VIP1_ARATH - dbPTM
VIP1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIP1_ARATH
UniProt AC Q9MA75
Protein Name Transcription factor VIP1
Gene Name VIP1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 341
Subcellular Localization Cytoplasm. Nucleus. Confined to nucleus when phosphorylated.
Protein Description Transcription activator that binds specifically to the VIP1 response elements (VREs) DNA sequence 5'-ACNGCT-3' found in some stress genes (e.g. TRX8 and MYB44), when phosphorylated/activated by MPK3. Required for Agrobacterium VirE2 nuclear import and tumorigenicity. Promotes transient expression of T-DNA in early stages by interacting with VirE2 in complex with the T-DNA and facilitating its translocation to the nucleus, and mediates stable genetic transformation by Agrobacterium by binding H2A histone. Prevents cell differentiation and shoot formation. Limits sulfate utilization efficiency (SUE) and sulfate uptake, especially in low-sulfur conditions..
Protein Sequence MEGGGRGPNQTILSEIEHMPEAPRQRISHHRRARSETFFSGESIDDLLLFDPSDIDFSSLDFLNAPPPPQQSQQQPQASPMSVDSEETSSNGVVPPNSLPPKPEARFGRHVRSFSVDSDFFDDLGVTEEKFIATSSGEKKKGNHHHSRSNSMDGEMSSASFNIESILASVSGKDSGKKNMGMGGDRLAELALLDPKRAKRILANRQSAARSKERKIRYTGELERKVQTLQNEATTLSAQVTMLQRGTSELNTENKHLKMRLQALEQQAELRDALNEALRDELNRLKVVAGEIPQGNGNSYNRAQFSSQQSAMNQFGNKTNQQMSTNGQPSLPSYMDFTKRG
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
79PhosphorylationSQQQPQASPMSVDSE
CCCCCCCCCCCCCCC
18.8517947581
113PhosphorylationRFGRHVRSFSVDSDF
HCCCCCCEEEECCCC
22.3023776212
115PhosphorylationGRHVRSFSVDSDFFD
CCCCCEEEECCCCCC
26.6830291188
118PhosphorylationVRSFSVDSDFFDDLG
CCEEEECCCCCCCCC
33.8723776212
127PhosphorylationFFDDLGVTEEKFIAT
CCCCCCCCCCEEEEC
36.3119376835
134PhosphorylationTEEKFIATSSGEKKK
CCCEEEECCCCCCCC
20.7130407730
135PhosphorylationEEKFIATSSGEKKKG
CCEEEECCCCCCCCC
27.5930407730
136PhosphorylationEKFIATSSGEKKKGN
CEEEECCCCCCCCCC
46.7630407730
149PhosphorylationGNHHHSRSNSMDGEM
CCCCCCCCCCCCCCC
35.9523776212
151PhosphorylationHHHSRSNSMDGEMSS
CCCCCCCCCCCCCCC
21.3523776212
157PhosphorylationNSMDGEMSSASFNIE
CCCCCCCCCCEEEHH
20.6023776212
158PhosphorylationSMDGEMSSASFNIES
CCCCCCCCCEEEHHH
26.9923776212
160PhosphorylationDGEMSSASFNIESIL
CCCCCCCEEEHHHHH
22.3023776212
165PhosphorylationSASFNIESILASVSG
CCEEEHHHHHHHHCC
21.0723776212
169PhosphorylationNIESILASVSGKDSG
EHHHHHHHHCCCCCC
17.2323172892
171PhosphorylationESILASVSGKDSGKK
HHHHHHHCCCCCCCC
37.3223172892
175PhosphorylationASVSGKDSGKKNMGM
HHHCCCCCCCCCCCC
56.8723172892

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 VIP1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIP1_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 VIP1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBB_ARATHAGB1physical
23974356
VIP1_ARATHVIP1physical
24057918
VIP1_ARATHVIP1physical
25093810
POF21_ARATHAT2G31370physical
25093810
MPK3_ARATHMPK3physical
17947581

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIP1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Trojan horse strategy in Agrobacterium transformation: abusing MAPKdefense signaling.";
Djamei A., Pitzschke A., Nakagami H., Rajh I., Hirt H.;
Science 318:453-456(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-79, INTERACTIONWITH MPK3, AND MUTAGENESIS OF SER-79.

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