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Protein

Neuronal migration protein doublecortin

Gene

Dcx

Organism
Mus musculus (Mouse)
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 participate along with PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that promotes neuronal migration.By similarity

GO - Molecular functioni

GO - Biological processi

  • axon extension Source: MGI
  • brain development Source: MGI
  • central nervous system projection neuron axonogenesis Source: MGI
  • dendrite morphogenesis Source: MGI
  • hippocampus development Source: MGI
  • intracellular signal transduction Source: GO_Central
  • layer formation in cerebral cortex Source: MGI
  • neuron migration Source: MGI
  • peptidyl-serine phosphorylation Source: GO_Central
  • protein autophosphorylation Source: GO_Central
  • pyramidal neuron development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

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:Dcn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1277171. Dcx.

Subcellular locationi

  • Cytoplasm Curated
  • Cell projection By similarity

  • Note: Localizes at neurite tips.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • microtubule Source: UniProtKB-KW
  • neuron projection Source: UniProtKB
  • nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28S → A: Reduces overall phosphorylation by 25%. 1 Publication1
Mutagenesisi287S → A: No effect on overall phosphorylation. 1 Publication1
Mutagenesisi289T → A: No effect on overall phosphorylation. 1 Publication1
Mutagenesisi297S → A: No effect on overall phosphorylation. 1 Publication1
Mutagenesisi326T → A: No effect on overall phosphorylation. 1 Publication1
Mutagenesisi332S → A: No effect on overall phosphorylation. Reduces overall phosphorylation by 36%; when associated with A-339. 1 Publication1
Mutagenesisi336T → A: No effect on overall phosphorylation. 1 Publication1
Mutagenesisi339S → A: No effect on overall phosphorylation. Reduces overall phosphorylation by 36%; when associated with A-332. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798341 – 366Neuronal migration protein doublecortinAdd BLAST366

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28Phosphoserine; by CDK51 Publication1
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 CK21 Publication1
Modified residuei287Phosphoserine; by CDK51 Publication1
Modified residuei289Phosphothreonine; by CDK51 Publication1
Modified residuei294Phosphoserine; by PKCSequence analysis1
Modified residuei297Phosphoserine2 Publications1
Modified residuei297Phosphoserine; by CDK52 Publications1
Modified residuei306PhosphoserineCombined sources1
Modified residuei326Phosphothreonine; by CDK51 Publication1
Modified residuei326Phosphothreonine; by PKC and MAPKSequence analysis1
Modified residuei332Phosphoserine; by CDK5Combined sources1 Publication1
Modified residuei332Phosphoserine; by MAPKSequence analysis1
Modified residuei336Phosphothreonine; by MAPKSequence analysis1
Modified residuei339Phosphoserine; by CDK5Combined sources1 Publication1
Modified residuei339Phosphoserine; by MAPKSequence analysis1
Modified residuei342Phosphoserine; by PKCSequence analysis1
Modified residuei355Phosphoserine; by CK2Sequence analysis1
Modified residuei361Phosphoserine; 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 (PubMed:15099191, PubMed:22807455).By similarity2 Publications
Ubiquitinated by MDM2, leading to its degradation by the proteasome (PubMed:25088421). Ubiquitinated by MDM2 and subsequent degradation leads to reduce the dendritic spine density of olfactory bulb granule cells (PubMed:25088421).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO88809.
PeptideAtlasiO88809.
PRIDEiO88809.

PTM databases

iPTMnetiO88809.
PhosphoSitePlusiO88809.

Expressioni

Tissue specificityi

In neonatal tissues, highly expressed in brain, but not expressed in heart, liver, kidney and spleen. In adult tissues, faintly expressed in brain but not expressed in muscle, heart, lung, liver, spleen, intestine, kidney, testis and placenta.

Developmental stagei

Already expressed by embryonic day 11 (E11), maximally around birth, expression decreasing gradually during the second postnatal week, with no expression in adult stages.

Gene expression databases

BgeeiENSMUSG00000031285.
CleanExiMM_DCN.
MM_DCX.
ExpressionAtlasiO88809. baseline and differential.
GenevisibleiO88809. MM.

Interactioni

Subunit structurei

Interacts with tubulin. Interacts with USP9X.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199073. 5 interactors.
MINTiMINT-216915.
STRINGi10090.ENSMUSP00000033642.

Structurei

3D structure databases

ProteinModelPortaliO88809.
SMRiO88809.
ModBaseiSearch...
MobiDBiSearch...

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 – 342Pro/Ser-richAdd BLAST56

Sequence similaritiesi

Contains 2 doublecortin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
GeneTreeiENSGT00840000129744.
HOVERGENiHBG003790.
InParanoidiO88809.
KOiK16579.
OMAiCRVMKGS.
OrthoDBiEOG091G02RF.
PhylomeDBiO88809.
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]

Sequencei

Sequence statusi: Complete.

O88809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELDFGHFDE RDKASRNMRG 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 AAGPKASPTP QKTSAKSPGP
310 320 330 340 350
MRRSKSPADS GNDQDANGTS SSQLSTPKSK QSPISTPTSP GSLRKHKVDL
360
YLPLSLDDSD SLGDSM
Length:366
Mass (Da):40,613
Last modified:November 1, 1998 - v1
Checksum:i323D0774C222F295
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti345K → R in AAC31799 (PubMed:9668176).Curated1
Sequence conflicti348Missing in AAC31799 (PubMed:9668176).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011678 mRNA. Translation: BAA33387.1.
AF045547 mRNA. Translation: AAC31799.1.
AY560329 mRNA. Translation: AAT58219.1.
BX530055 Genomic DNA. Translation: CAM25089.1.
CCDSiCCDS53209.1.
PIRiJE0368.
RefSeqiNP_001103692.1. NM_001110222.1.
NP_001103693.1. NM_001110223.1.
NP_001103694.1. NM_001110224.1.
NP_034155.2. NM_010025.2.
UniGeneiMm.12871.

Genome annotation databases

EnsembliENSMUST00000033642; ENSMUSP00000033642; ENSMUSG00000031285.
ENSMUST00000087313; ENSMUSP00000084570; ENSMUSG00000031285.
GeneIDi13193.
KEGGimmu:13193.
UCSCiuc033jun.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011678 mRNA. Translation: BAA33387.1.
AF045547 mRNA. Translation: AAC31799.1.
AY560329 mRNA. Translation: AAT58219.1.
BX530055 Genomic DNA. Translation: CAM25089.1.
CCDSiCCDS53209.1.
PIRiJE0368.
RefSeqiNP_001103692.1. NM_001110222.1.
NP_001103693.1. NM_001110223.1.
NP_001103694.1. NM_001110224.1.
NP_034155.2. NM_010025.2.
UniGeneiMm.12871.

3D structure databases

ProteinModelPortaliO88809.
SMRiO88809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199073. 5 interactors.
MINTiMINT-216915.
STRINGi10090.ENSMUSP00000033642.

PTM databases

iPTMnetiO88809.
PhosphoSitePlusiO88809.

Proteomic databases

PaxDbiO88809.
PeptideAtlasiO88809.
PRIDEiO88809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033642; ENSMUSP00000033642; ENSMUSG00000031285.
ENSMUST00000087313; ENSMUSP00000084570; ENSMUSG00000031285.
GeneIDi13193.
KEGGimmu:13193.
UCSCiuc033jun.1. mouse.

Organism-specific databases

CTDi1641.
MGIiMGI:1277171. Dcx.

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
GeneTreeiENSGT00840000129744.
HOVERGENiHBG003790.
InParanoidiO88809.
KOiK16579.
OMAiCRVMKGS.
OrthoDBiEOG091G02RF.
PhylomeDBiO88809.
TreeFamiTF318770.

Miscellaneous databases

ChiTaRSiDcx. mouse.
PROiO88809.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031285.
CleanExiMM_DCN.
MM_DCX.
ExpressionAtlasiO88809. baseline and differential.
GenevisibleiO88809. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: O88809
Secondary accession number(s): Q6E5A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.