VILI2_ARATH - dbPTM
VILI2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VILI2_ARATH
UniProt AC O81644
Protein Name Villin-2 {ECO:0000303|PubMed:10631247}
Gene Name VLN2 {ECO:0000303|PubMed:10631247}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 976
Subcellular Localization Cytoplasm, cytoskeleton . Present in the apical and subapical regions of pollen tubes.
Protein Description Ca(2+)-regulated actin-binding protein. Involved in actin filaments bundling. Caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts redundantly with VLN5 (AC Q9LVC6) to generate thick actin filament bundles and to regulate polarized pollen tube growth. [PubMed: 23715472 Acts redundantly with VLN3 (AC O81645) to regulate directional organ growth and in sclerenchyma development]
Protein Sequence MSTKVLDPAFQGAGQKPGTEIWRIENFEAVPVPKSEHGKFYMGDTYIVLQTTQNKGGAYLFDIHFWIGKDTSQDEAGTAAVKTVELDAVLGGRAVQHREIQGHESDKFLSYFKPCIIPLEGGVASGFKTVEEEVFETRLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGKLDTESDSGAFWVLFGGFAPIGRKVANDDDIVPESTPPKLYCITDGKMEPIDGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKATHVTRVIQGYESHSFKSNFDSWPSGSATPGNEEGRGKVAALLKQQGVGLKGIAKSAPVNEDIPPLLESGGKLEVWYVNGKVKTPLPKEDIGKLYSGDCYLVLYTYHSGERKDEYFLSCWFGKKSIPEDQDTAIRLANTMSNSLKGRPVQGRIYEGKEPPQFVALFQPMVVLKGGLSSGYKSSMGESESTDETYTPESIALVQVSGTGVHNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFLKPGITLKHAKEGTESSTFWFALGGKQNFTSKKASSETIRDPHLFSFAFNRGKFQVEEIYNFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDLAGSLEGLHPKVPIYKINEGNEPCFFTTYFSWDATKAIVQGNSFQKKASLLFGTHHVVEDKSNGGNQGLRQRAEALAALNSAFNSSSNRPAYSSQDRLNESHDGPRQRAEALAALSSAFNSSSSSTKSPPPPRPVGTSQASQRAAAVAALSQVLVAENKKSPDTSPTRRSTSSNPADDIPLTEAKDEEEASEVAGLEAKEEEEVSPAADETEAKQETEEQGDSEIQPSGATFTYEQLRAKSENPVTGIDFKRREAYLSEEEFQSVFGIEKEAFNNLPRWKQDLLKKKFDLF
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
346PhosphorylationFDSWPSGSATPGNEE
CCCCCCCCCCCCCCC		33.0522631563
348PhosphorylationSWPSGSATPGNEEGR
CCCCCCCCCCCCCCC		33.1723111157
375PhosphorylationGLKGIAKSAPVNEDI
CCCHHHCCCCCCCCC		28.8719880383
728PhosphorylationKAIVQGNSFQKKASL
HHHHCCCCHHHHHHH		35.5619880383
766PhosphorylationEALAALNSAFNSSSN
HHHHHHHHHHHCCCC		34.7827545962
770PhosphorylationALNSAFNSSSNRPAY
HHHHHHHCCCCCCCC		28.7927545962
771PhosphorylationLNSAFNSSSNRPAYS
HHHHHHCCCCCCCCC		32.5127545962
772PhosphorylationNSAFNSSSNRPAYSS
HHHHHCCCCCCCCCC		36.3627545962
777PhosphorylationSSSNRPAYSSQDRLN
CCCCCCCCCCHHCCC		16.1327545962
778PhosphorylationSSNRPAYSSQDRLNE
CCCCCCCCCHHCCCC		24.5127545962
779PhosphorylationSNRPAYSSQDRLNES
CCCCCCCCHHCCCCC		24.3527545962
786PhosphorylationSQDRLNESHDGPRQR
CHHCCCCCCCCHHHH		26.2927545962
808PhosphorylationSSAFNSSSSSTKSPP
HHHHCCCCCCCCCCC		28.2922631563
809PhosphorylationSAFNSSSSSTKSPPP
HHHCCCCCCCCCCCC		43.9322631563
813PhosphorylationSSSSSTKSPPPPRPV
CCCCCCCCCCCCCCC		42.6025561503
822PhosphorylationPPPRPVGTSQASQRA
CCCCCCCCCHHHHHH		20.2125561503
823PhosphorylationPPRPVGTSQASQRAA
CCCCCCCCHHHHHHH		20.1625561503
826PhosphorylationPVGTSQASQRAAAVA
CCCCCHHHHHHHHHH		16.7425561503
836PhosphorylationAAAVAALSQVLVAEN
HHHHHHHHHHHHHCC		17.3323776212
846PhosphorylationLVAENKKSPDTSPTR
HHHCCCCCCCCCCCC		29.6230291188
849PhosphorylationENKKSPDTSPTRRST
CCCCCCCCCCCCCCC		39.7323776212
850PhosphorylationNKKSPDTSPTRRSTS
CCCCCCCCCCCCCCC		31.4923776212
852PhosphorylationKSPDTSPTRRSTSSN
CCCCCCCCCCCCCCC		38.1823776212
855PhosphorylationDTSPTRRSTSSNPAD
CCCCCCCCCCCCCCC		29.3824601666
856PhosphorylationTSPTRRSTSSNPADD
CCCCCCCCCCCCCCC		34.0724601666
857PhosphorylationSPTRRSTSSNPADDI
CCCCCCCCCCCCCCC		29.3924601666
858PhosphorylationPTRRSTSSNPADDIP
CCCCCCCCCCCCCCC		47.0930291188
867PhosphorylationPADDIPLTEAKDEEE
CCCCCCCCCCCCHHH		28.6623776212
876PhosphorylationAKDEEEASEVAGLEA
CCCHHHHHHHCCCCH		35.5623776212
890PhosphorylationAKEEEEVSPAADETE
HHHHHCCCCCCCHHH		16.4623776212
896PhosphorylationVSPAADETEAKQETE
CCCCCCHHHHHHHHH		41.6223776212
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 VILI2_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VILI2_ARATH !!
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 VILI2_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VILI2_ARATH !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VILI2_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-846; THR-849; SER-850;SER-855; THR-856 AND SER-858, AND MASS SPECTROMETRY.

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