DNAJA2: Difference between revisions

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{{Underlinked|date=May 2016}}
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{{Infobox_gene}}
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'''DnaJ homolog subfamily A member 2''' is a [[protein]] that in humans is encoded by the ''DNAJA2'' [[gene]].<ref name="pmid9710638">{{cite journal | vauthors = Lorain S, Quivy JP, Monier-Gavelle F, Scamps C, Lecluse Y, Almouzni G, Lipinski M | title = Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA | journal = Mol Cell Biol | volume = 18 | issue = 9 | pages = 5546–56 |date=Sep 1998 | pmid = 9710638 | pmc = 109139 | doi =  }}</ref><ref name="pmid11147971">{{cite journal | vauthors = Ohtsuka K, Hata M | title = Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature | journal = Cell Stress Chaperones | volume = 5 | issue = 2 | pages = 98–112 |date=Jan 2001 | pmid = 11147971 | pmc = 312896 | doi =10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2 | issn = 1466-1268 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DNAJA2 DnaJ (Hsp40) homolog, subfamily A, member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10294| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = DnaJ (Hsp40) homolog, subfamily A, member 2
| HGNCid = 14884
| Symbol = DNAJA2
| AltSymbols =; CPR3; DJA2; DNAJ; DNJ3; HIRIP4; PRO3015; RDJ2
| OMIM = 
| ECnumber = 
| Homologene = 21193
| MGIid = 1931882
| GeneAtlas_image1 = PBB_GE_DNAJA2_209157_at_tn.png
| Function = {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
  | Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000080 |text = G1 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10294
    | Hs_Ensembl = ENSG00000069345
    | Hs_RefseqProtein = NP_005871
    | Hs_RefseqmRNA = NM_005880
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 45547796
    | Hs_GenLoc_end = 45565079
    | Hs_Uniprot = O60884
    | Mm_EntrezGene = 56445
    | Mm_Ensembl = ENSMUSG00000031701
    | Mm_RefseqmRNA = NM_019794
    | Mm_RefseqProtein = NP_062768
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 88427745
    | Mm_GenLoc_end = 88445376
    | Mm_Uniprot = Q3TFF0
  }}
}}
'''DnaJ (Hsp40) homolog, subfamily A, member 2''', also known as '''DNAJA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNAJA2 DnaJ (Hsp40) homolog, subfamily A, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10294| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: DNAJA2 DnaJ (Hsp40) homolog, subfamily A, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10294| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | vauthors=Bonwaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Edwards MC, Liegeois N, Horecka J, ''et al.'' |title=Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells. |journal=Genetics |volume=147 |issue= 3 |pages= 1063-76 |year= 1998 |pmid= 9383053 |doi= }}
*{{cite journal  | vauthors=Edwards MC, Liegeois N, Horecka J |title=Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells |journal=Genetics |volume=147 |issue= 3 |pages= 1063–76 |year= 1998 |pmid= 9383053 |doi=  | pmc=1208234  |display-authors=etal}}
*{{cite journal | author=Lorain S, Quivy JP, Monier-Gavelle F, ''et al.'' |title=Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA. |journal=Mol. Cell. Biol. |volume=18 |issue= 9 |pages= 5546-56 |year= 1998 |pmid= 9710638 |doi=  }}
*{{cite journal  | vauthors=Scanlan MJ, Gordan JD, Williamson B |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456–64 |year= 1999 |pmid= 10508479 |doi=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5 |display-authors=etal}}
*{{cite journal  | author=Scanlan MJ, Gordan JD, Williamson B, ''et al.'' |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma. |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456-64 |year= 1999 |pmid= 10508479 |doi=  }}
*{{cite journal  | vauthors=Diefenbach J, Kindl H |title=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 |journal=Eur. J. Biochem. |volume=267 |issue= 3 |pages= 746–54 |year= 2000 |pmid= 10651811 |doi=10.1046/j.1432-1327.2000.01053.x }}
*{{cite journal  | author=Diefenbach J, Kindl H |title=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. |journal=Eur. J. Biochem. |volume=267 |issue= 3 |pages= 746-54 |year= 2000 |pmid= 10651811 |doi=  }}
*{{cite journal  | vauthors=Terada K, Mori M |title=Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70 |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24728–34 |year= 2000 |pmid= 10816573 |doi= 10.1074/jbc.M002021200 }}
*{{cite journal  | author=Terada K, Mori M |title=Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24728-34 |year= 2000 |pmid= 10816573 |doi= 10.1074/jbc.M002021200 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Ohtsuka K, Hata M |title=Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature. |journal=Cell Stress Chaperones |volume=5 |issue= 2 |pages= 98-112 |year= 2001 |pmid= 11147971 |doi=  }}
*{{cite journal  | vauthors=Willingham S, Outeiro TF, DeVit MJ |title=Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein |journal=Science |volume=302 |issue= 5651 |pages= 1769–72 |year= 2003 |pmid= 14657499 |doi= 10.1126/science.1090389 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Kho Y, Kim SC, Jiang C |title=A tagging-via-substrate technology for detection and proteomics of farnesylated proteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 34 |pages= 12479–84 |year= 2004 |pmid= 15308774 |doi= 10.1073/pnas.0403413101 | pmc=515085 |display-authors=etal}}
*{{cite journal  | author=Willingham S, Outeiro TF, DeVit MJ, ''et al.'' |title=Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. |journal=Science |volume=302 |issue= 5651 |pages= 1769-72 |year= 2003 |pmid= 14657499 |doi= 10.1126/science.1090389 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Kho Y, Kim SC, Jiang C, ''et al.'' |title=A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 34 |pages= 12479-84 |year= 2004 |pmid= 15308774 |doi= 10.1073/pnas.0403413101 }}
*{{cite journal  | vauthors=Kimura K, Wakamatsu A, Suzuki Y |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Olsen JV, Blagoev B, Gnad F |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |display-authors=etal}}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC genome browser|DNAJA2}}
* {{UCSC gene details|DNAJA2}}
 
{{Chaperones}}
 
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[[Category:Heat shock proteins]]
 
 
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Latest revision as of 18:36, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DnaJ homolog subfamily A member 2 is a protein that in humans is encoded by the DNAJA2 gene.[1][2][3]

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.[3]

References

  1. ↑ Lorain S, Quivy JP, Monier-Gavelle F, Scamps C, Lecluse Y, Almouzni G, Lipinski M (Sep 1998). "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA". Mol Cell Biol. 18 (9): 5546–56. PMC 109139. PMID 9710638.
  2. ↑ Ohtsuka K, Hata M (Jan 2001). "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature". Cell Stress Chaperones. 5 (2): 98–112. doi:10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2. ISSN 1466-1268. PMC 312896. PMID 11147971.
  3. ↑ 3.0 3.1 "Entrez Gene: DNAJA2 DnaJ (Hsp40) homolog, subfamily A, member 2".

Further reading

External links


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