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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Polyhomeotic-like protein 1''' is a [[protein]] that in humans is encoded by the ''PHC1'' [[gene]].<ref name="pmid9121482">{{cite journal | vauthors = Gunster MJ, Satijn DP, Hamer KM, den Blaauwen JL, de Bruijn D, Alkema MJ, van Lohuizen M, van Driel R, Otte AP | title = Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic | journal = Molecular and Cellular Biology | volume = 17 | issue = 4 | pages = 2326–35 | date = Apr 1997 | pmid = 9121482 | pmc = 232081 | doi = 10.1128/mcb.17.4.2326}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PHC1 polyhomeotic homolog 1 (Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1911| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| 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 =
| image_source =
| PDB =
| Name = Polyhomeotic homolog 1 (Drosophila)
| HGNCid = 3182
| Symbol = PHC1
| AltSymbols =; EDR1; HPH1; RAE28
| OMIM = 602978
| ECnumber = 
| Homologene = 88704
| MGIid = 
| GeneAtlas_image1 = PBB_GE_PHC1_218338_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1911
    | Hs_Ensembl = ENSG00000179899
    | Hs_RefseqProtein = NP_004417
    | Hs_RefseqmRNA = NM_004426
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 54091773
    | Hs_GenLoc_end = 54094973
    | Hs_Uniprot = 
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Polyhomeotic homolog 1 (Drosophila)''', also known as '''PHC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PHC1 polyhomeotic homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1911| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene is a homolog of the Drosophila polyhomeotic gene, which is a member of the Polycomb group of genes. The gene product is a component of a multimeric protein complex that contains EDR2 and the vertebrate Polycomb protein BMH1. The gene product, the EDR2 protein, and the Drosophila polyhomeotic protein share 2 highly conserved domains, named homology domains I and II. These domains are involved in protein-protein interactions and may mediate heterodimerization of the protein encoded by this gene and the EDR2 protein.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene is a homolog of the Drosophila polyhomeotic gene, which is a member of the Polycomb group of genes. The gene product is a component of a multimeric protein complex that contains EDR2 and the vertebrate Polycomb protein BMH1. The gene product, the EDR2 protein, and the Drosophila polyhomeotic protein share 2 highly conserved domains, named homology domains I and II. These domains are involved in protein-protein interactions and may mediate heterodimerization of the protein encoded by this gene and the EDR2 protein.<ref name="entrez">{{cite web | title = Entrez Gene: PHC1 polyhomeotic homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1911| accessdate = }}</ref>
}}


==References==
Mutations in this gene have been associated to cases of primary [[microcephaly]] (doi: 10.1093/hmg/ddt072).
{{reflist|2}}
 
==Further reading==
== Interactions ==
 
PHC1 has been shown to [[Protein-protein interaction|interact]] with [[BMI1]]<ref name=pmid9121482 /><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> and [[PHC2]].<ref name=pmid9121482/><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>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Alkema MJ, Bronk M, Verhoeven E, Otte A, van 't Veer LJ, Berns A, van Lohuizen M | title = Identification of Bmi1-interacting proteins as constituents of a multimeric mammalian polycomb complex | journal = Genes & Development | volume = 11 | issue = 2 | pages = 226–40 | date = Jan 1997 | pmid = 9009205 | doi = 10.1101/gad.11.2.226 }}
| 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=Alkema MJ, Bronk M, Verhoeven E, ''et al.'' |title=Identification of Bmi1-interacting proteins as constituents of a multimeric mammalian polycomb complex. |journal=Genes Dev. |volume=11 |issue= 2 |pages= 226-40 |year= 1997 |pmid= 9009205 |doi= }}
* {{cite journal | vauthors = Tomotsune D, Takihara Y, Berger J, Duhl D, Joo S, Kyba M, Shirai M, Ohta H, Matsuda Y, Honda BM, Simon J, Shimada K, Brock HW, Randazzo F | title = A novel member of murine Polycomb-group proteins, Sex comb on midleg homolog protein, is highly conserved, and interacts with RAE28/mph1 in vitro | journal = Differentiation; Research in Biological Diversity | volume = 65 | issue = 4 | pages = 229–39 | date = Dec 1999 | pmid = 10653359 | doi = 10.1046/j.1432-0436.1999.6540229.x }}
*{{cite journal  | author=Gunster MJ, Satijn DP, Hamer KM, ''et al.'' |title=Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 2326-35 |year= 1997 |pmid= 9121482 |doi=  }}
* {{cite journal | vauthors = Ohta H, Tokimasa S, Zou Z, Funaki S, Kurahashi H, Takahashi Y, Kimura M, Matsuoka R, Horie M, Hara J, Shimada K, Takihara Y | title = Structure and chromosomal localization of the RAE28/HPH1 gene, a human homologue of the polyhomeotic gene | journal = DNA Sequence | volume = 11 | issue = 1-2 | pages = 61–73 | year = 2000 | pmid = 10902910 | doi = 10.3109/10425170009033970 }}
*{{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 = 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=Tomotsune D, Takihara Y, Berger J, ''et al.'' |title=A novel member of murine Polycomb-group proteins, Sex comb on midleg homolog protein, is highly conserved, and interacts with RAE28/mph1 in vitro. |journal=Differentiation |volume=65 |issue= 4 |pages= 229-39 |year= 2000 |pmid= 10653359 |doi= }}
* {{cite journal | vauthors = Suzuki M, Mizutani-Koseki Y, Fujimura Y, Miyagishima H, Kaneko T, Takada Y, Akasaka T, Tanzawa H, Takihara Y, Nakano M, Masumoto H, Vidal M, Isono K, Koseki H | title = Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice | journal = Development | volume = 129 | issue = 18 | pages = 4171–83 | date = Sep 2002 | pmid = 12183370 | doi =  }}
*{{cite journal | author=Ohta H, Tokimasa S, Zou Z, ''et al.'' |title=Structure and chromosomal localization of the RAE28/HPH1 gene, a human homologue of the polyhomeotic gene. |journal=DNA Seq. |volume=11 |issue= 1-2 |pages= 61-73 |year= 2000 |pmid= 10902910 |doi= }}
* {{cite journal | vauthors = Luo L, Yang X, Takihara Y, Knoetgen H, Kessel M | title = The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions | journal = Nature | volume = 427 | issue = 6976 | pages = 749–53 | date = Feb 2004 | pmid = 14973489 | doi = 10.1038/nature02305 }}
*{{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 = Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW | title = Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation | journal = Nature Biotechnology | volume = 22 | issue = 6 | pages = 707–16 | date = Jun 2004 | pmid = 15146197 | doi = 10.1038/nbt971 }}
*{{cite journal | author=Suzuki M, Mizutani-Koseki Y, Fujimura Y, ''et al.'' |title=Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice. |journal=Development |volume=129 |issue= 18 |pages= 4171-83 |year= 2002 |pmid= 12183370 |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 = Voncken JW, Niessen H, Neufeld B, Rennefahrt U, Dahlmans V, Kubben N, Holzer B, Ludwig S, Rapp UR | title = MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1 | journal = The Journal of Biological Chemistry | volume = 280 | issue = 7 | pages = 5178–87 | date = Feb 2005 | pmid = 15563468 | doi = 10.1074/jbc.M407155200 }}
*{{cite journal  | author=Luo L, Yang X, Takihara Y, ''et al.'' |title=The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions. |journal=Nature |volume=427 |issue= 6976 |pages= 749-53 |year= 2004 |pmid= 14973489 |doi= 10.1038/nature02305 }}
*{{cite journal | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{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=Voncken JW, Niessen H, Neufeld B, ''et al.'' |title=MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1. |journal=J. Biol. Chem. |volume=280 |issue= 7 |pages= 5178-87 |year= 2005 |pmid= 15563468 |doi= 10.1074/jbc.M407155200 }}
*{{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}}


{{protein-stub}}
{{gene-12-stub}}
{{WikiDoc Sources}}

Latest revision as of 18:02, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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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

Polyhomeotic-like protein 1 is a protein that in humans is encoded by the PHC1 gene.[1][2]

Function

This gene is a homolog of the Drosophila polyhomeotic gene, which is a member of the Polycomb group of genes. The gene product is a component of a multimeric protein complex that contains EDR2 and the vertebrate Polycomb protein BMH1. The gene product, the EDR2 protein, and the Drosophila polyhomeotic protein share 2 highly conserved domains, named homology domains I and II. These domains are involved in protein-protein interactions and may mediate heterodimerization of the protein encoded by this gene and the EDR2 protein.[2]

Mutations in this gene have been associated to cases of primary microcephaly (doi: 10.1093/hmg/ddt072).

Interactions

PHC1 has been shown to interact with BMI1[1][3] and PHC2.[1][4]

References

  1. ↑ 1.0 1.1 1.2 Gunster MJ, Satijn DP, Hamer KM, den Blaauwen JL, de Bruijn D, Alkema MJ, van Lohuizen M, van Driel R, Otte AP (Apr 1997). "Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic". Molecular and Cellular Biology. 17 (4): 2326–35. doi:10.1128/mcb.17.4.2326. PMC 232081. PMID 9121482.
  2. ↑ 2.0 2.1 "Entrez Gene: PHC1 polyhomeotic homolog 1 (Drosophila)".
  3. ↑ 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.
  4. ↑ 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.

Further reading

  • Alkema MJ, Bronk M, Verhoeven E, Otte A, van 't Veer LJ, Berns A, van Lohuizen M (Jan 1997). "Identification of Bmi1-interacting proteins as constituents of a multimeric mammalian polycomb complex". Genes & Development. 11 (2): 226–40. doi:10.1101/gad.11.2.226. PMID 9009205.
  • 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.
  • Tomotsune D, Takihara Y, Berger J, Duhl D, Joo S, Kyba M, Shirai M, Ohta H, Matsuda Y, Honda BM, Simon J, Shimada K, Brock HW, Randazzo F (Dec 1999). "A novel member of murine Polycomb-group proteins, Sex comb on midleg homolog protein, is highly conserved, and interacts with RAE28/mph1 in vitro". Differentiation; Research in Biological Diversity. 65 (4): 229–39. doi:10.1046/j.1432-0436.1999.6540229.x. PMID 10653359.
  • Ohta H, Tokimasa S, Zou Z, Funaki S, Kurahashi H, Takahashi Y, Kimura M, Matsuoka R, Horie M, Hara J, Shimada K, Takihara Y (2000). "Structure and chromosomal localization of the RAE28/HPH1 gene, a human homologue of the polyhomeotic gene". DNA Sequence. 11 (1–2): 61–73. doi:10.3109/10425170009033970. PMID 10902910.
  • Levine SS, Weiss A, Erdjument-Bromage H, Shao Z, Tempst P, Kingston RE (Sep 2002). "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans". Molecular and Cellular Biology. 22 (17): 6070–8. doi:10.1128/MCB.22.17.6070-6078.2002. PMC 134016. PMID 12167701.
  • Suzuki M, Mizutani-Koseki Y, Fujimura Y, Miyagishima H, Kaneko T, Takada Y, Akasaka T, Tanzawa H, Takihara Y, Nakano M, Masumoto H, Vidal M, Isono K, Koseki H (Sep 2002). "Involvement of the Polycomb-group gene Ring1B in the specification of the anterior-posterior axis in mice". Development. 129 (18): 4171–83. PMID 12183370.
  • Luo L, Yang X, Takihara Y, Knoetgen H, Kessel M (Feb 2004). "The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions". Nature. 427 (6976): 749–53. doi:10.1038/nature02305. PMID 14973489.
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
  • Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y (Oct 2004). "Role of histone H2A ubiquitination in Polycomb silencing". Nature. 431 (7010): 873–8. doi:10.1038/nature02985. PMID 15386022.
  • Voncken JW, Niessen H, Neufeld B, Rennefahrt U, Dahlmans V, Kubben N, Holzer B, Ludwig S, Rapp UR (Feb 2005). "MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1". The Journal of Biological Chemistry. 280 (7): 5178–87. doi:10.1074/jbc.M407155200. PMID 15563468.
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