Harmonizome 3.0

DnaJ (Hsp40) homolog, subfamily C, member 9 pseudogene

dnaJ homolog subfamily B member 6-like

dnaJ homolog subfamily B member 6-like

DnaJ (Hsp40) homolog, subfamily B, member 14 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 8

DnaJ (Hsp40) homolog, subfamily C, member 9 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 15

Predicted to enable ATPase activator activity. Predicted to be involved in protein import into mitochondrial matrix. Predicted to act upstream of or within several processes, including cellular response to starvation; negative regulation of mitochondrial electron transport, NADH to ubiquinone; and negative regulation of protein-containing complex assembly. Located in mitochondrion. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 16

Involved in regulation of autophagosome size. Located in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 17

Predicted to enable RNA binding activity. Predicted to be involved in spliceosomal complex disassembly. Predicted to act upstream of or within negative regulation of transcription by RNA polymerase II. Predicted to be located in cytoplasm and nucleus. Predicted to be part of spliceosomal complex. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 14

Predicted to enable dopamine receptor binding activity. Predicted to be involved in protein transport. Located in membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 12

This gene encodes a member of a subclass of the HSP40/DnaJ protein family. Members of this family of proteins are associated with complex assembly, protein folding, and export. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]

DnaJ (Hsp40) homolog, subfamily C, member 13

This gene encodes a member of the Dnaj protein family whose members act as co-chaperones of a partner heat-shock protein by binding to the latter and stimulating ATP hydrolysis. The encoded protein associates with the heat-shock protein Hsc70 and plays a role in clathrin-mediated endocytosis. It may also be involved in post-endocytic transport mechanisms via its associations with other proteins, including the sorting nexin SNX1. Mutations in this gene are associated with Parkinson's disease. [provided by RefSeq, Jun 2016]

DnaJ (Hsp40) homolog, subfamily C, member 10

This gene encodes an endoplasmic reticulum co-chaperone which is part of the endoplasmic reticulum-associated degradation complex involved in recognizing and degrading misfolded proteins. The encoded protein reduces incorrect disulfide bonds in misfolded glycoproteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Oct 2012]

DnaJ (Hsp40) homolog, subfamily C, member 11

Involved in cristae formation. Located in MICOS complex; SAM complex; and nuclear speck. Part of MIB complex. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 18

Predicted to enable Hsp70 protein binding activity. Predicted to be involved in cellular response to misfolded protein and chaperone cofactor-dependent protein refolding. Located in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 19

The protein encoded by this gene is thought to be part of a complex involved in the ATP-dependent transport of transit peptide-containing proteins from the inner cell membrane to the mitochondrial matrix. Defects in this gene are a cause of 3-methylglutaconic aciduria type 5 (MGA5), also known as dilated cardiomyopathy with ataxia (DCMA). Alternative splicing of this gene results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 1, 2, 6, 10, 14 and 19. [provided by RefSeq, Jan 2012]

DnaJ (Hsp40) homolog, subfamily B, member 13

This gene encodes a member of the heat shock protein 40 co-chaperone family which is produced in large amounts in the testis and is located on the radial spokes of the axoneme in human sperm flagella and other flagellar structures. The encoded protein associates with the sperm annulus, as part of the septin complex, through direct interaction with septin 4, during sperm terminal differentiation. Naturally occurring mutations in this gene are associated with primary ciliary dyskinesia and male infertility. [provided by RefSeq, Apr 2017]

DnaJ (Hsp40) homolog, subfamily B, member 12

DNAJB12 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata, 2000 [PubMed 11147971]).[supplied by OMIM, Mar 2008]

DnaJ (Hsp40) homolog, subfamily B, member 14

Enables Hsp70 protein binding activity. Involved in chaperone cofactor-dependent protein refolding and protein-containing complex assembly. Located in endoplasmic reticulum. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 28

This gene encodes a member of the DnaJ heat shock protein family. The encoded protein, which contains a conserved N-terminal DnaJ domain, is thought to play a role in protein folding or act as a molecular chaperone protein. [provided by RefSeq, Oct 2016]

DnaJ (Hsp40) homolog, subfamily C, member 27

Predicted to enable GTPase activity. Predicted to be involved in intracellular protein transport. Predicted to be located in cytoplasmic vesicle and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C , member 25

Predicted to be involved in protein folding. Predicted to be located in membrane. Predicted to be active in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 24

Diphthamide is a unique posttranslationally modified histidine found only in translation elongation factor-2 (EEF2; MIM 130610). This modification is conserved from archaebacteria to humans and serves as the target for ADP-ribosylation and inactivation of EEF2 by diphtheria toxin (DT) and Pseudomonas exotoxin A. DPH4 is 1 of several enzymes involved in synthesis of diphthamide in EEF2 (Liu et al., 2004 [PubMed 15485916]).[supplied by OMIM, Mar 2008]

DnaJ (Hsp40) homolog, subfamily C, member 22

Predicted to be active in membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 21

This gene encodes a member of the DNAJ heat shock protein 40 family of proteins that is characterized by two N-terminal tetratricopeptide repeat domains and a C-terminal DNAJ domain. This protein binds the precursor 45S ribosomal RNA and may be involved in early nuclear ribosomal RNA biogenesis and maturation of the 60S ribosomal subunit. Mutations in this gene result in Bone marrow failure syndrome 3. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Feb 2017]

DnaJ (Hsp40) homolog, subfamily B, member 2

This gene is almost exclusively expressed in the brain, mainly in the neuronal layers. It encodes a protein that shows sequence similarity to bacterial DnaJ protein and the yeast homologs. In bacteria, this protein is implicated in protein folding and protein complex dissociation. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Jul 2011]

DnaJ (Hsp40) homolog, subfamily B, member 4

The protein encoded by this gene is a molecular chaperone, tumor suppressor, and member of the heat shock protein-40 family. The encoded protein binds the cell adhesion protein E-cadherin and targets it to the plasma membrane. This protein also binds incorrectly folded E-cadherin and targets it for endoplasmic reticulum-associated degradation. This gene is a strong tumor suppressor for colorectal carcinoma, and downregulation of it may serve as a good biomarker for predicting patient outcomes. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]

DnaJ (Hsp40) homolog, subfamily B, member 9

This gene is a member of the J protein family. J proteins function in many cellular processes by regulating the ATPase activity of 70 kDa heat shock proteins. This gene is a member of the type 2 subgroup of DnaJ proteins. The encoded protein is localized to the endoplasmic reticulum. This protein is induced by endoplasmic reticulum stress and plays a role in protecting stressed cells from apoptosis. [provided by RefSeq, Dec 2010]

DnaJ (Hsp40) homolog, subfamily B, member 8

The protein encoded by this gene belongs to the DNAJ/HSP40 family of proteins that regulate chaperone activity. This family member suppresses aggregation and toxicity of polyglutamine proteins, and the C-terminal tail is essential for this activity. It has been implicated as a cancer-testis antigen and as a cancer stem-like cell antigen involved in renal cell carcinoma. [provided by RefSeq, Jun 2012]

DnaJ (Hsp40) homolog, subfamily B, member 3

Predicted to enable Hsp70 protein binding activity and unfolded protein binding activity. Predicted to be involved in chaperone-mediated protein folding. Predicted to be located in acrosomal vesicle and centrosome. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily B, member 1

This gene encodes a member of the DnaJ or Hsp40 (heat shock protein 40 kD) family of proteins. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. The encoded protein is a molecular chaperone that stimulates the ATPase activity of Hsp70 heat-shock proteins in order to promote protein folding and prevent misfolded protein aggregation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]

DnaJ (Hsp40) homolog, subfamily B, member 7

The protein encoded by this intronless gene belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain.[provided by RefSeq, Mar 2011]

DnaJ (Hsp40) homolog, subfamily B, member 6

This gene encodes a member of the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described. [provided by RefSeq, Jul 2008]

DnaJ (Hsp40) homolog, subfamily B, member 5

This gene encodes a member of the DNAJ heat shock protein 40 family of co-chaperone proteins. The encoded protein contains an N-terminal DNAJ domain and a C-terminal substrate binding domain but lacks the cysteine-rich domain found in other DNAJ family members. In mice, a multi-protein complex containing this protein, thioredoxin 1, and histone deacetylase 4, serves as a master negative regulator of cardiac hypertrophy. [provided by RefSeq, Mar 2017]

DnaJ (Hsp40) homolog, subfamily C, member 2 pseudogene

DnaJ (Hsp40) homolog, subfamily A, member 1 pseudogene 5

DnaJ (Hsp40) homolog, subfamily A, member 1 pseudogene 4

DnaJ (Hsp40) homolog, subfamily A, member 1 pseudogene 6

DnaJ (Hsp40) homolog, subfamily A, member 1 pseudogene 1

DnaJ (Hsp40) homolog, subfamily A, member 1 pseudogene 3

DnaJ (Hsp40) homolog, subfamily A, member 1 pseudogene 2

DnaJ (Hsp40) homolog, subfamily B, member 12 pseudogene

DnaJ (Hsp40) homolog, subfamily A, member 2

The protein encoded by this gene belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain. The product of this gene works as a cochaperone of Hsp70s in protein folding and mitochondrial protein import in vitro. [provided by RefSeq, Jul 2008]

DnaJ (Hsp40) homolog, subfamily A, member 3

This gene encodes a member of the DNAJ/Hsp40 protein family. DNAJ/Hsp40 proteins stimulate the ATPase activity of Hsp70 chaperones and play critical roles in protein folding, degradation, and multimeric complex assembly. The encoded protein is localized to mitochondria and mediates several cellular processes including proliferation, survival and apoptotic signal transduction. The encoded protein also plays a critical role in tumor suppression through interactions with oncogenic proteins including ErbB2 and the p53 tumor suppressor protein. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Aug 2011]

DnaJ (Hsp40) homolog, subfamily A, member 1

This gene encodes a member of the DnaJ family of proteins, which act as heat shock protein 70 cochaperones. Heat shock proteins facilitate protein folding, trafficking, prevention of aggregation, and proteolytic degradation. Members of this family are characterized by a highly conserved N-terminal J domain, a glycine/phenylalanine-rich region, four CxxCxGxG zinc finger repeats, and a C-terminal substrate-binding domain. The J domain mediates the interaction with heat shock protein 70 to recruit substrates and regulate ATP hydrolysis activity. In humans, this gene has been implicated in positive regulation of virus replication through co-option by the influenza A virus. Several pseudogenes of this gene are found on other chromosomes. [provided by RefSeq, Sep 2015]

DnaJ (Hsp40) homolog, subfamily A, member 4

Enables protein-folding chaperone binding activity and unfolded protein binding activity. Involved in several processes, including negative regulation of endothelial cell migration; negative regulation of inclusion body assembly; and protein refolding. Located in cytosol and membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily B, member 11

This gene encodes a soluble glycoprotein of the endoplasmic reticulum (ER) lumen that functions as a co-chaperone of binding immunoglobulin protein, a 70 kilodalton heat shock protein chaperone required for the proper folding and assembly of proteins in the ER. The encoded protein contains a highly conserved J domain of about 70 amino acids with a characteristic His-Pro-Asp (HPD) motif and may regulate the activity of binding immunoglobulin protein by stimulating ATPase activity. [provided by RefSeq, Mar 2014]

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 3

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 2

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 5

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 7

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 6

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 9

DnaJ (Hsp40) homolog, subfamily C, member 1

The membrane protein encoded by this gene is a DNAJ-like heat shock protein that binds the molecular chaperone BiP. In addition, the encoded protein contains two SANT domains that have been shown to bind serpin alpha1-antichymotrypsin and inter-alpha trypsin inhibitor heavy chain 4. [provided by RefSeq, Jul 2016]

DnaJ (Hsp40) homolog, subfamily C, member 17 pseudogene

dnaJ homolog subfamily C member 24 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 8 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 7 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 8 pseudogene 1

DnaJ (Hsp40) homolog, subfamily B, member 1 pseudogene 1

DnaJ (Hsp40) homolog, subfamily B, member 7 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 5 beta

This gene encodes a member of the DNAJ heat shock protein 40 family of co-chaperone proteins that is characterized by an N-terminal DNAJ domain, a linker region, and a cysteine-rich C-terminal domain. The encoded protein, together with heat shock protein 70, is thought to regulate the proper folding of other proteins. The orthologous mouse protein is membrane-associated and is targeted to the trans-golgi network. [provided by RefSeq, Mar 2017]

DnaJ (Hsp40) homolog, subfamily C, member 5 gamma

Predicted to be located in cytoplasm and membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 7 pseudogene

DnaJ (Hsp40) homolog, subfamily B, member 7 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 8

Enables Hsp70 protein binding activity. Located in cytosol; intercellular bridge; and nucleoplasm. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 9

Enables heat shock protein binding activity; histone binding activity; and protein-folding chaperone binding activity. Involved in nucleosome assembly and positive regulation of ATP-dependent activity. Located in several cellular components, including cytosol; extracellular space; and nucleoplasm. Part of protein folding chaperone complex. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 4

Predicted to enable unfolded protein binding activity. Predicted to be involved in protein folding and response to unfolded protein. Predicted to be located in membrane. [provided by Alliance of Genome Resources, Mar 2025]

DnaJ (Hsp40) homolog, subfamily C, member 5

This gene is a member of the J protein family. J proteins function in many cellular processes by regulating the ATPase activity of 70 kDa heat shock proteins. The encoded protein plays a role in membrane trafficking and protein folding, and has been shown to have anti-neurodegenerative properties. The encoded protein is known to play a role in cystic fibrosis and Huntington's disease. A pseudogene of this gene is located on the short arm of chromosome 8. [provided by RefSeq, Nov 2010]

DnaJ (Hsp40) homolog, subfamily C, member 6

DNAJC6 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus, a glycine/phenylalanine (G/F)-rich region, and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata, 2000 [PubMed 11147971]).[supplied by OMIM, Mar 2008]

DnaJ (Hsp40) homolog, subfamily C, member 7

This gene encodes a member of the DNAJ heat shock protein 40 family of proteins that is characterized by two N-terminal tetratricopeptide repeat domains and a C-terminal DNAJ domain. This protein binds the chaperone proteins heat shock proteins 70 and 90 in an ATP-dependent manner and may function as a co-chaperone. Pseudogenes of this gene are found on chromosomes 1 and 6. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Oct 2009]

DnaJ (Hsp40) homolog, subfamily C, member 2

This gene is a member of the M-phase phosphoprotein (MPP) family. The gene encodes a phosphoprotein with a J domain and a Myb DNA-binding domain which localizes to both the nucleus and the cytosol. The protein is capable of forming a heterodimeric complex that associates with ribosomes, acting as a molecular chaperone for nascent polypeptide chains as they exit the ribosome. This protein was identified as a leukemia-associated antigen and expression of the gene is upregulated in leukemic blasts. Also, chromosomal aberrations involving this gene are associated with primary head and neck squamous cell tumors. This gene has a pseudogene on chromosome 6. Alternatively spliced variants which encode different protein isoforms have been described. [provided by RefSeq, Jul 2008]

DnaJ (Hsp40) homolog, subfamily C, member 3

This gene encodes a protein with multiple tetratricopeptide repeat (TPR) motifs as well as the highly conserved J domain found in DNAJ chaperone family members. It is a member of the tetratricopeptide repeat family of proteins and acts as an inhibitor of the interferon-induced, dsRNA-activated protein kinase (PKR). [provided by RefSeq, Jul 2010]

DnaJ (Hsp40) homolog, subfamily B, member 5 pseudogene 1

DnaJ (Hsp40) homolog, subfamily B, member 3 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 5 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 8 pseudogene

DnaJ (Hsp40) homolog, subfamily B, member 7 pseudogene

dnaJ homolog subfamily B member 6-like

DnaJ (Hsp40) homolog, subfamily B, member 7 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 8 pseudogene

DnaJ (Hsp40) homolog, subfamily C, member 19 pseudogene 1

DnaJ (Hsp40) homolog, subfamily C, member 17 pseudogene

dnaJ homolog subfamily B member 6-like

DnaJ (Hsp40) homolog, subfamily C, member 30

This intronless gene encodes a member of the DNAJ molecular chaperone homology domain-containing protein family. This gene is deleted in Williams syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at 7q11.23. [provided by RefSeq, Jul 2008]

dnaJ homolog subfamily B member 6-like