VILI3_ARATH - dbPTM
VILI3_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VILI3_ARATH
UniProt AC O81645
Protein Name Villin-3 {ECO:0000303|PubMed:10631247}
Gene Name VLN3 {ECO:0000303|PubMed:10631247}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 965
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Binds actin and actin filament bundles in a Ca(2+)-insensitive manner, but severs actin filaments in a calcium-dependent manner, regardless of the presence or not of VLN1 (AC O81643). Acts redundantly with VLN2 (AC O81644) to generate thick actin filament bundles, to regulate directional organ growth. [PubMed: 22209875) and in sclerenchyma development]
Protein Sequence MSGSTKVLDPAFQGVGQKPGTEIWRIENFEPVPVPKSEHGKFYMGDTYIVLQTTQNKGGAYLFDIHFWIGKDTSQDEAGTAAVKTVELDAALGGRAVQYREIQGHESDKFLSYFKPCIIPLEGGVASGFKKPEEEEFETRLYTCKGKRAVHLKQVPFARSSLNHDDVFILDTKEKIYQFNGANSNIQERAKALVVIQYLKDKFHEGTSDVAIVDDGKLDTESDSGEFWVLFGGFAPIARKVASEDEIIPETTPPKLYSIADGQVESIDGDLSKSMLENNKCYLLDCGSEIFIWVGRVTQVEERKTAIQAAEDFVASENRPKATRITRVIQGYEPHSFKSNFDSWPSGSATPANEEGRGKVAALLKQQGVGLKGLSKSTPVNEDIPPLLEGGGKLEVWYIDANSKTVLSKDHVGKLYSGDCYLVLYTYHSGERKEDYFLCCWFGKNSNQEDQETAVRLASTMTNSLKGRPVQARIFEGKEPPQFVALFQHMVVLKGGLSSGYKNSMTEKGSSGETYTPESIALIQVSGTGVHNNKALQVEAVATSLNSYDCFLLQSGTSMFLWVGNHSTHEQQELAAKVAEFLKPGTTIKHAKEGTESSSFWFALGGKQNFTSKKVSSETVRDPHLFSFSFNRGKFQVEEIHNFDQDDLLTEEMHLLDTHAEVFVWVGQCVDPKEKQTAFEIGQRYINLAGSLEGLSPKVPLYKITEGNEPCFFTTYFSWDSTKATVQGNSYQKKAALLLGTHHVVEDQSSSGNQGPRQRAAALAALTSAFNSSSGRTSSPSRDRSNGSQGGPRQRAEALAALTSAFNSSPSSKSPPRRSGLTSQASQRAAAVAALSQVLTAEKKKSPDTSPSAEAKDEKAFSEVEATEEATEAKEEEEVSPAAEASAEEAKPKQDDSEVETTGVTFTYERLQAKSEKPVTGIDFKRREAYLSEVEFKTVFGMEKESFYKLPGWKQDLLKKKFNLF
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
243PhosphorylationPIARKVASEDEIIPE
HHHHHHCCCCCCCCC		48.8723111157
696PhosphorylationAGSLEGLSPKVPLYK
HHHHCCCCCCCCEEE		33.2730291188
767PhosphorylationAAALAALTSAFNSSS
HHHHHHHHHHHHCCC		17.1823172892
768PhosphorylationAALAALTSAFNSSSG
HHHHHHHHHHHCCCC		31.5423172892
772PhosphorylationALTSAFNSSSGRTSS
HHHHHHHCCCCCCCC		21.3023172892
773PhosphorylationLTSAFNSSSGRTSSP
HHHHHHCCCCCCCCC		37.6130407730
774PhosphorylationTSAFNSSSGRTSSPS
HHHHHCCCCCCCCCC		31.9223172892
779PhosphorylationSSSGRTSSPSRDRSN
CCCCCCCCCCCCCCC		26.7019880383
803PhosphorylationAEALAALTSAFNSSP
HHHHHHHHHHHHCCC		17.1824601666
804PhosphorylationEALAALTSAFNSSPS
HHHHHHHHHHHCCCC		31.5424601666
808PhosphorylationALTSAFNSSPSSKSP
HHHHHHHCCCCCCCC		36.8523776212
809PhosphorylationLTSAFNSSPSSKSPP
HHHHHHCCCCCCCCC		29.8823776212
811PhosphorylationSAFNSSPSSKSPPRR
HHHHCCCCCCCCCCC		52.9623776212
812PhosphorylationAFNSSPSSKSPPRRS
HHHCCCCCCCCCCCC		40.3023776212
814PhosphorylationNSSPSSKSPPRRSGL
HCCCCCCCCCCCCCC		41.9324601666
819PhosphorylationSKSPPRRSGLTSQAS
CCCCCCCCCCCCHHH		39.1627545962
822PhosphorylationPPRRSGLTSQASQRA
CCCCCCCCCHHHHHH		23.4828011693
823PhosphorylationPRRSGLTSQASQRAA
CCCCCCCCHHHHHHH		28.8827545962
826PhosphorylationSGLTSQASQRAAAVA
CCCCCHHHHHHHHHH		16.7423111157
840PhosphorylationAALSQVLTAEKKKSP
HHHHHHHHHHHHCCC		33.6323111157
846PhosphorylationLTAEKKKSPDTSPSA
HHHHHHCCCCCCCCH		36.5723776212
849PhosphorylationEKKKSPDTSPSAEAK
HHHCCCCCCCCHHHC		46.0223776212
850PhosphorylationKKKSPDTSPSAEAKD
HHCCCCCCCCHHHCC		25.0023776212
852PhosphorylationKSPDTSPSAEAKDEK
CCCCCCCCHHHCCHH		38.2123776212
862PhosphorylationAKDEKAFSEVEATEE
HCCHHHHHHHHHHHH		45.6630291188
867PhosphorylationAFSEVEATEEATEAK
HHHHHHHHHHHHHHH		22.3523776212
871PhosphorylationVEATEEATEAKEEEE
HHHHHHHHHHHHHHH		39.4923776212
880PhosphorylationAKEEEEVSPAAEASA
HHHHHHCCHHHHHHH		16.4630291188
886PhosphorylationVSPAAEASAEEAKPK
CCHHHHHHHHHHCCC		27.9323776212
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 VILI3_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VILI3_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 VILI3_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VILI3_ARATH !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VILI3_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-814 AND SER-880, ANDMASS SPECTROMETRY.

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