Q5NVM5 · CH60_PONAB
- Protein60 kDa heat shock protein, mitochondrial
- GeneHSPD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids573 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
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.
Catalytic activity
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial matrix | |
Cellular Component | protein-containing complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | isomerase activity | |
Molecular Function | protein-folding chaperone binding | |
Biological Process | apoptotic mitochondrial changes | |
Biological Process | mitochondrial unfolded protein response | |
Biological Process | positive regulation of interferon-alpha production | |
Biological Process | positive regulation of interleukin-6 production | |
Biological Process | positive regulation of T cell activation | |
Biological Process | positive regulation of type II interferon production | |
Biological Process | protein import into mitochondrial intermembrane space | |
Biological Process | protein refolding | |
Biological Process | response to cold | |
Biological Process | T cell activation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name60 kDa heat shock protein, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5NVM5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-26 | Mitochondrion | ||||
Sequence: MLRLPTVFRQMRPVSRVLAPHLTRAY | ||||||
Chain | PRO_0000005028 | 27-573 | 60 kDa heat shock protein, mitochondrial | |||
Sequence: AKDVKFGADARALMLRGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLEGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAAEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMVGDFVNMVGKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF | ||||||
Modified residue | 31 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 70 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 75 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 82 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 82 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 87 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 90 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 91 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 125 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 125 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 130 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-malonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 156 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 191 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 191 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 202 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 202 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 205 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 205 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 218 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 218 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 236 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 236 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 249 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 250 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 250 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 269 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 292 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 301 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 314 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 352 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 352 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 389 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 396 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 396 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 410 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 469 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 481 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 481 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 488 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 551 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Interaction
Subunit
Homoheptamer arranged in a ring structure. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex (By similarity).
Interacts with HRAS (By similarity).
Interacts with ATAD3A. Interacts with ETFBKMT and EEF1AKMT3 (By similarity).
Interacts with MFHAS1 (By similarity).
Interacts with HRAS (By similarity).
Interacts with ATAD3A. Interacts with ETFBKMT and EEF1AKMT3 (By similarity).
Interacts with MFHAS1 (By similarity).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length573
- Mass (Da)60,998
- Last updated2005-01-04 v1
- Checksum973612AC6570DD64
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR925996 EMBL· GenBank· DDBJ | CAI29638.1 EMBL· GenBank· DDBJ | mRNA |