BAG2: Difference between revisions

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{{Infobox_gene}}
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'''BAG family molecular chaperone regulator 2''' is a [[protein]] that in humans is encoded by the ''BAG2'' [[gene]].<ref name="pmid9873016">{{cite journal | vauthors = Takayama S, Xie Z, Reed JC | title = An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators | journal = J Biol Chem | volume = 274 | issue = 2 | pages = 781–6 |date=Feb 1999 | pmid = 9873016 | pmc =  | doi =10.1074/jbc.274.2.781 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BAG2 BCL2-associated athanogene 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9532| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = BCL2-associated athanogene 2
| HGNCid = 938
| Symbol = BAG2
| AltSymbols =; BAG-2; KIAA0576; MGC149462; dJ417I1.2
| OMIM = 603882
| ECnumber =
| Homologene = 31233
| MGIid = 1891254
  | GeneAtlas_image1 = PBB_GE_BAG2_209406_at_tn.png
  | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030188 |text = chaperone regulator activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0019538 |text = protein metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9532
    | Hs_Ensembl = ENSG00000112208
    | Hs_RefseqProtein = NP_004273
    | Hs_RefseqmRNA = NM_004282
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 57145083
    | Hs_GenLoc_end = 57157694
    | Hs_Uniprot = O95816
    | Mm_EntrezGene = 213539
    | Mm_Ensembl = ENSMUSG00000042215
    | Mm_RefseqmRNA = NM_145392
    | Mm_RefseqProtein = NP_663367
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 33690030
    | Mm_GenLoc_end = 33702317
    | Mm_Uniprot = Q91YN9
  }}
}}
'''BCL2-associated athanogene 2''', also known as '''BAG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BAG2 BCL2-associated athanogene 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9532| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.<ref name="entrez">{{cite web | title = Entrez Gene: BAG2 BCL2-associated athanogene 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9532| accessdate = }}</ref>
| summary_text = BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid [[BAG domain]] near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.<ref name="entrez"/>
}}
}}
==Interactions==
BAG2 has been shown to [[Protein-protein interaction|interact]] with [[HSPA8]].<ref name=pmid9873016 />


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|BAG2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Halse R, Rochford JJ, McCormack JG, ''et al.'' |title=Control of glycogen synthesis in cultured human muscle cells. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 776-80 |year= 1999 |pmid= 9873015 |doi= }}
*{{cite journal  | vauthors=Halse R, Rochford JJ, McCormack JG |title=Control of glycogen synthesis in cultured human muscle cells. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 776–80 |year= 1999 |pmid= 9873015 |doi=10.1074/jbc.274.2.776  |display-authors=etal}}
*{{cite journal  | author=Takayama S, Xie Z, Reed JC |title=An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 781-6 |year= 1999 |pmid= 9873016 |doi=  }}
*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | vauthors=Wiemann S, Weil B, Wellenreuther R |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072 |display-authors=etal}}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | vauthors=Simpson JC, Wellenreuther R, Poustka A |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 | pmc=1083732 |display-authors=etal}}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  | vauthors=Mungall AJ, Palmer SA, Sims SK |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 |display-authors=etal}}
*{{cite journal  | author=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Bouwmeester T, Bauch A, Ruffner H |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 |display-authors=etal}}
*{{cite journal  | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  | vauthors=Ueda K, Kosako H, Fukui Y, Hattori S |title=Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate. |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41815–21 |year= 2004 |pmid= 15271996 |doi= 10.1074/jbc.M406049200 }}
*{{cite journal  | author=Ueda K, Kosako H, Fukui Y, Hattori S |title=Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate. |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41815-21 |year= 2004 |pmid= 15271996 |doi= 10.1074/jbc.M406049200 }}
*{{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=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=Wiemann S, Arlt D, Huber W |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 |display-authors=etal}}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | vauthors=Dai Q, Qian SB, Li HH |title=Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. |journal=J. Biol. Chem. |volume=280 |issue= 46 |pages= 38673–81 |year= 2006 |pmid= 16169850 |doi= 10.1074/jbc.M507986200 |display-authors=etal}}
*{{cite journal  | author=Dai Q, Qian SB, Li HH, ''et al.'' |title=Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. |journal=J. Biol. Chem. |volume=280 |issue= 46 |pages= 38673-81 |year= 2006 |pmid= 16169850 |doi= 10.1074/jbc.M507986200 }}
*{{cite journal  | vauthors=Arndt V, Daniel C, Nastainczyk W |title=BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. |journal=Mol. Biol. Cell |volume=16 |issue= 12 |pages= 5891–900 |year= 2006 |pmid= 16207813 |doi= 10.1091/mbc.E05-07-0660 | pmc=1289430 |display-authors=etal}}
*{{cite journal  | author=Arndt V, Daniel C, Nastainczyk W, ''et al.'' |title=BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. |journal=Mol. Biol. Cell |volume=16 |issue= 12 |pages= 5891-900 |year= 2006 |pmid= 16207813 |doi= 10.1091/mbc.E05-07-0660 }}
*{{cite journal  | vauthors=Mehrle A, Rosenfelder H, Schupp I |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 | pmc=1347501 |display-authors=etal}}
*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
*{{cite journal  | vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 02:25, 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
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Wikidata
View/Edit Human

BAG family molecular chaperone regulator 2 is a protein that in humans is encoded by the BAG2 gene.[1][2]

BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.[2]

Interactions

BAG2 has been shown to interact with HSPA8.[1]

References

  1. ↑ 1.0 1.1 Takayama S, Xie Z, Reed JC (Feb 1999). "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". J Biol Chem. 274 (2): 781–6. doi:10.1074/jbc.274.2.781. PMID 9873016.
  2. ↑ 2.0 2.1 "Entrez Gene: BAG2 BCL2-associated athanogene 2".

External links

Further reading



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