DPYL3_MOUSE - dbPTM
DPYL3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPYL3_MOUSE
UniProt AC Q62188
Protein Name Dihydropyrimidinase-related protein 3
Gene Name Dpysl3
Organism Mus musculus (Mouse).
Sequence Length 570
Subcellular Localization Cytoplasm. Cell projection, growth cone. Colocalizes with synaptic vesicle protein 2 in the central region of the growth cone..
Protein Description Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity)..
Protein Sequence MSYQGKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSDYVYKRIKARRKMADLHAVPRGMYDGPVFDLTTTPKGGTPAGSTRGSPTRPNPPVRNLHQSGFSLSGTQVDEGVRSASKRIVAPPGGRSNITSLS
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------MSYQGKKNI
------CCCCCCCCC		26.6029514104
6Ubiquitination--MSYQGKKNIPRIT
--CCCCCCCCCCCCC		27.41-
7Ubiquitination-MSYQGKKNIPRITS
-CCCCCCCCCCCCCC		67.92-
13PhosphorylationKKNIPRITSDRLLIK
CCCCCCCCCCCEEEE		26.3420415495
14PhosphorylationKNIPRITSDRLLIKG
CCCCCCCCCCEEEEC		20.5426824392
30PhosphorylationRIVNDDQSFYADIYM
EECCCCCCCEEEEEE		27.5029899451
32PhosphorylationVNDDQSFYADIYMED
CCCCCCCEEEEEECC		14.4925338131
56UbiquitinationLIVPGGVKTIEANGK
EEECCCCEEEEECCE		47.2422790023
80PhosphorylationHTHFQMPYKGMTTVD
EECCCCCCCCCCCHH		18.1620116462
84PhosphorylationQMPYKGMTTVDDFFQ
CCCCCCCCCHHHHHH		32.1319655815
101PhosphorylationKAALAGGTTMIIDHV
HHHHCCCCEEEEECC		16.57-
102PhosphorylationAALAGGTTMIIDHVV
HHHCCCCEEEEECCC		15.06-
132S-palmitoylationEWADGKSCCDYALHV
HHCCCCCCCCEEEEE		2.0328680068
248S-nitrosylationTVASQTNCPLYVTKV
HHHHHCCCCEEEEEC		2.5222588120
248S-nitrosocysteineTVASQTNCPLYVTKV
HHHHHCCCCEEEEEC		2.52-
258SuccinylationYVTKVMSKSAADLIS
EEEECCCCCHHHHHH		26.47-
259PhosphorylationVTKVMSKSAADLISQ
EEECCCCCHHHHHHH		22.7630372032
290PhosphorylationLGIDGTHYWSKNWAK
CCCCCCEECCCCHHH		15.9422807455
292PhosphorylationIDGTHYWSKNWAKAA
CCCCEECCCCHHHHH		14.6729899451
293UbiquitinationDGTHYWSKNWAKAAA
CCCEECCCCHHHHHH		42.2222790023
304PhosphorylationKAAAFVTSPPLSPDP
HHHHEECCCCCCCCC		21.1525338131
308PhosphorylationFVTSPPLSPDPTTPD
EECCCCCCCCCCCHH		32.7925338131
316Nitrated tyrosinePDPTTPDYINSLLAS
CCCCCHHHHHHHHHH		11.82-
345UbiquitinationTAQKAIGKDNFTAIP
HHHHHHCCCCCEECC		43.3022790023
405PhosphorylationKGRIAVGSDSDLVIW
CCCEEECCCCCEEEE		27.6128066266
407PhosphorylationRIAVGSDSDLVIWDP
CEEECCCCCEEEECH		34.2428066266
423UbiquitinationALKIVSAKNHQSVAE
HEEEEECCCCCCHHE		47.6722790023
427PhosphorylationVSAKNHQSVAEYNIF
EECCCCCCHHEEECC		18.7522807455
431PhosphorylationNHQSVAEYNIFEGME
CCCCHHEEECCCCCC		12.1019060867
471S-nitrosylationGAGRFIPCSPFSDYV
CCCCCCCCCCCHHHH		7.4422588120
472PhosphorylationAGRFIPCSPFSDYVY
CCCCCCCCCCHHHHH		24.5126824392
475PhosphorylationFIPCSPFSDYVYKRI
CCCCCCCHHHHHHHH		31.2628066266
477PhosphorylationPCSPFSDYVYKRIKA
CCCCCHHHHHHHHHH		12.4125777480
479PhosphorylationSPFSDYVYKRIKARR
CCCHHHHHHHHHHHH		6.5825777480
487UbiquitinationKRIKARRKMADLHAV
HHHHHHHHHHCCCCC		32.6522790023
499PhosphorylationHAVPRGMYDGPVFDL
CCCCCCCCCCCEEEE		22.1424925903
507PhosphorylationDGPVFDLTTTPKGGT
CCCEEEEECCCCCCC		30.3925521595
508PhosphorylationGPVFDLTTTPKGGTP
CCEEEEECCCCCCCC		48.6925521595
509PhosphorylationPVFDLTTTPKGGTPA
CEEEEECCCCCCCCC		20.1225521595
511UbiquitinationFDLTTTPKGGTPAGS
EEEECCCCCCCCCCC		68.8122790023
514PhosphorylationTTTPKGGTPAGSTRG
ECCCCCCCCCCCCCC		20.7325521595
518PhosphorylationKGGTPAGSTRGSPTR
CCCCCCCCCCCCCCC		19.6225521595
519PhosphorylationGGTPAGSTRGSPTRP
CCCCCCCCCCCCCCC		37.8224925903
522PhosphorylationPAGSTRGSPTRPNPP
CCCCCCCCCCCCCCC		21.5825521595
524PhosphorylationGSTRGSPTRPNPPVR
CCCCCCCCCCCCCCC		61.5325521595
536PhosphorylationPVRNLHQSGFSLSGT
CCCCCCCCCCCCCCC		30.9325521595
539PhosphorylationNLHQSGFSLSGTQVD
CCCCCCCCCCCCCCC		25.7525521595
541PhosphorylationHQSGFSLSGTQVDEG
CCCCCCCCCCCCCHH		38.3026824392
543PhosphorylationSGFSLSGTQVDEGVR
CCCCCCCCCCCHHHH		23.2626824392
551PhosphorylationQVDEGVRSASKRIVA
CCCHHHHHCCCEEEC		34.1926824392
553PhosphorylationDEGVRSASKRIVAPP
CHHHHHCCCEEECCC		24.5826824392
563Asymmetric dimethylarginineIVAPPGGRSNITSLS
EECCCCCCCCCCCCC		32.23-
564PhosphorylationVAPPGGRSNITSLS-
ECCCCCCCCCCCCC-		35.5422324799
567PhosphorylationPGGRSNITSLS----
CCCCCCCCCCC----		28.0622324799
568PhosphorylationGGRSNITSLS-----
CCCCCCCCCC-----		23.8725521595
570PhosphorylationRSNITSLS-------
CCCCCCCC-------		37.6325521595
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
509TPhosphorylationKinaseGSK3BQ9WV60
PSP
509TPhosphorylationKinaseGSK-FAMILY-GPS
514TPhosphorylationKinaseGSK-FAMILY-GPS
514TPhosphorylationKinaseGSK3-Uniprot
518SPhosphorylationKinaseGSK-FAMILY-GPS
518SPhosphorylationKinaseGSK3-Uniprot
522SPhosphorylationKinaseDYRK2Q5U4C9
Uniprot
522SPhosphorylationKinaseMTORQ9JLN9
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
509TPhosphorylation

21183079
514TPhosphorylation

19131326
518SPhosphorylation

19131326
522SPhosphorylation

19131326
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 DPYL3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DPYL3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPYL3_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 THR-514; SER-518 ANDSER-522, 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-522 AND SER-541, ANDMASS SPECTROMETRY.
"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 THR-509, AND MASSSPECTROMETRY.
"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-499 AND THR-509, 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 THR-509, AND MASSSPECTROMETRY.

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