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Showing Protein DnaJ homolog subfamily A member 1 (HMDBP12599)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP12599
Secondary Accession Numbers None
Name DnaJ homolog subfamily A member 1
Synonyms
  1. DnaJ-like protein 1
  2. Heat shock protein J2
  3. HSJ-2
Gene Name DNAJA1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed:10816573).
Pathways
  • Protein processing in endoplasmic reticulum
Reactions Not Available
GO Classification
Biological Process
negative regulation of protein ubiquitination
toxin transport
regulation of protein transport
protein localization to mitochondrion
negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway
negative regulation of establishment of protein localization to mitochondrion
DNA damage response, detection of DNA damage
androgen receptor signaling pathway
response to heat
negative regulation of JUN kinase activity
sperm motility
negative regulation of apoptotic process
positive regulation of apoptotic process
spermatogenesis
protein folding
Cellular Component
endoplasmic reticulum
microtubule cytoskeleton
cytosol
perinuclear region of cytoplasm
membrane
mitochondrion
nucleus
Molecular Function
low-density lipoprotein particle receptor binding
metal ion binding
ATP binding
ubiquitin protein ligase binding
Tat protein binding
G protein-coupled receptor binding
C3HC4-type RING finger domain binding
ATPase activator activity
unfolded protein binding
Hsp70 protein binding
chaperone binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 397
Molecular Weight 44867.99
Theoretical pI 7.078
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P63036
UniProtKB/Swiss-Prot Entry Name DNJA1_RAT
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Lundby A, Secher A, Lage K, Nordsborg NB, Dmytriyev A, Lundby C, Olsen JV: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun. 2012 Jun 6;3:876. doi: 10.1038/ncomms1871. [PubMed:22673903 ]
  3. 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. doi: 10.1074/jbc.M002021200. [PubMed:10816573 ]
  4. Leng CH, Brodsky JL, Wang C: Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein. Protein Sci. 1998 May;7(5):1186-94. doi: 10.1002/pro.5560070513. [PubMed:9605323 ]