dbPTM

DPYL2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPYL2_MOUSE
UniProt AC	O08553
Protein Name	Dihydropyrimidinase-related protein 2
Gene Name	Dpysl2
Organism	Mus musculus (Mouse).
Sequence Length	572
Subcellular Localization	Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane. Tightly but non-covalently 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..
Protein Sequence	MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYQGKKNI ------CCCCCCCCC	26.60	29514104
6	Ubiquitination	--MSYQGKKNIPRIT --CCCCCCCCCCCCC	27.41	22790023
7	Ubiquitination	-MSYQGKKNIPRITS -CCCCCCCCCCCCCC	67.92	22790023
13	Phosphorylation	KKNIPRITSDRLLIK CCCCCCCCCCCEEEE	26.34	25521595
14	Phosphorylation	KNIPRITSDRLLIKG CCCCCCCCCCEEEEC	20.54	25266776
20	Ubiquitination	TSDRLLIKGGKIVND CCCCEEEECCEECCC	62.67	22790023
30	Phosphorylation	KIVNDDQSFYADIYM EECCCCCCCHHEEEE	27.50	29899451
32	Phosphorylation	VNDDQSFYADIYMED CCCCCCCHHEEEECC	14.49	15345747
56	Acetylation	LIVPGGVKTIEAHSR EEECCCCCEEEECCC	47.24	22826441
56	Ubiquitination	LIVPGGVKTIEAHSR EEECCCCCEEEECCC	47.24	22790023
57	Phosphorylation	IVPGGVKTIEAHSRM EECCCCCEEEECCCE	22.95	29899451
101	Phosphorylation	KAALAGGTTMIIDHV HHHHCCCCEEEEEEE	16.57	-
102	Phosphorylation	AALAGGTTMIIDHVV HHHCCCCEEEEEEEC	15.06	-
146	Ubiquitination	VDITEWHKGIQEEME EEHHHHHHHHHHHHH	59.80	-
157	Ubiquitination	EEMEALVKDHGVNSF HHHHHHHHHHCCCEE	44.87	27667366
177	Phosphorylation	FKDRFQLTDSQIYEV HCCCCCCCHHHHHHH	23.87	22817900
179	Phosphorylation	DRFQLTDSQIYEVLS CCCCCCHHHHHHHHH	17.16	20415495
182	Nitration	QLTDSQIYEVLSVIR CCCHHHHHHHHHHHH	7.73	-
182	Phosphorylation	QLTDSQIYEVLSVIR CCCHHHHHHHHHHHH	7.73	20415495
186	Phosphorylation	SQIYEVLSVIRDIGA HHHHHHHHHHHHHHH	22.22	20415495
248	S-nitrosocysteine	TIANQTNCPLYVTKV EEECCCCCCEEEEEE	2.52	-
248	S-nitrosylation	TIANQTNCPLYVTKV EEECCCCCCEEEEEE	2.52	24895380
258	Succinylation	YVTKVMSKSAAEVIA EEEEECCCCHHHHHH	26.47	23806337
258	Acetylation	YVTKVMSKSAAEVIA EEEEECCCCHHHHHH	26.47	23806337
258	Succinylation	YVTKVMSKSAAEVIA EEEEECCCCHHHHHH	26.47	-
259	Phosphorylation	VTKVMSKSAAEVIAQ EEEECCCCHHHHHHH	25.96	27708245
270	Ubiquitination	VIAQARKKGTVVYGE HHHHHHHCCEEEECC	55.02	27667366
282	Phosphorylation	YGEPITASLGTDGSH ECCCEEEEECCCCCC	20.77	25338131
288	Phosphorylation	ASLGTDGSHYWSKNW EEECCCCCCCCCCCH	19.06	29899451
290	Phosphorylation	LGTDGSHYWSKNWAK ECCCCCCCCCCCHHH	17.05	21082442
292	Phosphorylation	TDGSHYWSKNWAKAA CCCCCCCCCCHHHHE	14.67	25521595
293	Ubiquitination	DGSHYWSKNWAKAAA CCCCCCCCCHHHHEE	42.22	22790023
293	Acetylation	DGSHYWSKNWAKAAA CCCCCCCCCHHHHEE	42.22	23236377
297	Ubiquitination	YWSKNWAKAAAFVTS CCCCCHHHHEEEECC	30.12	-
304	Phosphorylation	KAAAFVTSPPLSPDP HHEEEECCCCCCCCC	21.15	25338131
308	Phosphorylation	FVTSPPLSPDPTTPD EECCCCCCCCCCCHH	32.79	25338131
345	Ubiquitination	TAQKAVGKDNFTLIP CHHHHHCCCCEEEEC	42.79	22790023
368	Acetylation	RMSVIWDKAVVTGKM HEEEEEEEEEEECCC	28.25	22826441
368	Ubiquitination	RMSVIWDKAVVTGKM HEEEEEEEEEEECCC	28.25	22790023
371	Ubiquitination	VIWDKAVVTGKMDEN EEEEEEEEECCCCCC	7.54	27667366
374	Sumoylation	DKAVVTGKMDENQFV EEEEEECCCCCCCEE	33.54	-
374	Ubiquitination	DKAVVTGKMDENQFV EEEEEECCCCCCCEE	33.54	22790023
394	Ubiquitination	NAAKVFNLYPRKGRI CHHHHCCCCCCCCCE	4.18	27667366
402	Phosphorylation	YPRKGRISVGSDADL CCCCCCEECCCCCCE	21.04	25521595
405	Phosphorylation	KGRISVGSDADLVIW CCCEECCCCCCEEEE	27.72	22817900
423	Ubiquitination	SVKTISAKTHNSALE CCEEEECCCCCCCCC	43.45	22790023
423	Acetylation	SVKTISAKTHNSALE CCEEEECCCCCCCCC	43.45	22826441
427	Phosphorylation	ISAKTHNSALEYNIF EECCCCCCCCCEECC	26.99	21082442
431	Nitration	THNSALEYNIFEGME CCCCCCCEECCCCCC	17.89	-
431	Phosphorylation	THNSALEYNIFEGME CCCCCCCEECCCCCC	17.89	21082442
439	S-nitrosylation	NIFEGMECRGSPLVV ECCCCCCCCCCCEEE	4.42	24895380
439	S-nitrosocysteine	NIFEGMECRGSPLVV ECCCCCCCCCCCEEE	4.42	-
442	Phosphorylation	EGMECRGSPLVVISQ CCCCCCCCCEEEEEC	8.84	25521595
446	Ubiquitination	CRGSPLVVISQGKIV CCCCCEEEEECCEEE	4.61	27667366
448	Phosphorylation	GSPLVVISQGKIVLE CCCEEEEECCEEEEC	22.67	28059163
458	Phosphorylation	KIVLEDGTLHVTEGS EEEECCCCEEEEECC	26.47	-
462	Phosphorylation	EDGTLHVTEGSGRYI CCCCEEEEECCCCCC	24.71	-
465	Phosphorylation	TLHVTEGSGRYIPRK CEEEEECCCCCCCCC	17.54	22817900
469	Ubiquitination	TEGSGRYIPRKPFPD EECCCCCCCCCCCCC	2.28	27667366
472	Acetylation	SGRYIPRKPFPDFVY CCCCCCCCCCCCHHH	45.73	22826441
472	Ubiquitination	SGRYIPRKPFPDFVY CCCCCCCCCCCCHHH	45.73	22790023
480	Acetylation	PFPDFVYKRIKARSR CCCCHHHHHHHHHHH	42.20	19860939
480	Ubiquitination	PFPDFVYKRIKARSR CCCCHHHHHHHHHHH	42.20	22790023
499	Phosphorylation	RGVPRGLYDGPVCEV HCCCCCCCCCCEEEE	22.98	24925903
504	S-nitrosocysteine	GLYDGPVCEVSVTPK CCCCCCEEEEEEECC	4.87	-
504	S-nitrosylation	GLYDGPVCEVSVTPK CCCCCCEEEEEEECC	4.87	24895380
504	Glutathionylation	GLYDGPVCEVSVTPK CCCCCCEEEEEEECC	4.87	24333276
507	Phosphorylation	DGPVCEVSVTPKTVT CCCEEEEEEECCCCC	9.66	18388127
507	O-linked_Glycosylation	DGPVCEVSVTPKTVT CCCEEEEEEECCCCC	9.66	28528544
509	Phosphorylation	PVCEVSVTPKTVTPA CEEEEEEECCCCCCC	16.15	18388127
511	Ubiquitination	CEVSVTPKTVTPASS EEEEEECCCCCCCCC	46.38	22790023
512	Phosphorylation	EVSVTPKTVTPASSA EEEEECCCCCCCCCC	30.71	25521595
514	Phosphorylation	SVTPKTVTPASSAKT EEECCCCCCCCCCCC	20.54	18388127
517	Phosphorylation	PKTVTPASSAKTSPA CCCCCCCCCCCCCCH	31.84	25521595
517	O-linked_Glycosylation	PKTVTPASSAKTSPA CCCCCCCCCCCCCCH	31.84	28528544
518	Phosphorylation	KTVTPASSAKTSPAK CCCCCCCCCCCCCHH	35.57	25521595
520	Acetylation	VTPASSAKTSPAKQQ CCCCCCCCCCCHHHC	52.03	23806337
520	Ubiquitination	VTPASSAKTSPAKQQ CCCCCCCCCCCHHHC	52.03	27667366
520	Succinylation	VTPASSAKTSPAKQQ CCCCCCCCCCCHHHC	52.03	23806337
521	Phosphorylation	TPASSAKTSPAKQQA CCCCCCCCCCHHHCC	39.39	25521595
522	Phosphorylation	PASSAKTSPAKQQAP CCCCCCCCCHHHCCC	23.35	18388127
525	Acetylation	SAKTSPAKQQAPPVR CCCCCCHHHCCCCCC	46.45	23806337
525	Succinylation	SAKTSPAKQQAPPVR CCCCCCHHHCCCCCC	46.45	23806337
525	Ubiquitination	SAKTSPAKQQAPPVR CCCCCCHHHCCCCCC	46.45	27667366
537	Phosphorylation	PVRNLHQSGFSLSGA CCCCCCCCCCCCCCC	30.93	25521595
540	Phosphorylation	NLHQSGFSLSGAQID CCCCCCCCCCCCCCC	25.75	25521595
542	Phosphorylation	HQSGFSLSGAQIDDN CCCCCCCCCCCCCCC	30.77	25521595
554	Phosphorylation	DDNIPRRTTQRIVAP CCCCCCCCCCEEECC	28.67	29899451
555	Phosphorylation	DNIPRRTTQRIVAPP CCCCCCCCCEEECCC	17.65	19735446
565	Methylation	IVAPPGGRANITSLG EECCCCCCCCCCCCC	30.31	24129315
565	Asymmetric dimethylarginine	IVAPPGGRANITSLG EECCCCCCCCCCCCC	30.31	-
569	Phosphorylation	PGGRANITSLG---- CCCCCCCCCCC----	20.08	27087446
570	Phosphorylation	GGRANITSLG----- CCCCCCCCCC-----	27.57	25521595
573	Ubiquitination	ANITSLG-------- CCCCCCC--------		27667366
621	Ubiquitination	-------------------------------------------------------- --------------------------------------------------------		27667366
626	Ubiquitination	------------------------------------------------------------- -------------------------------------------------------------		27667366

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
32	Y	Phosphorylation	Kinase	FYN	P39688	Uniprot
509	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
514	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
514	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
555	T	Phosphorylation	Kinase	PRKACA	P05132	GPS
555	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
555	T	Phosphorylation	Kinase	ROCK2	P70336	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
514	T	Phosphorylation	19131326
Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration.
522	S	Phosphorylation	19131326
Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B (By similarity).

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DPYL2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of DPYL2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-517; SER-518AND SER-522, AND MASS SPECTROMETRY.	19131326 [Abstract]
"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-542, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND MASSSPECTROMETRY.	15648052 [Abstract]
"ZNRF1 promotes Wallerian degeneration by degrading AKT to induceGSK3B-dependent CRMP2 phosphorylation."; Wakatsuki S., Saitoh F., Araki T.; Nat. Cell Biol. 13:1415-1423(2011). Cited for: FUNCTION, PHOSPHORYLATION AT THR-514, AND MUTAGENESIS OF THR-514.	22057101 [Abstract]
"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.	17114649 [Abstract]
"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-32; TYR-431; TYR-499 ANDTHR-509, AND MASS SPECTROMETRY.	18034455 [Abstract]
"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 THR-509 AND THR-514, ANDMASS SPECTROMETRY.	16452087 [Abstract]

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