VAR_007820
    Natural varianti140 – 1401R → L in LISX1 and SBHX. 1 Publication
    VAR_007821
    Natural varianti141 – 1411N → D in LISX1. 1 Publication
    VAR_026024
    Natural varianti143 – 1431D → N in LISX1 and SBHX. 1 Publication
    VAR_007823
    Natural varianti152 – 1521A → S in LISX1. 1 Publication
    VAR_026026
    Natural varianti181 – 1811G → A in LISX1 and SBHX. 2 Publications
    VAR_007826
    Natural varianti183 – 1831R → S in LISX1. 1 Publication
    VAR_007827
    Natural varianti206 – 2061Y → H in LISX1 and SBHX. 1 Publication
    VAR_007828
    Natural varianti273 – 2731R → W in LISX1 and SBHX. 2 Publications
    VAR_007833
    Natural varianti277 – 2771R → H in LISX1. 2 Publications
    Corresponds to variant rs56030372 [ dbSNP | Ensembl ].
    VAR_026031
    Natural varianti284 – 2841T → R in LISX1 and SBHX. 2 Publications
    VAR_007835
    Natural varianti324 – 3241F → L in LISX1. 1 Publication
    VAR_026036
    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.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281S → R in LISX1 and SBHX. 2 Publications
    VAR_007820
    Natural varianti131 – 1311K → N in SBHX. 1 Publication
    VAR_026023
    Natural varianti140 – 1401R → H in SBHX. 1 Publication
    VAR_007822
    Natural varianti140 – 1401R → L in LISX1 and SBHX. 1 Publication
    VAR_007821
    Natural varianti143 – 1431D → N in LISX1 and SBHX. 1 Publication
    VAR_007823
    Natural varianti148 – 1481G → E in SBHX. 1 Publication
    VAR_026025
    Natural varianti159 – 1591R → L in SBHX. 2 Publications
    VAR_007824
    Natural varianti167 – 1671D → H in SBHX. 1 Publication
    VAR_007825
    Natural varianti170 – 1701R → G in SBHX; mild. 2 Publications
    VAR_010536
    Natural varianti178 – 1781L → R in SBHX. 1 Publication
    VAR_026027
    Natural varianti181 – 1811G → A in LISX1 and SBHX. 2 Publications
    VAR_007826
    Natural varianti185 – 1851I → T in SBHX. 1 Publication
    VAR_026028
    Natural varianti206 – 2061Y → D in SBHX. 1 Publication
    VAR_007829
    Natural varianti206 – 2061Y → H in LISX1 and SBHX. 1 Publication
    VAR_007828
    Natural varianti259 – 2591R → C in SBHX. 1 Publication
    VAR_026029
    Natural varianti259 – 2591R → L in SBHX.
    VAR_007830
    Natural varianti267 – 2671R → C in SBHX. 3 Publications
    VAR_007831
    Natural varianti272 – 2721P → L in SBHX.
    VAR_026030
    Natural varianti272 – 2721P → R in SBHX.
    VAR_007832
    Natural varianti273 – 2731R → W in LISX1 and SBHX. 2 Publications
    VAR_007833
    Natural varianti281 – 2811N → I in SBHX. 1 Publication
    VAR_026033
    Natural varianti281 – 2811N → K in SBHX. 2 Publications
    VAR_007834
    Natural varianti284 – 2841T → A in SBHX. 1 Publication
    VAR_026034
    Natural varianti284 – 2841T → R in LISX1 and SBHX. 2 Publications
    VAR_007835
    Natural varianti295 – 2951I → T in SBHX. 1 Publication
    VAR_007836
    Natural varianti303 – 3031T → I in SBHX.
    VAR_007837
    Natural varianti304 – 3041G → E in SBHX. 1 Publication
    VAR_007838
    Natural varianti304 – 3041G → V in SBHX. 1 Publication
    VAR_026035
    Natural varianti317 – 3171V → I in SBHX.
    VAR_007839
    Natural varianti331 – 3311I → N in SBHX.
    VAR_007840
    Natural varianti331 – 3311I → T in SBHX. 1 Publication
    VAR_007841
    Natural varianti332 – 3321A → S in SBHX. 1 Publication
    VAR_026037
    Natural varianti332 – 3321A → V in SBHX. 1 Publication
    VAR_026038
    Natural varianti334 – 3341G → D in SBHX.
    VAR_007842
    A chromosomal aberration involving DCX is found in lissencephaly. Translocation t(X;2)(q22.3;p25.1).

    Keywords - Diseasei

    Disease mutation, Epilepsy, Lissencephaly

    Organism-specific databases

    MIMi300067. phenotype.
    Orphaneti2148. Lissencephaly type 1 due to doublecortin gene mutation.
    99796. Subcortical band heterotopia.
    PharmGKBiPA27184.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Neuronal migration protein doublecortinPRO_0000079833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei95 – 951Phosphothreonine; by PKCSequence Analysis
    Modified residuei109 – 1091Phosphoserine; by CDK5By similarity
    Modified residuei128 – 1281Phosphoserine; by MARK1 and PKABy similarity
    Modified residuei151 – 1511Phosphotyrosine; by ABLSequence Analysis
    Modified residuei155 – 1551Phosphoserine; by PKCSequence Analysis
    Modified residuei171 – 1711Phosphoserine; by CK2Sequence Analysis
    Modified residuei191 – 1911Phosphoserine; by PKCSequence Analysis
    Modified residuei196 – 1961Phosphoserine; by CK2, MARK1 and PKABy similarity
    Modified residuei346 – 3461Phosphoserine; by CK2By similarity
    Modified residuei368 – 3681Phosphoserine; by CDK5By similarity
    Modified residuei370 – 3701Phosphothreonine; by CDK5By similarity
    Modified residuei375 – 3751Phosphoserine; by PKCSequence Analysis
    Modified residuei378 – 3781Phosphoserine; by CDK5By similarity
    Modified residuei387 – 3871Phosphoserine; by CK2; alternateSequence Analysis
    Modified residuei387 – 3871Phosphoserine; by DYRK2; alternate1 Publication
    Modified residuei402 – 4021Phosphothreonine; by CDK5; alternateBy similarity
    Modified residuei402 – 4021Phosphothreonine; by PKC and MAPK; alternateSequence Analysis
    Modified residuei408 – 4081Phosphoserine; by CDK5; alternateBy similarity
    Modified residuei408 – 4081Phosphoserine; by MAPK; alternateSequence Analysis
    Modified residuei412 – 4121Phosphothreonine; by MAPKSequence Analysis
    Modified residuei415 – 4151Phosphoserine; by CDK5; alternateBy similarity
    Modified residuei415 – 4151Phosphoserine; by MAPK; alternateSequence Analysis
    Modified residuei418 – 4181Phosphoserine; by PKCSequence Analysis
    Modified residuei430 – 4301Phosphoserine; by CK2Sequence Analysis
    Modified residuei436 – 4361Phosphoserine; by CK2Sequence Analysis

    Post-translational modificationi

    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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43602.
    PaxDbiO43602.
    PRIDEiO43602.

    PTM databases

    PhosphoSiteiO43602.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiO43602.
    BgeeiO43602.
    CleanExiHS_DCX.
    GenevestigatoriO43602.

    Organism-specific databases

    HPAiCAB012243.

    Interactioni

    Subunit structurei

    Interacts with tubulin. Interacts with USP9X.1 Publication

    Protein-protein interaction databases

    BioGridi108008. 12 interactions.
    IntActiO43602. 2 interactions.
    STRINGi9606.ENSP00000337697.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi134 – 1407
    Beta strandi149 – 1535
    Turni155 – 1573
    Helixi161 – 17212
    Beta strandi175 – 1773
    Beta strandi184 – 1874
    Beta strandi191 – 1944
    Helixi197 – 1993
    Beta strandi205 – 2139
    Turni225 – 2273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MJDNMR-A126-231[»]
    2BQQX-ray2.20A126-231[»]
    2XRPelectron microscopy8.20I127-221[»]
    4ATUelectron microscopy8.30I83-441[»]
    ProteinModelPortaliO43602.
    SMRiO43602. Positions 132-237, 248-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43602.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 22087Doublecortin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini261 – 34484Doublecortin 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi368 – 41851Pro/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 doublecortin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG238212.
    HOVERGENiHBG003790.
    KOiK16579.
    OMAiCRVMKGS.
    PhylomeDBiO43602.
    TreeFamiTF318770.

    Family and domain databases

    Gene3Di3.10.20.230. 2 hits.
    InterProiIPR017302. Doublecortin_chordata.
    IPR003533. Doublecortin_dom.
    [Graphical view]
    PfamiPF03607. DCX. 2 hits.
    [Graphical view]
    PIRSFiPIRSF037870. Doublin. 1 hit.
    SMARTiSM00537. DCX. 2 hits.
    [Graphical view]
    PROSITEiPS50309. DC. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    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) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKTLPLHSHC TEMQRLLPKL EMLTLGSSFC SLQGEFCQAM DSFTTVSHVG    50
    MCEETDASFN VFSPKFQFDR SHCQSLRFHQ NMELDFGHFD ERDKTSRNMR 100
    GSRMNGLPSP THSAHCSFYR TRTLQALSNE KKAKKVRFYR NGDRYFKGIV 150
    YAVSSDRFRS FDALLADLTR SLSDNINLPQ GVRYIYTIDG SRKIGSMDEL 200
    EEGESYVCSS DNFFKKVEYT KNVNPNWSVN VKTSANMKAP QSLASSNSAQ 250
    ARENKDFVRP KLVTIIRSGV KPRKAVRVLL NKKTAHSFEQ VLTDITEAIK 300
    LETGVVKKLY TLDGKQVTCL HDFFGDDDVF IACGPEKFRY AQDDFSLDEN 350
    ECRVMKGNPS ATAGPKASPT PQKTSAKSPG PMRRSKSPAD SANGTSSSQL 400
    STPKSKQSPI STPTSPGSLR KHKDLYLPLS LDDSDSLGDS M 441
    Length:441
    Mass (Da):49,318
    Last modified:November 25, 2008 - v3
    Checksum:i945988E263F261CD
    GO
    Isoform 2 (identifier: O43602-2) [UniParc]FASTAAdd to Basket

    Also known as: LIS-XB

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: Missing.

    Show »
    Length:360
    Mass (Da):40,044
    Checksum:i91D0D89433AF52A0
    GO
    Isoform 3 (identifier: O43602-3) [UniParc]FASTAAdd to Basket

    Also known as: LIS-XC

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: Missing.
         391-391: S → SGNDQD

    Show »
    Length:365
    Mass (Da):40,574
    Checksum:i1E859F2114CC3BB1
    GO
    Isoform 4 (identifier: O43602-4) [UniParc]FASTAAdd to Basket

    Also known as: LIS-XD

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: Missing.
         405-405: S → SV

    Show »
    Length:361
    Mass (Da):40,143
    Checksum:i8DE5D9AE42D08AAF
    GO
    Isoform 5 (identifier: O43602-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-81: Missing.
         391-391: S → SGN

    Note: No experimental confirmation available.

    Show »
    Length:362
    Mass (Da):40,215
    Checksum:i1E144731B8671F4B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231T → I in LISX1. 1 Publication
    VAR_026022
    Natural varianti124 – 1241L → S in LISX1. 1 Publication
    VAR_007819
    Natural varianti128 – 1281S → R in LISX1 and SBHX. 2 Publications
    VAR_007820
    Natural varianti131 – 1311K → N in SBHX. 1 Publication
    VAR_026023
    Natural varianti140 – 1401R → H in SBHX. 1 Publication
    VAR_007822
    Natural varianti140 – 1401R → L in LISX1 and SBHX. 1 Publication
    VAR_007821
    Natural varianti141 – 1411N → D in LISX1. 1 Publication
    VAR_026024
    Natural varianti143 – 1431D → N in LISX1 and SBHX. 1 Publication
    VAR_007823
    Natural varianti148 – 1481G → E in SBHX. 1 Publication
    VAR_026025
    Natural varianti152 – 1521A → S in LISX1. 1 Publication
    VAR_026026
    Natural varianti159 – 1591R → H in SBH. 1 Publication
    VAR_010202
    Natural varianti159 – 1591R → L in SBHX. 2 Publications
    VAR_007824
    Natural varianti167 – 1671D → H in SBHX. 1 Publication
    VAR_007825
    Natural varianti170 – 1701R → G in SBHX; mild. 2 Publications
    VAR_010536
    Natural varianti178 – 1781L → R in SBHX. 1 Publication
    VAR_026027
    Natural varianti181 – 1811G → A in LISX1 and SBHX. 2 Publications
    VAR_007826
    Natural varianti183 – 1831R → S in LISX1. 1 Publication
    VAR_007827
    Natural varianti185 – 1851I → T in SBHX. 1 Publication
    VAR_026028
    Natural varianti206 – 2061Y → D in SBHX. 1 Publication
    VAR_007829
    Natural varianti206 – 2061Y → H in LISX1 and SBHX. 1 Publication
    VAR_007828
    Natural varianti259 – 2591R → C in SBHX. 1 Publication
    VAR_026029
    Natural varianti259 – 2591R → L in SBHX.
    VAR_007830
    Natural varianti267 – 2671R → C in SBHX. 3 Publications
    VAR_007831
    Natural varianti272 – 2721P → L in SBHX.
    VAR_026030
    Natural varianti272 – 2721P → R in SBHX.
    VAR_007832
    Natural varianti273 – 2731R → W in LISX1 and SBHX. 2 Publications
    VAR_007833
    Natural varianti277 – 2771R → H in LISX1. 2 Publications
    Corresponds to variant rs56030372 [ dbSNP | Ensembl ].
    VAR_026031
    Natural varianti277 – 2771R → S in epilepsy; resistant partial seizures; related to 'cryptogenic' epilepsy. 1 Publication
    VAR_026032
    Natural varianti281 – 2811N → I in SBHX. 1 Publication
    VAR_026033
    Natural varianti281 – 2811N → K in SBHX. 2 Publications
    VAR_007834
    Natural varianti284 – 2841T → A in SBHX. 1 Publication
    VAR_026034
    Natural varianti284 – 2841T → R in LISX1 and SBHX. 2 Publications
    VAR_007835
    Natural varianti295 – 2951I → T in SBHX. 1 Publication
    VAR_007836
    Natural varianti303 – 3031T → I in SBHX.
    VAR_007837
    Natural varianti304 – 3041G → E in SBHX. 1 Publication
    VAR_007838
    Natural varianti304 – 3041G → V in SBHX. 1 Publication
    VAR_026035
    Natural varianti317 – 3171V → I in SBHX.
    VAR_007839
    Natural varianti324 – 3241F → L in LISX1. 1 Publication
    VAR_026036
    Natural varianti331 – 3311I → N in SBHX.
    VAR_007840
    Natural varianti331 – 3311I → T in SBHX. 1 Publication
    VAR_007841
    Natural varianti332 – 3321A → S in SBHX. 1 Publication
    VAR_026037
    Natural varianti332 – 3321A → V in SBHX. 1 Publication
    VAR_026038
    Natural varianti334 – 3341G → D in SBHX.
    VAR_007842

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_004186Add
    BLAST
    Alternative sequencei391 – 3911S → SGNDQD in isoform 3. 2 PublicationsVSP_004187
    Alternative sequencei391 – 3911S → SGN in isoform 5. CuratedVSP_026375
    Alternative sequencei405 – 4051S → SV in isoform 4. CuratedVSP_004188

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003112 mRNA. Translation: CAA05867.1.
    AJ005592
    , 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.
    CCDSiCCDS14556.1. [O43602-1]
    CCDS14557.1. [O43602-2]
    CCDS14558.1. [O43602-3]
    RefSeqiNP_000546.2. NM_000555.3. [O43602-1]
    NP_835364.1. NM_178151.2. [O43602-2]
    NP_835365.1. NM_178152.2. [O43602-3]
    NP_835366.1. NM_178153.2. [O43602-2]
    UniGeneiHs.34780.

    Genome annotation databases

    EnsembliENST00000338081; ENSP00000337697; ENSG00000077279. [O43602-1]
    ENST00000356220; ENSP00000348553; ENSG00000077279. [O43602-3]
    ENST00000371993; ENSP00000361061; ENSG00000077279. [O43602-2]
    ENST00000488120; ENSP00000419861; ENSG00000077279. [O43602-2]
    GeneIDi1641.
    KEGGihsa:1641.
    UCSCiuc004epd.3. human. [O43602-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003112 mRNA. Translation: CAA05867.1 .
    AJ005592
    , 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 .
    CCDSi CCDS14556.1. [O43602-1 ]
    CCDS14557.1. [O43602-2 ]
    CCDS14558.1. [O43602-3 ]
    RefSeqi NP_000546.2. NM_000555.3. [O43602-1 ]
    NP_835364.1. NM_178151.2. [O43602-2 ]
    NP_835365.1. NM_178152.2. [O43602-3 ]
    NP_835366.1. NM_178153.2. [O43602-2 ]
    UniGenei Hs.34780.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MJD NMR - A 126-231 [» ]
    2BQQ X-ray 2.20 A 126-231 [» ]
    2XRP electron microscopy 8.20 I 127-221 [» ]
    4ATU electron microscopy 8.30 I 83-441 [» ]
    ProteinModelPortali O43602.
    SMRi O43602. Positions 132-237, 248-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108008. 12 interactions.
    IntActi O43602. 2 interactions.
    STRINGi 9606.ENSP00000337697.

    PTM databases

    PhosphoSitei O43602.

    Proteomic databases

    MaxQBi O43602.
    PaxDbi O43602.
    PRIDEi O43602.

    Protocols and materials databases

    DNASUi 1641.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338081 ; ENSP00000337697 ; ENSG00000077279 . [O43602-1 ]
    ENST00000356220 ; ENSP00000348553 ; ENSG00000077279 . [O43602-3 ]
    ENST00000371993 ; ENSP00000361061 ; ENSG00000077279 . [O43602-2 ]
    ENST00000488120 ; ENSP00000419861 ; ENSG00000077279 . [O43602-2 ]
    GeneIDi 1641.
    KEGGi hsa:1641.
    UCSCi uc004epd.3. human. [O43602-1 ]

    Organism-specific databases

    CTDi 1641.
    GeneCardsi GC0XM110537.
    GeneReviewsi DCX.
    HGNCi HGNC:2714. DCX.
    HPAi CAB012243.
    MIMi 300067. phenotype.
    300121. gene.
    neXtProti NX_O43602.
    Orphaneti 2148. Lissencephaly type 1 due to doublecortin gene mutation.
    99796. Subcortical band heterotopia.
    PharmGKBi PA27184.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238212.
    HOVERGENi HBG003790.
    KOi K16579.
    OMAi CRVMKGS.
    PhylomeDBi O43602.
    TreeFami TF318770.

    Enzyme and pathway databases

    Reactomei REACT_22312. Neurofascin interactions.

    Miscellaneous databases

    ChiTaRSi DCX. human.
    EvolutionaryTracei O43602.
    GeneWikii Doublecortin.
    GenomeRNAii 1641.
    NextBioi 6740.
    PROi O43602.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43602.
    Bgeei O43602.
    CleanExi HS_DCX.
    Genevestigatori O43602.

    Family and domain databases

    Gene3Di 3.10.20.230. 2 hits.
    InterProi IPR017302. Doublecortin_chordata.
    IPR003533. Doublecortin_dom.
    [Graphical view ]
    Pfami PF03607. DCX. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF037870. Doublin. 1 hit.
    SMARTi SM00537. DCX. 2 hits.
    [Graphical view ]
    PROSITEi PS50309. DC. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. "Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth."
      Homan C.C., Kumar R., Nguyen L.S., Haan E., Raymond F.L., Abidi F., Raynaud M., Schwartz C.E., Wood S.A., Gecz J., Jolly L.A.
      Am. J. Hum. Genet. 94:470-478(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP9X.
    10. Cited for: STRUCTURE BY NMR OF 126-231.
    11. "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.
    12. "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.
    13. Cited for: VARIANTS SBHX ASP-206; GLU-304 AND THR-331.
    14. Cited for: VARIANTS SBHX.
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. Cited for: VARIANTS SBHX GLU-148 AND CYS-259.
    22. "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.
    23. Cited for: VARIANTS LISX1 ILE-123; ASP-141; SER-152 AND LEU-324.

    Entry informationi

    Entry nameiDCX_HUMAN
    AccessioniPrimary (citable) accession number: O43602
    Secondary accession number(s): A6NFY6
    , A9Z1V8, D3DUY8, D3DUY9, D3DUZ0, O43911, Q5JYZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3