Details for: HSPA8

Gene ID: 3312

Symbol: HSPA8

Ensembl ID: ENSG00000109971

Description: heat shock protein family A (Hsp70) member 8

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 836.4448
    Cell Significance Index: -130.1100
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 540.5621
    Cell Significance Index: -137.1100
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 412.9166
    Cell Significance Index: -170.1000
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 370.8735
    Cell Significance Index: -150.6700
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 352.5143
    Cell Significance Index: -166.4300
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 329.5001
    Cell Significance Index: -169.4900
  • Cell Name: ileal goblet cell (CL1000326)
    Fold Change: 248.3972
    Cell Significance Index: -166.6800
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 161.2319
    Cell Significance Index: -153.9400
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 130.1588
    Cell Significance Index: -160.4800
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 43.6373
    Cell Significance Index: -134.0300
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 42.9100
    Cell Significance Index: -169.3300
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 27.6050
    Cell Significance Index: -73.9500
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 6.3792
    Cell Significance Index: 334.9300
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 6.1148
    Cell Significance Index: 783.8800
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 5.9458
    Cell Significance Index: 156.3500
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: 5.6414
    Cell Significance Index: 196.0400
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 4.9805
    Cell Significance Index: 234.0800
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 4.8728
    Cell Significance Index: 143.1100
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 4.6812
    Cell Significance Index: 552.0600
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 4.5929
    Cell Significance Index: 239.2400
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 4.4110
    Cell Significance Index: 56.4900
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 3.7700
    Cell Significance Index: 108.0700
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: 3.6526
    Cell Significance Index: 76.4600
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 3.4601
    Cell Significance Index: 61.1500
  • Cell Name: oral mucosa squamous cell (CL1001576)
    Fold Change: 3.1200
    Cell Significance Index: 26.8100
  • Cell Name: skeletal muscle myoblast (CL0000515)
    Fold Change: 3.0769
    Cell Significance Index: 33.4500
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 2.9475
    Cell Significance Index: 404.7800
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 2.7526
    Cell Significance Index: 177.5900
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 2.6852
    Cell Significance Index: 330.1700
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 2.6702
    Cell Significance Index: 1458.2800
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: 2.6223
    Cell Significance Index: 29.7900
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 2.5702
    Cell Significance Index: 463.3200
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 2.5040
    Cell Significance Index: 1107.1000
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 2.2241
    Cell Significance Index: 287.3400
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: 2.0335
    Cell Significance Index: 143.8200
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 2.0276
    Cell Significance Index: 346.2300
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 1.8241
    Cell Significance Index: 85.0500
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.7374
    Cell Significance Index: 344.7900
  • Cell Name: peg cell (CL4033014)
    Fold Change: 1.3721
    Cell Significance Index: 31.7000
  • Cell Name: kidney cell (CL1000497)
    Fold Change: 1.3702
    Cell Significance Index: 10.9400
  • Cell Name: germ cell (CL0000586)
    Fold Change: 1.3641
    Cell Significance Index: 10.3000
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 1.3160
    Cell Significance Index: 35.1400
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: 1.0952
    Cell Significance Index: 10.0900
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.8723
    Cell Significance Index: 65.0100
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: 0.8680
    Cell Significance Index: 52.1100
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 0.8083
    Cell Significance Index: 22.0000
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.6177
    Cell Significance Index: 557.7600
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.5641
    Cell Significance Index: 113.1500
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.3380
    Cell Significance Index: 255.8200
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.2243
    Cell Significance Index: 80.4500
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.2153
    Cell Significance Index: 7.5700
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: 0.2129
    Cell Significance Index: 156.1000
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.0617
    Cell Significance Index: 11.7500
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.0517
    Cell Significance Index: 5.1100
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.0046
    Cell Significance Index: 0.4700
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: -0.0574
    Cell Significance Index: -2.9800
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0724
    Cell Significance Index: -53.6400
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0729
    Cell Significance Index: -137.3100
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: -0.1010
    Cell Significance Index: -1.6900
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.1049
    Cell Significance Index: -193.5000
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.1240
    Cell Significance Index: -190.9100
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.1245
    Cell Significance Index: -169.2200
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.1280
    Cell Significance Index: -79.9600
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: -0.1404
    Cell Significance Index: -15.2700
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: -0.1863
    Cell Significance Index: -30.3000
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.2032
    Cell Significance Index: -129.0700
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.2111
    Cell Significance Index: -119.0700
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: -0.2335
    Cell Significance Index: -161.5000
  • Cell Name: cone retinal bipolar cell (CL0000752)
    Fold Change: -0.2335
    Cell Significance Index: -1.8000
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: -0.2959
    Cell Significance Index: -33.7800
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.3178
    Cell Significance Index: -144.2300
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.3385
    Cell Significance Index: -71.2900
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.5068
    Cell Significance Index: -145.8300
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: -0.6087
    Cell Significance Index: -15.5500
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.6216
    Cell Significance Index: -71.2200
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: -0.6693
    Cell Significance Index: -12.3700
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -0.7616
    Cell Significance Index: -48.0000
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: -0.9412
    Cell Significance Index: -11.2200
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.9488
    Cell Significance Index: -110.5700
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.9963
    Cell Significance Index: -61.2400
  • Cell Name: theca cell (CL0000503)
    Fold Change: -0.9991
    Cell Significance Index: -5.8700
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -1.0027
    Cell Significance Index: -145.7500
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -1.1303
    Cell Significance Index: -89.5200
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: -1.3201
    Cell Significance Index: -28.6000
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -1.4216
    Cell Significance Index: -39.7300
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -1.5073
    Cell Significance Index: -84.5800
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: -1.5557
    Cell Significance Index: -107.5900
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -1.6320
    Cell Significance Index: -169.9300
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: -1.6378
    Cell Significance Index: -43.8100
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -1.6779
    Cell Significance Index: -53.7400
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -1.7852
    Cell Significance Index: -120.0400
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -1.9024
    Cell Significance Index: -145.9900
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -1.9858
    Cell Significance Index: -90.0100
  • Cell Name: paneth cell of colon (CL0009009)
    Fold Change: -1.9975
    Cell Significance Index: -29.9300
  • Cell Name: cerebellar granule cell (CL0001031)
    Fold Change: -2.2740
    Cell Significance Index: -38.9700
  • Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
    Fold Change: -2.6591
    Cell Significance Index: -45.8400
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -2.7148
    Cell Significance Index: -166.4400
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: -2.7507
    Cell Significance Index: -37.5300
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -2.8085
    Cell Significance Index: -70.2100
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: -3.0573
    Cell Significance Index: -90.0500

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics** 1. **Molecular Chaperone Function**: HSPA8 acts as a molecular chaperone, facilitating the correct folding and unfolding of proteins, and promoting their stability and degradation. 2. **Heat Shock Protein Family**: HSPA8 belongs to the Hsp70 family, which is characterized by their ability to bind and release heat-shocked proteins, and their involvement in protein folding and degradation. 3. **Wide Expression Pattern**: HSPA8 is expressed in various cell types, including immune cells, thyroid follicular cells, and fibroblasts, indicating its importance in maintaining cellular homeostasis. 4. **Antiviral Mechanism**: HSPA8 has been implicated in the antiviral response, particularly in the context of viral infections such as respiratory syncytial virus (RSV). **Pathways and Functions** 1. **Autophagy**: HSPA8 is involved in the regulation of autophagy, a process by which cells degrade and recycle damaged or dysfunctional proteins and organelles. 2. **Chaperone-Mediated Autophagy**: HSPA8 plays a critical role in the regulation of chaperone-mediated autophagy, a process by which proteins are degraded by autophagosomes. 3. **Protein Folding and Degradation**: HSPA8 facilitates the correct folding and unfolding of proteins, and promotes their stability and degradation. 4. **Immune Response**: HSPA8 is involved in the regulation of immune responses, particularly in the context of viral infections and immune cell function. 5. **Stress Response**: HSPA8 is activated in response to stress, such as heat shock, and plays a critical role in maintaining protein homeostasis during this process. **Clinical Significance** 1. **Cancer**: HSPA8 has been implicated in cancer, particularly in the context of tumor progression and metastasis. 2. **Autoimmune Diseases**: HSPA8 has been implicated in autoimmune diseases, such as multiple sclerosis, where it is thought to play a role in the regulation of immune responses. 3. **Neurological Disorders**: HSPA8 has been implicated in neurological disorders, such as Alzheimer's disease, where it is thought to play a role in the regulation of protein homeostasis. 4. **Viral Infections**: HSPA8 has been implicated in the regulation of antiviral responses, particularly in the context of viral infections such as RSV. In conclusion, HSPA8 is a critical gene involved in maintaining protein homeostasis, and plays a significant role in the regulation of autophagy, immune responses, and stress responses. Its dysregulation has been implicated in various diseases, including cancer, autoimmune diseases, and neurological disorders. Further research is needed to fully understand the functions and clinical significance of HSPA8.

Genular Protein ID: 846328447

Symbol: HSP7C_HUMAN

Name: Heat shock 70 kDa protein 8

UniProtKB Accession Codes:

P11142 Q9H3R6

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 BRENDA 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 1 CORUM 1 CTD 1 ChEBI 17 ChEMBL 1 ChiTaRS 1 ComplexPortal 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 4 DrugCentral 1 EC 1 EMBL 6 Ensembl 4 EvolutionaryTrace 1 ExpressionAtlas 1 GO 100 Gene3D 3 GeneCards 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 5 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MetOSite 1 MoonDB 1 NCBI Taxonomy 1 OGP 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 38 PDBsum 38 PIR 1 PRIDE 1 PRINTS 1 PRO 1 PROSITE 3 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 2 Pumba 1 REPRODUCTION-2DPAGE 1 RNAct 1 Reactome 19 RefSeq 3 Rhea 1 SASBDB 1 SIGNOR 1 SMR 1 STRING 1 SUPFAM 3 SignaLink 1 SwissPalm 1 TopDownProteomics 2 TreeFam 1 UCSC 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 3037489

Title: Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein.

PubMed ID: 3037489

DOI: 10.1093/nar/15.13.5181

PubMed ID: 11093761

Title: Molecular and functional characterization of HSC54, a novel variant of human heat shock cognate protein 70.

PubMed ID: 11093761

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PubMed ID: 15489334

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PubMed ID: 15489334

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PubMed ID: 1286667

Title: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.

PubMed ID: 1286667

DOI: 10.1002/elps.11501301199

PubMed ID: 8713105

Title: Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes.

PubMed ID: 8713105

DOI: 10.1006/bbrc.1996.1082

PubMed ID: 23349634

Title: A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.

PubMed ID: 23349634

DOI: 10.1371/journal.pgen.1003210

PubMed ID: 2799391

Title: A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins.

PubMed ID: 2799391

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PubMed ID: 1586970

Title: Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.

PubMed ID: 1586970

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PubMed ID: 9305631

Title: BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

PubMed ID: 9305631

DOI: 10.1093/emboj/16.16.4887

PubMed ID: 9679980

Title: Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines.

PubMed ID: 9679980

PubMed ID: 9499401

Title: Molecular chaperones as HSF1-specific transcriptional repressors.

PubMed ID: 9499401

DOI: 10.1101/gad.12.5.654

PubMed ID: 11147964

Title: HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells.

PubMed ID: 11147964

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PubMed ID: 10722728

DOI: 10.1074/jbc.275.12.8825

PubMed ID: 11559757

Title: A molecular chaperone complex at the lysosomal membrane is required for protein translocation.

PubMed ID: 11559757

DOI: 10.1242/jcs.114.13.2491

PubMed ID: 11276205

Title: A CD14-independent LPS receptor cluster.

PubMed ID: 11276205

DOI: 10.1038/86342

PubMed ID: 12526792

Title: Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70.

PubMed ID: 12526792

DOI: 10.1016/s0092-8674(02)01250-3

PubMed ID: 14532270

Title: A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.

PubMed ID: 14532270

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PubMed ID: 14654843

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PubMed ID: 14654843

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PubMed ID: 15708368

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PubMed ID: 15708368

DOI: 10.1016/j.abb.2004.12.020

PubMed ID: 16139798

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PubMed ID: 16139798

DOI: 10.1016/j.bbrc.2005.08.132

PubMed ID: 15963462

Title: Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.

PubMed ID: 15963462

DOI: 10.1016/j.bbrc.2005.05.175

PubMed ID: 15936278

Title: HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome.

PubMed ID: 15936278

DOI: 10.1016/j.cub.2005.04.058

PubMed ID: 15894275

Title: Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens.

PubMed ID: 15894275

DOI: 10.1016/j.immuni.2005.03.009

PubMed ID: 17081065

Title: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

PubMed ID: 17081065

DOI: 10.1021/pr060363j

PubMed ID: 16815975

Title: HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets.

PubMed ID: 16815975

DOI: 10.1073/pnas.0600397103

PubMed ID: 17785435

Title: EWI-2/CD316 is an inducible receptor of HSPA8 on human dendritic cells.

PubMed ID: 17785435

DOI: 10.1128/mcb.00180-07

PubMed ID: 17182002

Title: HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain.

PubMed ID: 17182002

DOI: 10.1016/j.bbrc.2006.12.013

PubMed ID: 17947705

Title: Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase.

PubMed ID: 17947705

DOI: 10.4049/jimmunol.179.9.6291

PubMed ID: 17289661

Title: Molecular composition of IMP1 ribonucleoprotein granules.

PubMed ID: 17289661

DOI: 10.1074/mcp.m600346-mcp200

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18320024

Title: The human TPR protein TTC4 is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells.

PubMed ID: 18320024

DOI: 10.1371/journal.pone.0001737

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19131338

Title: Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation.

PubMed ID: 19131338

DOI: 10.1074/jbc.m805872200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 21150129

Title: A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR.

PubMed ID: 21150129

DOI: 10.1247/csf.10023

PubMed ID: 20053985

Title: Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha.

PubMed ID: 20053985

DOI: 10.1074/jbc.m109.040618

PubMed ID: 20176811

Title: Molecular architecture of the human Prp19/CDC5L complex.

PubMed ID: 20176811

DOI: 10.1128/mcb.01505-09

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21148293

Title: The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508.

PubMed ID: 21148293

DOI: 10.1091/mbc.e10-09-0760

PubMed ID: 23018488

Title: A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins.

PubMed ID: 23018488

DOI: 10.1247/csf.12017

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 24121476

Title: HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.

PubMed ID: 24121476

DOI: 10.4161/auto.26448

PubMed ID: 23865999

Title: The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.

PubMed ID: 23865999

DOI: 10.1021/bi4009209

PubMed ID: 23973223

Title: The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3.

PubMed ID: 23973223

DOI: 10.1016/j.immuni.2013.08.006

PubMed ID: 23921388

Title: Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation.

PubMed ID: 23921388

DOI: 10.1074/jbc.m113.483248

PubMed ID: 23990462

Title: Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase.

PubMed ID: 23990462

DOI: 10.1074/jbc.m113.479345

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24270810

Title: High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.

PubMed ID: 24270810

DOI: 10.1038/nature12748

PubMed ID: 24122553

Title: The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress.

PubMed ID: 24122553

DOI: 10.1007/s12192-013-0471-6

PubMed ID: 24880125

Title: Degradation of AF1Q by chaperone-mediated autophagy.

PubMed ID: 24880125

DOI: 10.1016/j.yexcr.2014.05.013

PubMed ID: 24318877

Title: Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.

PubMed ID: 24318877

DOI: 10.1074/jbc.m113.521997

PubMed ID: 25281747

Title: RING finger protein RNF207, a novel regulator of cardiac excitation.

PubMed ID: 25281747

DOI: 10.1074/jbc.m114.592295

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 24732912

Title: Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure.

PubMed ID: 24732912

DOI: 10.1371/journal.pone.0094322

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25760597

Title: Structural and functional analysis of Hikeshi, a new nuclear transport receptor of Hsp70s.

PubMed ID: 25760597

DOI: 10.1107/s1399004714026881

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27346687

Title: DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to corruption in 60S ribosome subunit maturation.

PubMed ID: 27346687

DOI: 10.1016/j.ajhg.2016.05.002

PubMed ID: 26865365

Title: The human HSP70 family of chaperones: where do we stand?

PubMed ID: 26865365

DOI: 10.1007/s12192-016-0676-6

PubMed ID: 26775844

Title: Salivary protein histatin 3 regulates cell proliferation by enhancing p27(Kip1) and heat shock cognate protein 70 ubiquitination.

PubMed ID: 26775844

DOI: 10.1016/j.bbrc.2016.01.072

PubMed ID: 27474739

Title: Non-canonical interactions between heat shock cognate protein 70 (Hsc70) and Bcl2-associated anthanogene (BAG) co-chaperones are important for client release.

PubMed ID: 27474739

DOI: 10.1074/jbc.m116.742502

PubMed ID: 27708256

Title: ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation.

PubMed ID: 27708256

DOI: 10.1038/ncomms12882

PubMed ID: 28934328

Title: The human VGF-derived bioactive peptide TLQP-21 binds heat shock 71 kDa protein 8 (HSPA8)on the surface of SH-SY5Y cells.

PubMed ID: 28934328

DOI: 10.1371/journal.pone.0185176

PubMed ID: 27916661

Title: Tetrameric assembly of K(+) channels requires ER-located chaperone proteins.

PubMed ID: 27916661

DOI: 10.1016/j.molcel.2016.10.027

PubMed ID: 29601588

Title: ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre-assembly of dynein arms.

PubMed ID: 29601588

DOI: 10.1371/journal.pgen.1007316

PubMed ID: 31748398

Title: The Herpes Simplex Virus 1 Immediate Early Protein ICP22 Is a Functional Mimic of a Cellular J Protein.

PubMed ID: 31748398

DOI: 10.1128/jvi.01564-19

PubMed ID: 33857403

Title: DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.

PubMed ID: 33857403

DOI: 10.1016/j.molcel.2021.03.041

PubMed ID: 35044787

Title: Loss-of-function mutations in the co-chaperone protein BAG5 cause dilated cardiomyopathy requiring heart transplantation.

PubMed ID: 35044787

DOI: 10.1126/scitranslmed.abf3274

PubMed ID: 36586411

Title: Palmitoylation prevents sustained inflammation by limiting NLRP3 inflammasome activation through chaperone-mediated autophagy.

PubMed ID: 36586411

DOI: 10.1016/j.molcel.2022.12.002

PubMed ID: 32671205

Title: A micropeptide encoded by lncRNA MIR155HG suppresses autoimmune inflammation via modulating antigen presentation.

PubMed ID: 32671205

DOI: 10.1126/sciadv.aaz2059

PubMed ID: 19586912

Title: Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering.

PubMed ID: 19586912

DOI: 10.1074/jbc.m109.033894

PubMed ID: 19256508

Title: Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design.

PubMed ID: 19256508

DOI: 10.1021/jm801627a

PubMed ID: 21526763

Title: Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity.

PubMed ID: 21526763

DOI: 10.1021/jm101625x

Sequence Information:

  • Length: 646
  • Mass: 70898
  • Checksum: 9AA27B210730670C
  • Sequence:
    • MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI 
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI 
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN 
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE 
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD

Genular Protein ID: 2970131813

Symbol: Q53HF2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q53HF2

Database IDs:

ARBA 10 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 1 CTD 1 ChEBI 5 DNASU 1 DisGeNET 1 EC 1 EMBL 2 GO 17 Gene3D 2 IntAct 1 InterPro 4 KEGG 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PRINTS 1 PROSITE 3 Pfam 1 RefSeq 2 Rhea 1 SAM 1 SUPFAM 2

Citations:

PubMed ID: 8125298

Title: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.

PubMed ID: 8125298

DOI: 10.1016/0378-1119(94)90802-8

PubMed ID: 9373149

Title: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.

PubMed ID: 9373149

DOI: 10.1016/S0378-1119(97)00411-3

Sequence Information:

  • Length: 493
  • Mass: 53500
  • Checksum: 518CE1F703509AFA
  • Sequence:
    • MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVT TVLIKRNTTI 
PIKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGMPGGMPG GFPGGGAPPS 
GGASSGPTIE EVD

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.