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{{Infobox_gene}}
{{PBB_Controls
'''Chromobox protein homolog 1''' is a [[protein]] that in humans is encoded by the ''CBX1'' [[gene]].<ref name="pmid9169582">{{cite journal | vauthors = Furuta K, Chan EK, Kiyosawa K, Reimer G, Luderschmidt C, Tan EM | title = Heterochromatin protein HP1Hsbeta (p25beta) and its localization with centromeres in mitosis | journal = Chromosoma | volume = 106 | issue = 1 | pages = 11–9 | date = Jun 1997 | pmid = 9169582 | pmc =  | doi = 10.1007/s004120050219 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10951| accessdate = }}</ref>
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<!-- 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_CBX1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ap0.
| PDB = {{PDB2|1ap0}}, {{PDB2|1dz1}}, {{PDB2|1guw}}, {{PDB2|1s4z}}, {{PDB2|2fmm}}
| Name = Chromobox homolog 1 (HP1 beta homolog Drosophila )
| HGNCid = 1551
| Symbol = CBX1
| AltSymbols =; CBX; HP1-BETA; HP1Hs-beta; M31; MOD1
| OMIM = 604511
| ECnumber = 
| Homologene = 38228
| MGIid = 105369
| GeneAtlas_image1 = PBB_GE_CBX1_201518_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0001939 |text = female pronucleus}} {{GNF_GO|id=GO:0001940 |text = male pronucleus}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005701 |text = polytene chromosome chromocenter}} {{GNF_GO|id=GO:0005720 |text = nuclear heterochromatin}} {{GNF_GO|id=GO:0005721 |text = centric heterochromatin}}
| Process = {{GNF_GO|id=GO:0006333 |text = chromatin assembly or disassembly}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10951
    | Hs_Ensembl = ENSG00000108468
    | Hs_RefseqProtein = NP_006798
    | Hs_RefseqmRNA = NM_006807
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 43502414
    | Hs_GenLoc_end = 43533806
    | Hs_Uniprot = P83916
    | Mm_EntrezGene = 12412
    | Mm_Ensembl = ENSMUSG00000018666
    | Mm_RefseqmRNA = XM_990275
    | Mm_RefseqProtein = XP_995369
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 96605249
    | Mm_GenLoc_end = 96624730
    | Mm_Uniprot = Q7TPM0
  }}
}}
'''Chromobox homolog 1 (HP1 beta homolog Drosophila )''', also known as '''CBX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10951| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein is localized at [[heterochromatin]] sites, where it mediates [[gene silencing]].<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Heterochromatin protein-1 (HP1) is localized at heterochromatin sites, where it mediates gene silencing.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10951| accessdate = }}</ref>
}}


==See also==
== Model organisms ==
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
|+ ''Cbx1'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
 
|-
| [[Homozygote]] viability || bgcolor="#C40000"|Abnormal
|-
| Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#C40000"|Abnormal<ref name="Indirect calorimetry">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAAT/indirect-calorimetry/ |title=Indirect calorimetry data for Cbx1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
|-
| [[Haematology]] || bgcolor="#488ED3"|Normal
|-
| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Eye Histopathology || bgcolor="#488ED3"|Normal
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of CBX1 function. A conditional [[knockout mouse]] line, called ''Cbx1<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Cbx1 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4432508 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the [[Wellcome Trust Sanger Institute]].<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism | journal = Genome Biology | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty two tests were carried out and two [[phenotypes]] were reported. No [[homozygous]] [[mutant]] animals survived until two weeks of age, therefore the remaining tests were carried out on [[heterozygous]] mutant mice. Male heterozygotes showed increased [[VO2 max|VO2]], rate of elimination of [[carbon dioxide]], and energy expenditure as determined by [[indirect calorimetry]].<ref name="mgp_reference" />
 
== Interactions ==
 
CBX1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[C11orf30]],<ref name = pmid14651845>{{cite journal | vauthors = Hughes-Davies L, Huntsman D, Ruas M, Fuks F, Bye J, Chin SF, Milner J, Brown LA, Hsu F, Gilks B, Nielsen T, Schulzer M, Chia S, Ragaz J, Cahn A, Linger L, Ozdag H, Cattaneo E, Jordanova ES, Schuuring E, Yu DS, Venkitaraman A, Ponder B, Doherty A, Aparicio S, Bentley D, Theillet C, Ponting CP, Caldas C, Kouzarides T | title = EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer | journal = Cell | volume = 115 | issue = 5 | pages = 523–35 | date = Nov 2003 | pmid = 14651845 | doi =  10.1016/s0092-8674(03)00930-9}}</ref>
* [[CBX3]]<ref name = pmid11336697/> and
* [[CBX5 (gene)|CBX5]],<ref name = pmid11336697>{{cite journal | vauthors = Nielsen AL, Oulad-Abdelghani M, Ortiz JA, Remboutsika E, Chambon P, Losson R | title = Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins | journal = Molecular Cell | volume = 7 | issue = 4 | pages = 729–39 | date = Apr 2001 | pmid = 11336697 | doi =  10.1016/S1097-2765(01)00218-0}}</ref>  and
* [[SUV39H1]].<ref name = pmid10202156>{{cite journal | vauthors = Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T | title = Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 | journal = The EMBO Journal | volume = 18 | issue = 7 | pages = 1923–38 | date = Apr 1999 | pmid = 10202156 | pmc = 1171278 | doi = 10.1093/emboj/18.7.1923 }}</ref>
{{Div col end}}
 
== See also ==
* [[Heterochromatin protein 1]]
* [[Heterochromatin protein 1]]


==References==
== References ==
{{reflist|2}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lessard J, Baban S, Sauvageau G | title = Stage-specific expression of polycomb group genes in human bone marrow cells | journal = Blood | volume = 91 | issue = 4 | pages = 1216–24 | date = Feb 1998 | pmid = 9454751 | doi =  }}
| citations =
* {{cite journal | vauthors = Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T | title = Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 | journal = The EMBO Journal | volume = 18 | issue = 7 | pages = 1923–38 | date = Apr 1999 | pmid = 10202156 | pmc = 1171278 | doi = 10.1093/emboj/18.7.1923 }}
*{{cite journal | author=Furuta K, Chan EK, Kiyosawa K, ''et al.'' |title=Heterochromatin protein HP1Hsbeta (p25beta) and its localization with centromeres in mitosis. |journal=Chromosoma |volume=106 |issue= 1 |pages= 11-9 |year= 1997 |pmid= 9169582 |doi=  }}
* {{cite journal | vauthors = Minc E, Allory Y, Worman HJ, Courvalin JC, Buendia B | title = Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells | journal = Chromosoma | volume = 108 | issue = 4 | pages = 220–34 | date = Aug 1999 | pmid = 10460410 | doi = 10.1007/s004120050372 }}
*{{cite journal | author=Lessard J, Baban S, Sauvageau G |title=Stage-specific expression of polycomb group genes in human bone marrow cells. |journal=Blood |volume=91 |issue= 4 |pages= 1216-24 |year= 1998 |pmid= 9454751 |doi= }}
* {{cite journal | vauthors = Murzina N, Verreault A, Laue E, Stillman B | title = Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins | journal = Molecular Cell | volume = 4 | issue = 4 | pages = 529–40 | date = Oct 1999 | pmid = 10549285 | doi = 10.1016/S1097-2765(00)80204-X }}
*{{cite journal | author=Aagaard L, Laible G, Selenko P, ''et al.'' |title=Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. |journal=EMBO J. |volume=18 |issue= 7 |pages= 1923-38 |year= 1999 |pmid= 10202156 |doi= 10.1093/emboj/18.7.1923 }}
* {{cite journal | vauthors = Nielsen AL, Ortiz JA, You J, Oulad-Abdelghani M, Khechumian R, Gansmuller A, Chambon P, Losson R | title = Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family | journal = The EMBO Journal | volume = 18 | issue = 22 | pages = 6385–95 | date = Nov 1999 | pmid = 10562550 | pmc = 1171701 | doi = 10.1093/emboj/18.22.6385 }}
*{{cite journal | author=Minc E, Allory Y, Worman HJ, ''et al.'' |title=Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells. |journal=Chromosoma |volume=108 |issue= 4 |pages= 220-34 |year= 1999 |pmid= 10460410 |doi= }}
* {{cite journal | vauthors = Brasher SV, Smith BO, Fogh RH, Nietlispach D, Thiru A, Nielsen PR, Broadhurst RW, Ball LJ, Murzina NV, Laue ED | title = The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer | journal = The EMBO Journal | volume = 19 | issue = 7 | pages = 1587–97 | date = Apr 2000 | pmid = 10747027 | pmc = 310228 | doi = 10.1093/emboj/19.7.1587 }}
*{{cite journal | author=Murzina N, Verreault A, Laue E, Stillman B |title=Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. |journal=Mol. Cell |volume=4 |issue= 4 |pages= 529-40 |year= 1999 |pmid= 10549285 |doi= }}
* {{cite journal | vauthors = Zhao T, Heyduk T, Allis CD, Eissenberg JC | title = Heterochromatin protein 1 binds to nucleosomes and DNA in vitro | journal = The Journal of Biological Chemistry | volume = 275 | issue = 36 | pages = 28332–8 | date = Sep 2000 | pmid = 10882726 | doi = 10.1074/jbc.M003493200 }}
*{{cite journal | author=Nielsen AL, Ortiz JA, You J, ''et al.'' |title=Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. |journal=EMBO J. |volume=18 |issue= 22 |pages= 6385-95 |year= 2000 |pmid= 10562550 |doi= 10.1093/emboj/18.22.6385 }}
* {{cite journal | vauthors = Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T | title = Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins | journal = Nature | volume = 410 | issue = 6824 | pages = 116–20 | date = Mar 2001 | pmid = 11242053 | doi = 10.1038/35065132 }}
*{{cite journal | author=Brasher SV, Smith BO, Fogh RH, ''et al.'' |title=The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer. |journal=EMBO J. |volume=19 |issue= 7 |pages= 1587-97 |year= 2000 |pmid= 10747027 |doi= 10.1093/emboj/19.7.1587 }}
* {{cite journal | vauthors = Bannister AJ, Zegerman P, Partridge JF, Miska EA, Thomas JO, Allshire RC, Kouzarides T | title = Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain | journal = Nature | volume = 410 | issue = 6824 | pages = 120–4 | date = Mar 2001 | pmid = 11242054 | doi = 10.1038/35065138 }}
*{{cite journal | author=Zhao T, Heyduk T, Allis CD, Eissenberg JC |title=Heterochromatin protein 1 binds to nucleosomes and DNA in vitro. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28332-8 |year= 2000 |pmid= 10882726 |doi= 10.1074/jbc.M003493200 }}
* {{cite journal | vauthors = Nielsen AL, Oulad-Abdelghani M, Ortiz JA, Remboutsika E, Chambon P, Losson R | title = Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins | journal = Molecular Cell | volume = 7 | issue = 4 | pages = 729–39 | date = Apr 2001 | pmid = 11336697 | doi = 10.1016/S1097-2765(01)00218-0 }}
*{{cite journal | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116-20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
* {{cite journal | vauthors = Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI | title = Directed proteomic analysis of the human nucleolus | journal = Current Biology | volume = 12 | issue = 1 | pages = 1–11 | date = Jan 2002 | pmid = 11790298 | doi = 10.1016/S0960-9822(01)00650-9 }}
*{{cite journal | author=Bannister AJ, Zegerman P, Partridge JF, ''et al.'' |title=Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. |journal=Nature |volume=410 |issue= 6824 |pages= 120-4 |year= 2001 |pmid= 11242054 |doi= 10.1038/35065138 }}
* {{cite journal | vauthors = Scholzen T, Endl E, Wohlenberg C, van der Sar S, Cowell IG, Gerdes J, Singh PB | title = The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure | journal = The Journal of Pathology | volume = 196 | issue = 2 | pages = 135–44 | date = Feb 2002 | pmid = 11793364 | doi = 10.1002/path.1016 }}
*{{cite journal | author=Nielsen AL, Oulad-Abdelghani M, Ortiz JA, ''et al.'' |title=Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. |journal=Mol. Cell |volume=7 |issue= 4 |pages= 729-39 |year= 2001 |pmid= 11336697 |doi= }}
* {{cite journal | vauthors = Nielsen PR, Nietlispach D, Mott HR, Callaghan J, Bannister A, Kouzarides T, Murzin AG, Murzina NV, Laue ED | title = Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9 | journal = Nature | volume = 416 | issue = 6876 | pages = 103–7 | date = Mar 2002 | pmid = 11882902 | doi = 10.1038/nature722 }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
* {{cite journal | vauthors = Vassallo MF, Tanese N | title = Isoform-specific interaction of HP1 with human TAFII130 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 9 | pages = 5919–24 | date = Apr 2002 | pmid = 11959914 | pmc = 122877 | doi = 10.1073/pnas.092025499 }}
*{{cite journal | author=Scholzen T, Endl E, Wohlenberg C, ''et al.'' |title=The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure. |journal=J. Pathol. |volume=196 |issue= 2 |pages= 135-44 |year= 2002 |pmid= 11793364 |doi= 10.1002/path.1016 }}
* {{cite journal | vauthors = Hwang KK, Worman HJ | title = Gene regulation by human orthologs of Drosophila heterochromatin protein 1 | journal = Biochemical and Biophysical Research Communications | volume = 293 | issue = 4 | pages = 1217–22 | date = May 2002 | pmid = 12054505 | doi = 10.1016/S0006-291X(02)00377-7 }}
*{{cite journal | author=Nielsen PR, Nietlispach D, Mott HR, ''et al.'' |title=Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. |journal=Nature |volume=416 |issue= 6876 |pages= 103-7 |year= 2002 |pmid= 11882902 |doi= 10.1038/nature722 }}
* {{cite journal | vauthors = Bhattacharya N, Wang Z, Davitt C, McKenzie IF, Xing PX, Magnuson NS | title = Pim-1 associates with protein complexes necessary for mitosis | journal = Chromosoma | volume = 111 | issue = 2 | pages = 80–95 | date = Jul 2002 | pmid = 12111331 | doi = 10.1007/s00412-002-0192-6 }}
*{{cite journal | author=Vassallo MF, Tanese N |title=Isoform-specific interaction of HP1 with human TAFII130. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 5919-24 |year= 2002 |pmid= 11959914 |doi= 10.1073/pnas.092025499 }}
* {{cite journal | vauthors = Lin CY, Li CC, Huang PH, Lee FJ | title = A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1 | journal = Journal of Cell Science | volume = 115 | issue = Pt 23 | pages = 4433–45 | date = Dec 2002 | pmid = 12414990 | doi = 10.1242/jcs.00123 }}
*{{cite journal | author=Hwang KK, Worman HJ |title=Gene regulation by human orthologs of Drosophila heterochromatin protein 1. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 4 |pages= 1217-22 |year= 2002 |pmid= 12054505 |doi= 10.1016/S0006-291X(02)00377-7 }}
* {{cite journal | vauthors = Festenstein R, Pagakis SN, Hiragami K, Lyon D, Verreault A, Sekkali B, Kioussis D | title = Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells | journal = Science | volume = 299 | issue = 5607 | pages = 719–21 | date = Jan 2003 | pmid = 12560554 | doi = 10.1126/science.1078694 }}
*{{cite journal | author=Bhattacharya N, Wang Z, Davitt C, ''et al.'' |title=Pim-1 associates with protein complexes necessary for mitosis. |journal=Chromosoma |volume=111 |issue= 2 |pages= 80-95 |year= 2003 |pmid= 12111331 |doi= 10.1007/s00412-002-0192-6 }}
*{{cite journal | author=Lin CY, Li CC, Huang PH, Lee FJ |title=A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1. |journal=J. Cell. Sci. |volume=115 |issue= Pt 23 |pages= 4433-45 |year= 2003 |pmid= 12414990 |doi=  }}
*{{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  | author=Festenstein R, Pagakis SN, Hiragami K, ''et al.'' |title=Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells. |journal=Science |volume=299 |issue= 5607 |pages= 719-21 |year= 2003 |pmid= 12560554 |doi= 10.1126/science.1078694 }}
}}
{{refend}}
{{refend}}


== External links ==
== External links ==
* {{MeshName|CBX1+protein,+human}}
* {{MeshName|CBX1+protein,+human}}
* {{UCSC gene info|CBX1}}


{{protein-stub}}
{{NLM content}}
{{NLM content}}
{{PDB Gallery|geneid=10951}}
{{Transcription factors}}
{{Transcription factors}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
{{WikiDoc Sources}}
[[Category:Genes mutated in mice]]

Latest revision as of 09:14, 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
PubMed searchn/an/a
Wikidata
View/Edit Human

Chromobox protein homolog 1 is a protein that in humans is encoded by the CBX1 gene.[1][2]

Function

The protein is localized at heterochromatin sites, where it mediates gene silencing.[2]

Model organisms

Model organisms have been used in the study of CBX1 function. A conditional knockout mouse line, called Cbx1tm1a(EUCOMM)Wtsi[6][7] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[8][9][10]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty two tests were carried out and two phenotypes were reported. No homozygous mutant animals survived until two weeks of age, therefore the remaining tests were carried out on heterozygous mutant mice. Male heterozygotes showed increased VO2, rate of elimination of carbon dioxide, and energy expenditure as determined by indirect calorimetry.[4]

Interactions

CBX1 has been shown to interact with:

See also

References

  1. ↑ Furuta K, Chan EK, Kiyosawa K, Reimer G, Luderschmidt C, Tan EM (Jun 1997). "Heterochromatin protein HP1Hsbeta (p25beta) and its localization with centromeres in mitosis". Chromosoma. 106 (1): 11–9. doi:10.1007/s004120050219. PMID 9169582.
  2. ↑ 2.0 2.1 "Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )".
  3. ↑ "Indirect calorimetry data for Cbx1". Wellcome Trust Sanger Institute.
  4. ↑ 4.0 4.1 4.2 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  5. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  6. ↑ "International Knockout Mouse Consortium".
  7. ↑ "Mouse Genome Informatics".
  8. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  9. ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  10. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  11. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  12. ↑ Hughes-Davies L, Huntsman D, Ruas M, Fuks F, Bye J, Chin SF, Milner J, Brown LA, Hsu F, Gilks B, Nielsen T, Schulzer M, Chia S, Ragaz J, Cahn A, Linger L, Ozdag H, Cattaneo E, Jordanova ES, Schuuring E, Yu DS, Venkitaraman A, Ponder B, Doherty A, Aparicio S, Bentley D, Theillet C, Ponting CP, Caldas C, Kouzarides T (Nov 2003). "EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer". Cell. 115 (5): 523–35. doi:10.1016/s0092-8674(03)00930-9. PMID 14651845.
  13. ↑ 13.0 13.1 Nielsen AL, Oulad-Abdelghani M, Ortiz JA, Remboutsika E, Chambon P, Losson R (Apr 2001). "Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins". Molecular Cell. 7 (4): 729–39. doi:10.1016/S1097-2765(01)00218-0. PMID 11336697.
  14. ↑ Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T (Apr 1999). "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31". The EMBO Journal. 18 (7): 1923–38. doi:10.1093/emboj/18.7.1923. PMC 1171278. PMID 10202156.

Further reading

External links

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