DPYL2_RAT - dbPTM
DPYL2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPYL2_RAT
UniProt AC P47942
Protein Name Dihydropyrimidinase-related protein 2
Gene Name Dpysl2
Organism Rattus norvegicus (Rat).
Sequence Length 572
Subcellular Localization Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane. Tightly but noncovalently associated with membranes.
Protein Description Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis (By similarity)..
Protein Sequence MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG
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
6Acetylation--MSYQGKKNIPRIT
--CCCCCCCCCCCCC		27.4122902405
13PhosphorylationKKNIPRITSDRLLIK
CCCCCCCCCCCEEEE		26.3422673903
14PhosphorylationKNIPRITSDRLLIKG
CCCCCCCCCCEEEEC		20.5422673903
20AcetylationTSDRLLIKGGKIVND
CCCCEEEECCEECCC		62.6722902405
20UbiquitinationTSDRLLIKGGKIVND
CCCCEEEECCEECCC		62.67-
32PhosphorylationVNDDQSFYADIYMED
CCCCCCCHHEEEECC		14.4919652227
56AcetylationLIVPGGVKTIEAHSR
EEECCCCCEEEECCC		47.2422902405
56UbiquitinationLIVPGGVKTIEAHSR
EEECCCCCEEEECCC		47.24-
57PhosphorylationIVPGGVKTIEAHSRM
EECCCCCEEEECCCE		22.9528551015
62PhosphorylationVKTIEAHSRMVIPGG
CCEEEECCCEEECCC		29.1728551015
101PhosphorylationKAALAGGTTMIIDHV
HHHHCCCCEEEEEEE		16.57-
102PhosphorylationAALAGGTTMIIDHVV
HHHCCCCEEEEEEEC		15.06-
241PhosphorylationEAVNRSITIANQTNC
HHHCCCEEEECCCCC		18.4525575281
246PhosphorylationSITIANQTNCPLYVT
CEEEECCCCCCEEEE		38.3025575281
248S-nitrosylationTIANQTNCPLYVTKV
EEECCCCCCEEEEEE		2.5222178444
248S-nitrosocysteineTIANQTNCPLYVTKV
EEECCCCCCEEEEEE		2.52-
251PhosphorylationNQTNCPLYVTKVMSK
CCCCCCEEEEEECCC		7.3925575281
253PhosphorylationTNCPLYVTKVMSKSA
CCCCEEEEEECCCCH		12.3625575281
257PhosphorylationLYVTKVMSKSAAEVI
EEEEEECCCCHHHHH		26.8425575281
258SuccinylationYVTKVMSKSAAEVIA
EEEEECCCCHHHHHH		26.47-
258SuccinylationYVTKVMSKSAAEVIA
EEEEECCCCHHHHHH		26.47-
259PhosphorylationVTKVMSKSAAEVIAQ
EEEECCCCHHHHHHH		25.9622673903
272PhosphorylationAQARKKGTVVYGEPI
HHHHHCCEEEECCCE		18.7128689409
290PhosphorylationLGTDGSHYWSKNWAK
ECCCCCCCCCCCHHH		17.0528689409
292PhosphorylationTDGSHYWSKNWAKAA
CCCCCCCCCCHHHHE		14.6728689409
345UbiquitinationTAQKAVGKDNFTLIP
CHHHHHCCCCEEEEC		42.79-
345AcetylationTAQKAVGKDNFTLIP
CHHHHHCCCCEEEEC		42.7922902405
368UbiquitinationRMSVIWDKAVVTGKM
HEEEEEEEEEEECCC		28.25-
374AcetylationDKAVVTGKMDENQFV
EEEEEECCCCCCCEE		33.5422902405
384PhosphorylationENQFVAVTSTNAAKV
CCCEEEEEECCHHHH		21.7925403869
385PhosphorylationNQFVAVTSTNAAKVF
CCEEEEEECCHHHHC		17.0525403869
386PhosphorylationQFVAVTSTNAAKVFN
CEEEEEECCHHHHCC		21.3625403869
402PhosphorylationYPRKGRISVGSDADL
CCCCCCEECCCCCCE		21.0427097102
405PhosphorylationKGRISVGSDADLVIW
CCCEECCCCCCEEEE		27.7227097102
418AcetylationIWDPDSVKTISAKTH
EECCCCCEEEECCCC		44.0622902405
431PhosphorylationTHNSALEYNIFEGME
CCCCCCCEECCCCCC		17.89-
442PhosphorylationEGMECRGSPLVVISQ
CCCCCCCCCEEEEEC		8.8425403869
462PhosphorylationEDGTLHVTEGSGRYI
CCCCEEEEECCCCCC		24.7125403869
465PhosphorylationTLHVTEGSGRYIPRK
CEEEEECCCCCCCCC		17.5425403869
472UbiquitinationSGRYIPRKPFPDFVY
CCCCCCCCCCCCHHH		45.73-
472AcetylationSGRYIPRKPFPDFVY
CCCCCCCCCCCCHHH		45.7322902405
479PhosphorylationKPFPDFVYKRIKARS
CCCCCHHHHHHHHHH		8.44-
480AcetylationPFPDFVYKRIKARSR
CCCCHHHHHHHHHHH		42.2022902405
499PhosphorylationRGVPRGLYDGPVCEV
HCCCCCCCCCCEEEE		22.9822276854
504S-nitrosylationGLYDGPVCEVSVTPK
CCCCCCEEEEEEECC		4.8716418269
504S-nitrosocysteineGLYDGPVCEVSVTPK
CCCCCCEEEEEEECC		4.87-
507PhosphorylationDGPVCEVSVTPKTVT
CCCEEEEEEECCCCC		9.6627097102
509PhosphorylationPVCEVSVTPKTVTPA
CEEEEEEECCCCCCC		16.1515466863
512PhosphorylationEVSVTPKTVTPASSA
EEEEECCCCCCCCCC		30.7130411139
514PhosphorylationSVTPKTVTPASSAKT
EEECCCCCCCCCCCC		20.5415466863
517PhosphorylationPKTVTPASSAKTSPA
CCCCCCCCCCCCCCH		31.8430411139
518PhosphorylationKTVTPASSAKTSPAK
CCCCCCCCCCCCCHH		35.5715466863
520UbiquitinationVTPASSAKTSPAKQQ
CCCCCCCCCCCHHHC		52.03-
521PhosphorylationTPASSAKTSPAKQQA
CCCCCCCCCCHHHCC		39.3930411139
522PhosphorylationPASSAKTSPAKQQAP
CCCCCCCCCHHHCCC		23.3515466863
525UbiquitinationSAKTSPAKQQAPPVR
CCCCCCHHHCCCCCC		46.45-
537PhosphorylationPVRNLHQSGFSLSGA
CCCCCCCCCCCCCCC		30.9330411139
540PhosphorylationNLHQSGFSLSGAQID
CCCCCCCCCCCCCCC		25.7530411139
542PhosphorylationHQSGFSLSGAQIDDN
CCCCCCCCCCCCCCC		30.7730411139
555PhosphorylationDNIPRRTTQRIVAPP
CCCCCCCCCEEECCC		17.6522817900
565MethylationIVAPPGGRANITSLG
EECCCCCCCCCCCCC		30.31-
565Asymmetric dimethylarginineIVAPPGGRANITSLG
EECCCCCCCCCCCCC		30.31-
569PhosphorylationPGGRANITSLG----
CCCCCCCCCCC----		20.0828551015
570PhosphorylationGGRANITSLG-----
CCCCCCCCCC-----		27.5728551015
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
32YPhosphorylationKinaseFESP07332
PSP
32YPhosphorylationKinaseFYNP06241
PSP
32YPhosphorylationKinaseFYNQ62844
Uniprot
509TPhosphorylationKinaseGSK3AP49840
PSP
509TPhosphorylationKinaseGSK3AP18265
PSP
509TPhosphorylationKinaseGSK3BP49841
PSP
514TPhosphorylationKinaseGSK3AP49840
PSP
514TPhosphorylationKinaseGSK3AP18265
PSP
514TPhosphorylationKinaseGSK3BP49841
PSP
518SPhosphorylationKinaseGSK3AP49840
PSP
518SPhosphorylationKinaseGSK3BP49841
PSP
522SPhosphorylationKinaseCDK5Q00535
PSP
522SPhosphorylationKinaseGSK3AP49840
PSP
522SPhosphorylationKinaseDYRK2-Uniprot
555TPhosphorylationKinaseROCK2O75116
PSP
555TPhosphorylationKinaseROCK2Q62868
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
514TPhosphorylation

22673903
522SPhosphorylation

10757975
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 DPYL2_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPYL2_RATDpysl2physical
12134159
TBA1A_RATTuba1aphysical
12134159
TBB3_RATTubb3physical
12134159
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPYL2_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Neurofibrillary tangle-associated collapsin response mediatorprotein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, andSer-522.";
Gu Y., Hamajima N., Ihara Y.;
Biochemistry 39:4267-4275(2000).
Cited for: PHOSPHORYLATION AT THR-509; SER-518 AND SER-522, AND MASSSPECTROMETRY.
S-nitrosylation
ReferencePubMed
"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures.";
Hao G., Derakhshan B., Shi L., Campagne F., Gross S.S.;
Proc. Natl. Acad. Sci. U.S.A. 103:1012-1017(2006).
Cited for: PROTEIN SEQUENCE OF 497-511, S-NITROSYLATION [LARGE SCALE ANALYSIS] ATCYS-504, AND MASS SPECTROMETRY.

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