dbPTM

HS901_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS901_ARATH
UniProt AC	P27323
Protein Name	Heat shock protein 90-1 {ECO:0000305}
Gene Name	HSP90-1 {ECO:0000303\|PubMed:11599565}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	700
Subcellular Localization	Cytoplasm .
Protein Description	Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non-covalent folding of proteins in an ATP-dependent manner. [PubMed: 23827697 Molecular chaperone involved in R gene-mediated disease resistance. Required for full RPS2-mediated resistance through interaction with RAR1. Possesses probably ATPase activity]
Protein Sequence	MADAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDGQPELFIRLVPDKSNKTLSIIDSGIGMTKADLVNNLGTIARSGTKEFMEALQAGADVSMIGQFGVGFYSAYLVAEKVVVTTKHNDDEQYVWESQAGGSFTVTRDVDGEPLGRGTKITLFLKDDQLEYLEERRLKDLVKKHSEFISYPIYLWTEKTTEKEISDDEDEDEPKKENEGEVEEVDEEKEKDGKKKKKIKEVSHEWELINKQKPIWLRKPEEITKEEYAAFYKSLTNDWEDHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTRKKLNNIKLYVRRVFIMDNCEELIPEYLSFVKGVVDSDDLPLNISRETLQQNKILKVIRKNLVKKCIEMFNEIAENKEDYTKFYEAFSKNLKLGIHEDSQNRGKIADLLRYHSTKSGDEMTSFKDYVTRMKEGQKDIFYITGESKKAVENSPFLERLKKRGYEVLYMVDAIDEYAVGQLKEYDGKKLVSATKEGLKLEDETEEEKKKREEKKKSFENLCKTIKEILGDKVEKVVVSDRIVDSPCCLVTGEYGWTANMERIMKAQALRDSSMSGYMSSKKTMEINPDNGIMEELRKRAEADKNDKSVKDLVMLLYETALLTSGFSLDEPNTFAARIHRMLKLGLSIDEDENVEEDGDMPELEEDAAEESKMEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MADAETFAFQAEI --CCCHHHHHHHHHH	23.22	25368622
213	Phosphorylation	IYLWTEKTTEKEISD EEEEECCCCCCCCCC	33.67	19376835
214	Phosphorylation	YLWTEKTTEKEISDD EEEECCCCCCCCCCC	57.01	19376835
219	Phosphorylation	KTTEKEISDDEDEDE CCCCCCCCCCCCCCC	39.85	30291188
597	Sulfoxidation	QALRDSSMSGYMSSK HHHHCCCCCCCCCCC	4.11	23289948
601	Sulfoxidation	DSSMSGYMSSKKTME CCCCCCCCCCCCEEE	4.10	23289948

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 HS901_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HS901_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 HS901_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
HS901_ARATH	HSP90.1	physical	23827697
HS903_ARATH	HSP81-3	physical	25293756

Drug and Disease Associations

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

Regulatory Network of HS901_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-219, 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-219, AND MASSSPECTROMETRY.	19245862 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.	18433157 [Abstract]