DPYL1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPYL1_RAT
• UniProt AC: Q62950
• Protein Name: Dihydropyrimidinase-related protein 1
• Gene Name: Crmp1
• Organism: Rattus norvegicus (Rat).
• 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 (By similarity)..
• Protein Sequence: MSHQGKKSIPHITSDRLLIRGGRIINDDQSFYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTSADDFFQGTRAALAGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDLYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAIAIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKMKTLTAKSHKSTVEYNIFEGMECHGSPLVVISQGKIVFEDGNISVSKGMGRFIPRKPFPEHLYQRVRIRSKVFGLHSVSRGMYDGPVYEVPATPKHAAPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG

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
7	Ubiquitination	-MSHQGKKSIPHITS -CCCCCCCCCCCCCC	61.51	-
8	Phosphorylation	MSHQGKKSIPHITSD CCCCCCCCCCCCCCC	44.85	30411139
32	Phosphorylation	INDDQSFYADVYLED ECCCCCCEEEEEECC	13.72	-
56	Acetylation	LIVPGGVKTIEANGR EEECCCCEEEEECCE	47.24	22902405
56	Ubiquitination	LIVPGGVKTIEANGR EEECCCCEEEEECCE	47.24	-
101	Phosphorylation	RAALAGGTTMIIDHV HHHHCCCCEEEEEEC	16.57	-
102	Phosphorylation	AALAGGTTMIIDHVV HHHCCCCEEEEEECC	15.06	-
258	Succinylation	YITKVMSKSAADIIA EEEECCCCCHHHHHH	26.47	-
259	Phosphorylation	ITKVMSKSAADIIAL EEECCCCCHHHHHHH	22.76	23984901
293	Acetylation	DGTHYWSKNWAKAAA CCCCCCCCCHHHHHH	42.22	22902405
293	Ubiquitination	DGTHYWSKNWAKAAA CCCCCCCCCHHHHHH	42.22	-
316	Nitrated tyrosine	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	-
316	Nitration	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	-
345	Ubiquitination	TAQKAVGKDNFTLIP HHHHHHCCCCEEECC	42.79	-
345	Acetylation	TAQKAVGKDNFTLIP HHHHHHCCCCEEECC	42.79	72599191
384	Phosphorylation	ENQFVAVTSTNAAKI CCCEEEEEECCHHHH	21.79	25403869
385	Phosphorylation	NQFVAVTSTNAAKIF CCEEEEEECCHHHHC	17.05	25403869
386	Phosphorylation	QFVAVTSTNAAKIFN CEEEEEECCHHHHCC	21.36	25403869
423	Ubiquitination	KMKTLTAKSHKSTVE HCCEEEECCCCCCEE	48.10	-
431	Phosphorylation	SHKSTVEYNIFEGME CCCCCEEEEEECCCC	14.82	-
442	Phosphorylation	EGMECHGSPLVVISQ CCCCCCCCCEEEEEC	7.44	25403869
460	Phosphorylation	VFEDGNISVSKGMGR EEECCCEEECCCCCC	25.08	28432305
462	Phosphorylation	EDGNISVSKGMGRFI ECCCEEECCCCCCCC	19.39	28432305
463	Ubiquitination	DGNISVSKGMGRFIP CCCEEECCCCCCCCC	51.25	-
463	Acetylation	DGNISVSKGMGRFIP CCCEEECCCCCCCCC	51.25	22902405
472	Ubiquitination	MGRFIPRKPFPEHLY CCCCCCCCCCCHHHH	45.73	-
487	Ubiquitination	QRVRIRSKVFGLHSV HHHHHHHHHCCCEEC	31.56	-
493	Phosphorylation	SKVFGLHSVSRGMYD HHHCCCEECCCCCCC	27.16	25403869
495	Phosphorylation	VFGLHSVSRGMYDGP HCCCEECCCCCCCCC	26.57	30240740
499	Phosphorylation	HSVSRGMYDGPVYEV EECCCCCCCCCCEEC	22.14	-
504	Phosphorylation	GMYDGPVYEVPATPK CCCCCCCEECCCCCC	17.84	25403869
509	Phosphorylation	PVYEVPATPKHAAPA CCEECCCCCCCCCCC	27.14	30411139
511	Ubiquitination	YEVPATPKHAAPAPS EECCCCCCCCCCCCC	41.33	-
518	Phosphorylation	KHAAPAPSAKSSPSK CCCCCCCCCCCCCCC	50.89	30411139
520	Ubiquitination	AAPAPSAKSSPSKHQ CCCCCCCCCCCCCCC	56.66	-
521	Phosphorylation	APAPSAKSSPSKHQP CCCCCCCCCCCCCCC	47.39	30411139
522	Phosphorylation	PAPSAKSSPSKHQPP CCCCCCCCCCCCCCC	32.27	30411139
524	Phosphorylation	PSAKSSPSKHQPPPI CCCCCCCCCCCCCCC	44.72	27097102
525	Ubiquitination	SAKSSPSKHQPPPIR CCCCCCCCCCCCCCC	50.04	-
537	Phosphorylation	PIRNLHQSNFSLSGA CCCCCCCCCCCCCCC	29.15	30411139
540	Phosphorylation	NLHQSNFSLSGAQID CCCCCCCCCCCCCCC	26.35	27097102
542	Phosphorylation	HQSNFSLSGAQIDDN CCCCCCCCCCCCCCC	30.77	30411139
565	Asymmetric dimethylarginine	IVAPPGGRSNITSLG EECCCCCCCCCCCCC	32.23	-
566	Phosphorylation	VAPPGGRSNITSLG- ECCCCCCCCCCCCC-	35.54	25403869
569	Phosphorylation	PGGRSNITSLG---- CCCCCCCCCCC----	23.34	25403869
570	Phosphorylation	GGRSNITSLG----- CCCCCCCCCC-----	27.57	25403869

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
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.	22673903

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DPYL1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of DPYL1_RAT !!

Drug and Disease Associations

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