DnaJ homolog

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'''DnaJ homolog subfamily A member 1''' (DnaJA1) is a co-chaperone for HSPA8/Hsc70. DnaJA1 stimulates ATP synthesis and has a role in protein transport into mitochondria<ref>PMID:10816573</ref>.<br />
'''DnaJ homolog subfamily A member 1''' (DnaJA1) is a co-chaperone for HSPA8/Hsc70. DnaJA1 stimulates ATP synthesis and has a role in protein transport into mitochondria<ref>PMID:10816573</ref>.<br />
'''DnaJ homolog subfamily B member 1''' (DnaJB1) interacts with HSP70. DnaJB1 stimulates ATP synthesis and the folding of unfolded proteins mediated by HSPA1A <ref>PMID:24318877</ref>.<br />
'''DnaJ homolog subfamily B member 1''' (DnaJB1) interacts with HSP70. DnaJB1 stimulates ATP synthesis and the folding of unfolded proteins mediated by HSPA1A <ref>PMID:24318877</ref>.<br />
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'''DnaJ homolog subfamily B member 6''' (DnaJB6) acts as co-chaperone of HSP70. <ref>PMID:10954706</ref>.<br />
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'''DnaJ homolog subfamily C member 2''' (DnaJC2) acts as a chaperone for nascent polypeptide chains exiting the ribosome.<br />
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'''DnaJ homolog subfamily C member 3''' (DnaJC3) acts as an inhibitor of the interferon-induced dsRNA-activated protein kinase.<br />
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'''DnaJ homolog subfamily C member 5''' (DnaJC5) acts in membrane trafficking and protein folding.<br />
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'''DnaJ homolog subfamily C member 9''' (DnaJC9) acts as co-chaperone of HSP70. <ref>PMID:17182002</ref>.<br />
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'''DnaJ homolog subfamily C member 10''' (DnaJC10) reduces incorrect disulfide bonds in misfolded glycoproteins.<br />
== Disease ==
== Disease ==
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</StructureSection>
</StructureSection>
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==3D structures of DnaJ homolog==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*DnaJ homolog subfamily A member 1
 
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**[[2lo1]], [[2m6y]] - hDnaJA1 J domain - human - NMR<br />
 
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*DnaJ homolog subfamily A member 3
 
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**[[2dn9]] - hDnaJA3 J domain - NMR<br />
 
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**[[2ctt]] - hDnaJ zinc finger domain - NMR<br />
 
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*DnaJ homolog subfamily B member 1
 
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**[[3agx]], [[2qld]] - hDnaJB1 peptide-binding domain <br />
 
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**[[3agy]], [[3agz]] - hDnaJB1 peptide-binding domain + HSP70 peptide<br />
 
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*DnaJ homolog subfamily B member 2
 
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**[[2lgw]] - hDnaJB2 J domain - NMR<br />
 
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*DnaJ homolog subfamily B member 8
 
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**[[2dmx]] - hDnaJB8 J domain - NMR<br />
 
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*DnaJ homolog subfamily B member 9
 
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**[[2ctr]] - hDnaJB9 J domain - NMR<br />
 
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*DnaJ homolog subfamily B member 12
 
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**[[2ctp]] - hDnaJB12 J domain - NMR<br />
 
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*DnaJ homolog subfamily C member 1
 
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**[[2cqq]], [[2cqr]] - hDnaJC1 DNA-binding domain - NMR<br />
 
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*DnaJ homolog subfamily C member 2
 
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**[[2m2e]] - hDnaJC2 SANT 2 domain residues 551-621 - NMR<br />
 
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**[[6cgh]] - hDnaJC2 residues 346-432- NMR<br />
 
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*DnaJ homolog subfamily C member 3
 
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**[[2y4t]], [[2y4u]] - hDnaJC3 residues 35-461 <br />
 
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**[[3ieg]] - mDnaJC3 TPR domain <br />
 
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*DnaJ homolog subfamily C member 5
 
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**[[2ctw]] - DnaJC5 J domain - mouse - NMR<br />
 
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**[[2n04]], [[2n05]] - hDnaJC5 N terminal domain - NMR<br />
 
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*DnaJ homolog subfamily C member 10
 
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**[[3apo]] - mDnaJC10 <br />
 
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**[[5ayk]], [[5ayl]] - mDnaJC10 (mutant)<br />
 
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**[[3aps]] - hDnaJC10 TRX4 domain <br />
 
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**[[3apq]] - mDnaJC10 TRX4 domain <br />
 
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*DnaJ homolog subfamily C member 12 see Hsp40 in [[Heat Shock Proteins]]
 
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*DnaJ homolog subfamily C member 17
 
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**[[2d9o]] - hDnaJC17 RNA recognition motif 168-254 - NMR<br />
 
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*DnaJ homolog subfamily C member 24
 
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**[[2l6l]] - hDnaJC24 - NMR<br />
 
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*DnaJ homolog subfamily C member 29 or sacsin. Domains: UBL 2-85; SR1 89-336; HEPN 4440-4579
 
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**[[5v44]] - hDnaJC29 Sr1 domain <br />
 
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**[[5v45]], [[5v46]] - hDnaJC29 Sr1 domain (mutant)<br />
 
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**[[5vsx]] - hDnaJC29 UBL domain<br />
 
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**[[5vsz]] - hDnaJC29 UBL domain (mutant)<br />
 
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**[[3o10]] - hDnaJC29 HEPN domain <br />
 
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*DnaJ homolog DnJ-2
 
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**[[2qsa]] - DnaJ-2 J domain - ''Caenorhabditis elegans''<br />
 
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}}
 
== References ==
== References ==

Current revision

Human DnaJ homolog subfamity B member 1 peptide-binding domain dimer (cyan and green) complex with 3 C-terminal peptides of heat shock protein 70 (pink, magenta, violet) (PDB code 3agy)

Drag the structure with the mouse to rotate

References

  1. Terada K, Mori M. Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J Biol Chem. 2000 Aug 11;275(32):24728-34. PMID:10816573 doi:http://dx.doi.org/10.1074/jbc.M002021200
  2. Rauch JN, Gestwicki JE. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J Biol Chem. 2014 Jan 17;289(3):1402-14. doi: 10.1074/jbc.M113.521997. Epub 2013 , Dec 5. PMID:24318877 doi:http://dx.doi.org/10.1074/jbc.M113.521997
  3. Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M. Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein. J Biol Chem. 2000 Nov 3;275(44):34521-7. PMID:10954706 doi:http://dx.doi.org/10.1074/jbc.M003492200
  4. Han C, Chen T, Li N, Yang M, Wan T, Cao X. HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. Biochem Biophys Res Commun. 2007 Feb 9;353(2):280-5. PMID:17182002 doi:10.1016/j.bbrc.2006.12.013
  5. Stark JL, Mehla K, Chaika N, Acton TB, Xiao R, Singh PK, Montelione GT, Powers R. Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer. Biochemistry. 2014 Mar 4;53(8):1360-72. doi: 10.1021/bi401329a. Epub 2014 Feb 19. PMID:24512202 doi:http://dx.doi.org/10.1021/bi401329a
  6. Suzuki H, Noguchi S, Arakawa H, Tokida T, Hashimoto M, Satow Y. Peptide-binding sites as revealed by the crystal structures of the human Hsp40 Hdj1 C-terminal domain in complex with the octapeptide from human Hsp70. Biochemistry. 2010 Oct 5;49(39):8577-84. Epub 2010 Sep 9. PMID:20809635 doi:10.1021/bi100876n

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