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0DNJA3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameDNAJA3
DescriptionDnaj homolog subfamily a member 3, mitochondrial precursor (tumorous imaginal discs protein tid56 homolog) (dnaj protein tid-1) (htid-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005759 mitochondrial matrix (IDA)
0051082 unfolded protein binding (TAS)
0006457 protein folding (TAS)
0042981 regulation of apoptosis (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding.ydrolysis.nd ADP release by an N-terminal ATP-hydrolizing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK.nd acts as a nucleotide exchange factor.timulating the rate of ADP release 5000-fold . DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone.naJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.Besides stimulating the ATPase activity of DnaK through its J-domain.naJ also associates with unfolded polypeptide chains and prevents their aggregation . Thus.naK and DnaJ may bind to one and the same polypeptide chain to form a ternary complex. The formation of a ternary complex may result in cis-interaction of the J-domain of DnaJ with the ATPase domain of DnaK. An unfolded polypeptide may enter the chaperone cycle by associating first either with ATP-liganded DnaK or with DnaJ. DnaK interacts with both the backbone and side chains of a peptide substrate; it thus shows binding polarity and admits only L-peptide segments. In contrast.naJ has been shown to bind both L- and D-peptides and is assumed to interact only with the side chains of the substrate. This domain consists of the C-terminal region of the DnaJ protein. Although the function of this region is unknown.t is always found associated with and .
  IPR002939:Chaperone DnaJ, C-terminal
The prokaryotic heat shock protein DnaJ interacts with the chaperone hsp70-like DnaK protein . Structurally.he DnaJ protein consists of an N-terminal conserved domain (called J domain) of about 70 amino acids. glycine-rich region (G domain) of about 30 residues. central domain containing four repeats of a CXXCXGXG motif (CRR domain) and a C-terminal region of 120 to 170 residues.Such a structure is shown in the following schematic representation:It is thought that the J domain of DnaJ mediates the interaction with the dnaK protein and consists of four helices.he second of which has a charged surface that includes at least one pair of basic residues that are essential for interaction with the ATPase domain of Hsp70. The J- and CRR-domains are found in many prokaryotic and eukaryotic proteins .ither together or separately. In yeast.-domains have been classified into 3 groups; the class III proteins are functionally distinct and do not appear to act as molecular chaperones .
  IPR001623:Heat shock protein DnaJ, N-terminal
Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding.ydrolysis.nd ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK.nd acts as a nucleotide exchange factor.timulating the rate of ADP release 5000-fold . DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone.naJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.Besides stimulating the ATPase activity of DnaK through its J-domain.naJ also associates with unfolded polypeptide chains and prevents their aggregation . Thus.naK and DnaJ may bind to one and the same polypeptide chain to form a ternary complex. The formation of a ternary complex may result in cis-interaction of the J-domain of DnaJ with the ATPase domain of DnaK. An unfolded polypeptide may enter the chaperone cycle by associating first either with ATP-liganded DnaK or with DnaJ. DnaK interacts with both the backbone and side chains of a peptide substrate; it thus shows binding polarity and admits only L-peptide segments. In contrast.naJ has been shown to bind both L- and D-peptides and is assumed to interact only with the side chains of the substrate.
  IPR001305:DnaJ central region
Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding.ydrolysis.nd ADP release by an N-terminal ATP-hydrolizing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK.nd acts as a nucleotide exchange factor.timulating the rate of ADP release 5000-fold . DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone.naJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.Besides stimulating the ATPase activity of DnaK through its J-domain.naJ also associates with unfolded polypeptide chains and prevents their aggregation . Thus.naK and DnaJ may bind to one and the same polypeptide chain to form a ternary complex. The formation of a ternary complex may result in cis-interaction of the J-domain of DnaJ with the ATPase domain of DnaK. An unfolded polypeptide may enter the chaperone cycle by associating first either with ATP-liganded DnaK or with DnaJ. DnaK interacts with both the backbone and side chains of a peptide substrate; it thus shows binding polarity and admits only L-peptide segments. In contrast.naJ has been shown to bind both L- and D-peptides and is assumed to interact only with the side chains of the substrate.DnaJ comprises a 70-residue N-terminal domain (the J-domain); a 30-residue glycine-rich region (the G-domain); a central domain containing 4 repeats of a CxxCxGxG motif (the CRR-domain); and a 120-170 residue C-terminal region. The J- and CRR-domains are found in many prokaryotic and eukaryotic proteins .ither together or separately.
  IPR003095:Heat shock protein DnaJ
The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at intermediate stages of folding.ssembly.nd translocation across membranes . Binding of protein substrates to the DnaK C-terminal domain is controlled by ATP binding and hydrolysis in the N-terminal ATPase domain. The interaction of DnaJ with DnaK is mediated at least in part by the highly conserved N-terminal J-domain of DnaJ. The J-domain interaction is localized to the ATPase domain of DnaK and is likely to be dominated by electrostatic interactions. J-domain may tether DnaK to DnaJ-bound substrates.hich DnaK then binds with its C-terminal peptide-binding domain. The peptide-binding domain of DnaJ is comprised of a beta sandwich made up of 6 beta-strands divided into 2 sheets.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008971:HSP40/DnaJ peptide-binding
IPR002939:DnaJ_C 
Evalue:-39.3098030090332 
Location:307-428IPR001623:DnaJ 
Evalue:-38.9586067199707 
Location:93-155IPR001305:DnaJ_CXXCXGXG 
Evalue:-18.9208183288574 
Location:223-303
SequencesProtein: DNJA3_HUMAN (480 aa)
mRNA: NM_005147
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 71 residues, 4415882-4416094Exon2: 46 residues, 4424385-4424519Exon3: 30 residues, 4427403-4427487Exon4: 69 residues, 4431376-4431577Exon5: 53 residues, 4432269-4432422Exon6: 51 residues, 4433018-4433166Exon7: 23 residues, 4434665-4434730Exon8: 45 residues, 4436887-4437016Exon9: 40 residues, 4438734-4438850Exon10: 34 residues, 4440401-4440499Exon11: 41 residues, 4444812-4444929Exon12: 411 residues, 4445547-4446774Exon13: 2 residues, -Jump to DNJA3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2921 4415882-4446774 ~-31K 13438(DNAJA3)(+)Loci: 2922 4466446-4500348 ~-34K 13441(HMOX2)(+)Loci: 4208 4872508-4927137 ~-55K 13462(PPL)(-)Loci: 4207 4247192-4262891 ~-16K 13431(TFAP4)(-)Link out to UCSC