dbPTM

ERD14_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERD14_ARATH
UniProt AC	P42763
Protein Name	Dehydrin ERD14
Gene Name	ERD14
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	185
Subcellular Localization
Protein Description	Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity..
Protein Sequence	MAEEIKNVPEQEVPKVATEESSAEVTDRGLFDFLGKKKDETKPEETPIASEFEQKVHISEPEPEVKHESLLEKLHRSDSSSSSSSEEEGSDGEKRKKKKEKKKPTTEVEVKEEEKKGFMEKLKEKLPGHKKPEDGSAVAAAPVVVPPPVEEAHPVEKKGILEKIKEKLPGYHPKTTVEEEKKDKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEEIKNVP ------CHHHHCCCC	24.11	-
6	Acetylation	--MAEEIKNVPEQEV --CHHHHCCCCHHHC	55.99	21311031
18	Phosphorylation	QEVPKVATEESSAEV HHCCCCCCCCCCCCC	43.18	25368622
21	Phosphorylation	PKVATEESSAEVTDR CCCCCCCCCCCCCHH	28.72	25368622
22	Phosphorylation	KVATEESSAEVTDRG CCCCCCCCCCCCHHH	31.56	23111157
26	Phosphorylation	EESSAEVTDRGLFDF CCCCCCCCHHHHHHH	16.10	25561503
46	Phosphorylation	DETKPEETPIASEFE CCCCCCCCCCCHHHH	20.52	30291188
59	Phosphorylation	FEQKVHISEPEPEVK HHHHCCCCCCCCCCC	32.02	30291188
69	Phosphorylation	EPEVKHESLLEKLHR CCCCCHHHHHHHHHC	37.66	23776212
77	Phosphorylation	LLEKLHRSDSSSSSS HHHHHHCCCCCCCCC	30.97	23776212
79	Phosphorylation	EKLHRSDSSSSSSSE HHHHCCCCCCCCCCC	33.11	23776212
80	Phosphorylation	KLHRSDSSSSSSSEE HHHCCCCCCCCCCCC	38.95	23776212
81	Phosphorylation	LHRSDSSSSSSSEEE HHCCCCCCCCCCCCC	37.89	23776212
82	Phosphorylation	HRSDSSSSSSSEEEG HCCCCCCCCCCCCCC	35.87	23776212
83	Phosphorylation	RSDSSSSSSSEEEGS CCCCCCCCCCCCCCC	39.57	23776212
84	Phosphorylation	SDSSSSSSSEEEGSD CCCCCCCCCCCCCCH	43.65	23776212
85	Phosphorylation	DSSSSSSSEEEGSDG CCCCCCCCCCCCCHH	51.48	23776212
90	Phosphorylation	SSSEEEGSDGEKRKK CCCCCCCCHHHHHHH	45.80	23776212
136	Phosphorylation	HKKPEDGSAVAAAPV CCCCCCCCCEECCCE	31.71	23111157

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 ERD14_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ERD14_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 ERD14_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NAC2_ARATH	ATAF1	physical	24823379
RAA1E_ARATH	RABA1e	physical	24823379
PUB35_ARATH	AT4G25160	physical	24823379

Drug and Disease Associations

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

Regulatory Network of ERD14_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-59, AND MASSSPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASSSPECTROMETRY.	19245862 [Abstract]