ミニ染色体維持複合体成分2

MCM2
PDBに登録されている構造
PDBオルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧

4UUZ, 5BNV, 5BNX, 5BO0, 5C3I, 5JA4

識別子
記号MCM2, BM28, CCNL1, CDCL1, D3S3194, MITOTIN, cdc19, minichromosome maintenance complex component 2, DFNA70
外部IDOMIM: 116945 MGI: 105380 HomoloGene: 3325 GeneCards: MCM2
遺伝子の位置 (ヒト)
3番染色体 (ヒト)
染色体3番染色体 (ヒト)[1]
3番染色体 (ヒト)
MCM2遺伝子の位置
MCM2遺伝子の位置
バンドデータ無し開始点127,598,410 bp[1]
終点127,622,436 bp[1]
遺伝子の位置 (マウス)
6番染色体 (マウス)
染色体6番染色体 (マウス)[2]
6番染色体 (マウス)
MCM2遺伝子の位置
MCM2遺伝子の位置
バンドデータ無し開始点88,860,456 bp[2]
終点88,875,762 bp[2]
RNA発現パターン
さらなる参照発現データ
遺伝子オントロジー
分子機能• DNA結合
• ヌクレオチド結合
• helicase activity
• histone binding
• 金属イオン結合
• DNA helicase activity
• 血漿タンパク結合
• 酵素結合
• DNA replication origin binding
• 加水分解酵素活性
• ATP binding
• single-stranded DNA binding
• single-stranded DNA helicase activity
• 3'-5' DNA helicase activity
細胞の構成要素• 細胞質
• microtubule cytoskeleton
• 核質
• nuclear origin of replication recognition complex
• クロマチン
• MCM complex
• 細胞核
• 細胞質基質
• 核小体
生物学的プロセス• cellular response to interleukin-4
• nucleosome assembly
• G1期
• DNA複製
• DNA replication initiation
• DNA unwinding involved in DNA replication
• アポトーシス
• 細胞周期
• cochlea development
• G1/S transition of mitotic cell cycle
• negative regulation of DNA helicase activity
• double-strand break repair via break-induced replication
• pre-replicative complex assembly involved in nuclear cell cycle DNA replication
• mitotic DNA replication initiation
出典:Amigo / QuickGO
オルソログ
種ヒトマウス
Entrez

4171

17216

Ensembl

ENSG00000073111

ENSMUSG00000002870

UniProt

P49736,H7C4N9

P97310

RefSeq
(mRNA)

NM_004526

NM_008564

RefSeq
(タンパク質)

NP_004517

NP_032590

場所
(UCSC)		Chr 3: 127.6 – 127.62 MbChr 3: 88.86 – 88.88 Mb
PubMed検索[3][4]
ウィキデータ
閲覧/編集 ヒト閲覧/編集 マウス

ミニ染色体維持複合体成分2（MCM2: minichromosome maintenance complex component 2）あるいはDNA複製ライセンス化因子MCM2（DNA replication licensing factor MCM2）は、ヒトではMCM2遺伝子によってコードされるタンパク質である[5][6]。

機能

MCM2は、真核生物のDNA複製の開始に関与する高度に保存されたミニ染色体維持複合体（MCM）の6つの構成タンパク質のうちの一つである。MCMは、複製前複合体（pre-RC）の重要な構成要素であり、複製フォークの形成や他のDNA複製関連タンパク質の動員に関与していると考えられている。MCM2は、他のMCM成分であるMCM4、MCM6、及びMCM7と結合し、MCMのDNAヘリカーゼ活性を調節することが示されている。このタンパク質はリン酸化を受けて活性化するため、プロテインキナーゼであるCDC2およびCDC7によって調節される[7]。

相互作用分子

MCM2は、以下の生体分子と相互作用する。

  • AKAP8[8]
  • CDC7関連タンパク質キナーゼ[9]
  • MCM3[9]
  • MCM4[9][10][11][12]
  • MCM5[9][13]
  • MCM6[9][10][11][14][15]
  • MCM7[9][10][11][15][16]
  • ORC1[9]
  • ORC2[9]
  • ORC4[9]
  • ORC5[9]
  • 複製タンパク質A1[9]

脚注

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000073111 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002870 - Ensembl, May 2017
  3. ^ Human PubMed Reference:
  4. ^ Mouse PubMed Reference:
  5. ^ “Nuclear matrix protein mitotin messenger RNA is expressed at constant levels during the cell cycle”. Biochem Biophys Res Commun 177 (1): 395–400. (Jul 1991). doi:10.1016/0006-291X(91)91996-P. PMID 1710453. 
  6. ^ “The human gene for nuclear protein BM28 (CDCL1), a new member of the early S-phase family of proteins, maps to chromosome band 3q21”. Cytogenet Cell Genet 65 (4): 276–7. (Jan 1994). doi:10.1159/000133647. PMID 8258304. 
  7. ^ “Entrez Gene: MCM2 MCM2 minichromosome maintenance deficient 2, mitotin (S. cerevisiae)”. 2021年7月27日閲覧。
  8. ^ “Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication”. J. Biol. Chem. 278 (29): 26750–6. (Jul 2003). doi:10.1074/jbc.M300765200. PMID 12740381. 
  9. ^ a b c d e f g h i j k “Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells”. J. Mol. Biol. 327 (1): 111–28. (Mar 2003). doi:10.1016/s0022-2836(03)00079-2. PMID 12614612. 
  10. ^ a b c “Mammalian Mcm2/4/6/7 complex forms a toroidal structure”. Genes Cells 8 (5): 413–21. (May 2003). doi:10.1046/j.1365-2443.2003.00645.x. PMID 12694531. 
  11. ^ a b c “Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity”. Mol. Cell. Biol. 19 (12): 8003–15. (Dec 1999). doi:10.1128/MCB.19.12.8003. PMC 84885. PMID 10567526. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84885/. 
  12. ^ “Binding of human minichromosome maintenance proteins with histone H3”. J. Biol. Chem. 271 (39): 24115–22. (Sep 1996). doi:10.1074/jbc.271.39.24115. PMID 8798650. 
  13. ^ “Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma”. Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3034–9. (Mar 2001). doi:10.1073/pnas.061487598. PMC 30602. PMID 11248027. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC30602/. 
  14. ^ “Towards a proteome-scale map of the human protein-protein interaction network”. Nature 437 (7062): 1173–8. (Oct 2005). doi:10.1038/nature04209. PMID 16189514. 
  15. ^ a b “Roles of Mcm7 and Mcm4 subunits in the DNA helicase activity of the mouse Mcm4/6/7 complex”. J. Biol. Chem. 277 (45): 42471–9. (Nov 2002). doi:10.1074/jbc.M205769200. PMID 12207017. 
  16. ^ “In vivo interaction of human MCM heterohexameric complexes with chromatin. Possible involvement of ATP”. J. Biol. Chem. 272 (16): 10928–35. (Apr 1997). doi:10.1074/jbc.272.16.10928. PMID 9099751. 

参考文献

 

  • “Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1.”. DNA Res. 1 (1): 27–35. (1995). doi:10.1093/dnares/1.1.27. PMID 7584026. 
  • “Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement).”. DNA Res. 1 (1): 47–56. (1995). doi:10.1093/dnares/1.1.47. PMID 7584028. 
  • “Isolation and mapping of a human gene (MCM2) encoding a product homologous to yeast proteins involved in DNA replication.”. Cytogenet. Cell Genet. 68 (3–4): 226–30. (1995). doi:10.1159/000133918. PMID 7842741. 
  • “A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division”. J. Cell Sci. 107 (1): 253–65. (1994). PMID 8175912. 
  • “Binding of human minichromosome maintenance proteins with histone H3”. J. Biol. Chem. 271 (39): 24115–22. (1996). doi:10.1074/jbc.271.39.24115. PMID 8798650. 
  • “Cell cycle- and chromatin binding state-dependent phosphorylation of human MCM heterohexameric complexes. A role for cdc2 kinase”. J. Biol. Chem. 273 (27): 17095–101. (1998). doi:10.1074/jbc.273.27.17095. PMID 9642275. 
  • “Mammalian Cdc7-Dbf4 protein kinase complex is essential for initiation of DNA replication”. EMBO J. 18 (20): 5703–13. (1999). doi:10.1093/emboj/18.20.5703. PMC 1171637. PMID 10523313. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171637/. 
  • “Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity”. Mol. Cell. Biol. 19 (12): 8003–15. (2000). doi:10.1128/MCB.19.12.8003. PMC 84885. PMID 10567526. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84885/. 
  • “Inhibition of Mcm4,6,7 helicase activity by phosphorylation with cyclin A/Cdk2”. J. Biol. Chem. 275 (21): 16235–41. (2000). doi:10.1074/jbc.M909040199. PMID 10748114. 
  • “Human Cdc7-related kinase complex. In vitro phosphorylation of MCM by concerted actions of Cdks and Cdc7 and that of a critical threonine residue of Cdc7 bY Cdks”. J. Biol. Chem. 275 (37): 29042–52. (2000). doi:10.1074/jbc.M002713200. PMID 10846177. 
  • “The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase”. Nucleic Acids Res. 28 (23): 4769–77. (2001). doi:10.1093/nar/28.23.4769. PMC 115166. PMID 11095689. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC115166/. 
  • “Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1”. J. Biol. Chem. 276 (18): 15397–408. (2001). doi:10.1074/jbc.M011556200. PMID 11278932. 
  • “MCM2--a promising marker for premalignant lesions of the lung: a cohort study”. BMC Cancer 1: 6. (2002). doi:10.1186/1471-2407-1-6. PMC 35283. PMID 11472637. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC35283/. 
  • “Biochemical activities associated with mouse Mcm2 protein”. J. Biol. Chem. 276 (46): 42744–52. (2001). doi:10.1074/jbc.M106861200. PMID 11568184. 
  • “Xenopus Mcm10 binds to origins of DNA replication after Mcm2-7 and stimulates origin binding of Cdc45”. Mol. Cell 9 (2): 233–40. (2002). doi:10.1016/S1097-2765(02)00456-2. PMID 11864598. 
  • “Expression of minichromosome maintenance 2 (MCM2), Ki-67, and cell-cycle-related molecules, and apoptosis in the normal-dysplasia-carcinoma sequence of the oral mucosa”. Pathobiology 69 (3): 150–8. (2002). doi:10.1159/000048770. PMID 11872961. 
  • “MCM2-7 complexes bind chromatin in a distributed pattern surrounding the origin recognition complex in Xenopus egg extracts”. J. Biol. Chem. 277 (36): 33049–57. (2002). doi:10.1074/jbc.M204438200. PMID 12087101. 
  • “Expression of minichromosome maintenance-2 in human malignant fibrous histiocytomas: Correlations with Ki-67 and P53 expression, and apoptosis”. Int. J. Mol. Med. 10 (2): 161–8. (2003). doi:10.3892/ijmm.10.2.161. PMID 12119552.