BMF (gene): Difference between revisions

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{{Infobox_gene}}
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'''Bcl-2-modifying factor''' is a [[protein]] that in humans is encoded by the ''BMF'' [[gene]].<ref name="pmid11546872">{{cite journal | vauthors = Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A | title = Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis | journal = Science | volume = 293 | issue = 5536 | pages = 1829–32 |date=Sep 2001 | pmid = 11546872 | pmc =  | doi = 10.1126/science.1062257 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BMF Bcl2 modifying factor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=90427| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = Bcl2 modifying factor
| HGNCid = 24132
| Symbol = BMF
| AltSymbols =; FLJ00065
| OMIM = 606266
| ECnumber = 
| Homologene = 14130
| MGIid = 2176433
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016459 |text = myosin complex}}
| Process = {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 90427
    | Hs_Ensembl = ENSG00000104081
    | Hs_RefseqProtein = NP_001003940
    | Hs_RefseqmRNA = NM_001003940
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 38167386
    | Hs_GenLoc_end = 38188367
    | Hs_Uniprot = Q96LC9
    | Mm_EntrezGene = 171543
    | Mm_Ensembl = ENSMUSG00000040093
    | Mm_RefseqmRNA = NM_138313
    | Mm_RefseqProtein = NP_612186
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 118220198
    | Mm_GenLoc_end = 118241119
    | Mm_Uniprot = Q3TAQ6
  }}
}}
'''Bcl2 modifying factor''', also known as '''BMF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BMF Bcl2 modifying factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=90427| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. This protein is found to be sequestered to myosin V motors by its association with dynein light chain 2, which may be important for sensing intracellular damage and triggering apoptosis. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: BMF Bcl2 modifying factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=90427| accessdate = }}</ref>
| summary_text = The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. This protein is found to be sequestered to myosin V motors by its association with dynein light chain 2, which may be important for sensing intracellular damage and triggering apoptosis. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: BMF Bcl2 modifying factor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=90427| accessdate = }}</ref>
}}
}}
==Interactions==
BMF (gene) has been shown to [[Protein-protein interaction|interact]] with [[Bcl-2]]<ref name=pmid11546872 /> and [[DYNLL2]].<ref name=pmid11546872/><ref name=pmid14561217>{{cite journal |last=Day |first=Catherine L |author2=Puthalakath Hamsa|author3=Skea Gretchen|author4=Strasser Andreas|author5=Barsukov Igor|author6=Lian Lu-Yun|author7=Huang David C S|author8=Hinds Mark G |date=Feb 2004 |title=Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands |journal=Biochem. J. |volume=377 |issue=Pt 3 |pages=597–605 |publisher= |location = England| issn = | pmid = 14561217 |doi = 10.1042/BJ20031251 |pmc=1223895 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Hattori A, Okumura K, Nagase T, ''et al.'' |title=Characterization of long cDNA clones from human adult spleen. |journal=DNA Res. |volume=7 |issue= 6 |pages= 357-66 |year= 2001 |pmid= 11214971 |doi= }}
*{{cite journal  | vauthors=Hattori A, Okumura K, Nagase T |title=Characterization of long cDNA clones from human adult spleen. |journal=DNA Res. |volume=7 |issue= 6 |pages= 357–66 |year= 2001 |pmid= 11214971 |doi=10.1093/dnares/7.6.357  |display-authors=etal}}
*{{cite journal  | author=Puthalakath H, Villunger A, O'Reilly LA, ''et al.'' |title=Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. |journal=Science |volume=293 |issue= 5536 |pages= 1829-32 |year= 2001 |pmid= 11546872 |doi= 10.1126/science.1062257 }}
*{{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=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=Lei K, Davis RJ |title=JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 5 |pages= 2432–7 |year= 2003 |pmid= 12591950 |doi= 10.1073/pnas.0438011100 | pmc=151358 }}
*{{cite journal  | author=Lei K, Davis RJ |title=JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 5 |pages= 2432-7 |year= 2003 |pmid= 12591950 |doi= 10.1073/pnas.0438011100 }}
*{{cite journal  | vauthors=Day CL, Puthalakath H, Skea G |title=Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. |journal=Biochem. J. |volume=377 |issue= Pt 3 |pages= 597–605 |year= 2004 |pmid= 14561217 |doi= 10.1042/BJ20031251 | pmc=1223895 |display-authors=etal}}
*{{cite journal  | author=Day CL, Puthalakath H, Skea G, ''et al.'' |title=Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. |journal=Biochem. J. |volume=377 |issue= Pt 3 |pages= 597-605 |year= 2004 |pmid= 14561217 |doi= 10.1042/BJ20031251 }}
*{{cite journal  | vauthors=Morales AA, Olsson A, Celsing F |title=Expression and transcriptional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells. |journal=Leukemia |volume=18 |issue= 1 |pages= 41–7 |year= 2004 |pmid= 14574334 |doi= 10.1038/sj.leu.2403183 |display-authors=etal}}
*{{cite journal  | author=Morales AA, Olsson A, Celsing F, ''et al.'' |title=Expression and transcriptional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells. |journal=Leukemia |volume=18 |issue= 1 |pages= 41-7 |year= 2004 |pmid= 14574334 |doi= 10.1038/sj.leu.2403183 }}
*{{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=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=Chen L, Willis SN, Wei A |title=Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. |journal=Mol. Cell |volume=17 |issue= 3 |pages= 393–403 |year= 2005 |pmid= 15694340 |doi= 10.1016/j.molcel.2004.12.030 |display-authors=etal}}
*{{cite journal  | author=Chen L, Willis SN, Wei A, ''et al.'' |title=Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. |journal=Mol. Cell |volume=17 |issue= 3 |pages= 393-403 |year= 2005 |pmid= 15694340 |doi= 10.1016/j.molcel.2004.12.030 }}
*{{cite journal  | vauthors=Kuwana T, Bouchier-Hayes L, Chipuk JE |title=BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. |journal=Mol. Cell |volume=17 |issue= 4 |pages= 525–35 |year= 2005 |pmid= 15721256 |doi= 10.1016/j.molcel.2005.02.003 |display-authors=etal}}
*{{cite journal  | author=Kuwana T, Bouchier-Hayes L, Chipuk JE, ''et al.'' |title=BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. |journal=Mol. Cell |volume=17 |issue= 4 |pages= 525-35 |year= 2005 |pmid= 15721256 |doi= 10.1016/j.molcel.2005.02.003 }}
*{{cite journal  | vauthors=Soung YH, Lee JW, Park WS |title=BH3 domain mutation of proapoptotic genes Bad, Bmf and Bcl-G is rare in transitional cell carcinomas of the urinary bladder. |journal=Pathology |volume=38 |issue= 1 |pages= 33–4 |year= 2006 |pmid= 16484005 |doi= 10.1080/00313020500455811 |display-authors=etal}}
*{{cite journal  | author=Soung YH, Lee JW, Park WS, ''et al.'' |title=BH3 domain mutation of proapoptotic genes Bad, Bmf and Bcl-G is rare in transitional cell carcinomas of the urinary bladder. |journal=Pathology |volume=38 |issue= 1 |pages= 33-4 |year= 2006 |pmid= 16484005 |doi= 10.1080/00313020500455811 }}
*{{cite journal  | vauthors=Zhang Y, Adachi M, Kawamura R |title=Bmf contributes to histone deacetylase inhibitor-mediated enhancing effects on apoptosis after ionizing radiation. |journal=Apoptosis |volume=11 |issue= 8 |pages= 1349–57 |year= 2007 |pmid= 16830229 |doi= 10.1007/s10495-006-8266-1 |display-authors=etal}}
*{{cite journal  | author=Zhang Y, Adachi M, Kawamura R, ''et al.'' |title=Bmf contributes to histone deacetylase inhibitor-mediated enhancing effects on apoptosis after ionizing radiation. |journal=Apoptosis |volume=11 |issue= 8 |pages= 1349-57 |year= 2007 |pmid= 16830229 |doi= 10.1007/s10495-006-8266-1 }}
*{{cite journal  | vauthors=Schmelzle T, Mailleux AA, Overholtzer M |title=Functional role and oncogene-regulated expression of the BH3-only factor Bmf in mammary epithelial anoikis and morphogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 10 |pages= 3787–92 |year= 2007 |pmid= 17360431 |doi= 10.1073/pnas.0700115104 | pmc=1820662 |display-authors=etal}}
*{{cite journal  | author=Schmelzle T, Mailleux AA, Overholtzer M, ''et al.'' |title=Functional role and oncogene-regulated expression of the BH3-only factor Bmf in mammary epithelial anoikis and morphogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 10 |pages= 3787-92 |year= 2007 |pmid= 17360431 |doi= 10.1073/pnas.0700115104 }}
*{{cite journal  | vauthors=Yoo NJ, Soung YH, Lee SH |title=Mutational analysis of the BH3 domains of proapoptotic Bcl-2 family genes Bad, Bmf and Bcl-G in laryngeal squamous cell carcinomas. |journal=Tumori |volume=93 |issue= 2 |pages= 195–7 |year= 2007 |pmid= 17557568 |doi=  |display-authors=etal}}
*{{cite journal  | author=Yoo NJ, Soung YH, Lee SH, ''et al.'' |title=Mutational analysis of the BH3 domains of proapoptotic Bcl-2 family genes Bad, Bmf and Bcl-G in laryngeal squamous cell carcinomas. |journal=Tumori |volume=93 |issue= 2 |pages= 195-7 |year= 2007 |pmid= 17557568 |doi=  }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|BMF}}
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{{gene-15-stub}}

Latest revision as of 12:45, 9 January 2019

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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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Wikidata
View/Edit Human

Bcl-2-modifying factor is a protein that in humans is encoded by the BMF gene.[1][2]

The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. This protein is found to be sequestered to myosin V motors by its association with dynein light chain 2, which may be important for sensing intracellular damage and triggering apoptosis. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]

Interactions

BMF (gene) has been shown to interact with Bcl-2[1] and DYNLL2.[1][3]

References

  1. ↑ 1.0 1.1 1.2 Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A (Sep 2001). "Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis". Science. 293 (5536): 1829–32. doi:10.1126/science.1062257. PMID 11546872.
  2. ↑ 2.0 2.1 "Entrez Gene: BMF Bcl2 modifying factor".
  3. ↑ Day, Catherine L; Puthalakath Hamsa; Skea Gretchen; Strasser Andreas; Barsukov Igor; Lian Lu-Yun; Huang David C S; Hinds Mark G (Feb 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". Biochem. J. England. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.

Further reading

External links


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