VILI_HUMAN - dbPTM
VILI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VILI_HUMAN
UniProt AC P09327
Protein Name Villin-1
Gene Name VIL1
Organism Homo sapiens (Human).
Sequence Length 827
Subcellular Localization Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, microvillus. Cell projection, filopodium tip. Cell projection, filopodium. Relocalized in the tip of cellular protrusions and filipodial extensions upo
Protein Description Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination..
Protein Sequence MTKLSAQVKGSLNITTPGLQIWRIEAMQMVPVPSSTFGSFFDGDCYIILAIHKTASSLSYDIHYWIGQDSSLDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESEAFRGYFKQGLVIRKGGVASGMKHVETNSYDVQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESTRMERLRGMTLAKEIRDQERGGRTYVGVVDGENELASPKLMEVMNHVLGKRRELKAAVPDTVVEPALKAALKLYHVSDSEGNLVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKKANEQEKKGAMSHALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTASNRTSGLGKTHTVGSVAKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHFYGGDCYLLLYTYLIGEKQHYLLYVWQGSQASQDEITASAYQAVILDQKYNGEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRTNNLETGPSTRLFQVQGTGANNTKAFEVPARANFLNSNDVFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENLVITPRLFECSNKTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKHANEEEKKAAATTAQEYLKTHPSGRDPETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYEDLKAELGNSRDWSQITAEVTSPKVDVFNANSNLSSGPLPIFPLEQLVNKPVEELPEGVDPSRKEEHLSIEDFTQAFGMTPAAFSALPRWKQQNLKKEKGLF
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------MTKLSAQVK
------CCCCCCEEE		40.47-
5Phosphorylation---MTKLSAQVKGSL
---CCCCCCEEECCE		20.43-
11PhosphorylationLSAQVKGSLNITTPG
CCCEEECCEECCCCC		16.7228857561
15PhosphorylationVKGSLNITTPGLQIW
EECCEECCCCCEEEE		26.35-
46PhosphorylationSFFDGDCYIILAIHK
HCCCCCEEEEEEEEH		8.8516921170
60PhosphorylationKTASSLSYDIHYWIG
HHHCCCCEEEEEECC		24.9812269817
64PhosphorylationSLSYDIHYWIGQDSS
CCCEEEEEECCCCCC		10.0812269817
81PhosphorylationEQGAAAIYTTQMDDF
HHCCEEEEEECHHHH		10.0612269817
104PhosphorylationREVQGNESEAFRGYF
EECCCCCCHHHHHHC		37.9226437602
119AcetylationKQGLVIRKGGVASGM
CCCEEEEECCHHCCC		49.2230593351
124PhosphorylationIRKGGVASGMKHVET
EEECCHHCCCEEEEC		36.69-
131PhosphorylationSGMKHVETNSYDVQR
CCCEEEECCCCCHHH		28.5123312004
133PhosphorylationMKHVETNSYDVQRLL
CEEEECCCCCHHHHH		30.0823312004
134PhosphorylationKHVETNSYDVQRLLH
EEEECCCCCHHHHHE		23.3923312004
156PhosphorylationVAGEVEMSWKSFNRG
EEEEEEECCCCCCCC		20.1828258704
192PhosphorylationMERLRGMTLAKEIRD
HHHHHCCCHHHHHHH		26.7924719451
206PhosphorylationDQERGGRTYVGVVDG
HHHCCCEEEEEEECC		26.32-
207PhosphorylationQERGGRTYVGVVDGE
HHCCCEEEEEEECCC		8.2120736484
219PhosphorylationDGENELASPKLMEVM
CCCCCCCCHHHHHHH		34.8828857561
237UbiquitinationLGKRRELKAAVPDTV
HHHHHHHHHHCCCCC		29.55-
256PhosphorylationLKAALKLYHVSDSEG
HHHHHHHHEEECCCC		9.8912269817
259PhosphorylationALKLYHVSDSEGNLV
HHHHHEEECCCCCEE		23.3123312004
261PhosphorylationKLYHVSDSEGNLVVR
HHHEEECCCCCEEEE		39.6423312004
286PhosphorylationLLSHEDCYILDQGGL
HHCCCCEEEEECCCE		19.4816921170
324PhosphorylationNFIKAKQYPPSTQVE
HHHHHCCCCCCCEEE		19.1916921170
350PhosphorylationQQLFQKWTASNRTSG
HHHHHHHHHCCCCCC		27.5223312004
352PhosphorylationLFQKWTASNRTSGLG
HHHHHHHCCCCCCCC		21.3323312004
355PhosphorylationKWTASNRTSGLGKTH
HHHHCCCCCCCCCCC		31.2523312004
356PhosphorylationWTASNRTSGLGKTHT
HHHCCCCCCCCCCCC		28.8723312004
363PhosphorylationSGLGKTHTVGSVAKV
CCCCCCCCCCCEEEE		31.6226657352
366PhosphorylationGKTHTVGSVAKVEQV
CCCCCCCCEEEEEEE		17.9929802988
378PhosphorylationEQVKFDATSMHVKPQ
EEEEECCEECCCCHH		28.5528857561
379PhosphorylationQVKFDATSMHVKPQV
EEEECCEECCCCHHH		14.4928857561
415PhosphorylationLELVPVDSKWLGHFY
CEEEECCCCCCCHHC		26.4326471730
461PhosphorylationDEITASAYQAVILDQ
HHHHHHHHHEEEECC		8.4316921170
490PhosphorylationKEPPHLMSIFKGRMV
CCCCCHHEEECCCEE		31.1024719451
514PhosphorylationNNLETGPSTRLFQVQ
CCCCCCCCEEEEEEE		27.7528857561
515PhosphorylationNLETGPSTRLFQVQG
CCCCCCCEEEEEEEC		34.2328857561
529UbiquitinationGTGANNTKAFEVPAR
CCCCCCCEEEECCCC		53.88-
552PhosphorylationVFVLKTQSCCYLWCG
EEEEEECCEEEEECC		16.0428857561
555PhosphorylationLKTQSCCYLWCGKGC
EEECCEEEEECCCCC		13.9416921170
604PhosphorylationALGGKAPYANTKRLQ
HHCCCCCCCCCCHHH		19.8316921170
618PhosphorylationQEENLVITPRLFECS
HHCCEEECCCEEECC		8.5523312004
681PhosphorylationAATTAQEYLKTHPSG
HHHHHHHHHHHCCCC		11.0421712546
693PhosphorylationPSGRDPETPIIVVKQ
CCCCCCCCCEEEEEC		25.7723312004
720PhosphorylationAWDPFKWSNTKSYED
EECCCCCCCCCCHHH		34.9028857561
722PhosphorylationDPFKWSNTKSYEDLK
CCCCCCCCCCHHHHH		18.8228857561
724PhosphorylationFKWSNTKSYEDLKAE
CCCCCCCCHHHHHHH		31.5428857561
725PhosphorylationKWSNTKSYEDLKAEL
CCCCCCCHHHHHHHH		18.2816921170
729AcetylationTKSYEDLKAELGNSR
CCCHHHHHHHHCCCC		52.737365989
735PhosphorylationLKAELGNSRDWSQIT
HHHHHCCCCCHHHHE		29.8029414761
739PhosphorylationLGNSRDWSQITAEVT
HCCCCCHHHHEEEEC		18.9228857561
746PhosphorylationSQITAEVTSPKVDVF
HHHEEEECCCCEEEE		30.7129414761
747PhosphorylationQITAEVTSPKVDVFN
HHEEEECCCCEEEEE		28.0928188228
810PhosphorylationGMTPAAFSALPRWKQ
CCCHHHHHHCHHHHH		24.9524719451
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
46YPhosphorylationKinaseSRCP12931
PSP
60YPhosphorylationKinaseSRCP12931
PSP
64YPhosphorylationKinaseSRCP12931
PSP
81YPhosphorylationKinaseSRCP12931
PSP
256YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VILI_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 VILI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEX11_HUMANTEX11physical
16189514
RAE1_HUMANCHMphysical
26344197
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 VILI_HUMAN

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Related Literatures of Post-Translational Modification

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