EVL_HUMAN - dbPTM
EVL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EVL_HUMAN
UniProt AC Q9UI08
Protein Name Ena/VASP-like protein
Gene Name EVL
Organism Homo sapiens (Human).
Sequence Length 416
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 MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSSQRQVQNGPSPDEMDIQRRQVMEQHQQQRQESLERRTSATGPILPPGHPSSAASAPVSCSGPPPPPPPPVPPPPTGATPPPPPPLPAGGAQGSSHDESSMSGLAAAIAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQSDKPAEKKEDESQMEDPSTSPSPGTRAASQPPNSSEAGRKPWERSNSVEKPVSSILSRTPSVAKSPEAKSPLQSQPHSRMKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT
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 Orthologous
Protein Cluster
2Phosphorylation------MSEQSICQA
------CCHHHHHHH		44.3224043423
3 (in isoform 2)Phosphorylation-47.2324043423
3 (in isoform 5)Phosphorylation-47.2324043423
4 (in isoform 2)Phosphorylation-30.6824043423
4 (in isoform 5)Phosphorylation-30.6824043423
5Phosphorylation---MSEQSICQARAS
---CCHHHHHHHCCE		22.6824043423
7 (in isoform 2)Phosphorylation-2.9124043423
7 (in isoform 5)Phosphorylation-2.9124043423
16PhosphorylationARASVMVYDDTSKKW
HCCEEEEEECCCCCE		7.0425839225
18PhosphorylationASVMVYDDTSKKWVP
CEEEEEECCCCCEEE		34.88-
18 (in isoform 2)Phosphorylation-34.8828064214
18 (in isoform 5)Phosphorylation-34.8828064214
20PhosphorylationVMVYDDTSKKWVPIK
EEEEECCCCCEEECC		38.95-
27UbiquitinationSKKWVPIKPGQQGFS
CCCEEECCCCCCCCE		36.71-
29UbiquitinationKWVPIKPGQQGFSRI
CEEECCCCCCCCEEE		27.69-
29 (in isoform 2)Ubiquitination-27.69-
33UbiquitinationIKPGQQGFSRINIYH
CCCCCCCCEEEEEEE		3.74-
39PhosphorylationGFSRINIYHNTASNT
CCEEEEEEEECCCCE		5.6425839225
41 (in isoform 2)Phosphorylation-21.9925147952
70AcetylationYSIVKGLKYNQATPT
EEHEECCCCCCCCCC		51.3125953088
71PhosphorylationSIVKGLKYNQATPTF
EHEECCCCCCCCCCC		19.9728258704
73UbiquitinationVKGLKYNQATPTFHQ
EECCCCCCCCCCCCC		43.45-
75PhosphorylationGLKYNQATPTFHQWR
CCCCCCCCCCCCCHH		17.0728258704
77PhosphorylationKYNQATPTFHQWRDA
CCCCCCCCCCCHHHH		29.4228258704
88PhosphorylationWRDARQVYGLNFASK
HHHHHHHHCCCCCCH		13.9323403867
94PhosphorylationVYGLNFASKEEATTF
HHCCCCCCHHHHHHH		36.1423403867
102PhosphorylationKEEATTFSNAMLFAL
HHHHHHHHHHHHHHH		22.9123403867
114PhosphorylationFALNIMNSQEGGPSS
HHHHHHCCCCCCCCH		16.5423403867
130PhosphorylationRQVQNGPSPDEMDIQ
CCHHCCCCCCHHHHH		46.5125849741
132PhosphorylationVQNGPSPDEMDIQRR
HHCCCCCCHHHHHHH		69.09-
132 (in isoform 2)Phosphorylation-69.0924719451
152PhosphorylationHQQQRQESLERRTSA
HHHHHHHHHHHHHHC		27.4823401153
154PhosphorylationQQRQESLERRTSATG
HHHHHHHHHHHHCCC		49.77-
154 (in isoform 2)Phosphorylation-49.7724719451
157PhosphorylationQESLERRTSATGPIL
HHHHHHHHHCCCCCC		29.0028787133
158PhosphorylationESLERRTSATGPILP
HHHHHHHHCCCCCCC		23.2522817901
160PhosphorylationLERRTSATGPILPPG
HHHHHHCCCCCCCCC		43.1710945997
160 (in isoform 2)Phosphorylation-43.17-
171PhosphorylationLPPGHPSSAASAPVS
CCCCCCCCCCCCCCC		32.10-
242PhosphorylationVQRPEDASGGSSPSG
ECCCCCCCCCCCCCC		56.8823401153
244PhosphorylationRPEDASGGSSPSGTS
CCCCCCCCCCCCCCC		23.58-
244 (in isoform 2)Phosphorylation-23.5824719451
245PhosphorylationPEDASGGSSPSGTSK
CCCCCCCCCCCCCCH		42.4723401153
246PhosphorylationEDASGGSSPSGTSKS
CCCCCCCCCCCCCHH		26.7623401153
247 (in isoform 2)Phosphorylation-38.1827251275
248PhosphorylationASGGSSPSGTSKSDA
CCCCCCCCCCCHHHH		57.5622115753
248 (in isoform 2)Phosphorylation-57.5624719451
250PhosphorylationGGSSPSGTSKSDANR
CCCCCCCCCHHHHCC		37.0022115753
250 (in isoform 2)Phosphorylation-37.0027251275
251PhosphorylationGSSPSGTSKSDANRA
CCCCCCCCHHHHCCC		33.4222115753
252PhosphorylationSSPSGTSKSDANRAS
CCCCCCCHHHHCCCC		52.7917924679
252 (in isoform 2)Phosphorylation-52.79-
253PhosphorylationSPSGTSKSDANRASS
CCCCCCHHHHCCCCC		41.5423911959
254UbiquitinationPSGTSKSDANRASSG
CCCCCHHHHCCCCCC		52.15-
255PhosphorylationSGTSKSDANRASSGG
CCCCHHHHCCCCCCC		17.94-
259PhosphorylationKSDANRASSGGGGGG
HHHHCCCCCCCCCHH		26.6923401153
260PhosphorylationSDANRASSGGGGGGL
HHHCCCCCCCCCHHH		40.2423401153
261PhosphorylationDANRASSGGGGGGLM
HHCCCCCCCCCHHHH		35.9520068231
261 (in isoform 2)Phosphorylation-35.9524719451
262PhosphorylationANRASSGGGGGGLME
HCCCCCCCCCHHHHH		33.26-
273AcetylationGLMEEMNKLLAKRRK
HHHHHHHHHHHHHHH		43.5025953088
282UbiquitinationLAKRRKAASQSDKPA
HHHHHHHHHCCCCCH		15.90-
283PhosphorylationAKRRKAASQSDKPAE
HHHHHHHHCCCCCHH		34.7725849741
285PhosphorylationRRKAASQSDKPAEKK
HHHHHHCCCCCHHHC		45.1426546556
285 (in isoform 2)Phosphorylation-45.1424719451
296PhosphorylationAEKKEDESQMEDPST
HHHCCCHHHCCCCCC		47.3424702127
298SulfoxidationKKEDESQMEDPSTSP
HCCCHHHCCCCCCCC		9.8121406390
302PhosphorylationESQMEDPSTSPSPGT
HHHCCCCCCCCCCCC		54.5623401153
303PhosphorylationSQMEDPSTSPSPGTR
HHCCCCCCCCCCCCC		50.4723927012
304PhosphorylationQMEDPSTSPSPGTRA
HCCCCCCCCCCCCCC		27.9323401153
304 (in isoform 2)Phosphorylation-27.9321406692
305 (in isoform 2)Phosphorylation-44.6327251275
306PhosphorylationEDPSTSPSPGTRAAS
CCCCCCCCCCCCCCC		35.4125159151
306 (in isoform 2)Phosphorylation-35.4124719451
308PhosphorylationPSTSPSPGTRAASQP
CCCCCCCCCCCCCCC		31.9718669648
308 (in isoform 2)Phosphorylation-31.9727251275
309PhosphorylationSTSPSPGTRAASQPP
CCCCCCCCCCCCCCC		22.1023927012
313PhosphorylationSPGTRAASQPPNSSE
CCCCCCCCCCCCCCC		42.0820068231
315PhosphorylationGTRAASQPPNSSEAG
CCCCCCCCCCCCCCC		27.78-
315 (in isoform 2)Phosphorylation-27.7824719451
318PhosphorylationAASQPPNSSEAGRKP
CCCCCCCCCCCCCCC		35.0220068231
319PhosphorylationASQPPNSSEAGRKPW
CCCCCCCCCCCCCCC		37.8020068231
320PhosphorylationSQPPNSSEAGRKPWE
CCCCCCCCCCCCCCC		55.7720068231
320 (in isoform 2)Phosphorylation-55.77-
321PhosphorylationQPPNSSEAGRKPWER
CCCCCCCCCCCCCCC		25.6620068231
321 (in isoform 2)Phosphorylation-25.66-
329PhosphorylationGRKPWERSNSVEKPV
CCCCCCCCCCCCCCH		23.1823927012
331PhosphorylationKPWERSNSVEKPVSS
CCCCCCCCCCCCHHH		32.6625159151
331 (in isoform 2)Phosphorylation-32.6624719451
333PhosphorylationWERSNSVEKPVSSIL
CCCCCCCCCCHHHHH		52.0020230923
333 (in isoform 2)Phosphorylation-52.0024719451
334AcetylationERSNSVEKPVSSILS
CCCCCCCCCHHHHHH		48.8725953088
337PhosphorylationNSVEKPVSSILSRTP
CCCCCCHHHHHHCCC		21.8623927012
338PhosphorylationSVEKPVSSILSRTPS
CCCCCHHHHHHCCCH		27.9923927012
339PhosphorylationVEKPVSSILSRTPSV
CCCCHHHHHHCCCHH		2.93-
339 (in isoform 2)Phosphorylation-2.9324719451
341PhosphorylationKPVSSILSRTPSVAK
CCHHHHHHCCCHHCC		32.2220164059
343PhosphorylationVSSILSRTPSVAKSP
HHHHHHCCCHHCCCC		19.2825159151
343 (in isoform 2)Phosphorylation-19.2824719451
345PhosphorylationSILSRTPSVAKSPEA
HHHHCCCHHCCCCCC		33.8123401153
345 (in isoform 2)Phosphorylation-33.8124719451
347PhosphorylationLSRTPSVAKSPEAKS
HHCCCHHCCCCCCCC		15.7918669648
347 (in isoform 2)Phosphorylation-15.7924719451
348AcetylationSRTPSVAKSPEAKSP
HCCCHHCCCCCCCCC		65.4725953088
349PhosphorylationRTPSVAKSPEAKSPL
CCCHHCCCCCCCCCC		20.4525159151
351PhosphorylationPSVAKSPEAKSPLQS
CHHCCCCCCCCCCCC		75.6718669648
351 (in isoform 2)Phosphorylation-75.6724719451
354PhosphorylationAKSPEAKSPLQSQPH
CCCCCCCCCCCCCCC		37.5823401153
355 (in isoform 3)Phosphorylation-33.4429116813
356PhosphorylationSPEAKSPLQSQPHSR
CCCCCCCCCCCCCCC		11.1920068231
356 (in isoform 2)Phosphorylation-11.1924719451
358PhosphorylationEAKSPLQSQPHSRMK
CCCCCCCCCCCCCCC		54.0525159151
360PhosphorylationKSPLQSQPHSRMKPA
CCCCCCCCCCCCCCC		32.44-
360 (in isoform 3)Phosphorylation-32.4425159151
362PhosphorylationPLQSQPHSRMKPAGS
CCCCCCCCCCCCCCC		40.5324702127
364PhosphorylationQSQPHSRMKPAGSVN
CCCCCCCCCCCCCCC		7.36-
364 (in isoform 2)Phosphorylation-7.3624719451
364 (in isoform 3)Phosphorylation-7.3625159151
367UbiquitinationPHSRMKPAGSVNDMA
CCCCCCCCCCCCHHH		19.85-
367 (in isoform 2)Ubiquitination-19.85-
369PhosphorylationSRMKPAGSVNDMALD
CCCCCCCCCCHHHHH		21.6120164059
371PhosphorylationMKPAGSVNDMALDAF
CCCCCCCCHHHHHHH		34.7320166139
371 (in isoform 2)Phosphorylation-34.7327251275
401UbiquitinationELHKVKEEIIDAIRQ
HHHHHHHHHHHHHHH		39.26-
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
158SPhosphorylationKinasePKACAP27791
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EVL_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNMBP_HUMANDNMBPphysical
14506234
EVL_HUMANEVLphysical
25416956
TRIM9_HUMANTRIM9physical
25416956
TRM61_HUMANTRMT61Aphysical
28514442
ENAH_HUMANENAHphysical
28514442
UBIP1_HUMANUBP1physical
28514442
DDX49_HUMANDDX49physical
28514442
NUCG_HUMANENDOGphysical
28514442
TACC3_HUMANTACC3physical
28514442
EXD2_HUMANEXD2physical
28514442
LTMD1_HUMANLETMD1physical
28514442
RL23_HUMANRPL23physical
28514442
TRAF7_HUMANTRAF7physical
28514442
FBLI1_HUMANFBLIM1physical
28514442
ETFR1_HUMANLYRM5physical
28514442
WASF2_HUMANWASF2physical
28514442
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 EVL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-331; SER-341;SER-354 AND SER-369, AND MASS SPECTROMETRY.
"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 SER-246; SER-304; SER-306;SER-329; SER-331; SER-345 AND SER-349, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-331, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250, AND MASSSPECTROMETRY.

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