DNAJB2: Difference between revisions

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Latest revision as of 14:02, 4 November 2018

DnaJ homolog subfamily B member 2 is a protein that in humans is encoded by the DNAJB2 gene.^[1]^[2]^[3]

References

↑ Cheetham ME, Brion JP, Anderton BH (Jul 1992). "Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons". Biochem J. 284 ( Pt 2) (Pt 2): 469–76. PMC 1132662. PMID 1599432.
↑ Chapple JP, Hardcastle AJ, Kurzik-Dumke U, Collier DA, Cheetham ME (Oct 1999). "Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32→q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids". Cytogenet Cell Genet. 86 (1): 62–3. doi:10.1159/000015411. PMID 10516435.
↑ "Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2".

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
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. doi:10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2. PMC 312896. PMID 11147971.
Wistow G, Bernstein SL, Wyatt MK (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. PMID 12107410.
Strausberg RL, Feingold EA, Grouse LH (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:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Chapple JP, Cheetham ME (2003). "The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation". J. Biol. Chem. 278 (21): 19087–94. doi:10.1074/jbc.M212349200. PMID 12754272.
Janket ML, Manickam P, Majumder B (2004). "Differential regulation of host cellular genes by HIV-1 viral protein R (Vpr): cDNA microarray analysis using isogenic virus". Biochem. Biophys. Res. Commun. 314 (4): 1126–32. doi:10.1016/j.bbrc.2004.01.008. PMID 14751250.
Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
Colland F, Jacq X, Trouplin V (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
Gerhard DS, Wagner L, Feingold EA (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:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Westhoff B, Chapple JP, van der Spuy J (2005). "HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome". Curr. Biol. 15 (11): 1058–64. doi:10.1016/j.cub.2005.04.058. PMID 15936278.
Rual JF, Venkatesan K, Hao T (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Borrell-Pagès M, Canals JM, Cordelières FP (2006). "Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase" (PDF). J. Clin. Invest. 116 (5): 1410–24. doi:10.1172/JCI27607. PMC 1430359. PMID 16604191.
Adaimy L, Chouery E, Megarbane H (2007). "Mutation in WNT10A Is Associated with an Autosomal Recessive Ectodermal Dysplasia: The Odonto-onycho-dermal Dysplasia". Am. J. Hum. Genet. 81 (4): 821–8. doi:10.1086/520064. PMC 1973944. PMID 17847007.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[pmid1599432-1] Cheetham ME, Brion JP, Anderton BH (Jul 1992). "Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons". Biochem J. 284 ( Pt 2) (Pt 2): 469–76. PMC 1132662. PMID 1599432.

[pmid10516435-2] Chapple JP, Hardcastle AJ, Kurzik-Dumke U, Collier DA, Cheetham ME (Oct 1999). "Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32→q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids". Cytogenet Cell Genet. 86 (1): 62–3. doi:10.1159/000015411. PMID 10516435.

[entrez-3] "Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2".

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
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+'''DnaJ homolog subfamily B member 2''' is a [[protein]] that in humans is encoded by the ''DNAJB2'' [[gene]].<ref name="pmid1599432">{{cite journal | vauthors = Cheetham ME, Brion JP, Anderton BH | title = Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons | journal = Biochem J | volume = 284 ( Pt 2) | issue =  Pt 2| pages = 469–76 |date=Jul 1992 | pmid = 1599432 | pmc = 1132662 | doi =  }}</ref><ref name="pmid10516435">{{cite journal | vauthors = Chapple JP, Hardcastle AJ, Kurzik-Dumke U, Collier DA, Cheetham ME | title = Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32→q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids | journal = Cytogenet Cell Genet | volume = 86 | issue = 1 | pages = 62–3 |date=Oct 1999 | pmid = 10516435 | pmc =  | doi =10.1159/000015411  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3300| accessdate = }}</ref>
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- | image =
- | image_source =
- | PDB =
- | Name = DnaJ (Hsp40) homolog, subfamily B, member 2
- | HGNCid = 5228
- | Symbol = DNAJB2
- | AltSymbols =; HSJ1; HSPF3
- | OMIM = 604139
- | ECnumber =
- | Homologene = 4902
- | MGIid = 1928739
- | GeneAtlas_image1 = PBB_GE_DNAJB2_202500_at_tn.png
- | Function = {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
- | Component =
-  | Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 3300
-    | Hs_Ensembl = ENSG00000135924
-    | Hs_RefseqProtein = NP_001034639
-    | Hs_RefseqmRNA = NM_001039550
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 2
-    | Hs_GenLoc_start = 219852342
-    | Hs_GenLoc_end = 219859866
-    | Hs_Uniprot = P25686
-    | Mm_EntrezGene = 56812
-    | Mm_Ensembl = ENSMUSG00000026203
-    | Mm_RefseqmRNA = NM_020266
-    | Mm_RefseqProtein = NP_064662
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 1
-    | Mm_GenLoc_start = 75119613
-    | Mm_GenLoc_end = 75128838
-    | Mm_Uniprot = Q9QYI5
-  }}
-}}
-'''DnaJ (Hsp40) homolog, subfamily B, member 2''', also known as '''DNAJB2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3300| accessdate = }}</ref>
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@@ Line 55: / Line 10: @@
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Cheetham ME, Brion JP, Anderton BH |title=Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons. |journal=Biochem. J. |volume=284 ( Pt 2) |issue=  |pages= 469-76 |year= 1992 |pmid= 1599432 |doi=  }}
+*{{cite journal  | vauthors=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=10.1101/gr.6.9.791  }}
-*{{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=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=10.1379/1466-1268(2000)005<0098:MHDHCO>2.0.CO;2  | pmc=312896  }}
-*{{cite journal  | author=Chapple JP, Hardcastle AJ, Kurzik-Dumke U, ''et al.'' |title=Assignment of the neuronal cochaperone, HSJ1, to human chromosome bands 2q32-->q34 between D2S295 and D2S339 by in situ hybridization and somatic cell and radiation hybrids. |journal=Cytogenet. Cell Genet. |volume=86 |issue= 1 |pages= 62-3 |year= 1999 |pmid= 10516435 |doi=  }}
+*{{cite journal  | vauthors=Wistow G, Bernstein SL, Wyatt MK |title=Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants |journal=Mol. Vis. |volume=8 |issue=  |pages= 205–20 |year= 2002 |pmid= 12107410 |doi=  }}
-*{{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=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 }}
-*{{cite journal  | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants. |journal=Mol. Vis. |volume=8 |issue=  |pages= 205-20 |year= 2002 |pmid= 12107410 |doi=  }}
+*{{cite journal  | vauthors=Chapple JP, Cheetham ME |title=The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 19087–94 |year= 2003 |pmid= 12754272 |doi= 10.1074/jbc.M212349200 }}
-*{{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=Janket ML, Manickam P, Majumder B |title=Differential regulation of host cellular genes by HIV-1 viral protein R (Vpr): cDNA microarray analysis using isogenic virus |journal=Biochem. Biophys. Res. Commun. |volume=314 |issue= 4 |pages= 1126–32 |year= 2004 |pmid= 14751250 |doi=10.1016/j.bbrc.2004.01.008  }}
-*{{cite journal  | author=Chapple JP, Cheetham ME |title=The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 19087-94 |year= 2003 |pmid= 12754272 |doi= 10.1074/jbc.M212349200 }}
+*{{cite journal  | vauthors=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8  | pmc=395752 }}
-*{{cite journal  | author=Janket ML, Manickam P, Majumder B, ''et al.'' |title=Differential regulation of host cellular genes by HIV-1 viral protein R (Vpr): cDNA microarray analysis using isogenic virus. |journal=Biochem. Biophys. Res. Commun. |volume=314 |issue= 4 |pages= 1126-32 |year= 2004 |pmid= 14751250 |doi=  }}
+*{{cite journal  | vauthors=Colland F, Jacq X, Trouplin V |title=Functional Proteomics Mapping of a Human Signaling Pathway |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104  | pmc=442148 }}
-*{{cite journal  | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
+*{{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 }}
-*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
+*{{cite journal  | vauthors=Westhoff B, Chapple JP, van der Spuy J |title=HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome |journal=Curr. Biol. |volume=15 |issue= 11 |pages= 1058–64 |year= 2005 |pmid= 15936278 |doi= 10.1016/j.cub.2005.04.058 }}
-*{{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=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
-*{{cite journal  | author=Westhoff B, Chapple JP, van der Spuy J, ''et al.'' |title=HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. |journal=Curr. Biol. |volume=15 |issue= 11 |pages= 1058-64 |year= 2005 |pmid= 15936278 |doi= 10.1016/j.cub.2005.04.058 }}
+*{{cite journal  | vauthors=Borrell-Pagès M, Canals JM, Cordelières FP |title=Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase |journal=J. Clin. Invest. |volume=116 |issue= 5 |pages= 1410–24 |year= 2006 |pmid= 16604191 |doi= 10.1172/JCI27607  | pmc=1430359 |url=http://diposit.ub.edu/dspace/bitstream/2445/8314/1/534664.pdf }}
-*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
+*{{cite journal  | vauthors=Adaimy L, Chouery E, Megarbane H |title=Mutation in WNT10A Is Associated with an Autosomal Recessive Ectodermal Dysplasia: The Odonto-onycho-dermal Dysplasia |journal=Am. J. Hum. Genet. |volume=81 |issue= 4 |pages= 821–8 |year= 2007 |pmid= 17847007 |doi= 10.1086/520064  | pmc=1973944 }}
-*{{cite journal  | author=Borrell-Pagès M, Canals JM, Cordelières FP, ''et al.'' |title=Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase. |journal=J. Clin. Invest. |volume=116 |issue= 5 |pages= 1410-24 |year= 2006 |pmid= 16604191 |doi= 10.1172/JCI27607 }}
-*{{cite journal  | author=Adaimy L, Chouery E, Megarbane H, ''et al.'' |title=Mutation in WNT10A is associated with an autosomal recessive ectodermal dysplasia: the odonto-onycho-dermal dysplasia. |journal=Am. J. Hum. Genet. |volume=81 |issue= 4 |pages= 821-8 |year= 2007 |pmid= 17847007 |doi= 10.1086/520064 }}
 }}
 {{refend}}
-{{protein-stub}}
+{{Chaperones}}
-{{WikiDoc Sources}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
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+| update_protein_box = yes
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+| update_citations = yes
+}}
+[[Category:Heat shock proteins]]
+{{gene-2-stub}}

DNAJB2: Difference between revisions

Latest revision as of 14:02, 4 November 2018

References

Further reading

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