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O88809

- DCX_MOUSE

UniProt

O88809 - DCX_MOUSE

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Protein

Neuronal migration protein doublecortin

Gene

Dcx

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

GO - Molecular functioni

  1. microtubule binding Source: UniProtKB

GO - Biological processi

  1. axon extension Source: MGI
  2. brain development Source: MGI
  3. central nervous system projection neuron axonogenesis Source: MGI
  4. dendrite morphogenesis Source: MGI
  5. intracellular signal transduction Source: InterPro
  6. neuron migration Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_235102. 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:Dcn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: 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

  1. cytoplasm Source: UniProtKB-KW
  2. intracellular Source: MGI
  3. microtubule Source: UniProtKB-KW
  4. neuron projection Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281S → A: Reduces overall phosphorylation by 25%. 1 Publication
Mutagenesisi287 – 2871S → A: No effect on overall phosphorylation. 1 Publication
Mutagenesisi289 – 2891T → A: No effect on overall phosphorylation. 1 Publication
Mutagenesisi297 – 2971S → A: No effect on overall phosphorylation. 1 Publication
Mutagenesisi326 – 3261T → A: No effect on overall phosphorylation. 1 Publication
Mutagenesisi332 – 3321S → A: No effect on overall phosphorylation. Reduces overall phosphorylation by 36%; when associated with A-339. 1 Publication
Mutagenesisi336 – 3361T → A: No effect on overall phosphorylation. 1 Publication
Mutagenesisi339 – 3391S → A: No effect on overall phosphorylation. Reduces overall phosphorylation by 36%; when associated with A-332. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Neuronal migration protein doublecortinPRO_0000079834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphoserine; by CDK51 Publication
Modified residuei47 – 471Phosphoserine; by MARK1 and PKABy similarity
Modified residuei70 – 701Phosphotyrosine; by ABLSequence Analysis
Modified residuei74 – 741Phosphoserine; by PKCSequence Analysis
Modified residuei90 – 901Phosphoserine; by CK2Sequence Analysis
Modified residuei110 – 1101Phosphoserine; by PKCSequence Analysis
Modified residuei115 – 1151Phosphoserine; by CK2, MARK1 and PKABy similarity
Modified residuei265 – 2651Phosphoserine; by CK21 Publication
Modified residuei287 – 2871Phosphoserine; by CDK51 Publication
Modified residuei289 – 2891Phosphothreonine; by CDK51 Publication
Modified residuei294 – 2941Phosphoserine; by PKCSequence Analysis
Modified residuei297 – 2971Phosphoserine; alternate2 Publications
Modified residuei297 – 2971Phosphoserine; by CDK5; alternate2 Publications
Modified residuei306 – 3061Phosphoserine; alternate1 Publication
Modified residuei306 – 3061Phosphoserine; by CK2; alternateSequence Analysis
Modified residuei306 – 3061Phosphoserine; by DYRK2; alternateBy similarity
Modified residuei326 – 3261Phosphothreonine; by CDK5; alternate1 Publication
Modified residuei326 – 3261Phosphothreonine; by PKC and MAPK; alternateSequence Analysis
Modified residuei332 – 3321Phosphoserine; by CDK5; alternate1 Publication
Modified residuei332 – 3321Phosphoserine; by MAPK; alternateSequence Analysis
Modified residuei336 – 3361Phosphothreonine; by MAPKSequence Analysis
Modified residuei339 – 3391Phosphoserine; by CDK5; alternate1 Publication
Modified residuei339 – 3391Phosphoserine; by MAPK; alternateSequence Analysis
Modified residuei342 – 3421Phosphoserine; by PKCSequence Analysis
Modified residuei355 – 3551Phosphoserine; by CK2Sequence Analysis
Modified residuei361 – 3611Phosphoserine; by CK2Sequence Analysis

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 21.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO88809.
PaxDbiO88809.
PRIDEiO88809.

PTM databases

PhosphoSiteiO88809.

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

BgeeiO88809.
CleanExiMM_DCN.
MM_DCX.
ExpressionAtlasiO88809. baseline and differential.
GenevestigatoriO88809.

Interactioni

Subunit structurei

Interacts with tubulin. Interacts with USP9X.By similarity

Protein-protein interaction databases

BioGridi199073. 5 interactions.
MINTiMINT-216915.

Structurei

3D structure databases

ProteinModelPortaliO88809.
SMRiO88809. Positions 51-156, 167-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 13987Doublecortin 1PROSITE-ProRule annotationAdd
BLAST
Domaini180 – 26384Doublecortin 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi287 – 34256Pro/Ser-richAdd
BLAST

Sequence similaritiesi

Contains 2 doublecortin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG238212.
GeneTreeiENSGT00770000120480.
HOVERGENiHBG003790.
InParanoidiO88809.
KOiK16579.
OMAiCRVMKGS.
OrthoDBiEOG7M98FQ.
PhylomeDBiO88809.
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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451K → R in AAC31799. (PubMed:9668176)Curated
Sequence conflicti348 – 3481Missing in AAC31799. (PubMed:9668176)Curated

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.
UCSCiuc009umn.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 .
CCDSi CCDS53209.1.
PIRi JE0368.
RefSeqi NP_001103692.1. NM_001110222.1.
NP_001103693.1. NM_001110223.1.
NP_001103694.1. NM_001110224.1.
NP_034155.2. NM_010025.2.
UniGenei Mm.12871.

3D structure databases

ProteinModelPortali O88809.
SMRi O88809. Positions 51-156, 167-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199073. 5 interactions.
MINTi MINT-216915.

PTM databases

PhosphoSitei O88809.

Proteomic databases

MaxQBi O88809.
PaxDbi O88809.
PRIDEi O88809.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033642 ; ENSMUSP00000033642 ; ENSMUSG00000031285 .
ENSMUST00000087313 ; ENSMUSP00000084570 ; ENSMUSG00000031285 .
GeneIDi 13193.
KEGGi mmu:13193.
UCSCi uc009umn.1. mouse.

Organism-specific databases

CTDi 1641.
MGIi MGI:1277171. Dcx.

Phylogenomic databases

eggNOGi NOG238212.
GeneTreei ENSGT00770000120480.
HOVERGENi HBG003790.
InParanoidi O88809.
KOi K16579.
OMAi CRVMKGS.
OrthoDBi EOG7M98FQ.
PhylomeDBi O88809.
TreeFami TF318770.

Enzyme and pathway databases

Reactomei REACT_235102. Neurofascin interactions.

Miscellaneous databases

ChiTaRSi Dcx. mouse.
NextBioi 283316.
PROi O88809.
SOURCEi Search...

Gene expression databases

Bgeei O88809.
CleanExi MM_DCN.
MM_DCX.
ExpressionAtlasi O88809. baseline and differential.
Genevestigatori O88809.

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. "Cloning and developmental expression of the murine homolog of doublecortin."
    Matsuo N., Kawamoto S., Matsubara K., Okubo K.
    Biochem. Biophys. Res. Commun. 252:571-576(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Hippocampus.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-28; SER-287; THR-289; SER-297; THR-326; SER-332 AND SER-339, MUTAGENESIS OF SER-28; SER-287; THR-289; SER-297; THR-326; SER-332; THR-336 AND SER-339.
    Strain: Swiss Webster.
    Tissue: Embryo.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "Comparative phosphoproteomic analysis of neonatal and adult murine brain."
    Goswami T., Li X., Smith A.M., Luderowski E.M., Vincent J.J., Rush J., Ballif B.A.
    Proteomics 12:2185-2189(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-265 AND SER-297.

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 26, 2014
This is version 120 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

External Data

Dasty 3