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doublecortin (human)

Overview doublecortin 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 DCAMKL1 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 LIS-1 of a overlapping, but distinct, signaling pathways that promote neuronal migration. Interacts with tubulin. 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. 5 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis Cellular Component: microtubule; neuron projection; microtubule associated complex; cytoskeleton; dendrite; cytosol Molecular Function: microtubule binding; protein kinase binding Biological Process: nervous system development; axon guidance; central nervous system development; axon extension; dendrite morphogenesis; neuron migration; central nervous system projection neuron axonogenesis; brain development; response to electrical stimulus Reference #:  O43602 (UniProtKB) Alt. Names/Synonyms: DBCN; DC; DCX; doublecortex; doublecortin; Doublin; Lis-X; Lissencephalin-X; LISX; Neuronal migration protein doublecortin; SCLH; XLIS Gene Symbols: DCX Molecular weight: 49,318 Da Basal Isoelectric point: 9.12  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below doublecortin 1MJD - A=87-192 (human) 2BQQ - A=87-192 (human) 2XRP - I=46-140 (human) 4ATU - I=2-360 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1MJD 2BQQ 2XRP 4ATU  |  Phospho3D  |  DISEASE 300067 300121  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cytoskeletal reorganization: S128‑p, S378‑p molecular association, regulation: S128‑p, S378‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human ► Hide Isoforms
1	1		S109-p	SRMNGLPsPTHSAHC
3	0		S128-p	TRTLQALsNEkkAKK
0	1		K131-a	LQALsNEkkAKKVRF
0	1		K132-a	QALsNEkkAKKVRFY
0	1		Y145-p	FYRNGDRyFKGIVYA
0	1		Y151	RyFKGIVYAVSsDRF
0	1		S155-p	GIVYAVSsDRFRSFD
0	1		S171	LLADLTRSLSDNINL
0	2		S173	ADLTRSLSDNINLPQ
0	2		Y184-p	NLPQGVRyIyTIDGS
0	1		Y186-p	PQGVRyIyTIDGSRK
0	1		S191	yIyTIDGSRKIGSMD
0	1		S246	APQSLASSNSAQARE
0	1		S248	QSLASSNSAQARENK
0	1		T284-p	RVLLNKKtAHsFEQV
0	3		S287-p	LNKKtAHsFEQVLTD
0	1		T303-p	TEAIKLEtGVVKKLY
1	1		S346	RYAQDDFSLDENECR
1	1		S368-p	ATAGPKAsPTPQKTS
1	2		T370	AGPKAsPTPQKTSAK
5	6		S378-p	PQKTSAKsPGPMRRs
0	1		S385-p	sPGPMRRsKSPADsA
1	6		S387	GPMRRsKSPADsANG
0	1		S391-p	RsKSPADsANGTsSs
0	1		S396-p	ADsANGTsSsQLsTP
0	1		S398-p	sANGTsSsQLsTPKs
0	1		S401-p	GTsSsQLsTPKsKQs
2	2		T402	TsSsQLsTPKsKQsP
0	6		S405-p	sQLsTPKsKQsPIsT
4	18		S408-p	sTPKsKQsPIsTPts
0	1		S411-p	KsKQsPIsTPtsPGs
1	3		T412	sKQsPIsTPtsPGsL
0	4		T414-p	QsPIsTPtsPGsLRk
3	20		S415-p	sPIsTPtsPGsLRkH
0	4		S418-p	sTPtsPGsLRkHkDL
0	1		K421-a	tsPGsLRkHkDLYLP
0	1		K423-a	PGsLRkHkDLYLPLS
0	3		S430	kDLYLPLSLDDSDSL
0	2		S434	LPLSLDDSDSLGDSM
0	2		S440	DSDSLGDSM______

	doublecortin iso2
S28	SRMNGLPSPTHSAHC
S47	TRTLQALSNEKKAKK
K50	LQALSNEKKAKKVRF
K51	QALSNEKKAKKVRFY
Y64	FYRNGDRYFKGIVYA
Y70	RYFKGIVYAVSSDRF
S74	GIVYAVSSDRFRSFD
S90	LLADLTRSLSDNINL
S92	ADLTRSLSDNINLPQ
Y103	NLPQGVRYIYTIDGS
Y105	PQGVRYIYTIDGSRK
S110	YIYTIDGSRKIGSMD
S165	APQSLASSNSAQARE
S167	QSLASSNSAQARENK
T203	RVLLNKKTAHSFEQV
S206	LNKKTAHSFEQVLTD
T222	TEAIKLETGVVKKLY
S265	RYAQDDFSLDENECR
S287	ATAGPKASPTPQKTS
T289	AGPKASPTPQKTSAK
S297	PQKTSAKSPGPMRRS
S304	SPGPMRRSKsPADSA
S306-p	GPMRRSKsPADSANG
S310	RSKsPADSANGTSSS
S315	ADSANGTSSSQLStP
S317	SANGTSSSQLStPKS
S320	GTSSSQLStPKSKQs
T321-p	TSSSQLStPKSKQsP
S324	SQLStPKSKQsPISt
S327-p	StPKSKQsPIStPTs
S330	KSKQsPIStPTsPGS
T331-p	SKQsPIStPTsPGSL
T333	QsPIStPTsPGSLRk
S334-p	sPIStPTsPGSLRkH
S337	StPTsPGSLRkHkDL
K340-a	TsPGSLRkHkDLYLP
K342-a	PGSLRkHkDLYLPLS
S349	kDLYLPLSLDDSDSL
S353	LPLSLDDSDSLGDSM
S359	DSDSLGDSM______

	mouse ► Hide Isoforms
S28-p	SRMNGLPsPTHSAHC
S47-p	TRTLQALsNEKKAKK
K50	LQALsNEKKAKKVRF
K51	QALsNEKKAKKVRFY
Y64	FYRNGDRYFKGIVYA
Y70	RYFKGIVYAVSSDRF
S74	GIVYAVSSDRFRSFD
S90	LLADLTRSLsDNINL
S92-p	ADLTRSLsDNINLPQ
Y103	NLPQGVRYIYTIDGS
Y105	PQGVRYIYTIDGSRK
S110	YIYTIDGSRKIGSMD
S165-p	APQSLASsNsAQARE
S167-p	QSLASsNsAQARENK
T203	RVLLNKKTAHsFEQV
S206-p	LNKKTAHsFEQVLTD
T222	TEAIKLETGVVKKLY
S265-p	RYAQDDFsLDENECR
S287-p	AAAGPKAsPtPQKTS
T289-p	AGPKAsPtPQKTSAK
S297-p	PQKTSAKsPGPMRRS
S304	sPGPMRRSKsPADsG
S306-p	GPMRRSKsPADsGND
S310-p	RSKsPADsGNDQDAN
S320	DQDANGTSSsQLStP
S322-p	DANGTSSsQLStPKs
S325	GTSSsQLStPKsKQs
T326-p	TSSsQLStPKsKQsP
S329-p	sQLStPKsKQsPISt
S332-p	StPKsKQsPIStPts
S335	KsKQsPIStPtsPGs
T336-p	sKQsPIStPtsPGsL
T338-p	QsPIStPtsPGsLRK
S339-p	sPIStPtsPGsLRKH
S342-p	StPtsPGsLRKHKVD
K345	tsPGsLRKHKVDLYL
K347	PGsLRKHKVDLYLPL
S355-p	VDLYLPLsLDDsDSL
S359-p	LPLsLDDsDSLGDsM
S365-p	DsDSLGDsM______

	doublecortin iso3
S28	SRMNGLPSPTHSAHC
S47	TRTLQALSNEKKAKK
K50	LQALSNEKKAKKVRF
K51	QALSNEKKAKKVRFY
Y64	FYRNGDRYFKGIVYA
Y70	RYFKGIVYAVSSDRF
S74	GIVYAVSSDRFRSFD
S90	LLADLTRSLSDNINL
S92	ADLTRSLSDNINLPQ
Y103	NLPQGVRYIYTIDGS
Y105	PQGVRYIYTIDGSRK
S110	YIYTIDGSRKIGSMD
S165	APQSLASSNSAQARE
S167	QSLASSNSAQARENK
T203	RVLLNKKTAHSFEQV
S206	LNKKTAHSFEQVLTD
T222	TEAIKLETGVVKKLY
S265	RYAQDDFSLDENECR
S287	AAAGPKASPTPQKTS
T289	AGPKASPTPQKTSAK
S297	PQKTSAKSPGPMRRs
S304-p	SPGPMRRsKsPADSA
S306-p	GPMRRsKsPADSANG
S310	RsKsPADSANGTSSS
S315	ADSANGTSSSQLStP
S317	SANGTSSSQLStPKS
S320	GTSSSQLStPKSKQS
T321-p	TSSSQLStPKSKQSP
S324	SQLStPKSKQSPIST
S327	StPKSKQSPISTPTS
S330	KSKQSPISTPTSPGS
T331	SKQSPISTPTSPGSL
T333	QSPISTPTSPGSLRK
S334	SPISTPTSPGSLRKH
S337	STPTSPGSLRKHKDL
K340	TSPGSLRKHKDLYLP
K342	PGSLRKHKDLYLPLs
S349-p	KDLYLPLsLDDsDSL
S353-p	LPLsLDDsDSLGDsM
S359-p	DsDSLGDsM______

	rat
S28	SRMNGLPSPTHSAHC
S47	TRTLQALSNEKKAKK
K50	LQALSNEKKAKKVRF
K51	QALSNEKKAKKVRFY
Y64	FYRNGDRYFKGIVyA
Y70-p	RYFKGIVyAVSSDRF
S74	GIVyAVSSDRFRSFD
S90-p	LLADLTRsLsDNINL
S92-p	ADLTRsLsDNINLLQ
Y103-p	NLLQGVRyIYTIDGs
Y105	LQGVRyIYTIDGsRK
S110-p	yIYTIDGsRKIGSMD
S165	APQSLASSNSAQARE
S167	QSLASSNSAQARENK
T203	RVLLNKKTAHSFEQV
S206	LNKKTAHSFEQVLTD
T222	TEAIKLETGVVKKLY
S265	RYAQDDFSLDENECR
S287	ATAGPKASPTPQKTS
T289	AGPKASPTPQKTSAK
S297	PQKTSAKSPGPMRRS
S304	SPGPMRRSKSPADSG
S306	GPMRRSKSPADSGND
S310	RSKSPADSGNDQDAN
S320	DQDANGTSSSQLSTP
S322	DANGTSSSQLSTPKS
S325	GTSSSQLSTPKSKQs
T326	TSSSQLSTPKSKQsP
S329	SQLSTPKSKQsPIST
S332-p	STPKSKQsPISTPTs
S335	KSKQsPISTPTsPGS
T336	SKQsPISTPTsPGSL
T338	QsPISTPTsPGSLRK
S339-p	sPISTPTsPGSLRKH
S342	STPTsPGSLRKHKDL
K345	TsPGSLRKHKDLYLP
K347	PGSLRKHKDLYLPLS
S354	KDLYLPLSLDDSDSL
S358	LPLSLDDSDSLGDSM
S364	DSDSLGDSM______

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