RING1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''E3 ubiquitin-protein ligase RING1''' is an [[enzyme]] that in humans is encoded by the ''RING1'' [[gene]].<ref name="pmid1906426">{{cite journal | vauthors = Hanson IM, Poustka A, Trowsdale J | title = New genes in the class II region of the human major histocompatibility complex | journal = Genomics | volume = 10 | issue = 2 | pages = 417–24 | date = Jun 1991 | pmid = 1906426 | pmc =  | doi = 10.1016/0888-7543(91)90327-B }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RING1 ring finger protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6015| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = n0
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_RING1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2h0d.
| PDB = {{PDB2|2h0d}}
| Name = Ring finger protein 1
| HGNCid = 10018
| Symbol = RING1
| AltSymbols =; RNF1
| OMIM = 602045
| ECnumber = 
| Homologene = 68283
| MGIid = 1101770
| GeneAtlas_image1 = PBB_GE_RING1_35685_at_tn.png
| GeneAtlas_image2 = PBB_GE_RING1_208371_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000151 |text = ubiquitin ligase complex}} {{GNF_GO|id=GO:0001739 |text = sex chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0016604 |text = nuclear body}} {{GNF_GO|id=GO:0031519 |text = PcG protein complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0009952 |text = anterior/posterior pattern formation}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}} {{GNF_GO|id=GO:0016574 |text = histone ubiquitination}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6015
    | Hs_Ensembl = ENSG00000204227
    | Hs_RefseqProtein = NP_002922
    | Hs_RefseqmRNA = NM_002931
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 33284255
    | Hs_GenLoc_end = 33288477
    | Hs_Uniprot = Q06587
    | Mm_EntrezGene = 19763
    | Mm_Ensembl = ENSMUSG00000024325
    | Mm_RefseqmRNA = NM_009066
    | Mm_RefseqProtein = NP_033092
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 33631538
    | Mm_GenLoc_end = 33635097
    | Mm_Uniprot = O35730
  }}
}}
'''Ring finger protein 1''', also known as '''RING1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RING1 ring finger protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6015| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene belongs to the RING finger family, members of which encode proteins characterized by a [[RING finger domain|RING domain]], a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is [[Contiguous distribution|contiguous]] with the RING finger genes FABGL and HKE4.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene belongs to the RING finger family, members of which encode proteins characterized by a [[RING finger domain|RING domain]], a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.<ref name="entrez">{{cite web | title = Entrez Gene: RING1 ring finger protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6015| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
RING1 has been shown to [[Protein-protein interaction|interact]] with [[CBX8]],<ref name=pmid10825164>{{cite journal | vauthors = Bárdos JI, Saurin AJ, Tissot C, Duprez E, Freemont PS | title = HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties | journal = The Journal of Biological Chemistry | volume = 275 | issue = 37 | pages = 28785–92 | date = Sep 2000 | pmid = 10825164 | doi = 10.1074/jbc.M001835200 }}</ref> [[BMI1]]<ref name=pmid9199346>{{cite journal | vauthors = Satijn DP, Gunster MJ, van der Vlag J, Hamer KM, Schul W, Alkema MJ, Saurin AJ, Freemont PS, van Driel R, Otte AP | title = RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor | journal = Molecular and Cellular Biology | volume = 17 | issue = 7 | pages = 4105–13 | date = Jul 1997 | pmid = 9199346 | pmc = 232264 | doi=10.1128/mcb.17.7.4105}}</ref><ref name=pmid9858531>{{cite journal | vauthors = Satijn DP, Otte AP | title = RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity | journal = Molecular and Cellular Biology | volume = 19 | issue = 1 | pages = 57–68 | date = Jan 1999 | pmid = 9858531 | pmc = 83865 | doi=10.1128/mcb.19.1.57}}</ref> and [[RYBP]].<ref name=pmid16189514>{{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}</ref><ref name=pmid10369680>{{cite journal | vauthors = García E, Marcos-Gutiérrez C, del Mar Lorente M, Moreno JC, Vidal M | title = RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1 | journal = The EMBO Journal | volume = 18 | issue = 12 | pages = 3404–18 | date = Jun 1999 | pmid = 10369680 | pmc = 1171420 | doi = 10.1093/emboj/18.12.3404 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lovering R, Hanson IM, Borden KL, Martin S, O'Reilly NJ, Evan GI, Rahman D, Pappin DJ, Trowsdale J, Freemont PS | title = Identification and preliminary characterization of a protein motif related to the zinc finger | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 90 | issue = 6 | pages = 2112–6 | date = Mar 1993 | pmid = 7681583 | pmc = 46035 | doi = 10.1073/pnas.90.6.2112 }}
| citations =
* {{cite journal | vauthors = Satijn DP, Gunster MJ, van der Vlag J, Hamer KM, Schul W, Alkema MJ, Saurin AJ, Freemont PS, van Driel R, Otte AP | title = RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor | journal = Molecular and Cellular Biology | volume = 17 | issue = 7 | pages = 4105–13 | date = Jul 1997 | pmid = 9199346 | pmc = 232264 | doi =  10.1128/mcb.17.7.4105}}
*{{cite journal  | author=Hanson IM, Poustka A, Trowsdale J |title=New genes in the class II region of the human major histocompatibility complex. |journal=Genomics |volume=10 |issue= 2 |pages= 417-24 |year= 1991 |pmid= 1906426 |doi=  }}
* {{cite journal | vauthors = Kikuti YY, Tamiya G, Ando A, Chen L, Kimura M, Ferreira E, Tsuji K, Trowsdale J, Inoko H | title = Physical mapping 220 kb centromeric of the human MHC and DNA sequence analysis of the 43-kb segment including the RING1, HKE6, and HKE4 genes | journal = Genomics | volume = 42 | issue = 3 | pages = 422–35 | date = Jun 1997 | pmid = 9205114 | doi = 10.1006/geno.1997.4745 }}
*{{cite journal | author=Lovering R, Hanson IM, Borden KL, ''et al.'' |title=Identification and preliminary characterization of a protein motif related to the zinc finger. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 6 |pages= 2112-6 |year= 1993 |pmid= 7681583 |doi= }}
* {{cite journal | vauthors = Satijn DP, Otte AP | title = RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity | journal = Molecular and Cellular Biology | volume = 19 | issue = 1 | pages = 57–68 | date = Jan 1999 | pmid = 9858531 | pmc = 83865 | doi =  10.1128/mcb.19.1.57}}
*{{cite journal | author=Satijn DP, Gunster MJ, van der Vlag J, ''et al.'' |title=RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor. |journal=Mol. Cell. Biol. |volume=17 |issue= 7 |pages= 4105-13 |year= 1997 |pmid= 9199346 |doi=  }}
* {{cite journal | vauthors = García E, Marcos-Gutiérrez C, del Mar Lorente M, Moreno JC, Vidal M | title = RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1 | journal = The EMBO Journal | volume = 18 | issue = 12 | pages = 3404–18 | date = Jun 1999 | pmid = 10369680 | pmc = 1171420 | doi = 10.1093/emboj/18.12.3404 }}
*{{cite journal | author=Kikuti YY, Tamiya G, Ando A, ''et al.'' |title=Physical mapping 220 kb centromeric of the human MHC and DNA sequence analysis of the 43-kb segment including the RING1, HKE6, and HKE4 genes. |journal=Genomics |volume=42 |issue= 3 |pages= 422-35 |year= 1997 |pmid= 9205114 |doi= 10.1006/geno.1997.4745 }}
* {{cite journal | vauthors = Bárdos JI, Saurin AJ, Tissot C, Duprez E, Freemont PS | title = HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties | journal = The Journal of Biological Chemistry | volume = 275 | issue = 37 | pages = 28785–92 | date = Sep 2000 | pmid = 10825164 | doi = 10.1074/jbc.M001835200 }}
*{{cite journal | author=Satijn DP, Otte AP |title=RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 57-68 |year= 1999 |pmid= 9858531 |doi=  }}
* {{cite journal | vauthors = Trimarchi JM, Fairchild B, Wen J, Lees JA | title = The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 4 | pages = 1519–24 | date = Feb 2001 | pmid = 11171983 | pmc = 29289 | doi = 10.1073/pnas.041597698 }}
*{{cite journal | author=García E, Marcos-Gutiérrez C, del Mar Lorente M, ''et al.'' |title=RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1. |journal=EMBO J. |volume=18 |issue= 12 |pages= 3404-18 |year= 1999 |pmid= 10369680 |doi= 10.1093/emboj/18.12.3404 }}
* {{cite journal | vauthors = Dahiya A, Wong S, Gonzalo S, Gavin M, Dean DC | title = Linking the Rb and polycomb pathways | journal = Molecular Cell | volume = 8 | issue = 3 | pages = 557–69 | date = Sep 2001 | pmid = 11583618 | doi = 10.1016/S1097-2765(01)00346-X }}
*{{cite journal | author=Bárdos JI, Saurin AJ, Tissot C, ''et al.'' |title=HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28785-92 |year= 2000 |pmid= 10825164 |doi= 10.1074/jbc.M001835200 }}
* {{cite journal | vauthors = Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y | title = A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells | journal = Science | volume = 296 | issue = 5570 | pages = 1132–6 | date = May 2002 | pmid = 12004135 | doi = 10.1126/science.1069861 }}
*{{cite journal | author=Trimarchi JM, Fairchild B, Wen J, Lees JA |title=The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 4 |pages= 1519-24 |year= 2001 |pmid= 11171983 |doi= 10.1073/pnas.041597698 }}
* {{cite journal | vauthors = Akasaka T, Takahashi N, Suzuki M, Koseki H, Bodmer R, Koga H | title = MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation | journal = Genes to Cells | volume = 7 | issue = 8 | pages = 835–50 | date = Aug 2002 | pmid = 12167161 | doi = 10.1046/j.1365-2443.2002.00565.x }}
*{{cite journal | author=Dahiya A, Wong S, Gonzalo S, ''et al.'' |title=Linking the Rb and polycomb pathways. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 557-69 |year= 2001 |pmid= 11583618 |doi= }}
* {{cite journal | vauthors = Levine SS, Weiss A, Erdjument-Bromage H, Shao Z, Tempst P, Kingston RE | title = The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans | journal = Molecular and Cellular Biology | volume = 22 | issue = 17 | pages = 6070–8 | date = Sep 2002 | pmid = 12167701 | pmc = 134016 | doi = 10.1128/MCB.22.17.6070-6078.2002 }}
*{{cite journal | author=Ogawa H, Ishiguro K, Gaubatz S, ''et al.'' |title=A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. |journal=Science |volume=296 |issue= 5570 |pages= 1132-6 |year= 2002 |pmid= 12004135 |doi= 10.1126/science.1069861 }}
* {{cite journal | vauthors = Gil J, Bernard D, Martínez D, Beach D | title = Polycomb CBX7 has a unifying role in cellular lifespan | journal = Nature Cell Biology | volume = 6 | issue = 1 | pages = 67–72 | date = Jan 2004 | pmid = 14647293 | doi = 10.1038/ncb1077 }}
*{{cite journal | author=Akasaka T, Takahashi N, Suzuki M, ''et al.'' |title=MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation. |journal=Genes Cells |volume=7 |issue= 8 |pages= 835-50 |year= 2003 |pmid= 12167161 |doi= }}
* {{cite journal | vauthors = Obuse C, Yang H, Nozaki N, Goto S, Okazaki T, Yoda K | title = Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase | journal = Genes to Cells | volume = 9 | issue = 2 | pages = 105–20 | date = Feb 2004 | pmid = 15009096 | doi = 10.1111/j.1365-2443.2004.00705.x }}
*{{cite journal | author=Levine SS, Weiss A, Erdjument-Bromage H, ''et al.'' |title=The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans. |journal=Mol. Cell. Biol. |volume=22 |issue= 17 |pages= 6070-8 |year= 2002 |pmid= 12167701 |doi=  }}
* {{cite journal | vauthors = Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y | title = Role of histone H2A ubiquitination in Polycomb silencing | journal = Nature | volume = 431 | issue = 7010 | pages = 873–8 | date = Oct 2004 | pmid = 15386022 | doi = 10.1038/nature02985 }}
*{{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 = Qin H, Du D, Zhu Y, Li J, Feng L, Liang Y, Han H | title = The PcG protein HPC2 inhibits RBP-J-mediated transcription by interacting with LIM protein KyoT2 | journal = FEBS Letters | volume = 579 | issue = 5 | pages = 1220–6 | date = Feb 2005 | pmid = 15710417 | doi = 10.1016/j.febslet.2005.01.022 }}
*{{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 | author=Gil J, Bernard D, Martínez D, Beach D |title=Polycomb CBX7 has a unifying role in cellular lifespan. |journal=Nat. Cell Biol. |volume=6 |issue= 1 |pages= 67-72 |year= 2004 |pmid= 14647293 |doi= 10.1038/ncb1077 }}
*{{cite journal | author=Obuse C, Yang H, Nozaki N, ''et al.'' |title=Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase. |journal=Genes Cells |volume=9 |issue= 2 |pages= 105-20 |year= 2004 |pmid= 15009096 |doi= }}
*{{cite journal | author=Wang H, Wang L, Erdjument-Bromage H, ''et al.'' |title=Role of histone H2A ubiquitination in Polycomb silencing. |journal=Nature |volume=431 |issue= 7010 |pages= 873-8 |year= 2004 |pmid= 15386022 |doi= 10.1038/nature02985 }}
*{{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  | author=Qin H, Du D, Zhu Y, ''et al.'' |title=The PcG protein HPC2 inhibits RBP-J-mediated transcription by interacting with LIM protein KyoT2. |journal=FEBS Lett. |volume=579 |issue= 5 |pages= 1220-6 |year= 2005 |pmid= 15710417 |doi= 10.1016/j.febslet.2005.01.022 }}
*{{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 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=6015}}


== External links ==
== External links ==
* {{MeshName|RING1+protein,+human}}
* {{MeshName|RING1+protein,+human}}


{{protein-stub}}
{{NLM content}}
{{NLM content}}
{{Transcription factors}}
{{Transcription factors}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
{{WikiDoc Sources}}
 
 
{{gene-6-stub}}

Latest revision as of 20:28, 15 May 2018

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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

E3 ubiquitin-protein ligase RING1 is an enzyme that in humans is encoded by the RING1 gene.[1][2]

Function

This gene belongs to the RING finger family, members of which encode proteins characterized by a RING domain, a zinc-binding motif related to the zinc finger domain. The gene product can bind DNA and can act as a transcriptional repressor. It is associated with the multimeric polycomb group protein complex. The gene product interacts with the polycomb group proteins BMI1, EDR1, and CBX4, and colocalizes with these proteins in large nuclear domains. It interacts with the CBX4 protein via its glycine-rich C-terminal domain. The gene maps to the HLA class II region, where it is contiguous with the RING finger genes FABGL and HKE4.[2]

Interactions

RING1 has been shown to interact with CBX8,[3] BMI1[4][5] and RYBP.[6][7]

References

  1. ↑ Hanson IM, Poustka A, Trowsdale J (Jun 1991). "New genes in the class II region of the human major histocompatibility complex". Genomics. 10 (2): 417–24. doi:10.1016/0888-7543(91)90327-B. PMID 1906426.
  2. ↑ 2.0 2.1 "Entrez Gene: RING1 ring finger protein 1".
  3. ↑ Bárdos JI, Saurin AJ, Tissot C, Duprez E, Freemont PS (Sep 2000). "HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties". The Journal of Biological Chemistry. 275 (37): 28785–92. doi:10.1074/jbc.M001835200. PMID 10825164.
  4. ↑ Satijn DP, Gunster MJ, van der Vlag J, Hamer KM, Schul W, Alkema MJ, Saurin AJ, Freemont PS, van Driel R, Otte AP (Jul 1997). "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor". Molecular and Cellular Biology. 17 (7): 4105–13. doi:10.1128/mcb.17.7.4105. PMC 232264. PMID 9199346.
  5. ↑ Satijn DP, Otte AP (Jan 1999). "RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity". Molecular and Cellular Biology. 19 (1): 57–68. doi:10.1128/mcb.19.1.57. PMC 83865. PMID 9858531.
  6. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  7. ↑ García E, Marcos-Gutiérrez C, del Mar Lorente M, Moreno JC, Vidal M (Jun 1999). "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1". The EMBO Journal. 18 (12): 3404–18. doi:10.1093/emboj/18.12.3404. PMC 1171420. PMID 10369680.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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