dbPTM

EVL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EVL_MOUSE
UniProt AC	P70429
Protein Name	Ena/VASP-like protein
Gene Name	Evl
Organism	Mus musculus (Mouse).
Sequence Length	414
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, lamellipodium . Targeted to the leading edge of lamellipodia and the dital tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the di
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 and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization..
Protein Sequence	MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	ARASVMVYDDTSKKW HCCEEEEEECCCCCE	7.04	-
39	Phosphorylation	GFSRINIYHNTASST CCEEEEEEECCCCCC	5.64	-
130	Phosphorylation	RQVQNGPSPEEMDIQ HHHHCCCCHHHHHHH	46.47	25521595
150	Phosphorylation	EQQHRQESLERRISA HHHHHHHHHHHHHHC	27.48	30635358
240	Phosphorylation	VQRPEDASGGSSPSG ECCCCCCCCCCCCCC	56.88	30635358
243	Phosphorylation	PEDASGGSSPSGTSK CCCCCCCCCCCCCCH	42.47	22942356
244	Phosphorylation	EDASGGSSPSGTSKS CCCCCCCCCCCCCHH	26.76	25521595
246	Phosphorylation	ASGGSSPSGTSKSDA CCCCCCCCCCCHHHH	57.56	22942356
248	Phosphorylation	GGSSPSGTSKSDANR CCCCCCCCCHHHHCC	37.00	28833060
249	Phosphorylation	GSSPSGTSKSDANRA CCCCCCCCHHHHCCC	33.42	28833060
251	Phosphorylation	SPSGTSKSDANRASS CCCCCCHHHHCCCCC	41.54	30635358
257	Phosphorylation	KSDANRASSGGGGGG HHHHCCCCCCCCCHH	26.69	25521595
258	Phosphorylation	SDANRASSGGGGGGL HHHCCCCCCCCCHHH	40.24	27087446
281	Phosphorylation	AKRRKAASQTDKPAD HHHHHHHHCCCCCCC	38.17	29899451
283	Phosphorylation	RRKAASQTDKPADRK HHHHHHCCCCCCCCC	43.42	30635358
294	Phosphorylation	ADRKEDESQTEDPST CCCCCCHHCCCCCCC	55.51	25619855
296	Phosphorylation	RKEDESQTEDPSTSP CCCCHHCCCCCCCCC	52.19	25619855
300	Phosphorylation	ESQTEDPSTSPSPGT HHCCCCCCCCCCCCC	54.56	25619855
301	Phosphorylation	SQTEDPSTSPSPGTR HCCCCCCCCCCCCCC	50.47	30635358
302	Phosphorylation	QTEDPSTSPSPGTRA CCCCCCCCCCCCCCC	27.93	25521595
304	Phosphorylation	EDPSTSPSPGTRATS CCCCCCCCCCCCCCC	35.41	25619855
307	Phosphorylation	STSPSPGTRATSQPP CCCCCCCCCCCCCCC	22.10	25619855
317	Phosphorylation	TSQPPNSSEAGRKPW CCCCCCCCCCCCCCC	37.80	29899451
327	Phosphorylation	GRKPWERSNSVEKPV CCCCCCCCCCCCCCH	23.18	24925903
329 (in isoform 2)	Phosphorylation	-	32.66	28285833
329	Phosphorylation	KPWERSNSVEKPVSS CCCCCCCCCCCCHHH	32.66	24925903
335	Phosphorylation	NSVEKPVSSLLSRTP CCCCCCHHHHHHCCC	24.64	25619855
339	Phosphorylation	KPVSSLLSRTPSVAK CCHHHHHHCCCHHCC	39.13	25619855
341	Phosphorylation	VSSLLSRTPSVAKSP HHHHHHCCCHHCCCC	19.28	28833060
343	Phosphorylation	SLLSRTPSVAKSPEA HHHHCCCHHCCCCCC	33.81	21082442
347	Phosphorylation	RTPSVAKSPEAKSPL CCCHHCCCCCCCCCC	20.45	26824392
352	Phosphorylation	AKSPEAKSPLQSQPH CCCCCCCCCCCCCCC	37.58	26824392
356	Phosphorylation	EAKSPLQSQPHSRVK CCCCCCCCCCCCCCC	54.05	25777480
360	Phosphorylation	PLQSQPHSRVKPAGS CCCCCCCCCCCCCCC	45.51	25777480
367	Phosphorylation	SRVKPAGSVNDVGLD CCCCCCCCCCCCCCC	21.61	27087446

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
Oops, there are no upstream regulatory protein records of EVL_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EVL_MOUSE !!

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 EVL_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of EVL_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-367, ANDMASS SPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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-329 AND SER-347, ANDMASS SPECTROMETRY.	17242355 [Abstract]