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HSC70

Gene
hsc70
Protein
Heat shock cognate 71 kDa protein
Organism
Oryzias latipes
Length
686 amino acids
Function
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Similarity
Belongs to the heat shock protein 70 family.
Mass
76.169 kDa
Sequence
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDHVVQSDMNDWPFNVINDNTRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVNNAVITVPAYFNDSQRQATKDAGTISGLNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKYKKDISDNKRAVRRLRSACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLDPVEKSLRDAKMDKGQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLNQVYEVGAMTKDNNLLGKFELTGIPPALWCPQIEVTFDIDANGIMNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDDVQRDKVSAKNGLESYAFNMKSTVEDEKLAGKISDEDKQKILDKCNEVISWLDKNQTAERDEYVHQQKELEKVCNPIITKLYQSAGGMPGGCQRECQEVSLELVVLLAVALLDQPLKKLIKHSMTSPSKIFTKKTLFKCNMQSIKSVMRLNQFPFITIT

Gene
HSC70
Protein
Luminal-binding protein
Organism
Spinacia oleracea
Length
668 amino acids
Function
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
Similarity
Belongs to the heat shock protein 70 family.
Mass
73.592 kDa
Sequence
MAVAWKSRASSIAFGIVLLGSLFAFVSAKDEAPKLGTVIGIDLGTTYSCVGVYKDGKVEIIANDQGNRITPSWVAFTNDERLIGEAAKNQAAANPERTIFDVKRLIGRKFEDKEVQKDMKLVPYKIVNRDGKPYIQVKVQEGETKVFSPEEISAMILTKMKETAETFLGKKIKDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKRGGEKNILVFDLGGGTFDVSVLTIDNGVFEVLATNGDTHLGGEDFDQRLMEYFIKLIKKKHTKDISKDNRALGKLRRECERAKRALSSQHQVRVEIESLFDGVDFSEPLTRARFEELNNDLFRKTMGPVKKAMDDAGLEKNQIDEIVLVGGSTRIPKVQQLLKEFFNGKEPSKGVNPDEAVAFGAAVQGSILSGEGGEETKEILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVTIQVFEGERSLTKDCRLLGKFDLTGIAPAPRGTPQIEVTFEVDANGILNVKAEDKASGKSEKITITNDKGRLSQEEIERMVREAEEFAEEDKKVKEKIDARNSLETYIYNMKNQISDADKLADKLESDEKEKIEGAVKEALEWLDDNQSAEKEDYDEKLKEVEAVCNPIITAVYQRSGGPSGESGADSEDSEEGHDEL

Gene
hsc70
Protein
Heat shock cognate 71 kDa protein
Organism
Ictalurus punctatus
Length
649 amino acids
Function
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Similarity
Belongs to the heat shock protein 70 family.
Mass
71.34 kDa
Sequence
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPTNTIFDAKRLIGRRFEDSVVQADMKHWPFKVISDGGRPRLEVEYKGEAKNFYPEEISSMVLVKMKEIAEAYLGKSINNAVITVPAYFNDSQRQRTKDAGTISGLNVLRIINEPTAAAIAYGLDKKVGSERNVLIFDLGGGTFDVSILTIEDGIFDLKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISDNKRAVRRLATACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLDPVEKALRDAKMDKAQVHDIVLVGGSTRIPKMEKLLQDFFNGKELNKSINPDEAVAYGAAVQAESSLGDKSENVQDLVLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGIMNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDDVQRDKVSAKNGLESYAFNMKSTVEDEKLKGKISDEDKHKILDKCNEVISWLDKNQTAEKDEYEHQQKDLEKVCNPIITKLYQSDGGMPGGMPDGMPGGFQELGAAPGGGSSGPTIEEVD