DCLK1_MOUSE - dbPTM
DCLK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCLK1_MOUSE
UniProt AC Q9JLM8
Protein Name Serine/threonine-protein kinase DCLK1
Gene Name Dclk1
Organism Mus musculus (Mouse).
Sequence Length 756
Subcellular Localization
Protein Description Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system (By similarity)..
Protein Sequence MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGGPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASASRRGTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRISQHGGSSTSLSSTKVCSSMDENDGPGEGDELGRRHSLQRGWRREESEEGFQIPATITERYKVGRTIGDGNFAVVKECIERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTSKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELINMMLLVNVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPSSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSFGRDMEL
------CCCCCCCCC		36.0926824392
22PhosphorylationRDKAQRYSRGSRVNG
HHHHHHHCCCCCCCC		32.1422871156
25PhosphorylationAQRYSRGSRVNGLPS
HHHHCCCCCCCCCCC		31.7626160508
32PhosphorylationSRVNGLPSPTHSAHC
CCCCCCCCCCCCCCC		47.6918388127
34PhosphorylationVNGLPSPTHSAHCSF
CCCCCCCCCCCCCHH		32.5726824392
36PhosphorylationGLPSPTHSAHCSFYR
CCCCCCCCCCCHHHH		23.3718388127
40PhosphorylationPTHSAHCSFYRTRTL
CCCCCCCHHHHHCCH		18.5526160508
42PhosphorylationHSAHCSFYRTRTLQT
CCCCCHHHHHCCHHH		8.5226160508
44PhosphorylationAHCSFYRTRTLQTLS
CCCHHHHHCCHHHHC		19.3429899451
46PhosphorylationCSFYRTRTLQTLSSE
CHHHHHCCHHHHCCC		23.7024899341
49PhosphorylationYRTRTLQTLSSEKKA
HHHCCHHHHCCCCCC		31.5529899451
51PhosphorylationTRTLQTLSSEKKAKK
HCCHHHHCCCCCCCE		39.5827149854
68PhosphorylationFYRNGDRYFKGIVYA
EEECCCCCCEEEEEE		17.87-
74PhosphorylationRYFKGIVYAISPDRF
CCCEEEEEEECHHHH		9.0428066266
77PhosphorylationKGIVYAISPDRFRSF
EEEEEEECHHHHHCH		16.7521082442
118PhosphorylationIDGLKKISSLDQLVE
ECHHHHHCCHHHHHC		33.4622807455
119PhosphorylationDGLKKISSLDQLVEG
CHHHHHCCHHHHHCC		39.1619060867
164PhosphorylationTSASRAVSSLATAKG
CCHHHHHHHHHHCCC		20.7426824392
193PhosphorylationKLVTIIRSGVKPRKA
HHHHHHHCCCCHHHH		37.2127149854
209PhosphorylationRILLNKKTAHSFEQV
HHHCCCCCCCCHHHH		31.0825177544
212PhosphorylationLNKKTAHSFEQVLTD
CCCCCCCCHHHHHHH		28.1919060867
283PhosphorylationCRVVKSTSYTKIASA
CEEEECCCCEEEEEC		37.5927149854
284PhosphorylationRVVKSTSYTKIASAS
EEEECCCCEEEEECC		16.4921454597
295PhosphorylationASASRRGTTKSPGPS
EECCCCCCCCCCCCC		29.2829899451
296PhosphorylationSASRRGTTKSPGPSR
ECCCCCCCCCCCCCC		32.1424453211
298PhosphorylationSRRGTTKSPGPSRRS
CCCCCCCCCCCCCCC		32.7526824392
302PhosphorylationTTKSPGPSRRSKSPA
CCCCCCCCCCCCCCC		46.3623375375
305PhosphorylationSPGPSRRSKSPASTS
CCCCCCCCCCCCCCC		36.0525521595
307PhosphorylationGPSRRSKSPASTSSV
CCCCCCCCCCCCCCC		27.2625521595
310PhosphorylationRRSKSPASTSSVNGT
CCCCCCCCCCCCCCC		32.0021082442
311PhosphorylationRSKSPASTSSVNGTP
CCCCCCCCCCCCCCC		27.4225177544
312PhosphorylationSKSPASTSSVNGTPG
CCCCCCCCCCCCCCC		29.7821082442
313PhosphorylationKSPASTSSVNGTPGS
CCCCCCCCCCCCCCC		21.4925177544
317PhosphorylationSTSSVNGTPGSQLST
CCCCCCCCCCCCCCC		21.1925619855
320PhosphorylationSVNGTPGSQLSTPRS
CCCCCCCCCCCCCCC		29.2025619855
323PhosphorylationGTPGSQLSTPRSGKS
CCCCCCCCCCCCCCC		28.8225619855
324PhosphorylationTPGSQLSTPRSGKSP
CCCCCCCCCCCCCCC		31.1725619855
327PhosphorylationSQLSTPRSGKSPSPS
CCCCCCCCCCCCCCC		52.3421082442
330PhosphorylationSTPRSGKSPSPSPTS
CCCCCCCCCCCCCCC		33.8525521595
332 (in isoform 2)Phosphorylation-45.1328285833
332PhosphorylationPRSGKSPSPSPTSPG
CCCCCCCCCCCCCCC		45.1325521595
334PhosphorylationSGKSPSPSPTSPGSL
CCCCCCCCCCCCCCC		45.1825521595
336 (in isoform 2)Phosphorylation-52.4725521595
336PhosphorylationKSPSPSPTSPGSLRK
CCCCCCCCCCCCCCH		52.4718388127
337 (in isoform 2)Phosphorylation-30.5525521595
337PhosphorylationSPSPSPTSPGSLRKQ
CCCCCCCCCCCCCHH		30.5525521595
340 (in isoform 2)Phosphorylation-28.5229899451
340PhosphorylationPSPTSPGSLRKQRIS
CCCCCCCCCCHHHHH		28.5225521595
347PhosphorylationSLRKQRISQHGGSST
CCCHHHHHHCCCCCC		20.5021082442
348 (in isoform 2)Phosphorylation-36.5527180971
352PhosphorylationRISQHGGSSTSLSST
HHHHCCCCCCCCCCC		34.7318388127
352 (in isoform 2)Phosphorylation-34.7325177544
353 (in isoform 2)Phosphorylation-25.8725177544
353PhosphorylationISQHGGSSTSLSSTK
HHHCCCCCCCCCCCC		25.8725177544
354PhosphorylationSQHGGSSTSLSSTKV
HHCCCCCCCCCCCCE		35.0725177544
355PhosphorylationQHGGSSTSLSSTKVC
HCCCCCCCCCCCCEE		28.3518388127
357PhosphorylationGGSSTSLSSTKVCSS
CCCCCCCCCCCEECC		35.4121082442
358PhosphorylationGSSTSLSSTKVCSSM
CCCCCCCCCCEECCC		37.2226824392
358 (in isoform 2)Phosphorylation-37.2227149854
359PhosphorylationSSTSLSSTKVCSSMD
CCCCCCCCCEECCCC		24.9129233185
362 (in isoform 2)Phosphorylation-2.3826824392
363PhosphorylationLSSTKVCSSMDENDG
CCCCCEECCCCCCCC		31.5222324799
364PhosphorylationSSTKVCSSMDENDGP
CCCCEECCCCCCCCC		25.7325521595
382PhosphorylationDELGRRHSLQRGWRR
CHHHHHHHHHCCCCH		25.1222324799
392PhosphorylationRGWRREESEEGFQIP
CCCCHHHCCCCCCCC		35.8725521595
421UbiquitinationDGNFAVVKECIERST
CCCCHHHHHHHHHHH		40.02-
498UbiquitinationDAITSTSKYTERDAS
HHHCCCCCCCCCCHH		57.17-
509PhosphorylationRDASGMLYNLASAIK
CCHHHHHHHHHHHHH		10.1522817900
529UbiquitinationNIVHRDIKPENLLVY
CCCCCCCCHHHEEEE		51.04-
536PhosphorylationKPENLLVYEHQDGSK
CHHHEEEEEECCCCC		13.9922817900
703PhosphorylationAGVSVIATTALDKER
HCCEEEEECCCHHHH		11.0722807455
736PhosphorylationPAPPELNSESEDYSP
CCCCCCCCCCCCCCC		55.9418388127
738PhosphorylationPPELNSESEDYSPSS
CCCCCCCCCCCCCCC		35.2725521595
741PhosphorylationLNSESEDYSPSSSET
CCCCCCCCCCCCCCC		20.5923527152
742PhosphorylationNSESEDYSPSSSETV
CCCCCCCCCCCCCCC		30.5425521595
744PhosphorylationESEDYSPSSSETVRS
CCCCCCCCCCCCCCC		40.3225521595
745PhosphorylationSEDYSPSSSETVRSP
CCCCCCCCCCCCCCC		35.2621183079
746PhosphorylationEDYSPSSSETVRSPN
CCCCCCCCCCCCCCC		41.4422807455
748PhosphorylationYSPSSSETVRSPNSP
CCCCCCCCCCCCCCC		24.1422817900
751PhosphorylationSSSETVRSPNSPF--
CCCCCCCCCCCCC--		24.8919060867
754PhosphorylationETVRSPNSPF-----
CCCCCCCCCC-----		30.9425521595
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
382SPhosphorylationKinaseDCLK1Q9JLM8
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCLK1_MOUSE !!
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 DCLK1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCLK1_MOUSEDclk1physical
16387639
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCLK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-332 ANDSER-337, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-36, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-332 ANDTHR-336, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-392, ANDMASS SPECTROMETRY.
"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-305; SER-307; SER-738AND SER-742, AND MASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-509 AND TYR-536, ANDMASS SPECTROMETRY.

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