dbPTM

DCX_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DCX_MOUSE
UniProt AC	O88809
Protein Name	Neuronal migration protein doublecortin
Gene Name	Dcx
Organism	Mus musculus (Mouse).
Sequence Length	366
Subcellular Localization	Cytoplasm . Cell projection . Localizes at neurite tips.
Protein Description	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..
Protein Sequence	MELDFGHFDERDKASRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSAAAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTSSSQLSTPKSKQSPISTPTSPGSLRKHKVDLYLPLSLDDSDSLGDSM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Phosphorylation	SRMNGLPSPTHSAHC CCCCCCCCCCHHHCC	47.69	22817900
30	Phosphorylation	MNGLPSPTHSAHCSF CCCCCCCCHHHCCHH	32.57	24759943
32	Phosphorylation	GLPSPTHSAHCSFYR CCCCCCHHHCCHHHH	23.37	22817900
36	Phosphorylation	PTHSAHCSFYRTRTL CCHHHCCHHHHHHHH	18.55	25177544
42	Phosphorylation	CSFYRTRTLQALSNE CHHHHHHHHHHHCCC	23.70	-
47	Phosphorylation	TRTLQALSNEKKAKK HHHHHHHCCCCHHCE	46.06	22367209
64	Phosphorylation	FYRNGDRYFKGIVYA EEECCCCCCEEEEEE	17.87	-
70	Phosphorylation	RYFKGIVYAVSSDRF CCCEEEEEEECCCHH	10.20	-
74	Phosphorylation	GIVYAVSSDRFRSFD EEEEEECCCHHHCHH	26.63	-
90	Phosphorylation	LLADLTRSLSDNINL HHHHHHHHHHCCCCC	27.30	-
92	Phosphorylation	ADLTRSLSDNINLPQ HHHHHHHHCCCCCCC	29.83	-
110	Phosphorylation	YIYTIDGSRKIGSMD EEEEEECCCEECCCC	27.01	-
115	Phosphorylation	DGSRKIGSMDELEEG ECCCEECCCCHHHCC	26.91	-
165	Phosphorylation	APQSLASSNSAQARE CCHHHHCCCHHHHHH	29.24	20139300
167	Phosphorylation	QSLASSNSAQARENK HHHHCCCHHHHHHCC	24.57	20139300
187	Phosphorylation	KLVTIIRSGVKPRKA HHHHHHHCCCCCHHH	37.21	27149854
203	Phosphorylation	RVLLNKKTAHSFEQV HHHCCCCCCCCHHHH	31.08	22807455
206	Phosphorylation	LNKKTAHSFEQVLTD CCCCCCCCHHHHHHH	28.19	22817900
265	Phosphorylation	RYAQDDFSLDENECR CCCCCCCCCCCCCCE	41.74	22807455
287	Phosphorylation	AAAGPKASPTPQKTS CCCCCCCCCCCCCCC	35.12	30372032
289	Phosphorylation	AGPKASPTPQKTSAK CCCCCCCCCCCCCCC	35.54	30372032
294	Phosphorylation	SPTPQKTSAKSPGPM CCCCCCCCCCCCCCC	40.51	-
297	Phosphorylation	PQKTSAKSPGPMRRS CCCCCCCCCCCCCCC	34.50	17482550
304	Phosphorylation	SPGPMRRSKSPADSG CCCCCCCCCCCCCCC	27.41	15345747
306	Phosphorylation	GPMRRSKSPADSGND CCCCCCCCCCCCCCC	26.94	23527152
310	Phosphorylation	RSKSPADSGNDQDAN CCCCCCCCCCCCCCC	41.42	30372032
322	Phosphorylation	DANGTSSSQLSTPKS CCCCCCHHHCCCCCC	34.60	15345747
326	Phosphorylation	TSSSQLSTPKSKQSP CCHHHCCCCCCCCCC	43.24	15345747
329	Phosphorylation	SQLSTPKSKQSPIST HHCCCCCCCCCCCCC	36.81	30372032
332	Phosphorylation	STPKSKQSPISTPTS CCCCCCCCCCCCCCC	28.12	20715151
335	Phosphorylation	KSKQSPISTPTSPGS CCCCCCCCCCCCCCC	31.55	30372032
336	Phosphorylation	SKQSPISTPTSPGSL CCCCCCCCCCCCCCC	31.16	30372032
338	Phosphorylation	QSPISTPTSPGSLRK CCCCCCCCCCCCCCC	47.87	23527152
339	Phosphorylation	SPISTPTSPGSLRKH CCCCCCCCCCCCCCC	28.59	23527152
342	Phosphorylation	STPTSPGSLRKHKVD CCCCCCCCCCCCCCE	28.52	30372032
355	Phosphorylation	VDLYLPLSLDDSDSL CEEEEECCCCCCCCC	28.01	19060867
359	Phosphorylation	LPLSLDDSDSLGDSM EECCCCCCCCCCCCC	28.85	29899451
361	Phosphorylation	LSLDDSDSLGDSM-- CCCCCCCCCCCCC--	37.90	29899451
365	Phosphorylation	DSDSLGDSM------ CCCCCCCCC------	25.29	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
28	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
47	S	Phosphorylation	Kinase	PKA	-	Uniprot
47	S	Phosphorylation	Kinase	MARK_GROUP	-	PhosphoELM
47	S	Phosphorylation	Kinase	MARK-SUBFAMILY	-	GPS
47	S	Phosphorylation	Kinase	MARK1	Q8VHJ5	Uniprot
47	S	Phosphorylation	Kinase	MARK1	Q9P0L2	PSP
47	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
70	Y	Phosphorylation	Kinase	ABL	P00520	Uniprot
74	S	Phosphorylation	Kinase	PKC	-	Uniprot
90	S	Phosphorylation	Kinase	CK2	-	Uniprot
110	S	Phosphorylation	Kinase	PKC	-	Uniprot
115	S	Phosphorylation	Kinase	PKA	-	Uniprot
115	S	Phosphorylation	Kinase	CK2	-	Uniprot
115	S	Phosphorylation	Kinase	MARK1	Q8VHJ5	Uniprot
125	Y	Phosphorylation	Kinase	ABL	P00520	PSP
265	S	Phosphorylation	Kinase	CK2	-	Uniprot
287	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
289	T	Phosphorylation	Kinase	CDK5	P49615	Uniprot
294	S	Phosphorylation	Kinase	PKC	-	Uniprot
297	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
326	T	Phosphorylation	Kinase	MAPK	-	Uniprot
326	T	Phosphorylation	Kinase	CDK5	P49615	PSP
326	T	Phosphorylation	Kinase	PKC	-	Uniprot
332	S	Phosphorylation	Kinase	CDK5	P49615	PSP
332	S	Phosphorylation	Kinase	MAPK	-	Uniprot
332	S	Phosphorylation	Kinase	JNK1	P45983	PSP
332	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
336	T	Phosphorylation	Kinase	MAPK	-	Uniprot
339	S	Phosphorylation	Kinase	CDK5	P49615	PSP
339	S	Phosphorylation	Kinase	MAPK	-	Uniprot
342	S	Phosphorylation	Kinase	PKC	-	Uniprot
355	S	Phosphorylation	Kinase	CK2	-	Uniprot
361	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
265	S	Phosphorylation	22807455
Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21.
297	S	Phosphorylation	15099191
Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DCX_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
USP9X_MOUSE	Usp9x	physical	15607950
CTNB1_MOUSE	Ctnnb1	physical	15607950
NEB2_MOUSE	Ppp1r9b	physical	14550532
DCLK1_MOUSE	Dclk1	physical	16387639

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DCX_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-322, ANDMASS SPECTROMETRY.	15345747 [Abstract]

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