DPYL3_HUMAN - dbPTM
DPYL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPYL3_HUMAN
UniProt AC Q14195
Protein Name Dihydropyrimidinase-related protein 3
Gene Name DPYSL3
Organism Homo sapiens (Human).
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 MSYQGKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIVSAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSDYVYKRIKARRKMADLHAVPRGMYDGPVFDLTTTPKGGTPAGSARGSPTRPNPPVRNLHQSGFSLSGTQVDEGVRSASKRIVAPPGGRSNITSLS
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		26.6021406692
3Phosphorylation-----MSYQGKKNIP
-----CCCCCCCCCC		21.7118083107
10 (in isoform 2)Phosphorylation-30.8926657352
11 (in isoform 2)Phosphorylation-40.8130266825
13PhosphorylationKKNIPRITSDRLLIK
CCCCCCCCCCCEEEE		26.3428450419
14PhosphorylationKNIPRITSDRLLIKG
CCCCCCCCCCEEEEC		20.5428450419
19 (in isoform 2)Phosphorylation-4.6327642862
25 (in isoform 2)Phosphorylation-6.5627251275
26 (in isoform 2)Phosphorylation-44.7827251275
30PhosphorylationRIVNDDQSFYADIYM
EECCCCCCCEEEEEE		27.5024076635
32PhosphorylationVNDDQSFYADIYMED
CCCCCCCEEEEEECC		14.4919652227
37SulfoxidationSFYADIYMEDGLIKQ
CCEEEEEECCCCEEE		3.7530846556
48 (in isoform 2)Acetylation-26.84-
49 (in isoform 2)Phosphorylation-5.0627732954
56 (in isoform 2)Phosphorylation-47.2422199227
60 (in isoform 2)Methylation-26.65-
67 (in isoform 2)Phosphorylation-24.4430177828
71 (in isoform 2)Phosphorylation-29.4430177828
73 (in isoform 2)Methylation-15.18-
75 (in isoform 2)Phosphorylation-8.9625850435
77 (in isoform 2)Phosphorylation-25.0825850435
83SulfoxidationFQMPYKGMTTVDDFF
CCCCCCCCCCHHHHH		2.1930846556
85 (in isoform 2)Phosphorylation-17.0330266825
95 (in isoform 2)Phosphorylation-13.9325850435
101PhosphorylationKAALAGGTTMIIDHV
HHHHCCCCEEEEECC		16.57-
102PhosphorylationAALAGGTTMIIDHVV
HHHCCCCEEEEECCC		15.0622798277
102 (in isoform 2)Phosphorylation-15.0630266825
103SulfoxidationALAGGTTMIIDHVVP
HHCCCCEEEEECCCC		2.2530846556
112 (in isoform 2)Phosphorylation-40.4724719451
114 (in isoform 2)Phosphorylation-41.1721406692
146 (in isoform 2)Phosphorylation-50.0127251275
251PhosphorylationSQTNCPLYVTKVMSK
HHCCCCEEEEECCCC		7.3925884760
253PhosphorylationTNCPLYVTKVMSKSA
CCCCEEEEECCCCCH		12.36-
257PhosphorylationLYVTKVMSKSAADLI
EEEEECCCCCHHHHH		26.84-
258SuccinylationYVTKVMSKSAADLIS
EEEECCCCCHHHHHH		26.47-
259PhosphorylationVTKVMSKSAADLISQ
EEECCCCCHHHHHHH		22.7622617229
265PhosphorylationKSAADLISQARKKGN
CCHHHHHHHHHHHCC		25.6923403867
280PhosphorylationVVFGEPITASLGIDG
EEECCCEEEECCCCC		22.4028348404
282PhosphorylationFGEPITASLGIDGTH
ECCCEEEECCCCCCE		20.6227251275
288PhosphorylationASLGIDGTHYWSKNW
EECCCCCCEECCCCH		14.1928348404
292PhosphorylationIDGTHYWSKNWAKAA
CCCCEECCCCHHHHE		14.6728348404
293UbiquitinationDGTHYWSKNWAKAAA
CCCEECCCCHHHHEE		42.22-
303PhosphorylationAKAAAFVTSPPLSPD
HHHEEEECCCCCCCC		29.1220068231
304PhosphorylationKAAAFVTSPPLSPDP
HHEEEECCCCCCCCC		21.1520068231
308PhosphorylationFVTSPPLSPDPTTPD
EECCCCCCCCCCCHH		32.7921406692
316Nitrated tyrosinePDPTTPDYINSLLAS
CCCCCHHHHHHHHHH		11.82-
345UbiquitinationTAQKAIGKDNFTAIP
HHHHHHCCCCCEECC		43.30-
362SulfoxidationTNGVEERMSVIWDKA
CCCHHHHHHHHHHHH		4.1930846556
363PhosphorylationNGVEERMSVIWDKAV
CCHHHHHHHHHHHHH		19.3725332170
373 (in isoform 2)Phosphorylation-17.3524719451
374UbiquitinationDKAVATGKMDENQFV
HHHHHCCCCCCCCEE		38.53-
375SulfoxidationKAVATGKMDENQFVA
HHHHCCCCCCCCEEE		9.1630846556
385PhosphorylationNQFVAVTSTNAAKIF
CCEEEEEECCHHHHC		17.0523911959
396 (in isoform 2)Phosphorylation-34.3727251275
398AcetylationIFNLYPRKGRISVGS
HCCCCCCCCCEECCC		48.3019666971
402PhosphorylationYPRKGRISVGSDSDL
CCCCCCEECCCCCCE		21.0426657352
405PhosphorylationKGRISVGSDSDLVIW
CCCEECCCCCCEEEE		31.6128857561
407PhosphorylationRISVGSDSDLVIWDP
CEECCCCCCEEEECC		34.2428857561
423UbiquitinationAVKIVSAKNHQSAAE
CEEEEECCCCCCHHH		47.67-
431PhosphorylationNHQSAAEYNIFEGME
CCCCHHHCCCCCCCC		14.6122817900
437SulfoxidationEYNIFEGMELRGAPL
HCCCCCCCCCCCCCE		3.2730846556
448S-palmitoylationGAPLVVICQGKIMLE
CCCEEEEECCEEEEE		2.7029575903
462PhosphorylationEDGNLHVTQGAGRFI
ECCCEEEEECCCCCC		15.5521406692
472PhosphorylationAGRFIPCSPFSDYVY
CCCCCCCCCCHHHHH		24.5126657352
475PhosphorylationFIPCSPFSDYVYKRI
CCCCCCCHHHHHHHH		31.2623403867
477PhosphorylationPCSPFSDYVYKRIKA
CCCCCHHHHHHHHHH		12.4123403867
479PhosphorylationSPFSDYVYKRIKARR
CCCHHHHHHHHHHHH		6.5821406692
488SulfoxidationRIKARRKMADLHAVP
HHHHHHHHHCCCCCC		3.1330846556
498SulfoxidationLHAVPRGMYDGPVFD
CCCCCCCCCCCCEEE		2.6630846556
499PhosphorylationHAVPRGMYDGPVFDL
CCCCCCCCCCCEEEE		22.1423403867
507PhosphorylationDGPVFDLTTTPKGGT
CCCEEEEECCCCCCC		30.3929255136
508PhosphorylationGPVFDLTTTPKGGTP
CCEEEEECCCCCCCC		48.6929255136
509PhosphorylationPVFDLTTTPKGGTPA
CEEEEECCCCCCCCC		20.1219664994
511UbiquitinationFDLTTTPKGGTPAGS
EEEECCCCCCCCCCC		68.81-
514PhosphorylationTTTPKGGTPAGSARG
ECCCCCCCCCCCCCC		20.7323401153
518PhosphorylationKGGTPAGSARGSPTR
CCCCCCCCCCCCCCC		19.5223401153
519 (in isoform 2)Phosphorylation-20.9527251275
521 (in isoform 2)Phosphorylation-37.3824719451
522PhosphorylationPAGSARGSPTRPNPP
CCCCCCCCCCCCCCC		19.9729255136
524PhosphorylationGSARGSPTRPNPPVR
CCCCCCCCCCCCCCC		61.5321955146
536PhosphorylationPVRNLHQSGFSLSGT
CCCCCCCCCCCCCCC		30.9326055452
539PhosphorylationNLHQSGFSLSGTQVD
CCCCCCCCCCCCCCC		25.7526846344
541PhosphorylationHQSGFSLSGTQVDEG
CCCCCCCCCCCCCHH		38.3026846344
543PhosphorylationSGFSLSGTQVDEGVR
CCCCCCCCCCCHHHH		23.2623403867
551PhosphorylationQVDEGVRSASKRIVA
CCCHHHHHCCCEEEC		34.1921712546
553PhosphorylationDEGVRSASKRIVAPP
CHHHHHCCCEEECCC		24.5829496963
563Asymmetric dimethylarginineIVAPPGGRSNITSLS
EECCCCCCCCCCCCC		32.23-
564PhosphorylationVAPPGGRSNITSLS-
ECCCCCCCCCCCCC-		35.5424670416
567PhosphorylationPGGRSNITSLS----
CCCCCCCCCCC----		28.0629514088
568PhosphorylationGGRSNITSLS-----
CCCCCCCCCC-----		23.8729514088
570PhosphorylationRSNITSLS-------
CCCCCCCC-------		37.6329514088
586 (in isoform 2)Phosphorylation-24719451
621 (in isoform 2)Phosphorylation-24719451
622 (in isoform 2)Phosphorylation-27251275
623 (in isoform 2)Phosphorylation-27251275
628 (in isoform 2)Phosphorylation-24719451
632 (in isoform 2)Phosphorylation-24719451
636 (in isoform 2)Phosphorylation-24719451
650 (in isoform 2)Phosphorylation-24719451
653 (in isoform 2)Phosphorylation-24719451
655 (in isoform 2)Phosphorylation-24719451
665 (in isoform 2)Phosphorylation-24719451
681 (in isoform 2)Phosphorylation-24719451
684 (in isoform 2)Phosphorylation-24719451
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
509TPhosphorylationKinaseGSK3BP49841
PSP
509TPhosphorylationKinaseGSK-FAMILY-GPS
509TPhosphorylationKinaseGSK3-Uniprot
514TPhosphorylationKinaseGSK3BP49841
PSP
514TPhosphorylationKinaseGSK-FAMILY-GPS
514TPhosphorylationKinaseGSK3-Uniprot
518SPhosphorylationKinaseGSK3BP49841
PSP
518SPhosphorylationKinaseGSK-FAMILY-GPS
518SPhosphorylationKinaseGSK3-Uniprot
522SPhosphorylationKinaseCDK5Q00535
PSP
522SPhosphorylationKinaseDYRK2Q92630
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
509TPhosphorylation

16611631
514TPhosphorylation

16611631
518SPhosphorylation

16611631
522SPhosphorylation

16611631
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBB5_BOVINTUBBphysical
12134159
CUL2_HUMANCUL2physical
22863883
PLAK_HUMANJUPphysical
22863883
F10A1_HUMANST13physical
22863883
DPYL1_HUMANCRMP1physical
28514442
DPYL2_HUMANDPYSL2physical
28514442
DPYL4_HUMANDPYSL4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPYL3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Distinct priming kinases contribute to differential regulation ofcollapsin response mediator proteins by glycogen synthase kinase-3 invivo.";
Cole A.R., Causeret F., Yadirgi G., Hastie C.J., McLauchlan H.,McManus E.J., Hernandez F., Eickholt B.J., Nikolic M., Sutherland C.;
J. Biol. Chem. 281:16591-16598(2006).
Cited for: PHOSPHORYLATION AT SER-522 BY DYRK2, AND PHOSPHORYLATION AT THR-509;THR-514 AND SER-518 BY GSK3.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-551, ANDMASS SPECTROMETRY.

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