HSP70_CHICK - dbPTM
HSP70_CHICK - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP70_CHICK
UniProt AC P08106
Protein Name Heat shock 70 kDa protein
Gene Name
Organism Gallus gallus (Chicken).
Sequence Length 634
Subcellular Localization
Protein Description 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..
Protein Sequence MSGKGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKYDDPTVQSDMKHWPFRVVNEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGKKVETAVITVPAYFNDSQRQATKDAGTITGLNVMRIINEPTAAAIAYGLDKKGTRAGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNRFVEEFKGKHKRDNAGNKRAVRRLRTACERARRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVTPLSLGIETAGGVMTALIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKDDIDRMVQEAEKYKAEDEANRDRVGAKNSLESYTYNMKQTVEDEKLKGKISDQDKQKVLDKCQEVISSLDRNQMAEKEEYEHKQKELEKLCNPIVTKLYQGAGGAGAGGSGGPTIEEVD
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 Orthologous
Protein Cluster

Oops, there are no PTM records of HSP70_CHICK !!

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 HSP70_CHICK !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP70_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 HSP70_CHICK !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCMA1_CHICKKCNMA1physical
22174833

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP70_CHICK

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Related Literatures of Post-Translational Modification

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