DNAJA2
From Wikipedia, the free encyclopedia
DnaJ (Hsp40) homolog, subfamily A, member 2
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Identifiers | ||||||||||||||
Symbol(s) | DNAJA2; CPR3; DJA2; DNAJ; DNJ3; HIRIP4; PRO3015; RDJ2 | |||||||||||||
External IDs | MGI: 1931882 HomoloGene: 21193 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 10294 | 56445 | ||||||||||||
Ensembl | ENSG00000069345 | ENSMUSG00000031701 | ||||||||||||
Uniprot | O60884 | Q3TFF0 | ||||||||||||
Refseq | NM_005880 (mRNA) NP_005871 (protein) |
NM_019794 (mRNA) NP_062768 (protein) |
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Location | Chr 16: 45.55 - 45.57 Mb | Chr 8: 88.43 - 88.45 Mb | ||||||||||||
Pubmed search | [1] | [2] |
DnaJ (Hsp40) homolog, subfamily A, member 2, also known as DNAJA2, is a human gene.[1]
The protein encoded by this gene shares sequence similarity with Hir1p and Hir2p, the two corepressors of histone gene transcription characterized in the yeast, Saccharomyces cerevisiae. The structural features of this protein suggest that it may function as part of a multiprotein complex. Several cDNAs encoding interacting proteins, HIRIPs, have been identified. HIRIP4 was isolated by virtue of its interaction with this protein; however, its exact function is not known. The sequence of HIRIP4 protein is highly homologous to the human DNJ3/CPR3, mouse Dj3 and rat Dj2 gene products.[1]
[edit] References
[edit] Further reading
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
- Edwards MC, Liegeois N, Horecka J, et al. (1998). "Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells.". Genetics 147 (3): 1063–76. PMID 9383053.
- Lorain S, Quivy JP, Monier-Gavelle F, et al. (1998). "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA.". Mol. Cell. Biol. 18 (9): 5546–56. PMID 9710638.
- Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma.". Int. J. Cancer 83 (4): 456–64. PMID 10508479.
- Diefenbach J, Kindl H (2000). "The membrane-bound DnaJ protein located at the cytosolic site of glyoxysomes specifically binds the cytosolic isoform 1 of Hsp70 but not other Hsp70 species.". Eur. J. Biochem. 267 (3): 746–54. PMID 10651811.
- Terada K, Mori M (2000). "Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70.". J. Biol. Chem. 275 (32): 24728–34. doi: . PMID 10816573.
- Ohtsuka K, Hata M (2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.". Cell Stress Chaperones 5 (2): 98–112. PMID 11147971.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Willingham S, Outeiro TF, DeVit MJ, et al. (2003). "Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein.". Science 302 (5651): 1769–72. doi: . PMID 14657499.
- Kho Y, Kim SC, Jiang C, et al. (2004). "A tagging-via-substrate technology for detection and proteomics of farnesylated proteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (34): 12479–84. doi: . PMID 15308774.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi: . PMID 15489334.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi: . PMID 16344560.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi: . PMID 17081983.