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)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: thyroid follicular cell (CL0002258)
    Fold Change: 4.95
    Marker Score: 3878
  • Cell Name: mature T cell (CL0002419)
    Fold Change: 4.61
    Marker Score: 45668
  • Cell Name: mature alpha-beta T cell (CL0000791)
    Fold Change: 4.25
    Marker Score: 224915
  • Cell Name: mature gamma-delta T cell (CL0000800)
    Fold Change: 4.24
    Marker Score: 13366
  • Cell Name: NKp46-positive innate lymphoid cell, human (CL0001076)
    Fold Change: 4.13
    Marker Score: 12052.5
  • Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
    Fold Change: 3.88
    Marker Score: 3309
  • Cell Name: double negative T regulatory cell (CL0011024)
    Fold Change: 3.85
    Marker Score: 3725
  • Cell Name: alpha-beta T cell (CL0000789)
    Fold Change: 3.84
    Marker Score: 2905
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 3.82
    Marker Score: 4609
  • Cell Name: radial glial cell (CL0000681)
    Fold Change: 3.81
    Marker Score: 1404
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 3.81
    Marker Score: 4065.5
  • Cell Name: T-helper 22 cell (CL0001042)
    Fold Change: 3.74
    Marker Score: 16049
  • Cell Name: type I NK T cell (CL0000921)
    Fold Change: 3.74
    Marker Score: 2934
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 3.72
    Marker Score: 126493
  • Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
    Fold Change: 3.71
    Marker Score: 10404
  • Cell Name: naive T cell (CL0000898)
    Fold Change: 3.7
    Marker Score: 2383
  • Cell Name: malignant cell (CL0001064)
    Fold Change: 3.69
    Marker Score: 49515
  • Cell Name: myeloid leukocyte (CL0000766)
    Fold Change: 3.65
    Marker Score: 4405
  • Cell Name: glycinergic amacrine cell (CL4030028)
    Fold Change: 3.65
    Marker Score: 3441
  • Cell Name: mesenchymal stem cell (CL0000134)
    Fold Change: 3.63
    Marker Score: 5595
  • Cell Name: naive thymus-derived CD4-positive, alpha-beta T cell (CL0000895)
    Fold Change: 3.62
    Marker Score: 6210
  • Cell Name: activated CD8-positive, alpha-beta T cell (CL0000906)
    Fold Change: 3.6
    Marker Score: 2613
  • Cell Name: central memory CD8-positive, alpha-beta T cell (CL0000907)
    Fold Change: 3.58
    Marker Score: 8722
  • Cell Name: blood cell (CL0000081)
    Fold Change: 3.57
    Marker Score: 41531.5
  • Cell Name: naive thymus-derived CD8-positive, alpha-beta T cell (CL0000900)
    Fold Change: 3.57
    Marker Score: 6378
  • Cell Name: decidual natural killer cell, human (CL0002343)
    Fold Change: 3.54
    Marker Score: 9788
  • Cell Name: natural T-regulatory cell (CL0000903)
    Fold Change: 3.45
    Marker Score: 1773.5
  • Cell Name: intraepithelial lymphocyte (CL0002496)
    Fold Change: 3.42
    Marker Score: 3800.5
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 3.42
    Marker Score: 22239.5
  • Cell Name: CD4-positive, alpha-beta memory T cell (CL0000897)
    Fold Change: 3.41
    Marker Score: 2000
  • Cell Name: effector memory CD8-positive, alpha-beta T cell, terminally differentiated (CL0001062)
    Fold Change: 3.41
    Marker Score: 5018
  • Cell Name: effector CD8-positive, alpha-beta T cell (CL0001050)
    Fold Change: 3.39
    Marker Score: 2854
  • Cell Name: granulocyte (CL0000094)
    Fold Change: 3.38
    Marker Score: 1517
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 3.36
    Marker Score: 29498
  • Cell Name: mucosal invariant T cell (CL0000940)
    Fold Change: 3.35
    Marker Score: 2980
  • Cell Name: skeletal muscle satellite cell (CL0000594)
    Fold Change: 3.33
    Marker Score: 2230
  • Cell Name: CD8-alpha alpha positive, gamma-delta intraepithelial T cell (CL0000802)
    Fold Change: 3.33
    Marker Score: 1083
  • Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
    Fold Change: 3.32
    Marker Score: 2816
  • Cell Name: mesodermal cell (CL0000222)
    Fold Change: 3.31
    Marker Score: 43645
  • Cell Name: class switched memory B cell (CL0000972)
    Fold Change: 3.3
    Marker Score: 3107
  • Cell Name: activated CD4-positive, alpha-beta T cell (CL0000896)
    Fold Change: 3.3
    Marker Score: 2386
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 3.25
    Marker Score: 7935
  • Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
    Fold Change: 3.23
    Marker Score: 28023
  • Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
    Fold Change: 3.22
    Marker Score: 4561
  • Cell Name: CD4-positive, alpha-beta cytotoxic T cell (CL0000934)
    Fold Change: 3.21
    Marker Score: 2820
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 3.18
    Marker Score: 760.5
  • Cell Name: DN3 thymocyte (CL0000807)
    Fold Change: 3.17
    Marker Score: 1582.5
  • Cell Name: naive B cell (CL0000788)
    Fold Change: 3.17
    Marker Score: 2827.5
  • Cell Name: chondrocyte (CL0000138)
    Fold Change: 3.15
    Marker Score: 1419
  • Cell Name: memory B cell (CL0000787)
    Fold Change: 3.15
    Marker Score: 2380
  • Cell Name: T follicular helper cell (CL0002038)
    Fold Change: 3.09
    Marker Score: 2565
  • Cell Name: erythroid progenitor cell (CL0000038)
    Fold Change: 3.09
    Marker Score: 3221.5
  • Cell Name: germinal center B cell (CL0000844)
    Fold Change: 3.07
    Marker Score: 1869
  • Cell Name: effector CD4-positive, alpha-beta T cell (CL0001044)
    Fold Change: 3.06
    Marker Score: 2864
  • Cell Name: basal cell of epithelium of trachea (CL1000348)
    Fold Change: 3.02
    Marker Score: 22458
  • Cell Name: CD16-negative, CD56-bright natural killer cell, human (CL0000938)
    Fold Change: 3.01
    Marker Score: 2467
  • Cell Name: kidney loop of Henle epithelial cell (CL1000909)
    Fold Change: 3.01
    Marker Score: 1885
  • Cell Name: exhausted T cell (CL0011025)
    Fold Change: 3.01
    Marker Score: 1729
  • Cell Name: double-positive, alpha-beta thymocyte (CL0000809)
    Fold Change: 3
    Marker Score: 5881
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: 3
    Marker Score: 2998
  • Cell Name: GABAergic amacrine cell (CL4030027)
    Fold Change: 2.99
    Marker Score: 6082
  • Cell Name: theca cell (CL0000503)
    Fold Change: 2.98
    Marker Score: 2132.5
  • Cell Name: CD4-positive, alpha-beta T cell (CL0000624)
    Fold Change: 2.97
    Marker Score: 6693
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 2.97
    Marker Score: 2662.5
  • Cell Name: regulatory T cell (CL0000815)
    Fold Change: 2.96
    Marker Score: 3278
  • Cell Name: CD8-positive, alpha-beta cytotoxic T cell (CL0000794)
    Fold Change: 2.96
    Marker Score: 2610
  • Cell Name: squamous epithelial cell (CL0000076)
    Fold Change: 2.96
    Marker Score: 2016
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 2.96
    Marker Score: 4704
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 2.96
    Marker Score: 8771
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 2.95
    Marker Score: 10467.5
  • Cell Name: CD4-positive, CD25-positive, alpha-beta regulatory T cell (CL0000792)
    Fold Change: 2.95
    Marker Score: 782
  • Cell Name: CD4-positive helper T cell (CL0000492)
    Fold Change: 2.94
    Marker Score: 3197
  • Cell Name: memory T cell (CL0000813)
    Fold Change: 2.93
    Marker Score: 1261
  • Cell Name: hematopoietic cell (CL0000988)
    Fold Change: 2.93
    Marker Score: 1949.5
  • Cell Name: Sertoli cell (CL0000216)
    Fold Change: 2.93
    Marker Score: 17351
  • Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
    Fold Change: 2.91
    Marker Score: 4211
  • Cell Name: renal intercalated cell (CL0005010)
    Fold Change: 2.91
    Marker Score: 1551
  • Cell Name: B-1 B cell (CL0000819)
    Fold Change: 2.91
    Marker Score: 5069
  • Cell Name: Unknown (CL0000548)
    Fold Change: 2.91
    Marker Score: 2118
  • Cell Name: effector memory CD4-positive, alpha-beta T cell (CL0000905)
    Fold Change: 2.9
    Marker Score: 2124
  • Cell Name: medullary thymic epithelial cell (CL0002365)
    Fold Change: 2.9
    Marker Score: 4752.5
  • Cell Name: bronchial epithelial cell (CL0002328)
    Fold Change: 2.89
    Marker Score: 765.5
  • Cell Name: effector memory CD8-positive, alpha-beta T cell (CL0000913)
    Fold Change: 2.88
    Marker Score: 1774
  • Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
    Fold Change: 2.88
    Marker Score: 1807
  • Cell Name: capillary endothelial cell (CL0002144)
    Fold Change: 2.88
    Marker Score: 3093
  • Cell Name: oogonial cell (CL0000024)
    Fold Change: 2.87
    Marker Score: 4124
  • Cell Name: alternatively activated macrophage (CL0000890)
    Fold Change: 2.87
    Marker Score: 1195
  • Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
    Fold Change: 2.87
    Marker Score: 5585.5
  • Cell Name: gamma-delta T cell (CL0000798)
    Fold Change: 2.87
    Marker Score: 1928
  • Cell Name: DN1 thymic pro-T cell (CL0000894)
    Fold Change: 2.86
    Marker Score: 888
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: 2.86
    Marker Score: 3273
  • Cell Name: late pro-B cell (CL0002048)
    Fold Change: 2.84
    Marker Score: 3351
  • Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
    Fold Change: 2.84
    Marker Score: 1182
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 2.83
    Marker Score: 18122.5
  • Cell Name: ependymal cell (CL0000065)
    Fold Change: 2.82
    Marker Score: 984
  • Cell Name: skin fibroblast (CL0002620)
    Fold Change: 2.82
    Marker Score: 731.5
  • Cell Name: pro-B cell (CL0000826)
    Fold Change: 2.82
    Marker Score: 2719
  • Cell Name: CD8-positive, alpha-beta thymocyte (CL0000811)
    Fold Change: 2.82
    Marker Score: 1554
  • Cell Name: adipocyte of epicardial fat of left ventricle (CL1000311)
    Fold Change: 2.81
    Marker Score: 740.5
  • Cell Name: unswitched memory B cell (CL0000970)
    Fold Change: 2.81
    Marker Score: 1646

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Other Information

**Key characteristics:** * HSPA8 is a chaperone protein that helps to maintain the proper folding and stability of other proteins. * It is a member of the HSP70 family of heat shock proteins, which are induced in response to stress conditions. * HSPA8 is a key regulator of autophagy, a process by which cells selectively degrade their own components to maintain cellular homeostasis. * It is also involved in the regulation of cell cycle progression, apoptosis (programmed cell death), and inflammation. * HSPA8 is a key regulator of the immune system, where it plays a role in the activation and regulation of immune cells. **Pathways and functions:** * HSPA8 is involved in the regulation of autophagy. It is a key regulator of the clearance of damaged or dysfunctional proteins and organelles by promoting the initiation and execution of autophagy. * It is also involved in the regulation of cell cycle progression, where it helps to prevent the initiation of cell cycle arrest or senescence in response to stress conditions. * HSPA8 is also involved in the regulation of inflammation. It is a key regulator of the production of inflammatory cytokines and chemokines, and it helps to promote the migration of immune cells to sites of inflammation. * In addition to its role in inflammation, HSPA8 is also involved in the regulation of cell cycle progression, apoptosis, and senescence. **Clinical significance:** * Mutations in HSPA8 have been linked to a number of human diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. * Overexpression of HSPA8 has been linked to the development of cancer, while decreased expression has been linked to the progression of neurodegenerative diseases. * Inhibition of HSPA8 has been shown to inhibit autophagy and promote cell death, suggesting that it may be a potential therapeutic target for cancer and neurodegenerative diseases. **Additional information:** * HSPA8 is a highly conserved protein that is found in all eukaryotic cells. * It is a member of the HSP70 family of heat shock proteins, which are induced in response to a variety of stress conditions, including heat, oxidative stress, and hypoxia. * HSPA8 is a well-documented regulator of autophagy. It is induced by a variety of stress conditions, including heat, oxidative stress, and nutrient deprivation. * It acts as a chaperone protein that helps to maintain the proper folding and stability of other proteins. * It is also involved in the regulation of cell cycle progression, apoptosis, and inflammation.

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 10 ChEMBL 1 ChiTaRS 1 ComplexPortal 1 DIP 1 DMDM 1 DNASU 1 DOSAC-COBS-2DPAGE 1 DisGeNET 1 DrugBank 4 DrugCentral 1 EC 1 EMBL 6 EPD 1 Ensembl 4 EvolutionaryTrace 1 ExpressionAtlas 1 GO 69 Gene3D 3 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 2 HOGENOM 1 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 5 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MaxQB 1 MetOSite 1 MoonDB 1 NCBI Taxonomy 1 OGP 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 45 PDBsum 38 PIR 1 PRIDE 1 PRO 1 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 18 RefSeq 3 Rhea 1 SASBDB 1 SIGNOR 1 SMR 1 STRING 1 SWISS-2DPAGE 1 SignaLink 1 SwissPalm 1 TopDownProteomics 2 TreeFam 1 UCD-2DPAGE 1 UCSC 1 UniProtKB 4 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

DOI: 10.1124/mol.58.6.1257

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

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

DOI: 10.1126/science.2799391

PubMed ID: 1586970

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

PubMed ID: 1586970

DOI: 10.1247/csf.17.77

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

DOI: 10.1379/1466-1268(2000)005<0132:hiwsvp>2.0.co;2

PubMed ID: 10722728

Title: The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors.

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

DOI: 10.1074/jbc.m309655200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15708368

Title: Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions.

PubMed ID: 15708368

DOI: 10.1016/j.abb.2004.12.020

PubMed ID: 16139798

Title: Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.

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: 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 6 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 1 CTD 1 DNASU 1 EMBL 2 GO 2 Gene3D 2 Genevisible 1 GenomeRNAi 1 IntAct 1 InterPro 4 KEGG 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PRINTS 1 PROSITE 3 Pfam 1 RefSeq 2 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. For the full schema, download it here.