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Ask your administrator if you think this is wrong. ======= HSPA6 ======= == Gene Information == * **<color #00a2e8>Official Symbol</color>**: HSPA6 * **<color #00a2e8>Official Name</color>**: heat shock protein family A (Hsp70) member 6 * **<color #00a2e8>Aliases and Previous Symbols</color>**: N/A * **<color #00a2e8>Entrez ID</color>**: [[https://www.ncbi.nlm.nih.gov/gene/?term=3310|3310]] * **<color #00a2e8>UniProt</color>**: [[https://www.uniprot.org/uniprot/P17066|P17066]] * **<color #00a2e8>Interactions</color>**: [[https://thebiogrid.org/search.php?search=HSPA6&organism=9606|BioGRID]] * **<color #00a2e8>PubMed articles</color>**: [[https://www.ncbi.nlm.nih.gov/pubmed/?term=gene%20HSPA6|Open PubMed]] * **<color #00a2e8>OMIM</color>**: [[https://omim.org/entry/140555|Open OMIM]] == Function Summary == * **<color #00a2e8>Entrez Summary</color>**: N/A * **<color #00a2e8>UniProt Summary</color>**: 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 (PubMed:26865365). {ECO:0000303|PubMed:26865365}. <button type='primary' size='sm' modal='Pfam_Domains'>Pfam Domains</button> <button type='primary' size='sm' modal='GO_terms'>GO Terms</button> <modal id='Pfam_Domains' size='lg' title='Pfam Domains'> |HSP70| |MreB Mbl| </modal> <modal id='GO_terms' size='lg' title='GO Terms'> |heat acclimation| |cellular heat acclimation| |ATPase activity, coupled| |protein folding chaperone| |misfolded protein binding| |chaperone cofactor-dependent protein refolding| |COP9 signalosome| |de novo posttranslational protein folding| |protein refolding| |de novo protein folding| |heat shock protein binding| |chaperone-mediated protein folding| |cellular response to heat| |response to heat| |secretory granule lumen| |ficolin-1-rich granule lumen| |cellular response to unfolded protein| |unfolded protein binding| |blood microparticle| |centriole| |cellular response to topologically incorrect protein| |response to unfolded protein| |response to temperature stimulus| |response to topologically incorrect protein| |protein folding| |ATPase activity| |enzyme binding| |neutrophil degranulation| |neutrophil activation involved in immune response| |neutrophil mediated immunity| |neutrophil activation| |granulocyte activation| |leukocyte degranulation| |myeloid leukocyte mediated immunity| |myeloid cell activation involved in immune response| |myeloid leukocyte activation| |protein-containing complex| |leukocyte activation involved in immune response| |cell activation involved in immune response| |regulated exocytosis| |leukocyte mediated immunity| |exocytosis| |leukocyte activation| |secretion by cell| |export from cell| |cell activation| |immune effector process| |secretion| |response to abiotic stimulus| |ATP binding| |cellular response to stress| |immune response| |extracellular region| |vesicle-mediated transport| </modal> \\ === CRISPR Data === <button type='default' size='small' modal='Compound_Hit'>Compound Hit</button> <button type='default' size='small' modal='Most_Correlated_Genes'>Most Correlated Genes in Chemogenomics</button> <button type='primary' size='small' modal='Essential_Avana'>Tissues where Essential in the Avana Dataset (DepMap 20Q1)</button> <modal id='Compound_Hit' size='lg' title='Compound Hit'> No hits were found. </modal> <modal id='Most_Correlated_Genes' size='lg' title='Most Correlated Genes in Chemogenomics'> No correlation found to any other genes in chemogenomics. </modal> <modal id='Essential_Avana' size='lg' title='Tissues where Essential in the Avana Dataset (DepMap 20Q1)'> Global Fraction of Cell Lines Where Essential: 0/739 ^Tissue^Fraction Of Cell Lines Where Essential^ |1290807.0|0/1| |909776.0|0/1| |bile duct|0/28| |blood|0/28| |bone|0/26| |breast|0/33| |central nervous system|0/56| |cervix|0/4| |colorectal|0/17| |esophagus|0/13| |fibroblast|0/1| |gastric|0/16| |kidney|0/21| |liver|0/20| |lung|0/75| |lymphocyte|0/16| |ovary|0/26| |pancreas|0/24| |peripheral nervous system|0/16| |plasma cell|0/15| |prostate|0/1| |skin|0/24| |soft tissue|0/9| |thyroid|0/2| |upper aerodigestive|0/22| |urinary tract|0/29| |uterus|0/5| </modal> == Essentiality in NALM6 == * **<color #00a2e8>Essentiality Rank</color>**: 15909 * **<color #00a2e8>Expression level (log2 read counts)</color>**: -1.69 <button type='primary' size='small' modal='Dist_expr'>Expression Distribution</button> <modal id='Dist_expr' size='lg' title='HSPA6 Expression in NALM6 Cells: -1.69'> {{:chemogenomics:nalm6 dist.png?nolink |}} </modal> Last modified: 2025/12/10 20:19by 127.0.0.1