dbPTM

CH10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CH10_HUMAN
UniProt AC	P61604
Protein Name	10 kDa heat shock protein, mitochondrial
Gene Name	HSPE1
Organism	Homo sapiens (Human).
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. [PubMed: 7912672]
Protein Sequence	MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGQAFRKF ------CCCHHHHHH	20.85	-
8	Methylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	11922599
8	2-Hydroxyisobutyrylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	-
8	Ubiquitination	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	21890473
8	Acetylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	23954790
8	Succinylation	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	27452117
8	Ubiquitination	MAGQAFRKFLPLFDR CCCHHHHHHHHHHHH	44.81	21890473
15	Methylation	KFLPLFDRVLVERSA HHHHHHHHHHCCCHH	19.14	115480015
21	O-linked_Glycosylation	DRVLVERSAAETVTK HHHHCCCHHCCEEEC	20.51	20305658
21	Phosphorylation	DRVLVERSAAETVTK HHHHCCCHHCCEEEC	20.51	28985074
25	Phosphorylation	VERSAAETVTKGGIM CCCHHCCEEECCCEE	28.84	27050516
27	Phosphorylation	RSAAETVTKGGIMLP CHHCCEEECCCEECC	31.24	23312004
28	Succinylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	-
28	Acetylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	25953088
28	Succinylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	27452117
28	Ubiquitination	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	21890473
28	Ubiquitination	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	21890473
28	2-Hydroxyisobutyrylation	SAAETVTKGGIMLPE HHCCEEECCCEECCC	51.29	-
32	Sulfoxidation	TVTKGGIMLPEKSQG EEECCCEECCCCCCC	6.05	21406390
36	Methylation	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	-
36	Ubiquitination	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	-
36	2-Hydroxyisobutyrylation	GGIMLPEKSQGKVLQ CCEECCCCCCCCEEE	46.25	-
37	Phosphorylation	GIMLPEKSQGKVLQA CEECCCCCCCCEEEE	42.37	28857561
40	N6-malonyllysine	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	-
40	Malonylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	26320211
40	Succinylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	-
40	Acetylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	23954790
40	Ubiquitination	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	21890473
40	2-Hydroxyisobutyrylation	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	-
40	Ubiquitination	LPEKSQGKVLQATVV CCCCCCCCEEEEEEE	31.94	21890473
45	Phosphorylation	QGKVLQATVVAVGSG CCCEEEEEEEEECCC	11.53	30108239
51	Phosphorylation	ATVVAVGSGSKGKGG EEEEEECCCCCCCCC	33.04	29255136
53	Phosphorylation	VVAVGSGSKGKGGEI EEEECCCCCCCCCCE	39.67	29255136
54	Succinylation	VAVGSGSKGKGGEIQ EEECCCCCCCCCCEE	69.07	27452117
54	N6-malonyllysine	VAVGSGSKGKGGEIQ EEECCCCCCCCCCEE	69.07	-
54	Acetylation	VAVGSGSKGKGGEIQ EEECCCCCCCCCCEE	69.07	26051181
54	Malonylation	VAVGSGSKGKGGEIQ EEECCCCCCCCCCEE	69.07	26320211
56	2-Hydroxyisobutyrylation	VGSGSKGKGGEIQPV ECCCCCCCCCCEECE	68.43	-
56	Ubiquitination	VGSGSKGKGGEIQPV ECCCCCCCCCCEECE	68.43	19608861
56	Acetylation	VGSGSKGKGGEIQPV ECCCCCCCCCCEECE	68.43	19608861
56	Succinylation	VGSGSKGKGGEIQPV ECCCCCCCCCCEECE	68.43	-
56	Malonylation	VGSGSKGKGGEIQPV ECCCCCCCCCCEECE	68.43	26320211
56	N6-malonyllysine	VGSGSKGKGGEIQPV ECCCCCCCCCCEECE	68.43	-
64	Phosphorylation	GGEIQPVSVKVGDKV CCCEECEEEEECCEE	23.93	25850435
66	Succinylation	EIQPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	-
66	Ubiquitination	EIQPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	21890473
66	Acetylation	EIQPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	21339330
66	Malonylation	EIQPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	26320211
66	Succinylation	EIQPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	-
66	Ubiquitination	EIQPVSVKVGDKVLL CEECEEEEECCEEEE	32.75	21890473
70	Succinylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	-
70	Malonylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	26320211
70	Acetylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	23954790
70	Succinylation	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	27452117
70	Ubiquitination	VSVKVGDKVLLPEYG EEEEECCEEEECCCC	28.93	19608861
76	Phosphorylation	DKVLLPEYGGTKVVL CEEEECCCCCEEEEE	20.93	25159151
79	Phosphorylation	LLPEYGGTKVVLDDK EECCCCCEEEEECCC	19.12	25159151
80	Acetylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	23954790
80	Ubiquitination	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	-
80	Sumoylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	-
80	Succinylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	27452117
80	2-Hydroxyisobutyrylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	-
80	Succinylation	LPEYGGTKVVLDDKD ECCCCCEEEEECCCC	33.35	-
86	Ubiquitination	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	21890473
86	Ubiquitination	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	21890473
86	2-Hydroxyisobutyrylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	-
86	Acetylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	19608861
86	Succinylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	27452117
86	Succinylation	TKVVLDDKDYFLFRD EEEEECCCCEEEEEC	54.73	-
88	Phosphorylation	VVLDDKDYFLFRDGD EEECCCCEEEEECCC	14.12	28152594
88	Nitration	VVLDDKDYFLFRDGD EEECCCCEEEEECCC	14.12	-
92	Methylation	DKDYFLFRDGDILGK CCCEEEEECCCCCCC	49.50	115480007
99	Succinylation	RDGDILGKYVD---- ECCCCCCCCCC----	38.36	27452117
99	Ubiquitination	RDGDILGKYVD---- ECCCCCCCCCC----	38.36	19608861
99	Acetylation	RDGDILGKYVD---- ECCCCCCCCCC----	38.36	19608861
99	2-Hydroxyisobutyrylation	RDGDILGKYVD---- ECCCCCCCCCC----	38.36	-

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 CH10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CH10_HUMAN !!

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 CH10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GBP2_HUMAN	GBP2	physical	16169070
APLP1_HUMAN	APLP1	physical	16169070
ZHX1_HUMAN	ZHX1	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
ERG28_HUMAN	C14orf1	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
CH60_HUMAN	HSPD1	physical	22939629
GRP75_HUMAN	HSPA9	physical	22939629
MPI_HUMAN	MPI	physical	22939629
CH60_HUMAN	HSPD1	physical	14717702
STK3_HUMAN	STK3	physical	21988832
RBBP7_HUMAN	RBBP7	physical	22863883
ALDR_HUMAN	AKR1B1	physical	26344197
CATA_HUMAN	CAT	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
TCPE_HUMAN	CCT5	physical	26344197
ESTD_HUMAN	ESD	physical	26344197
GRHPR_HUMAN	GRHPR	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
HS74L_HUMAN	HSPA4L	physical	26344197
HS105_HUMAN	HSPH1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
MPI_HUMAN	MPI	physical	26344197
PGK2_HUMAN	PGK2	physical	26344197
PGM2L_HUMAN	PGM2L1	physical	26344197
PIN1_HUMAN	PIN1	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
PPIF_HUMAN	PPIF	physical	26344197
RGN_HUMAN	RGN	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197

Drug and Disease Associations

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

Regulatory Network of CH10_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-70; LYS-86 ANDLYS-99, AND MASS SPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-40; LYS-54 AND LYS-56.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-40; LYS-54 AND LYS-56.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88, AND MASSSPECTROMETRY.	18083107 [Abstract]