dbPTM

DPYL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPYL1_MOUSE
UniProt AC	P97427
Protein Name	Dihydropyrimidinase-related protein 1
Gene Name	Crmp1
Organism	Mus musculus (Mouse).
Sequence Length	572
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Associated with centrosomes and the mitotic spindle during metaphase..
Protein Description	Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis..
Protein Sequence	MSHQGKKSIPHITSDRLLIRGGRIINDDQSFYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDLYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAIAIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKMKTITAKSHKSTVEYNIFEGMECHGSPLVVISQGKIVFEDGNISVSKGMGRFIPRKPFPEHLYQRVRIRSKVFGLHSVSRGMYDGPVYEVPATPKHAAPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MSHQGKKSIPHITS -CCCCCCCCCCCCCC	61.51	22790023
8	Phosphorylation	MSHQGKKSIPHITSD CCCCCCCCCCCCCCC	44.85	25521595
13	Phosphorylation	KKSIPHITSDRLLIR CCCCCCCCCCCEEEE	22.88	28833060
14	Phosphorylation	KSIPHITSDRLLIRG CCCCCCCCCCEEEEC	21.82	28833060
32	Phosphorylation	INDDQSFYADVYLED ECCCCCCEEEEEECC	13.72	-
56	Ubiquitination	LIVPGGVKTIEANGR EEECCCCEEEEECCE	47.24	-
101	Phosphorylation	KAALAGGTTMIIDHV HHHHCCCCEEEEEEC	16.57	-
102	Phosphorylation	AALAGGTTMIIDHVV HHHCCCCEEEEEECC	15.06	-
177	Phosphorylation	YKDLYQMSDSQLYEA HHHHHHCCHHHHHHH	20.70	29899451
179	Phosphorylation	DLYQMSDSQLYEAFT HHHHCCHHHHHHHHH	18.12	29899451
248	S-nitrosocysteine	AIAGRINCPVYITKV HHHHHCCCCEEEEEC	1.93	-
248	S-nitrosylation	AIAGRINCPVYITKV HHHHHCCCCEEEEEC	1.93	22588120
258	Succinylation	YITKVMSKSAADIIA EEEECCCCCHHHHHH	26.47	-
259	Phosphorylation	ITKVMSKSAADIIAL EEECCCCCHHHHHHH	22.76	-
288	Phosphorylation	ASLGTDGTHYWSKNW HHCCCCCCCCCCCCH	18.01	29899451
290	Phosphorylation	LGTDGTHYWSKNWAK CCCCCCCCCCCCHHH	15.94	19060867
290	Nitration	LGTDGTHYWSKNWAK CCCCCCCCCCCCHHH	15.94	-
292	Phosphorylation	TDGTHYWSKNWAKAA CCCCCCCCCCHHHHH	14.67	29899451
293	Ubiquitination	DGTHYWSKNWAKAAA CCCCCCCCCHHHHHH	42.22	-
304	Phosphorylation	KAAAFVTSPPLSPDP HHHHEECCCCCCCCC	21.15	25338131
308	Phosphorylation	FVTSPPLSPDPTTPD EECCCCCCCCCCCHH	32.79	25338131
316	Nitrated tyrosine	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	-
316	Nitration	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	16800626
316	Nitration	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	16800626
345	Ubiquitination	TAQKAVGKDNFTLIP HHHHHHCCCCEEECC	42.79	-
427	Phosphorylation	ITAKSHKSTVEYNIF EEECCCCCCEEEEEE	32.06	20415495
428	Phosphorylation	TAKSHKSTVEYNIFE EECCCCCCEEEEEEC	23.35	20415495
431	Phosphorylation	SHKSTVEYNIFEGME CCCCCEEEEEECCCC	14.82	20415495
439	S-palmitoylation	NIFEGMECHGSPLVV EEECCCCCCCCCEEE	3.06	28680068
442	Phosphorylation	EGMECHGSPLVVISQ CCCCCCCCCEEEEEC	7.44	20415495
448	Phosphorylation	GSPLVVISQGKIVFE CCCEEEEECCEEEEE	22.67	28059163
460	Phosphorylation	VFEDGNISVSKGMGR EEECCCEEECCCCCC	25.08	25521595
462	Phosphorylation	EDGNISVSKGMGRFI ECCCEEECCCCCCCC	19.39	20415495
463	Ubiquitination	DGNISVSKGMGRFIP CCCEEECCCCCCCCC	51.25	-
472	Ubiquitination	MGRFIPRKPFPEHLY CCCCCCCCCCCHHHH	45.73	-
486	Phosphorylation	YQRVRIRSKVFGLHS HHHHHHHHHHCCCEE	30.69	-
487	Ubiquitination	QRVRIRSKVFGLHSV HHHHHHHHHCCCEEC	31.56	-
493	Phosphorylation	SKVFGLHSVSRGMYD HHHCCCEECCCCCCC	27.16	22324799
495	Phosphorylation	VFGLHSVSRGMYDGP HCCCEECCCCCCCCC	26.57	22324799
495	O-linked_Glycosylation	VFGLHSVSRGMYDGP HCCCEECCCCCCCCC	26.57	31439587
499	Phosphorylation	HSVSRGMYDGPVYEV EECCCCCCCCCCEEC	22.14	25521595
504	Phosphorylation	GMYDGPVYEVPATPK CCCCCCCEECCCCCC	17.84	17178402
509	Phosphorylation	PVYEVPATPKHAAPA CCEECCCCCCCCCCC	27.14	25521595
511	Ubiquitination	YEVPATPKHAAPAPS EECCCCCCCCCCCCC	41.33	-
518	Phosphorylation	KHAAPAPSAKSSPSK CCCCCCCCCCCCCCC	50.89	25521595
520	Ubiquitination	AAPAPSAKSSPSKHQ CCCCCCCCCCCCCCC	56.66	-
521	Phosphorylation	APAPSAKSSPSKHQP CCCCCCCCCCCCCCC	47.39	25521595
522	Phosphorylation	PAPSAKSSPSKHQPP CCCCCCCCCCCCCCC	32.27	25521595
524	Phosphorylation	PSAKSSPSKHQPPPI CCCCCCCCCCCCCCC	44.72	25521595
525	Ubiquitination	SAKSSPSKHQPPPIR CCCCCCCCCCCCCCC	50.04	-
537	Phosphorylation	PIRNLHQSNFSLSGA CCCCCCCCCCCCCCC	29.15	25521595
540	Phosphorylation	NLHQSNFSLSGAQID CCCCCCCCCCCCCCC	26.35	25521595
542	Phosphorylation	HQSNFSLSGAQIDDN CCCCCCCCCCCCCCC	30.77	21082442
554	Phosphorylation	DDNNPRRTGHRIVAP CCCCCCCCCCEEECC	38.32	29899451
565	Asymmetric dimethylarginine	IVAPPGGRSNITSLG EECCCCCCCCCCCCC	32.23	-
566	Phosphorylation	VAPPGGRSNITSLG- ECCCCCCCCCCCCC-	35.54	25521595
569	Phosphorylation	PGGRSNITSLG---- CCCCCCCCCCC----	23.34	25521595
570	Phosphorylation	GGRSNITSLG----- CCCCCCCCCC-----	27.57	25521595

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
101	T	Phosphorylation	Kinase	AURKA	P97477	Uniprot
102	T	Phosphorylation	Kinase	AURKA	P97477	Uniprot
504	Y	Phosphorylation	Kinase	FYN	P39688	GPS
509	T	Phosphorylation	Kinase	CDK5	Q00535	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
522	S	Phosphorylation		-
Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of FLNA ternary structure and FLNA dissociation from F-actin.

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 DPYL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DPYL2_MOUSE	Dpysl2	physical	10956643
DPYL3_MOUSE	Dpysl3	physical	10956643

Drug and Disease Associations

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

Regulatory Network of DPYL1_MOUSE

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease."; Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.; Biochemistry 45:8009-8022(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-316, AND MASS SPECTROMETRY.	16800626 [Abstract]
Phosphorylation
Reference	PubMed
"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-431; TYR-504 ANDTHR-509, AND MASS SPECTROMETRY.	18034455 [Abstract]
"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.	15345747 [Abstract]

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