HSP7J_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP7J_ARATH
• UniProt AC: Q9LDZ0
• Protein Name: Heat shock 70 kDa protein 10, mitochondrial
• Gene Name: HSP70-10
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 682
• Subcellular Localization: Mitochondrion .
• Protein Description: In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity)..
• Protein Sequence: MATAALLRSIRRREVVSSPFSAYRCLSSSGKASLNSSYLGQNFRSFSRAFSSKPAGNDVIGIDLGTTNSCVAVMEGKNPKVIENAEGARTTPSVVAFNTKGELLVGTPAKRQAVTNPTNTVSGTKRLIGRKFDDPQTQKEMKMVPYKIVRAPNGDAWVEANGQQYSPSQIGAFILTKMKETAEAYLGKSVTKAVVTVPAYFNDAQRQATKDAGRIAGLDVERIINEPTAAALSYGMTNKEGLIAVFDLGGGTFDVSVLEISNGVFEVKATNGDTFLGGEDFDNALLDFLVNEFKTTEGIDLAKDRLALQRLREAAEKAKIELSSTSQTEINLPFITADASGAKHFNITLTRSRFETLVNHLIERTRDPCKNCLKDAGISAKEVDEVLLVGGMTRVPKVQSIVAEIFGKSPSKGVNPDEAVAMGAALQGGILRGDVKELLLLDVTPLSLGIETLGGVFTRLITRNTTIPTKKSQVFSTAADNQTQVGIRVLQGEREMATDNKLLGEFDLVGIPPSPRGVPQIEVTFDIDANGIVTVSAKDKTTGKVQQITIRSSGGLSEDDIQKMVREAELHAQKDKERKELIDTKNTADTTIYSIEKSLGEYREKIPSEIAKEIEDAVADLRSASSGDDLNEIKAKIEAANKAVSKIGEHMSGGSGGGSAPGGGSEGGSDQAPEAEYEEVKK

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
90	Phosphorylation	ENAEGARTTPSVVAF ECCCCCCCCCCEEEE	42.39	29797451
107	Phosphorylation	KGELLVGTPAKRQAV CCCEEECCCCCCCCC	16.76	24894044
122	Phosphorylation	TNPTNTVSGTKRLIG CCCCCCCCCCHHHHC	38.41	23328941
146	Phosphorylation	KEMKMVPYKIVRAPN HHHCCCCEEEEECCC	11.26	23776212
181	Phosphorylation	ILTKMKETAEAYLGK HHHHHHHHHHHHCCC	25.04	24894044
392	Sulfoxidation	EVLLVGGMTRVPKVQ EEEEECCCCCCHHHH	1.45	23289948
409	Phosphorylation	VAEIFGKSPSKGVNP HHHHHCCCCCCCCCH	34.48	30291188
444	Phosphorylation	ELLLLDVTPLSLGIE HHEEEECCCCCCCCE	20.41	27545962
447	Phosphorylation	LLDVTPLSLGIETLG EEECCCCCCCCEEHH	26.25	27545962
452	Phosphorylation	PLSLGIETLGGVFTR CCCCCCEEHHHHHHH	28.87	27545962
458	Phosphorylation	ETLGGVFTRLITRNT EEHHHHHHHHHHCCC	23.35	27545962
469	Phosphorylation	TRNTTIPTKKSQVFS HCCCCCCCCCHHHEE	47.45	24894044
496	Sulfoxidation	VLQGEREMATDNKLL EEECCHHCCCCCCCC	6.44	23289948
557	Phosphorylation	IRSSGGLSEDDIQKM EECCCCCCHHHHHHH	42.10	29797451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HSP7J_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP7J_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HSP7J_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of HSP7J_ARATH !!

Drug and Disease Associations

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