CH60_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CH60_RAT
• UniProt AC: P63039
• Protein Name: 60 kDa heat shock protein, mitochondrial
• Gene Name: Hspd1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 573
• Subcellular Localization: Mitochondrion matrix .
• Protein Description: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, 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: MLRLPTVLRQMRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKDIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLGKVGEVIVTKDDAMLLKGKGDKAHIEKRIQEITEQLDITTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLKPANEDQKIGIEIIKRALKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEAVVTEIPKEEKDPGMGAMGGMGGGMGGGMF

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
31	Acetylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	22902405
31	Succinylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	-
31	Succinylation	RAYAKDVKFGADARA HHHHCCCCCCHHHHH	48.49	-
54	Phosphorylation	LADAVAVTMGPKGRT HHHEEEHHCCCCCCE	13.48	28689409
61	Phosphorylation	TMGPKGRTVIIEQSW HCCCCCCEEEEEECC	25.40	28689409
67	O-linked_Glycosylation	RTVIIEQSWGSPKVT CEEEEEECCCCCCCC	22.18	27213235
67	Phosphorylation	RTVIIEQSWGSPKVT CEEEEEECCCCCCCC	22.18	27775022
70	Phosphorylation	IIEQSWGSPKVTKDG EEEECCCCCCCCCCC	18.45	23991683
75	Acetylation	WGSPKVTKDGVTVAK CCCCCCCCCCEEEEE	56.31	22902405
82	Acetylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	22902405
82	Succinylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	-
82	Succinylation	KDGVTVAKSIDLKDK CCCEEEEEECCCHHH	43.54	-
83	Phosphorylation	DGVTVAKSIDLKDKY CCEEEEEECCCHHHH	16.17	28689409
87	Acetylation	VAKSIDLKDKYKNIG EEEECCCHHHHHHHH	48.72	22902405
89	Acetylation	KSIDLKDKYKNIGAK EECCCHHHHHHHHHH	57.44	55169303
90	Phosphorylation	SIDLKDKYKNIGAKL ECCCHHHHHHHHHHH	21.28	28689409
91	Acetylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	22902405
91	Succinylation	IDLKDKYKNIGAKLV CCCHHHHHHHHHHHH	48.07	26843850
96	Acetylation	KYKNIGAKLVQDVAN HHHHHHHHHHHHHHH	43.93	22902405
105	Phosphorylation	VQDVANNTNEEAGDG HHHHHHCCCCCCCCC	43.76	23991683
113	Phosphorylation	NEEAGDGTTTATVLA CCCCCCCHHHHHHHH	26.22	23991683
114	Phosphorylation	EEAGDGTTTATVLAR CCCCCCHHHHHHHHH	21.69	23991683
115	Phosphorylation	EAGDGTTTATVLARS CCCCCHHHHHHHHHH	21.84	23991683
125	Acetylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	18530333
125	Succinylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	-
125	Succinylation	VLARSIAKEGFEKIS HHHHHHHHHHHHHHH	57.61	26843850
130	Acetylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	22902405
130	Succinylation	IAKEGFEKISKGANP HHHHHHHHHHCCCCC	50.44	26843850
133	N6-malonyllysine	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	Acetylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	22902405
133	Malonylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
133	Succinylation	EGFEKISKGANPVEI HHHHHHHCCCCCHHH	66.57	-
156	Acetylation	DAVIAELKKQSKPVT HHHHHHHHHCCCCCC	40.03	22902405
156	Succinylation	DAVIAELKKQSKPVT HHHHHHHHHCCCCCC	40.03	26843850
159	Phosphorylation	IAELKKQSKPVTTPE HHHHHHCCCCCCCHH	48.05	23984901
160	Acetylation	AELKKQSKPVTTPEE HHHHHCCCCCCCHHH	40.80	22902405
163	Phosphorylation	KKQSKPVTTPEEIAQ HHCCCCCCCHHHHHH	45.20	23984901
164	Phosphorylation	KQSKPVTTPEEIAQV HCCCCCCCHHHHHHH	29.01	23984901
180	Acetylation	TISANGDKDIGNIIS HCCCCCCCHHHHHHH	53.28	22902405
191	Acetylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	22902405
191	Succinylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	-
191	Succinylation	NIISDAMKKVGRKGV HHHHHHHHHHCCCCE	46.13	-
192	Acetylation	IISDAMKKVGRKGVI HHHHHHHHHCCCCEE	36.52	26302492
196	Succinylation	AMKKVGRKGVITVKD HHHHHCCCCEEEEEC	52.15	26843850
202	Acetylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	25786129
202	Succinylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	-
202	Succinylation	RKGVITVKDGKTLND CCCEEEEECCCCCCC	52.71	-
205	Acetylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	22902405
205	Succinylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
205	Succinylation	VITVKDGKTLNDELE EEEEECCCCCCCHHH	61.03	-
218	Acetylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	22902405
218	Succinylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	-
218	Succinylation	LEIIEGMKFDRGYIS HHHEECCCCCCCCCC	55.78	-
223	Phosphorylation	GMKFDRGYISPYFIN CCCCCCCCCCCEEEE	10.10	28689409
225	Phosphorylation	KFDRGYISPYFINTS CCCCCCCCCEEEECC	12.69	30181290
227	Phosphorylation	DRGYISPYFINTSKG CCCCCCCEEEECCCC	15.42	23991683
231	Phosphorylation	ISPYFINTSKGQKCE CCCEEEECCCCCCCC	27.31	23991683
232	Phosphorylation	SPYFINTSKGQKCEF CCEEEECCCCCCCCC	30.24	23991683
236	Acetylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	22902405
236	Succinylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
236	Succinylation	INTSKGQKCEFQDAY EECCCCCCCCCCEEE	44.38	-
243	Phosphorylation	KCEFQDAYVLLSEKK CCCCCEEEEEEECCH	10.42	30181290
249	Acetylation	AYVLLSEKKISSVQS EEEEEECCHHCCHHH	52.62	26302492
250	Acetylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	26302492
250	Succinylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	-
250	Succinylation	YVLLSEKKISSVQSI EEEEECCHHCCHHHH	43.71	-
252	Phosphorylation	LLSEKKISSVQSIVP EEECCHHCCHHHHHH	33.08	28689409
253	Phosphorylation	LSEKKISSVQSIVPA EECCHHCCHHHHHHH	27.87	28689409
256	Phosphorylation	KKISSVQSIVPALEI CHHCCHHHHHHHHHH	24.33	28689409
269	Acetylation	EIANAHRKPLVIIAE HHHHHCCCCEEEEEE	32.60	22902405
292	Acetylation	TLVLNRLKVGLQVVA HHHHHHHCCCEEEEE	30.90	-
301	Acetylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	25786129
301	Succinylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
301	Succinylation	GLQVVAVKAPGFGDN CEEEEEEECCCCCCC	38.84	-
314	Acetylation	DNRKNQLKDMAIATG CCHHHHHHHHHHHHC	35.38	22902405
352	Acetylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	22902405
352	Succinylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	-
352	Succinylation	VGEVIVTKDDAMLLK CCEEEEECCCCEECC	42.59	-
359	Acetylation	KDDAMLLKGKGDKAH CCCCEECCCCCCHHH	55.40	22640725
359	Succinylation	KDDAMLLKGKGDKAH CCCCEECCCCCCHHH	55.40	26843850
364	Acetylation	LLKGKGDKAHIEKRI ECCCCCCHHHHHHHH	51.00	25786129
369	Acetylation	GDKAHIEKRIQEITE CCHHHHHHHHHHHHH	54.95	22902405
375	Phosphorylation	EKRIQEITEQLDITT HHHHHHHHHHHCCCC	19.54	25575281
381	Phosphorylation	ITEQLDITTSEYEKE HHHHHCCCCHHHHHH	24.76	25575281
382	Phosphorylation	TEQLDITTSEYEKEK HHHHCCCCHHHHHHH	21.64	25575281
383	Phosphorylation	EQLDITTSEYEKEKL HHHCCCCHHHHHHHH	29.54	25575281
385	Phosphorylation	LDITTSEYEKEKLNE HCCCCHHHHHHHHHH	31.88	25575281
387	Acetylation	ITTSEYEKEKLNERL CCCHHHHHHHHHHHH	60.28	22902405
389	Acetylation	TSEYEKEKLNERLAK CHHHHHHHHHHHHHH	68.62	22902405
396	Acetylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	25786129
396	Succinylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	-
396	Succinylation	KLNERLAKLSDGVAV HHHHHHHHHCCCEEE	53.79	-
398	O-linked_Glycosylation	NERLAKLSDGVAVLK HHHHHHHCCCEEEEE	31.45	27213235
409	Phosphorylation	AVLKVGGTSDVEVNE EEEEECCCCCEECCC	18.80	23984901
410	Phosphorylation	VLKVGGTSDVEVNEK EEEECCCCCEECCCH	42.82	23991683
418	Acetylation	DVEVNEKKDRVTDAL CEECCCHHHHHHHHH	44.59	22902405
442	S-nitrosocysteine	GIVLGGGCALLRCIP CCEEEHHHHHHHHHH	2.46	-
442	S-nitrosylation	GIVLGGGCALLRCIP CCEEEHHHHHHHHHH	2.46	16418269
455	Acetylation	IPALDSLKPANEDQK HHHHHCCCCCCCCCC	46.14	22902405
455	Succinylation	IPALDSLKPANEDQK HHHHHCCCCCCCCCC	46.14	-
455	Succinylation	IPALDSLKPANEDQK HHHHHCCCCCCCCCC	46.14	26843850
462	Acetylation	KPANEDQKIGIEIIK CCCCCCCCHHHHHHH	56.04	26302492
469	Acetylation	KIGIEIIKRALKIPA CHHHHHHHHHHCCCH	36.96	26302492
473	Acetylation	EIIKRALKIPAMTIA HHHHHHHCCCHHHHH	45.73	25786129
473	Succinylation	EIIKRALKIPAMTIA HHHHHHHCCCHHHHH	45.73	26843850
481	Acetylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	-
481	Succinylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	-
481	Succinylation	IPAMTIAKNAGVEGS CCHHHHHHHCCCCCC	43.40	-
488	Phosphorylation	KNAGVEGSLIVEKIL HHCCCCCCHHHHHHH	11.04	23991683
497	Phosphorylation	IVEKILQSSSEVGYD HHHHHHHCCCCCCHH	32.17	23991683
498	Phosphorylation	VEKILQSSSEVGYDA HHHHHHCCCCCCHHH	19.98	23991683
499	Phosphorylation	EKILQSSSEVGYDAM HHHHHCCCCCCHHHH	41.36	23991683
503	Phosphorylation	QSSSEVGYDAMLGDF HCCCCCCHHHHHHHH	13.00	23991683
516	Acetylation	DFVNMVEKGIIDPTK HHHHHHHCCCCCHHH	43.96	22902405
523	Acetylation	KGIIDPTKVVRTALL CCCCCHHHHHHHHHH	44.09	22902405

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

Oops, there are no upstream regulatory protein records of CH60_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CH60_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CH60_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
B2CL1_RAT	Bcl2l1	physical	12967636

Drug and Disease Associations

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