HSPA1B [The Human Chemical-Genetic Interaction Map Project]

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======= HSPA1B =======


== Gene Information ==
  * **<color #00a2e8>Official Symbol</color>**: HSPA1B
  * **<color #00a2e8>Official Name</color>**: heat shock protein family A (Hsp70) member 1B
  * **<color #00a2e8>Aliases and Previous Symbols</color>**: N/A
  * **<color #00a2e8>Entrez ID</color>**: [[https://www.ncbi.nlm.nih.gov/gene/?term=3304|3304]]
  * **<color #00a2e8>UniProt</color>**: [[https://www.uniprot.org/uniprot/P0DMV9|P0DMV9]]
  * **<color #00a2e8>Interactions</color>**: [[https://thebiogrid.org/search.php?search=HSPA1B&organism=9606|BioGRID]]
  * **<color #00a2e8>PubMed articles</color>**: [[https://www.ncbi.nlm.nih.gov/pubmed/?term=gene%20HSPA1B|Open PubMed]]
  * **<color #00a2e8>OMIM</color>**: [[https://omim.org/entry/603012|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 co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. 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. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP- bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). {ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256, ECO:0000303|PubMed:24012426, 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'>
|positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway|
|positive regulation of nucleotide-binding oligomerization domain containing signaling pathway|
|positive regulation of microtubule nucleation|
|heat acclimation|
|regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway|
|C3HC4-type RING finger domain binding|
|cellular heat acclimation|
|regulation of microtubule nucleation|
|regulation of nucleotide-binding oligomerization domain containing signaling pathway|
|positive regulation of tumor necrosis factor-mediated signaling pathway|
|negative regulation of inclusion body assembly|
|regulation of inclusion body assembly|
|inclusion body|
|ATPase activity, coupled|
|regulation of mitotic spindle assembly|
|protein folding chaperone|
|misfolded protein binding|
|regulation of spindle assembly|
|positive regulation of microtubule polymerization|
|positive regulation of erythrocyte differentiation|
|chaperone cofactor-dependent protein refolding|
|positive regulation of microtubule polymerization or depolymerization|
|negative regulation of signal transduction in absence of ligand|
|negative regulation of extrinsic apoptotic signaling pathway in absence of ligand|
|COP9 signalosome|
|de novo posttranslational protein folding|
|protein refolding|
|regulation of mitotic spindle organization|
|de novo protein folding|
|regulation of spindle organization|
|aggresome|
|regulation of extrinsic apoptotic signaling pathway in absence of ligand|
|regulation of erythrocyte differentiation|
|positive regulation of interleukin-8 production|
|positive regulation of cytokine-mediated signaling pathway|
|regulation of microtubule polymerization|
|positive regulation of response to cytokine stimulus|
|heat shock protein binding|
|chaperone-mediated protein folding|
|regulation of tumor necrosis factor-mediated signaling pathway|
|G protein-coupled receptor binding|
|regulation of interleukin-8 production|
|cellular response to heat|
|negative regulation of protein ubiquitination|
|virus receptor activity|
|regulation of cellular response to heat|
|regulation of microtubule polymerization or depolymerization|
|positive regulation of proteasomal ubiquitin-dependent protein catabolic process|
|negative regulation of protein modification by small protein conjugation or removal|
|positive regulation of myeloid cell differentiation|
|viral entry into host cell|
|positive regulation of ubiquitin-dependent protein catabolic process|
|negative regulation of extrinsic apoptotic signaling pathway|
|entry into host cell|
|entry into host|
|positive regulation of proteasomal protein catabolic process|
|protein N-terminus binding|
|response to heat|
|histone deacetylase binding|
|positive regulation of proteolysis involved in cellular protein catabolic process|
|regulation of proteasomal ubiquitin-dependent protein catabolic process|
|ficolin-1-rich granule lumen|
|cellular response to unfolded protein|
|positive regulation of protein polymerization|
|unfolded protein binding|
|positive regulation of cellular protein catabolic process|
|blood microparticle|
|centriole|
|vesicle|
|cellular response to topologically incorrect protein|
|positive regulation of NF-kappaB transcription factor activity|
|regulation of ubiquitin-dependent protein catabolic process|
|regulation of extrinsic apoptotic signaling pathway|
|ribonucleoprotein complex|
|interaction with host|
|response to unfolded protein|
|regulation of cytokine-mediated signaling pathway|
|regulation of mitotic nuclear division|
|regulation of response to cytokine stimulus|
|response to temperature stimulus|
|protein stabilization|
|regulation of proteasomal protein catabolic process|
|negative regulation of cell growth|
|response to topologically incorrect protein|
|positive regulation of hemopoiesis|
|regulation of microtubule cytoskeleton organization|
|regulation of nuclear division|
|positive regulation of supramolecular fiber organization|
|regulation of protein ubiquitination|
|viral life cycle|
|ATP metabolic process|
|regulation of proteolysis involved in cellular protein catabolic process|
|mRNA catabolic process|
|positive regulation of protein catabolic process|
|regulation of organelle assembly|
|positive regulation of cytoskeleton organization|
|regulation of microtubule-based process|
|regulation of protein polymerization|
|regulation of myeloid cell differentiation|
|negative regulation of apoptotic signaling pathway|
|regulation of protein modification by small protein conjugation or removal|
|protein folding|
|ATPase activity|
|cellular response to oxidative stress|
|negative regulation of growth|
|RNA catabolic process|
|positive regulation of protein complex assembly|
|regulation of cellular protein catabolic process|
|positive regulation of DNA-binding transcription factor activity|
|regulation of protein stability|
|ubiquitin protein ligase binding|
|signaling receptor binding|
|positive regulation of innate immune response|
|enzyme binding|
|regulation of supramolecular fiber organization|
|positive regulation of proteolysis|
|positive regulation of response to biotic stimulus|
|positive regulation of cellular catabolic process|
|nucleobase-containing compound catabolic process|
|regulation of protein catabolic process|
|response to oxidative stress|
|regulation of apoptotic signaling pathway|
|nuclear speck|
|focal adhesion|
|regulation of cell growth|
|regulation of DNA-binding transcription factor activity|
|positive regulation of catabolic process|
|heterocycle catabolic process|
|cellular nitrogen compound catabolic process|
|aromatic compound catabolic process|
|positive regulation of cytokine production|
|regulation of hemopoiesis|
|regulation of protein complex assembly|
|regulation of innate immune response|
|positive regulation of defense response|
|organic cyclic compound catabolic process|
|neutrophil degranulation|
|centrosome|
|neutrophil activation involved in immune response|
|neutrophil mediated immunity|
|neutrophil activation|
|granulocyte activation|
|positive regulation of multi-organism process|
|leukocyte degranulation|
|myeloid leukocyte mediated immunity|
|positive regulation of cellular component biogenesis|
|regulation of response to biotic stimulus|
|myeloid cell activation involved in immune response|
|regulation of cytoskeleton organization|
|myeloid leukocyte activation|
|negative regulation of protein modification process|
|protein-containing complex|
|positive regulation of response to external stimulus|
|positive regulation of organelle organization|
|leukocyte activation involved in immune response|
|cell activation involved in immune response|
|regulation of mitotic cell cycle|
|regulation of growth|
|negative regulation of cell population proliferation|
|mRNA metabolic process|
|regulation of cytokine production|
|perinuclear region of cytoplasm|
|viral process|
|regulated exocytosis|
|negative regulation of cellular component organization|
|regulation of proteolysis|
|regulation of cellular response to stress|
|regulation of cell cycle process|
|regulation of defense response|
|leukocyte mediated immunity|
|regulation of multi-organism process|
|symbiotic process|
|exocytosis|
|interspecies interaction between organisms|
|regulation of cellular catabolic process|
|positive regulation of immune response|
|negative regulation of apoptotic process|
|cellular macromolecule catabolic process|
|negative regulation of programmed cell death|
|leukocyte activation|
|regulation of cellular component biogenesis|
|positive regulation of cell differentiation|
|negative regulation of cell death|
|regulation of catabolic process|
|secretion by cell|
|endoplasmic reticulum|
|positive regulation of intracellular signal transduction|
|negative regulation of cellular protein metabolic process|
|export from cell|
|macromolecule catabolic process|
|cell activation|
|immune effector process|
|regulation of response to external stimulus|
|negative regulation of protein metabolic process|
|secretion|
|regulation of immune response|
|positive regulation of immune system process|
|response to abiotic stimulus|
|regulation of cell cycle|
|positive regulation of cellular component organization|
|mitochondrion|
|negative regulation of signal transduction|
|regulation of organelle organization|
|negative regulation of cell communication|
|negative regulation of signaling|
|positive regulation of developmental process|
|RNA binding|
|regulation of response to stress|
|ATP binding|
|regulation of apoptotic process|
|regulation of programmed cell death|
|positive regulation of cellular protein metabolic process|
|regulation of cell population proliferation|
|negative regulation of response to stimulus|
|positive regulation of signal transduction|
|regulation of immune system process|
|RNA metabolic process|
|regulation of cell death|
|cellular response to stress|
|positive regulation of protein metabolic process|
|negative regulation of gene expression|
|positive regulation of multicellular organismal process|
|organic substance catabolic process|
|positive regulation of molecular function|
|cellular catabolic process|
|regulation of cell differentiation|
|positive regulation of cell communication|
|positive regulation of signaling|
|regulation of intracellular signal transduction|
|regulation of protein modification process|
|immune response|
|extracellular region|
|vesicle-mediated transport|
|positive regulation of gene expression|
</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>**: 8331
    * **<color #00a2e8>Expression level (log2 read counts)</color>**: 4.78 
<button type='primary' size='small' modal='Dist_expr'>Expression Distribution</button>
<modal id='Dist_expr' size='lg' title='HSPA1B Expression in NALM6 Cells: 4.78'>
{{:chemogenomics:nalm6 dist.png?nolink |}}
</modal>