dbPTM

DPYL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DPYL1_HUMAN
UniProt AC	Q14194
Protein Name	Dihydropyrimidinase-related protein 1
Gene Name	CRMP1
Organism	Homo sapiens (Human).
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	MSYQGKKSIPHITSDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFPEHLYQRVKIRNKVFGLQGVSRGMYDGPVYEVPATPKYATPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYQGKKSI ------CCCCCCCCC	26.60	21406692
3	Phosphorylation	-----MSYQGKKSIP -----CCCCCCCCCC	21.71	29759185
8	Phosphorylation	MSYQGKKSIPHITSD CCCCCCCCCCCCCCC	44.85	23911959
10 (in isoform 2)	Phosphorylation	-	21.66	-
13	Phosphorylation	KKSIPHITSDRLLIK CCCCCCCCCCCEEEE	22.88	24719451
14	Phosphorylation	KSIPHITSDRLLIKG CCCCCCCCCCEEEEC	21.82	28857561
17 (in isoform 2)	Phosphorylation	-	7.52	-
23 (in isoform 2)	Phosphorylation	-	34.97	24076635
27 (in isoform 2)	Phosphorylation	-	44.94	-
32 (in isoform 2)	Phosphorylation	-	13.15	-
32	Phosphorylation	INDDQSLYADVYLED CCCCCCCEEEEEECC	13.15	24927040
53 (in isoform 2)	Phosphorylation	-	42.50	25884760
54 (in isoform 2)	Phosphorylation	-	16.21	24076635
66 (in isoform 2)	Phosphorylation	-	1.59	22210691
89 (in isoform 2)	Phosphorylation	-	5.18	22210691
92 (in isoform 2)	Phosphorylation	-	16.41	27732954
94 (in isoform 2)	Phosphorylation	-	25.37	27732954
97 (in isoform 2)	Phosphorylation	-	3.43	22210691
98 (in isoform 2)	Phosphorylation	-	5.95	22210691
101	Phosphorylation	RAALVGGTTMIIDHV HHHHCCCEEEEEEEE	13.78	19799413
102	Phosphorylation	AALVGGTTMIIDHVV HHHCCCEEEEEEEEC	15.06	19799413
253	Phosphorylation	INCPVYITKVMSKSA CCCCEEEEECCCCCH	10.41	-
257	Phosphorylation	VYITKVMSKSAADII EEEEECCCCCHHHHH	26.84	-
258	Succinylation	YITKVMSKSAADIIA EEEECCCCCHHHHHH	26.47	-
259	Phosphorylation	ITKVMSKSAADIIAL EEECCCCCHHHHHHH	22.76	-
303	Phosphorylation	AKAAAFVTSPPLSPD HHHHHEECCCCCCCC	29.12	20068231
304	Phosphorylation	KAAAFVTSPPLSPDP HHHHEECCCCCCCCC	21.15	20068231
308	Phosphorylation	FVTSPPLSPDPTTPD EECCCCCCCCCCCHH	32.79	20068231
316	Nitrated tyrosine	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	-
316	Nitration	PDPTTPDYLTSLLAC CCCCCHHHHHHHHHC	17.06	-
345	Acetylation	TAQKAVGKDNFTLIP HHHHHHCCCCEEECC	42.79	23954790
374	Ubiquitination	DKAVATGKMDENQFV EHHHHCCCCCCCCEE	38.53	-
385	Phosphorylation	NQFVAVTSTNAAKIF CCEEEEEECCHHHHC	17.05	23911959
398	Acetylation	IFNLYPRKGRIAVGS HCCCCCCCCCEECCC	48.30	19666957
431	Phosphorylation	SHKSAVEYNIFEGME CCCCCCEEEECCCCC	13.63	21082442
442	Phosphorylation	EGMECHGSPLVVISQ CCCCCCCCCEEEEEC	7.44	30266825
448	Phosphorylation	GSPLVVISQGKIVFE CCCEEEEECCEEEEE	22.67	30266825
495	Phosphorylation	VFGLQGVSRGMYDGP CCCCCCCCCCCCCCC	29.91	24076635
499	Phosphorylation	QGVSRGMYDGPVYEV CCCCCCCCCCCEEEC	22.14	25884760
504	Phosphorylation	GMYDGPVYEVPATPK CCCCCCEEECCCCCC	17.84	21082442
509	Phosphorylation	PVYEVPATPKYATPA CEEECCCCCCCCCCC	17.78	21712546
512	Phosphorylation	EVPATPKYATPAPSA ECCCCCCCCCCCCCC	19.53	21406692
514	Phosphorylation	PATPKYATPAPSAKS CCCCCCCCCCCCCCC	19.52	25307156
518	Phosphorylation	KYATPAPSAKSSPSK CCCCCCCCCCCCCCC	50.89	29900121
521	Phosphorylation	TPAPSAKSSPSKHQP CCCCCCCCCCCCCCC	47.39	21712546
522	Phosphorylation	PAPSAKSSPSKHQPP CCCCCCCCCCCCCCC	32.27	21712546
524	Phosphorylation	PSAKSSPSKHQPPPI CCCCCCCCCCCCCCC	44.72	29691806
537	Phosphorylation	PIRNLHQSNFSLSGA CCCCCCCCCCCCCCC	29.15	24117733
540	Phosphorylation	NLHQSNFSLSGAQID CCCCCCCCCCCCCCC	26.35	24117733
542	Phosphorylation	HQSNFSLSGAQIDDN CCCCCCCCCCCCCCC	30.77	24117733
554	Phosphorylation	DDNNPRRTGHRIVAP CCCCCCCCCCEEECC	38.32	28555341
565	Asymmetric dimethylarginine	IVAPPGGRSNITSLG EECCCCCCCCCCCCC	32.23	-
569	Phosphorylation	PGGRSNITSLG---- CCCCCCCCCCC----	23.34	-
570	Phosphorylation	GGRSNITSLG----- CCCCCCCCCC-----	27.57	-

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	AURA	O14965	PSP
102	T	Phosphorylation	Kinase	AURA	O14965	PSP
504	Y	Phosphorylation	Kinase	FYN	P06241	PSP
509	T	Phosphorylation	Kinase	CDK2	P24941	PSP
509	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
509	T	Phosphorylation	Kinase	CDK5	P49615	PSP
522	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
522	S	Phosphorylation	Kinase	CDK5	P49615	PSP
522	S	Phosphorylation	Kinase	DYRK2	Q92630	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
522	S	Phosphorylation		25358863
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPYL2_HUMAN	DPYSL2	physical	12482610
DUS4_HUMAN	DUSP4	physical	21900206
HD_HUMAN	HTT	physical	15383276
VIME_HUMAN	VIM	physical	15383276
TBB5_BOVIN	TUBB	physical	12134159
VATB2_HUMAN	ATP6V1B2	physical	22863883
COR1B_HUMAN	CORO1B	physical	22863883
CUL1_HUMAN	CUL1	physical	22863883
HSP74_HUMAN	HSPA4	physical	22863883
JMJD6_HUMAN	JMJD6	physical	22863883
OTU6B_HUMAN	OTUD6B	physical	22863883
PARVA_HUMAN	PARVA	physical	22863883
SC24C_HUMAN	SEC24C	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
DPYL2_HUMAN	DPYSL2	physical	24722188
DPYL1_HUMAN	CRMP1	physical	24722188
EXOS8_HUMAN	EXOSC8	physical	24722188
GOGA2_HUMAN	GOLGA2	physical	24722188
DPYL1_HUMAN	CRMP1	physical	25416956
DPYL3_HUMAN	DPYSL3	physical	25416956
AP3M1_HUMAN	AP3M1	physical	25416956

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 DPYL1_HUMAN

Related Literatures of Post-Translational Modification

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