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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
 
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'''ATP-binding cassette super-family G member 2''' is a [[protein]] that in humans is encoded by the ''ABCG2'' [[gene]].<ref name="pmid8894702">{{cite journal | vauthors = Allikmets R, Gerrard B, Hutchinson A, Dean M | title = Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database | journal = Hum Mol Genet | volume = 5 | issue = 10 | pages = 1649–55 |date=Feb 1997 | pmid = 8894702 | pmc =  | doi =10.1093/hmg/5.10.1649  }}</ref><ref name="pmid9861027">{{cite journal | vauthors = Doyle LA, Yang W, Abruzzo LV, Krogmann T, Gao Y, Rishi AK, Ross DD | title = A multidrug resistance transporter from human MCF-7 breast cancer cells | journal = Proc Natl Acad Sci U S A | volume = 95 | issue = 26 | pages = 15665–70 |date=Jan 1999 | pmid = 9861027 | pmc = 28101 | doi =10.1073/pnas.95.26.15665  }}</ref> ABCG2 has also been designated as '''CDw338''' ([[cluster of differentiation]] w338).
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== Function ==
| update_summary = yes
 
| update_citations = yes
The membrane-associated protein encoded by this gene is included in the superfamily of [[ATP-binding cassette transporter|ATP-binding cassette (ABC) transporters]]. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. Alternatively referred to as the [[breast cancer]] resistance protein, this protein functions as a xenobiotic transporter which may play a role in multi-drug resistance to chemotherapeutic agents including mitoxantrone and camptothecin analogues. Early observations of significant ABCG2-mediated resistance to anthracyclines were subsequently attributed mutations encountered in vitro but not in nature or the clinic. Significant expression of this protein has been observed in the [[placenta]],<ref>{{cite web | title = Entrez Gene: ABCG2 ATP-binding cassette, sub-family G (WHITE), member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9429| accessdate = }}</ref> and it has been shown to have a role in protecting the fetus from [[xenobiotic]]s in the maternal circulation.<ref name = "Vlaming">{{cite journal | vauthors = Vlaming ML, Lagas JS, Schinkel AH | title = Physiological and pharmacological roles of ABCG2 (BCRP): recent findings in Abcg2 knockout mice | journal = Adv. Drug Deliv. Rev. | volume = 61 | issue = 1 | pages = 14–25 | date = January  2009 | pmid = 19118589 | doi = 10.1016/j.addr.2008.08.007 | url = }}</ref>
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The transporter has also been shown to play protective roles in blocking absorption at the [[apical membrane]] of the intestine, and at the [[blood-testis barrier]],<ref name = "Vlaming"/> the [[blood–brain barrier]],<ref name = "Vlaming"/> and the membranes of [[Hematopoietic stem cell|hematopoietic progenitor]] and other [[stem cell]]s. At the apical membranes of the liver and kidney, it enhances excretion of xenobiotics. In the lactating mammary gland, it has a role on excreting vitamins such as [[riboflavin]] and [[biotin]] into milk.<ref name = "Vlaming"/> In the kidney and gastrointestinal tract, it has a role in urate excretion.
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = ATP-binding cassette, sub-family G (WHITE), member 2
| HGNCid = 74
| Symbol = ABCG2
| AltSymbols =; MRX; BCRP1; ABC15; ABCP; BCRP; BMDP; CDw338; EST157481; MGC102821; MXR; MXR1
| OMIM = 603756
| ECnumber = 
| Homologene = 55852
| MGIid = 1347061
| GeneAtlas_image1 = PBB_GE_ABCG2_209735_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008559 |text = xenobiotic-transporting ATPase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0042493 |text = response to drug}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9429
    | Hs_Ensembl = ENSG00000118777
    | Hs_RefseqProtein = NP_004818
    | Hs_RefseqmRNA = NM_004827
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 89230441
    | Hs_GenLoc_end = 89299035
    | Hs_Uniprot = Q9UNQ0
    | Mm_EntrezGene = 26357
    | Mm_Ensembl = ENSMUSG00000029802
    | Mm_RefseqmRNA = NM_011920
    | Mm_RefseqProtein = NP_036050
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 58526249
    | Mm_GenLoc_end = 58622028
    | Mm_Uniprot = Q7TMS5
  }}
}}
'''ATP-binding cassette, sub-family G (WHITE), member 2''', also known as '''ABCG2''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactive pathway map ==
{{PBB_Summary
{|
| section_title =
|{{FluoropyrimidineActivity WP1601|highlight=ABCG2}}
| summary_text = The membrane-associated protein encoded by this gene is included in the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. Alternatively referred to as a breast cancer resistance protein, this protein functions as a xenobiotic transporter which may play a major role in multi-drug resistance. It likely serves as a cellular defense mechanism in response to mitoxantrone and anthracycline exposure. Significant expression of this protein has been observed in the placenta, which may suggest a potential role for this molecule in placenta tissue.<ref>{{cite web | title = Entrez Gene: ABCG2 ATP-binding cassette, sub-family G (WHITE), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9429| accessdate = }}</ref>
|{{IrinotecanPathway_WP229|highlight=ABCG2}}
}}
|}


==See also==
==See also==
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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal  | vauthors=Hazai E, Bikadi Z |title=Homology modeling of breast cancer resistance protein (ABCG2) |journal=J Struct Biol |volume=162 |issue= 1 |pages= 63–74 |year= 2008 |pmid= 18249138 |doi= 10.1016/j.jsb.2007.12.001 }}
*{{cite journal | author=Abbott BL | title=ABCG2 (BCRP): a cytoprotectant in normal and malignant stem cells | journal=Clin Adv Hematol Oncol | volume=4 | issue=1 | year=2006 | pmid=16562373 | pages=63–72}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Schmitz G, Langmann T, Heimerl S |title=Role of ABCG1 and other ABCG family members in lipid metabolism. |journal=J. Lipid Res. |volume=42 |issue= 10 |pages= 1513-20 |year= 2002 |pmid= 11590207 |doi=  }}
*{{cite journal  | vauthors=Schmitz G, Langmann T, Heimerl S |title=Role of ABCG1 and other ABCG family members in lipid metabolism |journal=J. Lipid Res. |volume=42 |issue= 10 |pages= 1513–20 |year= 2002 |pmid= 11590207 |doi=  }}
*{{cite journal  | author=Ejendal KF, Hrycyna CA |title=Multidrug resistance and cancer: the role of the human ABC transporter ABCG2. |journal=Curr. Protein Pept. Sci. |volume=3 |issue= 5 |pages= 503-11 |year= 2003 |pmid= 12369998 |doi=  }}
*{{cite journal  | vauthors=Ejendal KF, Hrycyna CA |title=Multidrug resistance and cancer: the role of the human ABC transporter ABCG2 |journal=Curr. Protein Pept. Sci. |volume=3 |issue= 5 |pages= 503–11 |year= 2003 |pmid= 12369998 |doi=10.2174/1389203023380521 }}
*{{cite journal  | author=Doyle LA, Ross DD |title=Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2). |journal=Oncogene |volume=22 |issue= 47 |pages= 7340-58 |year= 2003 |pmid= 14576842 |doi= 10.1038/sj.onc.1206938 }}
*{{cite journal  | vauthors=Doyle LA, Ross DD |title=Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2) |journal=Oncogene |volume=22 |issue= 47 |pages= 7340–58 |year= 2003 |pmid= 14576842 |doi= 10.1038/sj.onc.1206938 }}
*{{cite journal  | author=Sugimoto Y, Tsukahara S, Ishikawa E, Mitsuhashi J |title=Breast cancer resistance protein: molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics. |journal=Cancer Sci. |volume=96 |issue= 8 |pages= 457-65 |year= 2005 |pmid= 16108826 |doi= 10.1111/j.1349-7006.2005.00081.x }}
*{{cite journal  | vauthors=Sugimoto Y, Tsukahara S, Ishikawa E, Mitsuhashi J |title=Breast cancer resistance protein: molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics |journal=Cancer Sci. |volume=96 |issue= 8 |pages= 457–65 |year= 2005 |pmid= 16108826 |doi= 10.1111/j.1349-7006.2005.00081.x }}
*{{cite journal  | author=Ishikawa T, Tamura A, Saito H, ''et al.'' |title=Pharmacogenomics of the human ABC transporter ABCG2: from functional evaluation to drug molecular design. |journal=Naturwissenschaften |volume=92 |issue= 10 |pages= 451-63 |year= 2006 |pmid= 16160819 |doi= 10.1007/s00114-005-0019-4 }}
*{{cite journal  | vauthors=Ishikawa T, Tamura A, Saito H |title=Pharmacogenomics of the human ABC transporter ABCG2: from functional evaluation to drug molecular design |journal=Naturwissenschaften |volume=92 |issue= 10 |pages= 451–63 |year= 2006 |pmid= 16160819 |doi= 10.1007/s00114-005-0019-4 |display-authors=etal}}
*{{cite journal  | author=Krishnamurthy P, Schuetz JD |title=Role of ABCG2/BCRP in biology and medicine. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=46 |issue=  |pages= 381-410 |year= 2006 |pmid= 16402910 |doi= 10.1146/annurev.pharmtox.46.120604.141238 }}
*{{cite journal  | vauthors=Krishnamurthy P, Schuetz JD |title=Role of ABCG2/BCRP in biology and medicine |journal=Annu. Rev. Pharmacol. Toxicol. |volume=46 |issue=  |pages= 381–410 |year= 2006 |pmid= 16402910 |doi= 10.1146/annurev.pharmtox.46.120604.141238 }}
*{{cite journal  | author=Robey RW, Polgar O, Deeken J, ''et al.'' |title=ABCG2: determining its relevance in clinical drug resistance. |journal=Cancer Metastasis Rev. |volume=26 |issue= 1 |pages= 39-57 |year= 2007 |pmid= 17323127 |doi= 10.1007/s10555-007-9042-6 }}
*{{cite journal  | vauthors=Robey RW, Polgar O, Deeken J |title=ABCG2: determining its relevance in clinical drug resistance |journal=Cancer Metastasis Rev. |volume=26 |issue= 1 |pages= 39–57 |year= 2007 |pmid= 17323127 |doi= 10.1007/s10555-007-9042-6 |display-authors=etal}}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{Membrane transport proteins}}
* {{MeshName|ABCG2+protein,+human}}
* {{UCSC gene info|ABCG2}}
 
{{NLM content}}
{{Clusters of differentiation}}
{{ABC transporters}}


{{DEFAULTSORT:Abcg2}}
[[Category:Clusters of differentiation]]
[[Category:ABC transporters]]
[[Category:ABC transporters]]
{{WikiDoc Help Menu}}
{{WikiDoc Sources}}

Latest revision as of 12:01, 10 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

ATP-binding cassette super-family G member 2 is a protein that in humans is encoded by the ABCG2 gene.[1][2] ABCG2 has also been designated as CDw338 (cluster of differentiation w338).

Function

The membrane-associated protein encoded by this gene is included in the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. Alternatively referred to as the breast cancer resistance protein, this protein functions as a xenobiotic transporter which may play a role in multi-drug resistance to chemotherapeutic agents including mitoxantrone and camptothecin analogues. Early observations of significant ABCG2-mediated resistance to anthracyclines were subsequently attributed mutations encountered in vitro but not in nature or the clinic. Significant expression of this protein has been observed in the placenta,[3] and it has been shown to have a role in protecting the fetus from xenobiotics in the maternal circulation.[4]

The transporter has also been shown to play protective roles in blocking absorption at the apical membrane of the intestine, and at the blood-testis barrier,[4] the blood–brain barrier,[4] and the membranes of hematopoietic progenitor and other stem cells. At the apical membranes of the liver and kidney, it enhances excretion of xenobiotics. In the lactating mammary gland, it has a role on excreting vitamins such as riboflavin and biotin into milk.[4] In the kidney and gastrointestinal tract, it has a role in urate excretion.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
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Fluorouracil (5-FU) Activity edit
  1. The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
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Irinotecan Pathway edit
  1. The interactive pathway map can be edited at WikiPathways: "IrinotecanPathway_WP46359".

See also

References

  1. Allikmets R, Gerrard B, Hutchinson A, Dean M (Feb 1997). "Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database". Hum Mol Genet. 5 (10): 1649–55. doi:10.1093/hmg/5.10.1649. PMID 8894702.
  2. Doyle LA, Yang W, Abruzzo LV, Krogmann T, Gao Y, Rishi AK, Ross DD (Jan 1999). "A multidrug resistance transporter from human MCF-7 breast cancer cells". Proc Natl Acad Sci U S A. 95 (26): 15665–70. doi:10.1073/pnas.95.26.15665. PMC 28101. PMID 9861027.
  3. "Entrez Gene: ABCG2 ATP-binding cassette, sub-family G (WHITE), member 2".
  4. 4.0 4.1 4.2 4.3 Vlaming ML, Lagas JS, Schinkel AH (January 2009). "Physiological and pharmacological roles of ABCG2 (BCRP): recent findings in Abcg2 knockout mice". Adv. Drug Deliv. Rev. 61 (1): 14–25. doi:10.1016/j.addr.2008.08.007. PMID 19118589.

Further reading

  • Hazai E, Bikadi Z (2008). "Homology modeling of breast cancer resistance protein (ABCG2)". J Struct Biol. 162 (1): 63–74. doi:10.1016/j.jsb.2007.12.001. PMID 18249138.
  • Abbott BL (2006). "ABCG2 (BCRP): a cytoprotectant in normal and malignant stem cells". Clin Adv Hematol Oncol. 4 (1): 63–72. PMID 16562373.
  • Schmitz G, Langmann T, Heimerl S (2002). "Role of ABCG1 and other ABCG family members in lipid metabolism". J. Lipid Res. 42 (10): 1513–20. PMID 11590207.
  • Ejendal KF, Hrycyna CA (2003). "Multidrug resistance and cancer: the role of the human ABC transporter ABCG2". Curr. Protein Pept. Sci. 3 (5): 503–11. doi:10.2174/1389203023380521. PMID 12369998.
  • Doyle LA, Ross DD (2003). "Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2)". Oncogene. 22 (47): 7340–58. doi:10.1038/sj.onc.1206938. PMID 14576842.
  • Sugimoto Y, Tsukahara S, Ishikawa E, Mitsuhashi J (2005). "Breast cancer resistance protein: molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics". Cancer Sci. 96 (8): 457–65. doi:10.1111/j.1349-7006.2005.00081.x. PMID 16108826.
  • Ishikawa T, Tamura A, Saito H, et al. (2006). "Pharmacogenomics of the human ABC transporter ABCG2: from functional evaluation to drug molecular design". Naturwissenschaften. 92 (10): 451–63. doi:10.1007/s00114-005-0019-4. PMID 16160819.
  • Krishnamurthy P, Schuetz JD (2006). "Role of ABCG2/BCRP in biology and medicine". Annu. Rev. Pharmacol. Toxicol. 46: 381–410. doi:10.1146/annurev.pharmtox.46.120604.141238. PMID 16402910.
  • Robey RW, Polgar O, Deeken J, et al. (2007). "ABCG2: determining its relevance in clinical drug resistance". Cancer Metastasis Rev. 26 (1): 39–57. doi:10.1007/s10555-007-9042-6. PMID 17323127.

External links

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