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Protein

Neuronal migration protein doublecortin

Gene

DCX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • central nervous system development Source: ProtInc
  • intracellular signal transduction Source: GO_Central
  • nervous system development Source: ProtInc
  • neuron migration Source: UniProtKB
  • peptidyl-serine phosphorylation Source: GO_Central
  • protein autophosphorylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000077279-MONOMER.
ReactomeiR-HSA-447043. Neurofascin interactions.
SIGNORiO43602.

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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:2714. DCX.

Subcellular locationi

  • Cytoplasm Curated
  • Cell projection By similarity

  • Note: Localizes at neurite tips.By similarity

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoskeleton Source: ProtInc
  • cytosol Source: Reactome
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: ProtInc
  • neuron projection Source: UniProtKB
  • nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Microtubule

Pathology & Biotechi

Involvement in diseasei

Lissencephaly, X-linked 1 (LISX1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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'.
See also OMIM:300067
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02602242T → I in LISX1. 1 Publication1
Natural variantiVAR_00781943L → S in LISX1. 1 PublicationCorresponds to variant rs587783521dbSNPEnsembl.1
Natural variantiVAR_00782047S → R in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894783dbSNPEnsembl.1
Natural variantiVAR_00782159R → L in LISX1 and SBHX. 1 PublicationCorresponds to variant rs122457137dbSNPEnsembl.1
Natural variantiVAR_02602460N → D in LISX1. 1 Publication1
Natural variantiVAR_00782362D → N in LISX1 and SBHX. 1 PublicationCorresponds to variant rs104894779dbSNPEnsembl.1
Natural variantiVAR_02602671A → S in LISX1. 1 PublicationCorresponds to variant rs104894786dbSNPEnsembl.1
Natural variantiVAR_007826100G → A in LISX1 and SBHX. 2 Publications1
Natural variantiVAR_007827102R → S in LISX1. 1 Publication1
Natural variantiVAR_007828125Y → H in LISX1 and SBHX. 1 PublicationCorresponds to variant rs104894781dbSNPEnsembl.1
Natural variantiVAR_007833192R → W in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894780dbSNPEnsembl.1
Natural variantiVAR_026031196R → H in LISX1. 2 PublicationsCorresponds to variant rs56030372dbSNPEnsembl.1
Natural variantiVAR_007835203T → R in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894782dbSNPEnsembl.1
Natural variantiVAR_026036243F → L in LISX1. 1 Publication1
Subcortical band heterotopia X-linked (SBHX)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSBHX 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.
See also OMIM:300067
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00782047S → R in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894783dbSNPEnsembl.1
Natural variantiVAR_02602350K → N in SBHX. 1 PublicationCorresponds to variant rs587783523dbSNPEnsembl.1
Natural variantiVAR_00782259R → H in SBHX. 1 PublicationCorresponds to variant rs122457137dbSNPEnsembl.1
Natural variantiVAR_00782159R → L in LISX1 and SBHX. 1 PublicationCorresponds to variant rs122457137dbSNPEnsembl.1
Natural variantiVAR_00782362D → N in LISX1 and SBHX. 1 PublicationCorresponds to variant rs104894779dbSNPEnsembl.1
Natural variantiVAR_02602567G → E in SBHX. 1 Publication1
Natural variantiVAR_00782478R → L in SBHX. 2 PublicationsCorresponds to variant rs104894784dbSNPEnsembl.1
Natural variantiVAR_00782586D → H in SBHX. 1 Publication1
Natural variantiVAR_01053689R → G in SBHX; mild. 2 PublicationsCorresponds to variant rs104894785dbSNPEnsembl.1
Natural variantiVAR_02602797L → R in SBHX. 1 PublicationCorresponds to variant rs587783537dbSNPEnsembl.1
Natural variantiVAR_007826100G → A in LISX1 and SBHX. 2 Publications1
Natural variantiVAR_026028104I → T in SBHX. 1 Publication1
Natural variantiVAR_007829125Y → D in SBHX. 1 Publication1
Natural variantiVAR_007828125Y → H in LISX1 and SBHX. 1 PublicationCorresponds to variant rs104894781dbSNPEnsembl.1
Natural variantiVAR_026029178R → C in SBHX. 1 PublicationCorresponds to variant rs587783558dbSNPEnsembl.1
Natural variantiVAR_007830178R → L in SBHX. Corresponds to variant rs587783559dbSNPEnsembl.1
Natural variantiVAR_007831186R → C in SBHX. 3 PublicationsCorresponds to variant rs587783562dbSNPEnsembl.1
Natural variantiVAR_026030191P → L in SBHX. 1
Natural variantiVAR_007832191P → R in SBHX. Corresponds to variant rs587783566dbSNPEnsembl.1
Natural variantiVAR_007833192R → W in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894780dbSNPEnsembl.1
Natural variantiVAR_026033200N → I in SBHX. 1 Publication1
Natural variantiVAR_007834200N → K in SBHX. 2 Publications1
Natural variantiVAR_026034203T → A in SBHX. 1 PublicationCorresponds to variant rs587783570dbSNPEnsembl.1
Natural variantiVAR_007835203T → R in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894782dbSNPEnsembl.1
Natural variantiVAR_007836214I → T in SBHX. 1 PublicationCorresponds to variant rs587783574dbSNPEnsembl.1
Natural variantiVAR_007837222T → I in SBHX. 1
Natural variantiVAR_007838223G → E in SBHX. 1 Publication1
Natural variantiVAR_026035223G → V in SBHX. 1 Publication1
Natural variantiVAR_007839236V → I in SBHX. 1
Natural variantiVAR_007840250I → N in SBHX. 1
Natural variantiVAR_007841250I → T in SBHX. 1 Publication1
Natural variantiVAR_026037251A → S in SBHX. 1 PublicationCorresponds to variant rs587783585dbSNPEnsembl.1
Natural variantiVAR_026038251A → V in SBHX. 1 Publication1
Natural variantiVAR_007842253G → D in SBHX. 1

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

DisGeNETi1641.
MalaCardsiDCX.
MIMi300067. phenotype.
OpenTargetsiENSG00000077279.
Orphaneti2148. Lissencephaly type 1 due to doublecortin gene mutation.
99796. Subcortical band heterotopia.
PharmGKBiPA27184.

Polymorphism and mutation databases

BioMutaiDCX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798331 – 365Neuronal migration protein doublecortinAdd BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14Phosphothreonine; by PKCSequence analysis1
Modified residuei28Phosphoserine; by CDK5By similarity1
Modified residuei47Phosphoserine; by MARK1 and PKABy similarity1
Modified residuei70Phosphotyrosine; by ABLSequence analysis1
Modified residuei74Phosphoserine; by PKCSequence analysis1
Modified residuei90Phosphoserine; by CK2Sequence analysis1
Modified residuei110Phosphoserine; by PKCSequence analysis1
Modified residuei115Phosphoserine; by CK2, MARK1 and PKABy similarity1
Modified residuei265Phosphoserine; by CK2By similarity1
Modified residuei287Phosphoserine; by CDK5By similarity1
Modified residuei289Phosphothreonine; by CDK5By similarity1
Modified residuei294Phosphoserine; by PKCSequence analysis1
Modified residuei297Phosphoserine; by CDK5By similarity1
Modified residuei306Phosphoserine; by CK2Sequence analysisBy similarity1
Modified residuei306Phosphoserine; by DYRK21 Publication1
Modified residuei326Phosphothreonine; by CDK5By similarity1
Modified residuei326Phosphothreonine; by PKC and MAPKSequence analysis1
Modified residuei332Phosphoserine; by CDK5By similarity1
Modified residuei332Phosphoserine; by MAPKSequence analysis1
Modified residuei336Phosphothreonine; by MAPKSequence analysis1
Modified residuei339Phosphoserine; by CDK5By similarity1
Modified residuei339Phosphoserine; by MAPKSequence analysis1
Modified residuei342Phosphoserine; by PKCSequence analysis1
Modified residuei354Phosphoserine; by CK2Sequence analysis1
Modified residuei360Phosphoserine; by CK2Sequence analysis1

Post-translational modificationi

Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 (By similarity).By similarity
Ubiquitinated by MDM2, leading to its degradation by the proteasome. Ubiquitinated by MDM2 and subsequent degradation leads to reduce the dendritic spine density of olfactory bulb granule cells.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO43602.
PeptideAtlasiO43602.
PRIDEiO43602.

PTM databases

iPTMnetiO43602.
PhosphoSitePlusiO43602.

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

BgeeiENSG00000077279.
CleanExiHS_DCX.
ExpressionAtlasiO43602. baseline and differential.
GenevisibleiO43602. HS.

Organism-specific databases

HPAiHPA036121.
HPA059243.

Interactioni

Subunit structurei

Interacts with tubulin. Interacts with USP9X (PubMed:24607389).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO2Q131373EBI-8646694,EBI-739580
GOLGA2Q083794EBI-8646694,EBI-618309
IKZF1Q134224EBI-8646694,EBI-745305
KIFC3Q9BVG83EBI-8646694,EBI-2125614
KRT40Q6A1623EBI-8646694,EBI-10171697
KRTAP10-8P604103EBI-8646694,EBI-10171774
MEOX1P502213EBI-8646694,EBI-2864512
MID2Q9UJV3-23EBI-8646694,EBI-10172526
RINT1Q6NUQ13EBI-8646694,EBI-726876
SPAG5Q96R063EBI-8646694,EBI-413317
TINF2Q9BSI42EBI-8646694,EBI-717399
TRIM23P364063EBI-8646694,EBI-740098
TRIM27P143733EBI-8646694,EBI-719493
ZBTB5O150623EBI-8646694,EBI-722671

GO - Molecular functioni

  • calmodulin binding Source: GO_Central
  • microtubule binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108008. 41 interactors.
IntActiO43602. 17 interactors.
STRINGi9606.ENSP00000337697.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 59Combined sources7
Beta strandi68 – 72Combined sources5
Turni74 – 76Combined sources3
Beta strandi77 – 79Combined sources3
Helixi80 – 91Combined sources12
Turni94 – 96Combined sources3
Beta strandi103 – 106Combined sources4
Beta strandi110 – 113Combined sources4
Helixi116 – 118Combined sources3
Beta strandi124 – 131Combined sources8
Turni138 – 141Combined sources4
Turni144 – 147Combined sources4
Turni175 – 177Combined sources3
Beta strandi180 – 191Combined sources12
Beta strandi194 – 199Combined sources6
Turni201 – 203Combined sources3
Helixi207 – 217Combined sources11
Beta strandi228 – 230Combined sources3
Helixi239 – 242Combined sources4
Beta strandi243 – 245Combined sources3
Beta strandi248 – 252Combined sources5
Helixi254 – 256Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MJDNMR-A45-150[»]
2BQQX-ray2.20A45-150[»]
2XRPelectron microscopy8.20I46-140[»]
4ATUelectron microscopy8.30I2-365[»]
5IKCX-ray2.06M/N52-140[»]
5IN7X-ray2.48A/B46-150[»]
5IO9X-ray1.30A/B52-149[»]
5IOIX-ray2.40A/B/C/D/E/F52-150[»]
5IP4X-ray1.81D/E170-260[»]
ProteinModelPortaliO43602.
SMRiO43602.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 139Doublecortin 1PROSITE-ProRule annotationAdd BLAST87
Domaini180 – 263Doublecortin 2PROSITE-ProRule annotationAdd BLAST84

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi287 – 365Pro/Ser-richAdd BLAST79

Sequence similaritiesi

Contains 2 doublecortin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
GeneTreeiENSGT00840000129744.
HOVERGENiHBG003790.
InParanoidiO43602.
KOiK16579.
OrthoDBiEOG091G02RF.
TreeFamiTF318770.

Family and domain databases

CDDicd01617. DCX. 2 hits.
Gene3Di3.10.20.230. 2 hits.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR017302. Doublecortin_chordata.
IPR003533. Doublecortin_dom.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF03607. DCX. 2 hits.
[Graphical view]
PIRSFiPIRSF037870. Doublin. 1 hit.
SMARTiSM00537. DCX. 2 hits.
[Graphical view]
PROSITEiPS50309. DC. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O43602-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MELDFGHFDE RDKTSRNMRG SRMNGLPSPT HSAHCSFYRT RTLQALSNEK
60 70 80 90 100
KAKKVRFYRN GDRYFKGIVY AVSSDRFRSF DALLADLTRS LSDNINLPQG
110 120 130 140 150
VRYIYTIDGS RKIGSMDELE EGESYVCSSD NFFKKVEYTK NVNPNWSVNV
160 170 180 190 200
KTSANMKAPQ SLASSNSAQA RENKDFVRPK LVTIIRSGVK PRKAVRVLLN
210 220 230 240 250
KKTAHSFEQV LTDITEAIKL ETGVVKKLYT LDGKQVTCLH DFFGDDDVFI
260 270 280 290 300
ACGPEKFRYA QDDFSLDENE CRVMKGNPSA TAGPKASPTP QKTSAKSPGP
310 320 330 340 350
MRRSKSPADS GNDQDANGTS SSQLSTPKSK QSPISTPTSP GSLRKHKDLY
360
LPLSLDDSDS LGDSM
Length:365
Mass (Da):40,574
Last modified:March 16, 2016 - v4
Checksum:i1E859F2114CC3BB1
GO
Isoform 2 (identifier: O43602-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     310-315: SGNDQD → S

Show »
Length:360
Mass (Da):40,044
Checksum:i91D0D89433AF52A0
GO

Sequence cautioni

The sequence EAX02642 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAX02644 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAX02649 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02602242T → I in LISX1. 1 Publication1
Natural variantiVAR_00781943L → S in LISX1. 1 PublicationCorresponds to variant rs587783521dbSNPEnsembl.1
Natural variantiVAR_00782047S → R in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894783dbSNPEnsembl.1
Natural variantiVAR_02602350K → N in SBHX. 1 PublicationCorresponds to variant rs587783523dbSNPEnsembl.1
Natural variantiVAR_00782259R → H in SBHX. 1 PublicationCorresponds to variant rs122457137dbSNPEnsembl.1
Natural variantiVAR_00782159R → L in LISX1 and SBHX. 1 PublicationCorresponds to variant rs122457137dbSNPEnsembl.1
Natural variantiVAR_02602460N → D in LISX1. 1 Publication1
Natural variantiVAR_00782362D → N in LISX1 and SBHX. 1 PublicationCorresponds to variant rs104894779dbSNPEnsembl.1
Natural variantiVAR_02602567G → E in SBHX. 1 Publication1
Natural variantiVAR_02602671A → S in LISX1. 1 PublicationCorresponds to variant rs104894786dbSNPEnsembl.1
Natural variantiVAR_01020278R → H in SBH. 1 PublicationCorresponds to variant rs104894784dbSNPEnsembl.1
Natural variantiVAR_00782478R → L in SBHX. 2 PublicationsCorresponds to variant rs104894784dbSNPEnsembl.1
Natural variantiVAR_00782586D → H in SBHX. 1 Publication1
Natural variantiVAR_01053689R → G in SBHX; mild. 2 PublicationsCorresponds to variant rs104894785dbSNPEnsembl.1
Natural variantiVAR_02602797L → R in SBHX. 1 PublicationCorresponds to variant rs587783537dbSNPEnsembl.1
Natural variantiVAR_007826100G → A in LISX1 and SBHX. 2 Publications1
Natural variantiVAR_007827102R → S in LISX1. 1 Publication1
Natural variantiVAR_026028104I → T in SBHX. 1 Publication1
Natural variantiVAR_007829125Y → D in SBHX. 1 Publication1
Natural variantiVAR_007828125Y → H in LISX1 and SBHX. 1 PublicationCorresponds to variant rs104894781dbSNPEnsembl.1
Natural variantiVAR_026029178R → C in SBHX. 1 PublicationCorresponds to variant rs587783558dbSNPEnsembl.1
Natural variantiVAR_007830178R → L in SBHX. Corresponds to variant rs587783559dbSNPEnsembl.1
Natural variantiVAR_007831186R → C in SBHX. 3 PublicationsCorresponds to variant rs587783562dbSNPEnsembl.1
Natural variantiVAR_026030191P → L in SBHX. 1
Natural variantiVAR_007832191P → R in SBHX. Corresponds to variant rs587783566dbSNPEnsembl.1
Natural variantiVAR_007833192R → W in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894780dbSNPEnsembl.1
Natural variantiVAR_026031196R → H in LISX1. 2 PublicationsCorresponds to variant rs56030372dbSNPEnsembl.1
Natural variantiVAR_026032196R → S in epilepsy; resistant partial seizures; related to 'cryptogenic' epilepsy. 1 PublicationCorresponds to variant rs587783568dbSNPEnsembl.1
Natural variantiVAR_026033200N → I in SBHX. 1 Publication1
Natural variantiVAR_007834200N → K in SBHX. 2 Publications1
Natural variantiVAR_026034203T → A in SBHX. 1 PublicationCorresponds to variant rs587783570dbSNPEnsembl.1
Natural variantiVAR_007835203T → R in LISX1 and SBHX. 2 PublicationsCorresponds to variant rs104894782dbSNPEnsembl.1
Natural variantiVAR_007836214I → T in SBHX. 1 PublicationCorresponds to variant rs587783574dbSNPEnsembl.1
Natural variantiVAR_007837222T → I in SBHX. 1
Natural variantiVAR_007838223G → E in SBHX. 1 Publication1
Natural variantiVAR_026035223G → V in SBHX. 1 Publication1
Natural variantiVAR_007839236V → I in SBHX. 1
Natural variantiVAR_026036243F → L in LISX1. 1 Publication1
Natural variantiVAR_007840250I → N in SBHX. 1
Natural variantiVAR_007841250I → T in SBHX. 1 Publication1
Natural variantiVAR_026037251A → S in SBHX. 1 PublicationCorresponds to variant rs587783585dbSNPEnsembl.1
Natural variantiVAR_026038251A → V in SBHX. 1 Publication1
Natural variantiVAR_007842253G → D in SBHX. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_058155310 – 315SGNDQD → S in isoform 2. 4 Publications6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. No translation available.
AL450490 Genomic DNA. No translation available.
CH471120 Genomic DNA. Translation: EAX02644.1. Sequence problems.
CH471120 Genomic DNA. Translation: EAX02645.1.
CH471120 Genomic DNA. Translation: EAX02642.1. Sequence problems.
CH471120 Genomic DNA. Translation: EAX02643.1.
CH471120 Genomic DNA. Translation: EAX02646.1.
CH471120 Genomic DNA. Translation: EAX02647.1.
CH471120 Genomic DNA. Translation: EAX02649.1. Sequence problems.
BC027925 mRNA. Translation: AAH27925.1.
CCDSiCCDS14557.1. [O43602-2]
CCDS14558.1. [O43602-1]
RefSeqiNP_000546.2. NM_000555.3.
NP_835364.1. NM_178151.2. [O43602-2]
NP_835365.1. NM_178152.2. [O43602-1]
NP_835366.1. NM_178153.2. [O43602-2]
UniGeneiHs.34780.

Genome annotation databases

EnsembliENST00000358070; ENSP00000350776; ENSG00000077279. [O43602-2]
ENST00000371993; ENSP00000361061; ENSG00000077279. [O43602-2]
ENST00000488120; ENSP00000419861; ENSG00000077279. [O43602-2]
ENST00000496551; ENSP00000490448; ENSG00000077279. [O43602-1]
ENST00000635795; ENSP00000489635; ENSG00000077279. [O43602-1]
GeneIDi1641.
KEGGihsa:1641.
UCSCiuc004epd.4. human. [O43602-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. No translation available.
AL450490 Genomic DNA. No translation available.
CH471120 Genomic DNA. Translation: EAX02644.1. Sequence problems.
CH471120 Genomic DNA. Translation: EAX02645.1.
CH471120 Genomic DNA. Translation: EAX02642.1. Sequence problems.
CH471120 Genomic DNA. Translation: EAX02643.1.
CH471120 Genomic DNA. Translation: EAX02646.1.
CH471120 Genomic DNA. Translation: EAX02647.1.
CH471120 Genomic DNA. Translation: EAX02649.1. Sequence problems.
BC027925 mRNA. Translation: AAH27925.1.
CCDSiCCDS14557.1. [O43602-2]
CCDS14558.1. [O43602-1]
RefSeqiNP_000546.2. NM_000555.3.
NP_835364.1. NM_178151.2. [O43602-2]
NP_835365.1. NM_178152.2. [O43602-1]
NP_835366.1. NM_178153.2. [O43602-2]
UniGeneiHs.34780.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MJDNMR-A45-150[»]
2BQQX-ray2.20A45-150[»]
2XRPelectron microscopy8.20I46-140[»]
4ATUelectron microscopy8.30I2-365[»]
5IKCX-ray2.06M/N52-140[»]
5IN7X-ray2.48A/B46-150[»]
5IO9X-ray1.30A/B52-149[»]
5IOIX-ray2.40A/B/C/D/E/F52-150[»]
5IP4X-ray1.81D/E170-260[»]
ProteinModelPortaliO43602.
SMRiO43602.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108008. 41 interactors.
IntActiO43602. 17 interactors.
STRINGi9606.ENSP00000337697.

PTM databases

iPTMnetiO43602.
PhosphoSitePlusiO43602.

Polymorphism and mutation databases

BioMutaiDCX.

Proteomic databases

PaxDbiO43602.
PeptideAtlasiO43602.
PRIDEiO43602.

Protocols and materials databases

DNASUi1641.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358070; ENSP00000350776; ENSG00000077279. [O43602-2]
ENST00000371993; ENSP00000361061; ENSG00000077279. [O43602-2]
ENST00000488120; ENSP00000419861; ENSG00000077279. [O43602-2]
ENST00000496551; ENSP00000490448; ENSG00000077279. [O43602-1]
ENST00000635795; ENSP00000489635; ENSG00000077279. [O43602-1]
GeneIDi1641.
KEGGihsa:1641.
UCSCiuc004epd.4. human. [O43602-1]

Organism-specific databases

CTDi1641.
DisGeNETi1641.
GeneCardsiDCX.
GeneReviewsiDCX.
HGNCiHGNC:2714. DCX.
HPAiHPA036121.
HPA059243.
MalaCardsiDCX.
MIMi300067. phenotype.
300121. gene.
neXtProtiNX_O43602.
OpenTargetsiENSG00000077279.
Orphaneti2148. Lissencephaly type 1 due to doublecortin gene mutation.
99796. Subcortical band heterotopia.
PharmGKBiPA27184.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
GeneTreeiENSGT00840000129744.
HOVERGENiHBG003790.
InParanoidiO43602.
KOiK16579.
OrthoDBiEOG091G02RF.
TreeFamiTF318770.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000077279-MONOMER.
ReactomeiR-HSA-447043. Neurofascin interactions.
SIGNORiO43602.

Miscellaneous databases

ChiTaRSiDCX. human.
EvolutionaryTraceiO43602.
GeneWikiiDoublecortin.
GenomeRNAii1641.
PROiO43602.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000077279.
CleanExiHS_DCX.
ExpressionAtlasiO43602. baseline and differential.
GenevisibleiO43602. HS.

Family and domain databases

CDDicd01617. DCX. 2 hits.
Gene3Di3.10.20.230. 2 hits.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR017302. Doublecortin_chordata.
IPR003533. Doublecortin_dom.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF03607. DCX. 2 hits.
[Graphical view]
PIRSFiPIRSF037870. Doublin. 1 hit.
SMARTiSM00537. DCX. 2 hits.
[Graphical view]
PROSITEiPS50309. DC. 2 hits.
[Graphical view]
ProtoNetiSearch...

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: March 16, 2016
Last modified: November 2, 2016
This is version 172 of the entry and version 4 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.