dbPTM

VILI4_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VILI4_ARATH
UniProt AC	O65570
Protein Name	Villin-4 {ECO:0000303\|PubMed:10631247}
Gene Name	VLN4 {ECO:0000303\|PubMed:10631247}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	974
Subcellular Localization	Cytoplasm, cytoskeleton .
Protein Description	Binds actin and actin filament bundles in a Ca(2+)-insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Involved in root hair growth through regulating actin organization in a Ca(2+)-dependent manner..
Protein Sequence	MSVSMRDLDPAFQGAGQKAGIEIWRIENFIPTPIPKSSIGKFFTGDSYIVLKTTALKTGALRHDIHYWLGKDTSQDEAGTAAVKTVELDAALGGRAVQYREVQGHETEKFLSYFKPCIIPQEGGVASGFKHVVAEEHITRLFVCRGKHVVHVKEVPFARSSLNHDDIYILDTKSKIFQFNGSNSSIQERAKALEVVQYIKDTYHDGTCEVATVEDGKLMADADSGEFWGFFGGFAPLPRKTANDEDKTYNSDITRLFCVEKGQANPVEGDTLKREMLDTNKCYILDCGIEVFVWMGRTTSLDDRKIASKAAEEMIRSSERPKSQMIRIIEGFETVPFRSKFESWTQETNTTVSEDGRGRVAALLQRQGVNVRGLMKAAPPKEEPQVFIDCTGNLQVWRVNGQAKTLLQAADHSKFYSGDCYVFQYSYPGEEKEEVLIGTWFGKQSVEEERGSAVSMASKMVESMKFVPAQARIYEGKEPIQFFVIMQSFIVFKGGISSGYKKYIAEKEVDDDTYNENGVALFRIQGSGPENMQAIQVDPVAASLNSSYYYILHNDSSVFTWAGNLSTATDQELAERQLDLIKPNQQSRAQKEGSESEQFWELLGGKAEYSSQKLTKEPERDPHLFSCTFTKEVLKVTEIYNFTQDDLMTEDIFIIDCHSEIFVWVGQEVVPKNKLLALTIGEKFIEKDSLLEKLSPEAPIYVIMEGGEPSFFTRFFTSWDSSKSAMHGNSFQRKLKIVKNGGTPVADKPKRRTPASYGGRASVPDKSQQRSRSMSFSPDRVRVRGRSPAFNALAATFESQNARNLSTPPPVVRKLYPRSVTPDSSKFAPAPKSSAIASRSALFEKIPPQEPSIPKPVKASPKTPESPAPESNSKEQEEKKENDKEEGSMSSRIESLTIQEDAKEGVEDEEDLPAHPYDRLKTTSTDPVSDIDVTRREAYLSSEEFKEKFGMTKEAFYKLPKWKQNKFKMAVQLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
248	Phosphorylation	TANDEDKTYNSDITR CCCCCCCCCCCCCCE	40.01	25561503
445	Phosphorylation	GTWFGKQSVEEERGS EEECCCCCHHHHHHH	34.67	22074104
743	Phosphorylation	KIVKNGGTPVADKPK EEHHCCCCCCCCCCC	18.91	25561503
771	Phosphorylation	PDKSQQRSRSMSFSP CCHHHHHHHHCCCCC	25.11	25561503
773	Phosphorylation	KSQQRSRSMSFSPDR HHHHHHHHCCCCCCC	21.74	23776212
775	Phosphorylation	QQRSRSMSFSPDRVR HHHHHHCCCCCCCEE	24.66	23776212
777	Phosphorylation	RSRSMSFSPDRVRVR HHHHCCCCCCCEEEC	20.70	30291188
787	Phosphorylation	RVRVRGRSPAFNALA CEEECCCCHHHHHHH	24.33	30291188
796	Phosphorylation	AFNALAATFESQNAR HHHHHHHHHHHHCCC	23.48	23776212
799	Phosphorylation	ALAATFESQNARNLS HHHHHHHHHCCCCCC	25.25	23776212
806	Phosphorylation	SQNARNLSTPPPVVR HHCCCCCCCCCCCHH	42.28	30291188
807	Phosphorylation	QNARNLSTPPPVVRK HCCCCCCCCCCCHHH	42.87	23776212
821	Phosphorylation	KLYPRSVTPDSSKFA HHCCCCCCCCCCCCC	23.71	25561503
860	Phosphorylation	IPKPVKASPKTPESP CCCCCCCCCCCCCCC	22.63	25561503
863	Phosphorylation	PVKASPKTPESPAPE CCCCCCCCCCCCCCC	35.36	30407730
866	Phosphorylation	ASPKTPESPAPESNS CCCCCCCCCCCCCCC	27.80	25561503
888	Phosphorylation	ENDKEEGSMSSRIES HHHCCCCCHHHHHEE	20.83	30407730
890	Phosphorylation	DKEEGSMSSRIESLT HCCCCCHHHHHEEEE	20.40	25561503
891	Phosphorylation	KEEGSMSSRIESLTI CCCCCHHHHHEEEEE	28.74	25561503

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 VILI4_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VILI4_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 VILI4_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of VILI4_ARATH !!

Drug and Disease Associations

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

Regulatory Network of VILI4_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-777; SER-787 ANDSER-806, AND MASS SPECTROMETRY.	19376835 [Abstract]