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O43602

- DCX_HUMAN

UniProt

O43602 - DCX_HUMAN

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Protein

Neuronal migration protein doublecortin

Gene
DCX, DBCN, LISX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 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
Complete GO annotation...

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
Complete GO annotation...

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'.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.8 Publications
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 PKC Reviewed prediction
Modified residuei109 – 1091Phosphoserine; by CDK5 By similarity
Modified residuei128 – 1281Phosphoserine; by MARK1 and PKA By similarity
Modified residuei151 – 1511Phosphotyrosine; by ABL Reviewed prediction
Modified residuei155 – 1551Phosphoserine; by PKC Reviewed prediction
Modified residuei171 – 1711Phosphoserine; by CK2 Reviewed prediction
Modified residuei191 – 1911Phosphoserine; by PKC Reviewed prediction
Modified residuei196 – 1961Phosphoserine; by CK2, MARK1 and PKA By similarity
Modified residuei346 – 3461Phosphoserine; by CK2 By similarity
Modified residuei368 – 3681Phosphoserine; by CDK5 By similarity
Modified residuei370 – 3701Phosphothreonine; by CDK5 By similarity
Modified residuei375 – 3751Phosphoserine; by PKC Reviewed prediction
Modified residuei378 – 3781Phosphoserine; by CDK5 By similarity
Modified residuei387 – 3871Phosphoserine; by CK2; alternate Reviewed prediction
Modified residuei387 – 3871Phosphoserine; by DYRK2; alternate1 Publication
Modified residuei402 – 4021Phosphothreonine; by CDK5; alternate By similarity
Modified residuei402 – 4021Phosphothreonine; by PKC and MAPK; alternate Reviewed prediction
Modified residuei408 – 4081Phosphoserine; by CDK5; alternate By similarity
Modified residuei408 – 4081Phosphoserine; by MAPK; alternate Reviewed prediction
Modified residuei412 – 4121Phosphothreonine; by MAPK Reviewed prediction
Modified residuei415 – 4151Phosphoserine; by CDK5; alternate By similarity
Modified residuei415 – 4151Phosphoserine; by MAPK; alternate Reviewed prediction
Modified residuei418 – 4181Phosphoserine; by PKC Reviewed prediction
Modified residuei430 – 4301Phosphoserine; by CK2 Reviewed prediction
Modified residuei436 – 4361Phosphoserine; by CK2 Reviewed prediction

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.

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.

Miscellaneous databases

EvolutionaryTraceiO43602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 22087Doublecortin 1Add
BLAST
Domaini261 – 34484Doublecortin 2Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 2 doublecortin domains.

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. VSP_004186Add
BLAST
Alternative sequencei391 – 3911S → SGNDQD in isoform 3. VSP_004187
Alternative sequencei391 – 3911S → SGN in isoform 5. VSP_026375
Alternative sequencei405 – 4051S → SV in isoform 4. VSP_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]
ENST00000356915; ENSP00000349385; 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 ]
ENST00000356915 ; ENSP00000349385 ; 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

« Hide 'large scale' publications
  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. 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. Cited for: VARIANTS SBHX ASP-206; GLU-304 AND THR-331.
  13. 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. 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. 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: September 3, 2014
This is version 149 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

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