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Protein

Neuronal migration protein doublecortin

Gene

Dcx

Organism
Rattus norvegicus (Rat)
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.1 Publication

GO - Molecular functioni

GO - Biological processi

  • intracellular signal transduction Source: GO_Central
  • neuron migration Source: RGD
  • peptidyl-serine phosphorylation Source: GO_Central
  • protein autophosphorylation Source: GO_Central
  • response to electrical stimulus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal migration protein doublecortin
Gene namesi
Name:Dcx
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620670. Dcx.

Subcellular locationi

  • Cytoplasm Curated
  • Cell projection 1 Publication

  • Note: Localizes at neurite tips (PubMed:14741102).

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • dendrite Source: RGD
  • 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
Mutagenesisi47S → A: Impairs phosphorylation by MARK1 and PKA; when associated with A-115. 1 Publication1
Mutagenesisi115S → A: Impairs phosphorylation by MARK1 and PKA; when associated with A-47. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798351 – 365Neuronal migration protein doublecortinAdd BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28Phosphoserine; by CDK5By similarity1
Modified residuei47Phosphoserine; by MARK1 and PKA1 Publication1
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 PKA1 Publication1
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 DYRK2By similarity1
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 (PubMed:14741102). 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 similarity1 Publication
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

PaxDbiQ9ESI7.
PRIDEiQ9ESI7.

PTM databases

iPTMnetiQ9ESI7.
PhosphoSitePlusiQ9ESI7.

Interactioni

Subunit structurei

Interacts with tubulin. Interacts with USP9X.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000065381.

Structurei

3D structure databases

ProteinModelPortaliQ9ESI7.
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.
HOGENOMiHOG000230855.
HOVERGENiHBG003790.
InParanoidiQ9ESI7.

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.

Q9ESI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELDFGHFDE RDKASRNMRG SRMNGLPSPT HSAHCSFYRT RTLQALSNEK
60 70 80 90 100
KAKKVRFYRN GDRYFKGIVY AVSSDRFRSF DALLADLTRS LSDNINLLQG
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):40,560
Last modified:June 1, 2003 - v2
Checksum:i6FCF92406ECC57D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155959 mRNA. Translation: AAG18479.2.
UniGeneiRn.121471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155959 mRNA. Translation: AAG18479.2.
UniGeneiRn.121471.

3D structure databases

ProteinModelPortaliQ9ESI7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000065381.

PTM databases

iPTMnetiQ9ESI7.
PhosphoSitePlusiQ9ESI7.

Proteomic databases

PaxDbiQ9ESI7.
PRIDEiQ9ESI7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi620670. Dcx.

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
HOGENOMiHOG000230855.
HOVERGENiHBG003790.
InParanoidiQ9ESI7.

Miscellaneous databases

PROiQ9ESI7.

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_RAT
AccessioniPrimary (citable) accession number: Q9ESI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 102 of the entry and version 2 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. 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.