VASP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VASP_MOUSE
• UniProt AC: P70460
• Protein Name: Vasodilator-stimulated phosphoprotein
• Gene Name: Vasp
• Organism: Mus musculus (Mouse).
• Sequence Length: 375
• 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 wi
• 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 (By similarity)..
• Protein Sequence: MSETVICSSRATVMLYDDSNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIIRGVKYNQATPIFHQWRDARQVWGLNFGSKEDAIQFATGMANALEALEGGGPPPAPAPPAWSAQNGPSPEELEQQKRQPEHMERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPSSGVSGAGHGAGAAPPPAPPLPTAQGPNSGGSGAPGLAAAIAGAKLRKVSKQEEASGGPLAPKAENSRSTGGGLMEEMNAMLARRRKATQVGEKPPKDESASEESEARLPAQSEPVRRPWEKNSTTLPRMKSSSSVTTSEAHPSTPCSSDDSDLERVKQELLEEVRKELQKMKEEIIEVFVQELRKRGSP

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
2	Phosphorylation	------MSETVICSS ------CCCEEEECC	41.81	29176673
2	Acetylation	------MSETVICSS ------CCCEEEECC	41.81	-
4	Phosphorylation	----MSETVICSSRA ----CCCEEEECCCC	14.09	29176673
16	Phosphorylation	SRATVMLYDDSNKRW CCCEEEEEECCCCEE	10.29	22345495
39	Phosphorylation	AFSRVQIYHNPTANS CCCEEEEECCCCCCC	4.39	26824392
43	Phosphorylation	VQIYHNPTANSFRVV EEEECCCCCCCEEEE	43.73	29472430
46	Phosphorylation	YHNPTANSFRVVGRK ECCCCCCCEEEEEEC	16.38	29472430
64	Glutathionylation	DQQVVINCAIIRGVK CCEEEEEEEEEECCC	1.66	24333276
153	Phosphorylation	EHMERRVSNAGGPPA HHHHHHHHHCCCCCC	21.10	12087107
235	Phosphorylation	GAKLRKVSKQEEASG HHHHEEHHCCHHHCC	31.49	12087107
241	Phosphorylation	VSKQEEASGGPLAPK HHCCHHHCCCCCCCC	47.78	28833060
274	Phosphorylation	LARRRKATQVGEKPP HHHHHHHHHCCCCCC	27.16	21945940
279	Acetylation	KATQVGEKPPKDESA HHHHCCCCCCCCCCC	61.77	-
285	Phosphorylation	EKPPKDESASEESEA CCCCCCCCCCHHHHC	47.42	26824392
287	Phosphorylation	PPKDESASEESEARL CCCCCCCCHHHHCCC	51.69	26160508
290	Phosphorylation	DESASEESEARLPAQ CCCCCHHHHCCCCCC	32.29	26160508
309	Phosphorylation	RRPWEKNSTTLPRMK CCCCCCCCCCCCCCC	33.56	24453211
310	Phosphorylation	RPWEKNSTTLPRMKS CCCCCCCCCCCCCCC	41.57	27600695
311	Phosphorylation	PWEKNSTTLPRMKSS CCCCCCCCCCCCCCC	34.29	21082442
317	Phosphorylation	TTLPRMKSSSSVTTS CCCCCCCCCCCCCCC	26.55	27087446
318	Phosphorylation	TLPRMKSSSSVTTSE CCCCCCCCCCCCCCC	22.55	27742792
319	Phosphorylation	LPRMKSSSSVTTSEA CCCCCCCCCCCCCCC	35.60	27742792
320	Phosphorylation	PRMKSSSSVTTSEAH CCCCCCCCCCCCCCC	25.98	27087446
322	Phosphorylation	MKSSSSVTTSEAHPS CCCCCCCCCCCCCCC	26.93	27742792
323	Phosphorylation	KSSSSVTTSEAHPST CCCCCCCCCCCCCCC	23.55	25619855
324	Phosphorylation	SSSSVTTSEAHPSTP CCCCCCCCCCCCCCC	24.34	25619855
329	Phosphorylation	TTSEAHPSTPCSSDD CCCCCCCCCCCCCCH	34.80	25619855
330	Phosphorylation	TSEAHPSTPCSSDDS CCCCCCCCCCCCCHH	32.53	25619855
332	S-nitrosocysteine	EAHPSTPCSSDDSDL CCCCCCCCCCCHHHH	6.52	-
332	S-nitrosylation	EAHPSTPCSSDDSDL CCCCCCCCCCCHHHH	6.52	21278135
333	Phosphorylation	AHPSTPCSSDDSDLE CCCCCCCCCCHHHHH	37.70	25619855
334	Phosphorylation	HPSTPCSSDDSDLER CCCCCCCCCHHHHHH	52.75	25619855
337	Phosphorylation	TPCSSDDSDLERVKQ CCCCCCHHHHHHHHH	49.43	25619855

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
153	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
153	S	Phosphorylation	Kinase	PKG1	Q13976	PSP
153	S	Phosphorylation	Kinase	KGP1	P0C605	PhosphoELM
153	S	Phosphorylation	Kinase	PRKG1	P0C605-2	GPS
153	S	Phosphorylation	Kinase	ROCK1	P70335	Uniprot
153	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
153	S	Phosphorylation	Kinase	PKC	-	Uniprot
153	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
153	S	Phosphorylation	Kinase	PKA	-	Uniprot
235	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
235	S	Phosphorylation	Kinase	PKG	-	Uniprot
235	S	Phosphorylation	Kinase	PKA	-	Uniprot
235	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
274	T	Phosphorylation	Kinase	PRKG1	P0C605	Uniprot
274	T	Phosphorylation	Kinase	PKA	-	Uniprot
274	T	Phosphorylation	Kinase	AMPK	-	Uniprot
317	S	Phosphorylation	Kinase	PRKAA2	P54646	GPS
317	S	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
318	S	Phosphorylation	Kinase	AMPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
153	S	Phosphorylation	Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235.	10882740
153	S	Phosphorylation	In ADP-activated platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen receptor inhibition.	10882740
153	S	Phosphorylation	Phosphorylation at Ser-153 by PKA is required for localization to the tight junctions in epithelial cells.	10882740
153	S	Phosphorylation	Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235.	10882740
153	S	Phosphorylation	Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235.	10882740
235	S	Phosphorylation	Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235.	10882740
235	S	Phosphorylation	Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235.	10882740
235	S	Phosphorylation	Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235.	10882740
274	T	Phosphorylation	Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235.	10882740
274	T	Phosphorylation	Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235.	10882740
318	S	Phosphorylation	Phosphorylation at Ser-318 by AMPK also alters actin filament binding.	21945940

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIM9_MOUSE	Trim9	physical	26702829

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-318, ANDMASS SPECTROMETRY.
PubMed: 17242355