EDR4_ARATH - dbPTM
EDR4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDR4_ARATH
UniProt AC Q9FHK4
Protein Name Protein ENHANCED DISEASE RESISTANCE 4 {ECO:0000303|PubMed:25747881}
Gene Name EDR4 {ECO:0000303|PubMed:25747881}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 615
Subcellular Localization Cell membrane . Endosome . Displays dynamic movement in cells with accumulation at the plasma membrane around pathogenic fungus penetration site.
Protein Description Plays a negative role in salicylic acid (SA)-mediated resistance to powdery mildew (e.g. Golovinomyces cichoracearum). May modulate plant immunity by regulating the relocation of EDR1 by interacting with CHC2 and modulating endocytosis..
Protein Sequence MASQTGQKIRLVRCPKCLKILQEDEDVPVYQCGGCSAILQAKRRNIAPSSTPSAGETERAQANEPQSVPETNNVSSSSGQDTVLPSSPGRSVDQEYEKGRNASMESTEKELDDLELSNGDGTNEIQEQECSLGDSEKNEREDNSRLESHMMNTVAEAAGSGSSSGSLSVDHVVAARASNPSGNSEISPDASPVEEKQSQLDILANKTPSAYDVVAARASNSSGNAEISPDASPVEEKQSQLDYPANKTSSAYDGSESSSDEREGQLLDDDEQWNALQKIRSGKFEMHRYPGYKEQGASSSSPFSENRRNGITTYNERHQNRSLQLEGPGGRLGRQGRRHVTEQLRPDMPFYPRESYTRGSPSHPSHDEFDRYPRAHSLQMPSYAGGMNHDFVDYMYHNNPRARGQGQGSRISGEMGRNHGGWYSGQLHNSYSSYSASPQRPMEQPEYHPRWRREIVSDVEDHQRNRHAGHHHELQTRRLRERQRVAKRHVRPTAGGAPFVSCYSCSENLQLPVDFLIFKRKHHLLRCGTCTTVLRFSLQSRNHLVPAVTHDINANRNSNSTSESPIDKAPSKPEKLRSSVQDEELPVARGSPLHRLMGYSTVSQVFKVSQRPPSI
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
87PhosphorylationQDTVLPSSPGRSVDQ
CCCCCCCCCCCCHHH
30589143
181PhosphorylationAARASNPSGNSEISP
EEECCCCCCCCCCCC
25561503
184PhosphorylationASNPSGNSEISPDAS
CCCCCCCCCCCCCCC
25561503
187PhosphorylationPSGNSEISPDASPVE
CCCCCCCCCCCCCHH
25561503
191PhosphorylationSEISPDASPVEEKQS
CCCCCCCCCHHHHHH
25561503
222PhosphorylationAARASNSSGNAEISP
HHHCCCCCCCCCCCC
30407730
228PhosphorylationSSGNAEISPDASPVE
CCCCCCCCCCCCCHH
30407730
232PhosphorylationAEISPDASPVEEKQS
CCCCCCCCCHHHHHH
30407730
298PhosphorylationGYKEQGASSSSPFSE
CCCCCCCCCCCCCCC
25561503
299PhosphorylationYKEQGASSSSPFSEN
CCCCCCCCCCCCCCC
30407730
300PhosphorylationKEQGASSSSPFSENR
CCCCCCCCCCCCCCC
25561503
301PhosphorylationEQGASSSSPFSENRR
CCCCCCCCCCCCCCC
30407730
304PhosphorylationASSSSPFSENRRNGI
CCCCCCCCCCCCCCC
30407730
322PhosphorylationNERHQNRSLQLEGPG
HHHHCCCCCEECCCC
30589143
360PhosphorylationRESYTRGSPSHPSHD
CCCCCCCCCCCCCCC
30291188
362PhosphorylationSYTRGSPSHPSHDEF
CCCCCCCCCCCCCCH
25561503
365PhosphorylationRGSPSHPSHDEFDRY
CCCCCCCCCCCHHCC
25561503
457PhosphorylationRWRREIVSDVEDHQR
HHHHHHHHHHHHHHH
30291188
578PhosphorylationSKPEKLRSSVQDEEL
CCCHHHHHCCCCCCC
23111157
579PhosphorylationKPEKLRSSVQDEELP
CCHHHHHCCCCCCCC
30407730
601PhosphorylationHRLMGYSTVSQVFKV
HHHCCCCHHHHHHHH
24894044
603PhosphorylationLMGYSTVSQVFKVSQ
HCCCCHHHHHHHHHC
30589143
609PhosphorylationVSQVFKVSQRPPSI-
HHHHHHHHCCCCCC-
25561503
614PhosphorylationKVSQRPPSI------
HHHCCCCCC------
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 EDR4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDR4_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 EDR4_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APRR1_ARATHTOC1physical
21798944

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDR4_ARATH

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Related Literatures of Post-Translational Modification

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