dbPTM

CH60_CHICK - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CH60_CHICK
UniProt AC	Q5ZL72
Protein Name	60 kDa heat shock protein, mitochondrial
Gene Name	HSPD1 {ECO:0000250\|UniProtKB:P10809}
Organism	Gallus gallus (Chicken).
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	MLRLPAVLRQIRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKAIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKEGFEKISKGANPVEIRRGVMLAVDAITAELKKLSKPVTTPEEIAQVATISANGDQEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLISEKKISSVQSIVPALEIANSHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLSLNVEDIQPHDFGKVGEVIVTKDDTMLLKGKGEKAQIEKRIQEIIEQLEVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVPGGGCALLRCIPALDALKPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKILQSSSEVGYDAMLGEFVNMVEKGIIDPTKVVRTALMDAAGVASLLSTAEAVVTEVPKEEKEPAMGGMGGMGGGMGGGMF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
70	Phosphorylation	IIEQSWGSPKVTKDG EEEECCCCCCCCCCC	18.45	23106611
227	Phosphorylation	DRGYISPYFINTAKG CCCCCCCCEEECCCC	15.42	-

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 CH60_CHICK !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CH60_CHICK !!

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 CH60_CHICK !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCMA1_CHICK	KCNMA1	physical	22174833
HSP70_CHICK	HSPA2	physical	8603045
HS90B_CHICK	HSP90AB1	physical	8603045

Drug and Disease Associations

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

Regulatory Network of CH60_CHICK

Related Literatures of Post-Translational Modification