dbPTM

VASP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VASP_HUMAN
UniProt AC	P50552
Protein Name	Vasodilator-stimulated phosphoprotein
Gene Name	VASP
Organism	Homo sapiens (Human).
Sequence Length	380
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Targeted to stress fibers and focal adhesions through interaction with a
Protein Description	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation..
Protein Sequence	MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGVKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVEQQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPPLPAAQGPGGGGAGAPGLAAAIAGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQVGEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQELLEEVKKELQKVKEEIIEAFVQELRKRGSP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSETVICSS ------CCCEEEECC	41.81	19413330
2	Phosphorylation	------MSETVICSS ------CCCEEEECC	41.81	30108239
4	Phosphorylation	----MSETVICSSRA ----CCCEEEECCCC	14.09	30108239
8	Phosphorylation	MSETVICSSRATVML CCCEEEECCCCEEEE	16.25	-
14	Sulfoxidation	CSSRATVMLYDDGNK ECCCCEEEEEECCCE	2.20	30846556
16	Phosphorylation	SRATVMLYDDGNKRW CCCEEEEEECCCEEE	8.22	25839225
21	Acetylation	MLYDDGNKRWLPAGT EEEECCCEEEEECCC	50.94	26051181
39	Phosphorylation	AFSRVQIYHNPTANS CCCEEEEECCCCCCC	4.39	21945579
43	Phosphorylation	VQIYHNPTANSFRVV EEEECCCCCCCEEEE	43.73	21945579
46	Phosphorylation	YHNPTANSFRVVGRK ECCCCCCCEEEEEEC	16.38	21945579
68	Methylation	VINCAIVRGVKYNQA EEEEEEECCCCCCCC	37.77	115385805
71	Ubiquitination	CAIVRGVKYNQATPN EEEECCCCCCCCCCC	41.11	21890473
71	Malonylation	CAIVRGVKYNQATPN EEEECCCCCCCCCCC	41.11	26320211
71	Acetylation	CAIVRGVKYNQATPN EEEECCCCCCCCCCC	41.11	26051181
76	Phosphorylation	GVKYNQATPNFHQWR CCCCCCCCCCCHHHH	14.70	25690035
126	Phosphorylation	PPPPALPTWSVPNGP CCCCCCCCCCCCCCC	31.08	28348404
134	Phosphorylation	WSVPNGPSPEEVEQQ CCCCCCCCHHHHHHH	46.47	28348404
157	Phosphorylation	EHIERRVSNAGGPPA HHHHHHHHCCCCCCC	21.10	23927012
239	Phosphorylation	GAKLRKVSKQEEASG HHHHHHHHCCHHHCC	31.49	23927012
240	Acetylation	AKLRKVSKQEEASGG HHHHHHHCCHHHCCC	65.79	26051181
245	Phosphorylation	VSKQEEASGGPTAPK HHCCHHHCCCCCCCC	47.78	23403867
249	Phosphorylation	EEASGGPTAPKAESG HHHCCCCCCCCHHCC	59.89	23927012
252	Acetylation	SGGPTAPKAESGRSG CCCCCCCCHHCCCCC	63.42	7683629
255	Phosphorylation	PTAPKAESGRSGGGG CCCCCHHCCCCCCCH	44.35	30576142
258	Phosphorylation	PKAESGRSGGGGLME CCHHCCCCCCCHHHH	45.36	22199227
264	Sulfoxidation	RSGGGGLMEEMNAML CCCCCHHHHHHHHHH	4.66	21406390
276	Acetylation	AMLARRRKATQVGEK HHHHHHHHHHHCCCC	54.71	26051181
278	Phosphorylation	LARRRKATQVGEKTP HHHHHHHHHCCCCCC	27.16	8182057
283	Acetylation	KATQVGEKTPKDESA HHHHCCCCCCCCCCC	65.29	19608861
284	Phosphorylation	ATQVGEKTPKDESAN HHHCCCCCCCCCCCC	31.13	23401153
286	Sumoylation	QVGEKTPKDESANQE HCCCCCCCCCCCCCC	78.38	-
286	Sumoylation	QVGEKTPKDESANQE HCCCCCCCCCCCCCC	78.38	-
289	Phosphorylation	EKTPKDESANQEEPE CCCCCCCCCCCCCCC	42.53	25159151
303	Phosphorylation	EARVPAQSESVRRPW CCCCCCCCHHCCCCC	33.67	23401153
305	Phosphorylation	RVPAQSESVRRPWEK CCCCCCHHCCCCCCC	26.60	23401153
312	Ubiquitination	SVRRPWEKNSTTLPR HCCCCCCCCCCCCCC	52.94	-
314	Phosphorylation	RRPWEKNSTTLPRMK CCCCCCCCCCCCCCC	33.56	23401153
315	Phosphorylation	RPWEKNSTTLPRMKS CCCCCCCCCCCCCCC	41.57	23401153
316	Phosphorylation	PWEKNSTTLPRMKSS CCCCCCCCCCCCCCC	34.29	26846344
321	Ubiquitination	STTLPRMKSSSSVTT CCCCCCCCCCCCCCC	48.76	-
321	Methylation	STTLPRMKSSSSVTT CCCCCCCCCCCCCCC	48.76	115978835
322	Phosphorylation	TTLPRMKSSSSVTTS CCCCCCCCCCCCCCC	26.55	22167270
323	Phosphorylation	TLPRMKSSSSVTTSE CCCCCCCCCCCCCCC	22.55	22167270
324	Phosphorylation	LPRMKSSSSVTTSET CCCCCCCCCCCCCCC	35.60	22167270
325	Phosphorylation	PRMKSSSSVTTSETQ CCCCCCCCCCCCCCC	25.98	22167270
327	Phosphorylation	MKSSSSVTTSETQPC CCCCCCCCCCCCCCC	26.93	22167270
328	Phosphorylation	KSSSSVTTSETQPCT CCCCCCCCCCCCCCC	23.55	23927012
329	Phosphorylation	SSSSVTTSETQPCTP CCCCCCCCCCCCCCC	29.31	23927012
331	Phosphorylation	SSVTTSETQPCTPSS CCCCCCCCCCCCCCC	37.26	23927012
335	Phosphorylation	TSETQPCTPSSSDYS CCCCCCCCCCCCCHH	32.65	27273156
337	Phosphorylation	ETQPCTPSSSDYSDL CCCCCCCCCCCHHHH	25.07	23927012
338	Phosphorylation	TQPCTPSSSDYSDLQ CCCCCCCCCCHHHHH	28.56	28152594
339	Phosphorylation	QPCTPSSSDYSDLQR CCCCCCCCCHHHHHH	44.92	28152594
341	Phosphorylation	CTPSSSDYSDLQRVK CCCCCCCHHHHHHHH	13.16	23927012
342	Phosphorylation	TPSSSDYSDLQRVKQ CCCCCCHHHHHHHHH	36.51	28152594
348	Ubiquitination	YSDLQRVKQELLEEV HHHHHHHHHHHHHHH	40.00	-
348	Acetylation	YSDLQRVKQELLEEV HHHHHHHHHHHHHHH	40.00	26051181
356	Acetylation	QELLEEVKKELQKVK HHHHHHHHHHHHHHH	43.75	26051181
363	Ubiquitination	KKELQKVKEEIIEAF HHHHHHHHHHHHHHH	57.58	21890473
363	Acetylation	KKELQKVKEEIIEAF HHHHHHHHHHHHHHH	57.58	26051181

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
39	Y	Phosphorylation	Kinase	ALK	Q9UM73	PSP
157	S	Phosphorylation	Kinase	PKG/CGK_GROUP	-	PhosphoELM
157	S	Phosphorylation	Kinase	PKA	-	Uniprot
157	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
157	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
157	S	Phosphorylation	Kinase	PKC	-	Uniprot
157	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
157	S	Phosphorylation	Kinase	ROCK1	Q13464	Uniprot
157	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
157	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
157	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
157	S	Phosphorylation	Kinase	PKG1	Q13976	PSP
157	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
157	S	Phosphorylation	Kinase	PRKG1	P00516	GPS
157	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
157	S	Phosphorylation	Kinase	PKACA	P17612	PSP
239	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
239	S	Phosphorylation	Kinase	PKG1	Q13976	PSP
239	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
239	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
239	S	Phosphorylation	Kinase	PKACA	P17612	PSP
239	S	Phosphorylation	Kinase	PKA	-	Uniprot
239	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
239	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
239	S	Phosphorylation	Kinase	PKG/CGK_GROUP	-	PhosphoELM
239	S	Phosphorylation	Kinase	PRKG1	P00516	GPS
278	T	Phosphorylation	Kinase	PKA	-	Uniprot
278	T	Phosphorylation	Kinase	PKG/CGK_GROUP	-	PhosphoELM
278	T	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
278	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
278	T	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
278	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
278	T	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
278	T	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
278	T	Phosphorylation	Kinase	PKG1	Q13976	PSP
278	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
278	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
322	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
322	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
322	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
157	S	Phosphorylation	8182057
Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239.
157	S	Phosphorylation	8182057
In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition.
157	S	Phosphorylation	8182057
Phosphorylation at Ser-157 by PKA is required for localization to the tight junctions in epithelial cells.
157	S	Phosphorylation	8182057
Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239.
157	S	Phosphorylation	8182057
Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239.
157	S	Phosphorylation	8182057
Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239.
239	S	Phosphorylation	8182057
Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239.
239	S	Phosphorylation	8182057
Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239.
239	S	Phosphorylation	8182057
Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239.
239	S	Phosphorylation	8182057
Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239.
278	T	Phosphorylation	8182057
Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239.
278	T	Phosphorylation	8182057
Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239.
322	S	Phosphorylation	18669648
Phosphorylation at Ser-322 by AMPK also alters actin filament binding.

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 VASP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DMRTB_HUMAN	DMRTB1	physical	16189514
NOL3_HUMAN	NOL3	physical	16189514
WWP2_HUMAN	WWP2	physical	16189514
TRIM9_HUMAN	TRIM9	physical	16189514
ZYX_HUMAN	ZYX	physical	10882740
PROF1_HUMAN	PFN1	physical	10882740
PROF2_HUMAN	PFN2	physical	10882740
VINC_HUMAN	VCL	physical	10882740
VASP_HUMAN	VASP	physical	12220179
IRAK1_HUMAN	IRAK1	physical	20044140
FAN_HUMAN	NSMAF	physical	17599063
VATC1_HUMAN	ATP6V1C1	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
DMRTB_HUMAN	DMRTB1	physical	19060904
SAT1_HUMAN	SAT1	physical	19060904
1433T_HUMAN	YWHAQ	physical	20618440
DDB1_HUMAN	DDB1	physical	22863883
PAAF1_HUMAN	PAAF1	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
XIRP1_HUMAN	XIRP1	physical	16631741
ABI2_HUMAN	ABI2	physical	25416956
FR1OP_HUMAN	FGFR1OP	physical	25416956
ABI3_HUMAN	ABI3	physical	25416956
ENAH_HUMAN	ENAH	physical	26186194
GTPB1_HUMAN	GTPBP1	physical	26186194
CYFP2_HUMAN	CYFIP2	physical	26186194
EVL_HUMAN	EVL	physical	26186194
UTP4_HUMAN	CIRH1A	physical	26186194
ABI1_HUMAN	ABI1	physical	26186194
LRP4_HUMAN	LRP4	physical	26186194
CTU1_HUMAN	CTU1	physical	26186194
ENAH_HUMAN	ENAH	physical	26344197
EVL_HUMAN	EVL	physical	26344197
ACTG_HUMAN	ACTG1	physical	25241761
GEPH_HUMAN	GPHN	physical	16376568
ACTN1_HUMAN	ACTN1	physical	16376568
EVL_HUMAN	EVL	physical	28514442
ZYX_HUMAN	ZYX	physical	28514442
ENAH_HUMAN	ENAH	physical	28514442
ABI1_HUMAN	ABI1	physical	28514442
GTPB1_HUMAN	GTPBP1	physical	28514442
FR1OP_HUMAN	FGFR1OP	physical	28514442
UTP4_HUMAN	CIRH1A	physical	28514442
CTU1_HUMAN	CTU1	physical	28514442
UFM1_HUMAN	UFM1	physical	27173435
ARPC3_HUMAN	ARPC3	physical	27173435
PREP_HUMAN	PITRM1	physical	27173435
CB071_HUMAN	C2orf71	physical	27173435

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 VASP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.	12665801 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316 AND SER-322, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Carbon monoxide and nitric oxide mediate cytoskeletal reorganizationin microvascular cells via vasodilator-stimulated phosphoproteinphosphorylation: evidence for blunted responsiveness in diabetes."; Li Calzi S., Purich D.L., Chang K.H., Afzal A., Nakagawa T.,Busik J.V., Agarwal A., Segal M.S., Grant M.B.; Diabetes 57:2488-2494(2008). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-157 ANDSER-239.	18559661 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser157 by protein kinase C-dependent and -independent mechanisms inthrombin-stimulated human platelets."; Wentworth J.K., Pula G., Poole A.W.; Biochem. J. 393:555-564(2006). Cited for: PHOSPHORYLATION AT SER-157, AND SUBCELLULAR LOCATION.	16197368 [Abstract]
"Phosphorylation of focal adhesion vasodilator-stimulatedphosphoprotein at Ser157 in intact human platelets correlates withfibrinogen receptor inhibition."; Horstrup K., Jablonka B., Honig-Liedl P., Just M., Kochsiek K.,Walter U.; Eur. J. Biochem. 225:21-27(1994). Cited for: PHOSPHORYLATION AT SER-157, AND FIBRINOGEN RECEPTOR INHIBITION.	7925440 [Abstract]
"cAMP- and cGMP-dependent protein kinase phosphorylation sites of thefocal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitroand in intact human platelets."; Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.; J. Biol. Chem. 269:14509-14517(1994). Cited for: PROTEIN SEQUENCE OF 143-164; 235-244 AND 267-285, AND PHOSPHORYLATIONAT SER-157; SER-239 AND THR-278 BY PRKG1.	8182057 [Abstract]
"AMP-activated protein kinase impairs endothelial actin cytoskeletonassembly by phosphorylating vasodilator-stimulated phosphoprotein."; Blume C., Benz P.M., Walter U., Ha J., Kemp B.E., Renne T.; J. Biol. Chem. 282:4601-4612(2007). Cited for: PHOSPHORYLATION AT THR-278, MUTAGENESIS OF SER-157; SER-239 ANDTHR-278, AND FUNCTION.	17082196 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, AND MASSSPECTROMETRY.	15592455 [Abstract]

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