CH10_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CH10_MOUSE
• UniProt AC: Q64433
• Protein Name: 10 kDa heat shock protein, mitochondrial
• Gene Name: Hspe1
• Organism: Mus musculus (Mouse).
• Sequence Length: 102
• Subcellular Localization: Mitochondrion matrix .
• Protein Description: Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein..
• Protein Sequence: MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKSGEIEPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDSDILGKYVD

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
2	Acetylation	------MAGQAFRKF ------CCCHHHHHH	20.85	-
8	Malonylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	26320211
8	Acetylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	23576753
8	Succinylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	23806337
8	Ubiquitination	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	-
8	Glutarylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	24703693
21	Phosphorylation	DRVLVERSAAETVTK HHHHCCCHHCCEEEC	20.51	29514104
28	Succinylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	-
28	Malonylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	26320211
28	Succinylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	23806337
28	Ubiquitination	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	-
28	Acetylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	23806337
36	Acetylation	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	23806337
36	Malonylation	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	26320211
36	Succinylation	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	23806337
36	Glutarylation	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	24703693
36	Ubiquitination	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	-
37	Phosphorylation	GIMLPEKSQGKVLQA CEECCCCCCCCEEEE	42.37	-
40	Glutarylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	24703693
40	N6-malonyllysine	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	-
40	Succinylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	23806337
40	Ubiquitination	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	-
40	Acetylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	23576753
40	Malonylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	26320211
45	Phosphorylation	QGKVLQATVVAVGSG CCCEEEEEEEEECCC	11.53	28285833
51	Phosphorylation	ATVVAVGSGGKGKSG EEEEEECCCCCCCCC	37.46	30352176
54	Glutarylation	VAVGSGGKGKSGEIE EEECCCCCCCCCCEE	67.69	24703693
54	Malonylation	VAVGSGGKGKSGEIE EEECCCCCCCCCCEE	67.69	-
54	Succinylation	VAVGSGGKGKSGEIE EEECCCCCCCCCCEE	67.69	23806337
54	Acetylation	VAVGSGGKGKSGEIE EEECCCCCCCCCCEE	67.69	23806337
54	N6-malonyllysine	VAVGSGGKGKSGEIE EEECCCCCCCCCCEE	67.69	-
56	Succinylation	VGSGGKGKSGEIEPV ECCCCCCCCCCEECE	59.79	23806337
56	Malonylation	VGSGGKGKSGEIEPV ECCCCCCCCCCEECE	59.79	26320211
56	Glutarylation	VGSGGKGKSGEIEPV ECCCCCCCCCCEECE	59.79	24703693
56	Acetylation	VGSGGKGKSGEIEPV ECCCCCCCCCCEECE	59.79	23806337
56	N6-malonyllysine	VGSGGKGKSGEIEPV ECCCCCCCCCCEECE	59.79	-
57	Phosphorylation	GSGGKGKSGEIEPVS CCCCCCCCCCEECEE	50.78	25521595
64	Phosphorylation	SGEIEPVSVKVGDKV CCCEECEEEEECCEE	27.25	24759943
66	Acetylation	EIEPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	23576753
66	Succinylation	EIEPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	-
66	Glutarylation	EIEPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	24703693
66	Succinylation	EIEPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	23806337
70	Succinylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	-
70	Acetylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	23576753
70	Succinylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	23806337
70	Glutarylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	24703693
76	Phosphorylation	DKVLLPEYGGTKVVL CEEEECCCCCEEEEE	20.93	25521595
79	Phosphorylation	LLPEYGGTKVVLDDK EECCCCCEEEEECCC	19.12	24899341
80	Glutarylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	24703693
80	Succinylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	23806337
80	Acetylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	23576753
80	Succinylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	-
86	Malonylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	26073543
86	Succinylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	-
86	Succinylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	23806337
86	Acetylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	23576753
86	Ubiquitination	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	-
94	Phosphorylation	DYFLFRDSDILGKYV CEEEEECHHHCCCCC	23.46	26643407
99	Acetylation	RDSDILGKYVD---- ECHHHCCCCCC----	38.36	23576753
99	Succinylation	RDSDILGKYVD---- ECHHHCCCCCC----	38.36	23954790

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

Oops, there are no upstream regulatory protein records of CH10_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CH10_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CH10_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CH10_MOUSE !!

Drug and Disease Associations

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