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血清応答因子

ウィキペディアから、無料の百科事典
SRF
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

1HBX, 1K6O, 1SRS

識別子
記号SRF, MCM1, serum response factor
外部IDOMIM: 600589 MGI: 106658 HomoloGene: 31135 GeneCards: SRF
遺伝子の位置 (ヒト)
6番染色体 (ヒト)
染色体6番染色体 (ヒト)[1]
6番染色体 (ヒト)
SRF遺伝子の位置
SRF遺伝子の位置
バンドデータ無し開始点43,171,269 bp[1]
終点43,181,506 bp[1]
遺伝子の位置 (マウス)
17番染色体 (マウス)
染色体17番染色体 (マウス)[2]
17番染色体 (マウス)
SRF遺伝子の位置
SRF遺伝子の位置
バンドデータ無し開始点46,859,255 bp[2]
終点46,867,101 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• protein dimerization activity
• DNA-binding transcription factor activity
• DNA-binding transcription activator activity, RNA polymerase II-specific
• RNA polymerase II general transcription initiation factor activity
• primary miRNA binding
• 転写因子結合
• RNA polymerase II cis-regulatory region sequence-specific DNA binding
• protein homodimerization activity
• serum response element binding
• クロマチン結合
• 血漿タンパク結合
• DNA結合
• sequence-specific DNA binding
• transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding
• chromatin DNA binding
• transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding
• cis-regulatory region sequence-specific DNA binding
• DNA-binding transcription factor activity, RNA polymerase II-specific
• ヒストンデアセチラーゼ結合
• RNA polymerase II-specific DNA-binding transcription factor binding
細胞の構成要素• 細胞質
• 細胞核
• 核質
生物学的プロセス• dorsal aorta morphogenesis
• 気管支軟骨発生
• muscle cell cellular homeostasis
• lung smooth muscle development
• regulation of water loss via skin
• transcription by RNA polymerase II
• stress fiber assembly
• cell migration involved in sprouting angiogenesis
• platelet activation
• cardiac myofibril assembly
• heart looping
• 細胞老化
• face development
• regulation of cell adhesion
• 長期抑圧
• neuron projection development
• morphogenesis of an epithelial sheet
• positive regulation of filopodium assembly
• primitive streak formation
• cellular response to glucose stimulus
• negative regulation of cell population proliferation
• response to cytokine
• regulation of transcription, DNA-templated
• heart trabecula formation
• actin filament organization
• 胸腺発生
• angiogenesis involved in wound healing
• 血小板形成
• neuron development
• in utero embryonic development
• transcription, DNA-templated
• positive regulation of transcription, DNA-templated
• 心臓発生
• positive regulation of cell differentiation
• branching involved in blood vessel morphogenesis
• positive regulation of axon extension
• positive regulation of smooth muscle contraction
• 気管軟骨発生
• 毒性物質への反応
• positive regulation of pri-miRNA transcription by RNA polymerase II
• positive regulation of transcription by glucose
• regulation of smooth muscle cell differentiation
• epithelial structure maintenance
• associative learning
• skin morphogenesis
• positive regulation of DNA-binding transcription factor activity
• epithelial cell-cell adhesion
• neuron migration
• positive regulation of transcription initiation from RNA polymerase II promoter
• eyelid development in camera-type eye
• 甲状腺発生
• negative regulation of amyloid-beta clearance
• negative regulation of cell migration
• developmental growth
• hematopoietic stem cell differentiation
• 原腸形成
• trophectodermal cell differentiation
• positive thymic T cell selection
• ホルモンへの反応
• cell-matrix adhesion
• sarcomere organization
• actin cytoskeleton organization
• megakaryocyte development
• 低酸素症への反応
• lung morphogenesis
• mesoderm formation
• cardiac vascular smooth muscle cell differentiation
• mRNA transcription by RNA polymerase II
• 多細胞個体の発生
• tangential migration from the subventricular zone to the olfactory bulb
• 長期記憶
• contractile actin filament bundle assembly
• bicellular tight junction assembly
• leukocyte differentiation
• 海馬発生
• positive regulation of transcription by RNA polymerase II
• erythrocyte development
• negative regulation of pri-miRNA transcription by RNA polymerase II
• 前脳発生
• cell-cell adhesion
出典:Amigo / QuickGO
オルソログ
種ヒトマウス
Entrez

6722

20807

Ensembl

ENSG00000112658

ENSMUSG00000015605

UniProt

P11831,A0A024RD16

Q9JM73

RefSeq
(mRNA)

NM_003131
NM_001292001

NM_020493

RefSeq
(タンパク質)

NP_001278930
NP_003122
NP_003122.1

NP_065239

場所
(UCSC)		Chr 6: 43.17 – 43.18 MbChr 6: 46.86 – 46.87 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

血清応答因子（けっせいおうとういんし、英: serum response factor、略称: SRF）は、転写因子として機能するタンパク質である[5]。

機能

血清応答因子はMADSボックススーパーファミリーに属する転写因子である[6]。このタンパク質は、標的遺伝子のプロモーター内の血清応答エレメント（serum response element; SRE）に結合する。このタンパク質はc-fosを含む多くの最初期遺伝子の活性を調節しており、それによって細胞周期の調節、アポトーシス、細胞成長、細胞分化に関与している。SRFは多くのシグナル伝達経路の下流の標的となっており、一例としてMAPK経路はTCFファミリー（ternary complex factor）を介してSRFの転写活性を調節する[7][8]。

SRFは胚発生時に重要であり、中胚葉の形成と関連づけられている[9][10]。完全に発達した哺乳類では、SRFは骨格筋の成長に重要である[11]。SRFとステロイドホルモン受容体（英語版）などとの相互作用は、ステロイドによる筋成長の調節に寄与している可能性がある[12]。またELK1などのTCFとミオカルディン（英語版）はSRFをめぐって競合し、それぞれ平滑筋遺伝子の発現を抑制、促進する[13]。

臨床的意義

SRFの欠損は乾癬やその他の皮膚疾患と関連している[14]。

相互作用

SRFは次に挙げる因子と相互作用することが示されている。

出典

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000112658 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000015605 - Ensembl, May 2017
  3. ↑ Human PubMed Reference:
  4. ↑ Mouse PubMed Reference:
  5. ↑ “Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element”. Cell 55 (6): 989–1003. (December 1988). doi:10.1016/0092-8674(88)90244-9. PMID 3203386.
  6. ↑ “The MADS-box family of transcription factors”. Eur. J. Biochem. 229 (1): 1–13. (April 1995). doi:10.1111/j.1432-1033.1995.0001l.x. PMID 7744019.
  7. ↑ “Isolation and characterization of SRF accessory proteins”. Philos. Trans. R. Soc. Lond. B Biol. Sci. 340 (1293): 325–32. (June 1993). Bibcode: 1993RSPTB.340..325D. doi:10.1098/rstb.1993.0074. PMID 8103935.
  8. ↑ “SRF serum response factor [Homo sapiens (human) - Gene - NCBI]”. www.ncbi.nlm.nih.gov. 2024年10月5日閲覧。
  9. ↑ “Combinatorial expression of GATA4, Nkx2-5, and serum response factor directs early cardiac gene activity”. J. Biol. Chem. 277 (28): 25775–82. (July 2002). doi:10.1074/jbc.M203122200. PMID 11983708.
  10. ↑ “Serum response factor, an enriched cardiac mesoderm obligatory factor, is a downstream gene target for Tbx genes”. J. Biol. Chem. 280 (12): 11816–28. (March 2005). doi:10.1074/jbc.M412408200. PMID 15591049.
  11. ↑ “Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice”. Proc. Natl. Acad. Sci. U.S.A. 102 (4): 1082–7. (January 2005). Bibcode: 2005PNAS..102.1082L. doi:10.1073/pnas.0409103102. PMC 545866. PMID 15647354.
  12. ↑ “Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene”. J. Biol. Chem. 280 (9): 7786–92. (March 2005). doi:10.1074/jbc.M413992200. PMID 15623502.
  13. ↑ Wang, Zhigao; Wang, Da-Zhi; Hockemeyer, Dirk; McAnally, John; Nordheim, Alfred; Olson, Eric N. (2004-03-11). “Myocardin and ternary complex factors compete for SRF to control smooth muscle gene expression”. Nature 428 (6979): 185–189. doi:10.1038/nature02382. ISSN 1476-4687. PMID 15014501.
  14. ↑ “Loss of serum response factor in keratinocytes results in hyperproliferative skin disease in mice”. J. Clin. Invest. 119 (4): 899–910. (April 2009). doi:10.1172/JCI37771. PMC 2662566. PMID 19307725.
  15. ↑ “Novel transcription coactivator complex containing activating signal cointegrator 1”. Mol. Cell. Biol. 22 (14): 5203–11. (July 2002). doi:10.1128/mcb.22.14.5203-5211.2002. PMC 139772. PMID 12077347.
  16. 1 2 “Interaction of ATF6 and serum response factor”. Mol. Cell. Biol. 17 (9): 4957–66. (September 1997). doi:10.1128/MCB.17.9.4957. PMC 232347. PMID 9271374.
  17. ↑ “Ras regulates the association of serum response factor and CCAAT/enhancer-binding protein beta”. J. Biol. Chem. 274 (20): 14224–8. (May 1999). doi:10.1074/jbc.274.20.14224. PMID 10318842.
  18. ↑ “Regulation of the cfos serum response element by C/EBPbeta”. Mol. Cell. Biol. 17 (3): 1744–55. (March 1997). doi:10.1128/mcb.17.3.1744. PMC 231899. PMID 9032301.
  19. 1 2 “PML-nuclear bodies are involved in cellular serum response”. Genes Cells 8 (3): 275–86. (March 2003). doi:10.1046/j.1365-2443.2003.00632.x. PMID 12622724.
  20. ↑ “The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex”. EMBO J. 20 (12): 3018–28. (June 2001). doi:10.1093/emboj/20.12.3018. PMC 150215. PMID 11406578.
  21. ↑ “Cardiac tissue enriched factors serum response factor and GATA-4 are mutual coregulators”. Mol. Cell. Biol. 20 (20): 7550–8. (October 2000). doi:10.1128/mcb.20.20.7550-7558.2000. PMC 86307. PMID 11003651.
  22. ↑ “Serum response factor-GATA ternary complex required for nuclear signaling by a G-protein-coupled receptor”. Mol. Cell. Biol. 21 (4): 1036–44. (February 2001). doi:10.1128/MCB.21.4.1036-1044.2001. PMC 99558. PMID 11158291.
  23. ↑ “Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor”. Nature 373 (6515): 632–5. (February 1995). Bibcode: 1995Natur.373..632J. doi:10.1038/373632a0. PMID 7854423.
  24. ↑ “Role of transcription factor TFIIF in serum response factor-activated transcription”. J. Biol. Chem. 269 (5): 3489–97. (February 1994). doi:10.1016/S0021-9258(17)41889-8. PMID 8106390.
  25. ↑ “A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I”. Genes Dev. 11 (19): 2482–93. (October 1997). doi:10.1101/gad.11.19.2482. PMC 316568. PMID 9334314.
  26. ↑ “TFII-I enhances activation of the c-fos promoter through interactions with upstream elements”. Mol. Cell. Biol. 18 (6): 3310–20. (June 1998). doi:10.1128/mcb.18.6.3310. PMC 108912. PMID 9584171.
  27. ↑ “Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins”. J. Biol. Chem. 271 (9): 5258–64. (March 1996). doi:10.1074/jbc.271.9.5258. PMID 8617811.
  28. ↑ “Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter”. Mol. Cell. Biol. 19 (4): 2577–84. (April 1999). doi:10.1128/MCB.19.4.2577. PMC 84050. PMID 10082523.
  29. ↑ “Identification of proteins that interact with NF-YA”. FEBS Lett. 460 (1): 41–5. (October 1999). Bibcode: 1999FEBSL.460...41Y. doi:10.1016/s0014-5793(99)01311-3. PMID 10571058.
  30. ↑ “Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor”. J. Biol. Chem. 275 (17): 12470–4. (April 2000). doi:10.1074/jbc.275.17.12470. PMID 10777532.
  31. ↑ “Steroid receptor coactivator-1 interacts with serum response factor and coactivates serum response element-mediated transactivations”. J. Biol. Chem. 273 (44): 28564–7. (October 1998). doi:10.1074/jbc.273.44.28564. PMID 9786846.
  32. ↑ “Physical interaction between the MADS box of serum response factor and the TEA/ATTS DNA-binding domain of transcription enhancer factor-1”. J. Biol. Chem. 276 (13): 10413–22. (March 2001). doi:10.1074/jbc.M008625200. PMID 11136726.

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