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Histone Modification Table(ヒストン修飾表)

Histone Modification Table Description

ヌクレオソームは、4つのコアとなるヒストン蛋白(H2A、H2B、H3、H4)と、リンカーヒストン H1で構成されるクロマチンの基本構成単位である。元々、DNA をパッケージングする静的な足場として機能すると考えられてきたが、より最近になって、ヒストンは、クロマチン凝集や DNA へのアクセスし易さを調節する多様な翻訳後修飾を受ける機能的な蛋白であることが示されている。例えば、リジン残基のアセチル化は、長い間、ヒストンのクロマチンへの組込みと転写の活性化に関わっているとされていたが、より最近では、DNA 修復に関与することが確認された。セリンおよびスレオニン残基のリン酸化は、細胞増殖と前初期遺伝子の転写亢進の際に、クロマチン凝集を促進する。リジンおよびアルギニン残基のメチル化は、クロマチンの転写レベルでの活性化または不活性化領域の形成の際、主要な決定要素として機能し、さらには、発生過程におけるゲノムの適正なプログラミングをする上で欠くことはできない。この表は、多くの既知のヒストン修飾因子、関連修飾酵素、提唱されている機能などの引用リストである。


Histone Site Histone-modifying Enzymes Proposed Function Ref. #
H2A Lys4 (S. cerevisiae) Esa1 transcriptional activation (1)
Lys5 (mammals) Tip60, p300/CBP transcriptional activation (2, 3)
Lys7 (S. cerevisiae) Hat1 unknown (4)
Esa1 transcriptional activation (1)
H2B Lys5 p300, ATF2 transcriptional activation (3, 5)
Lys11 (S. cerevisiae) Gcn5 transcriptional activation (6)
Lys12 (mammals) p300/CBP, ATF2 transcriptional activation (3, 5)
Lys15 (mammals) p300/CBP, ATF2 transcriptional activation (3, 5)
Lys16 (S. cerevisiae) Gcn5, Esa1 transcriptional activation (6)
Lys20 p300 transcriptional activation (3)
H3 Lys4 (S. cerevisiae) Esa1 transcriptional activation (1)
Hpa2 unknown (7)
Lys9 unknown histone deposition (8)
Gcn5, SRC-1 transcriptional activation (9, 10)
Lys14 unknown histone deposition (8)
Gcn5, PCAF transcriptional activation (3, 11)
Esal, Tip60 transcriptional activation (1, 2)
DNA repair (11, 12)
SRC-1 transcriptional activation (10)
Elp3 transcriptional activation (elongation) (13)
Hpa2 unknown (7)
hTFIIIC90 RNA polymerase III transcription (14)
TAF1 RNA polymerase II transcription (15)
Sas2 euchromatin (16)
Sas3 transcriptional activation (elongation) (17)
p300 transcriptional activation (3)
Lys18 Gcn5 transcriptional activation, DNA repair (9)
p300/CBP DNA replication, transcriptional activation (3, 18)
Lys23 unknown histone deposition (8)
Gcn5 transcriptional activation, DNA repair (9)
Sas3 transcriptional activation (elongation) (17)
p300/CBP transcriptional activation (3, 18)
Lys27 Gcn5 transcriptional activation (6)
Lys56 (S. cerevisiae) Spt10 transcriptional activation (19)
DNA repair (20)
H4 Lys5 Hat1 histone deposition (21)
Esal, Tip60 transcriptional activation (1, 2)
DNA repair (11, 12)
ATF2 transcriptional activation (5)
Hpa2 unknown (7)
p300 transcriptional activation (3)
Lys8 Gcn5, PCAF transcriptional activation (3, 22)
Esal, Tip60 transcriptional activation (1, 2)
DNA repair (11, 12)
ATF2 transcriptional activation (5)
Elp3 transcriptional activation (elongation) (13)
p300 transcriptional activation (3)
Lys12 Hat1 histone deposition (21)
telomeric silencing (23)
Esal, Tip60 transcriptional activation (1, 2)
DNA repair (11, 12)
Hpa2 unknown (7)
p300 transcriptional activation (3)
Lys16 Gcn5 transcriptional activation (22)
MOF (D. melanogaster) transcriptional activation (24)
Esal, Tip60 transcriptional activation (1, 2)
DNA repair (11, 12)
ATF2 transcriptional activation (5)
Sas2 euchromatin (2, 6)
Lys91 (S. cerevisiae) Hat1/Hat2 chromatin assembly (25)


Histone Site Histone-modifying Enzymes Proposed Function Ref. #
H1 Lys26 Ezh2 transcriptional silencing (48, 49)
H3 Lys4 Set1 (S. cerevisiae) permissive euchromatin (di-Me) (26)
Set7/9 (vertebrates) transcriptional activation (tri-Me) (27)
MLL, ALL-1 transcriptional activation (28, 29)
Ash1 (D. melanogaster) transcriptional activation (30)
Arg8 PRMT5 transcriptional repression (31)
Lys9 Suv39h,Clr4 transcriptional silencing (tri-Me) (32, 33)
G9a transcriptional repression genomic imprinting (34)
SETDB1 transcriptional repression (tri-Me) (35)
Dim-5 (N.crassa), Kryptonite (A. thaliana) DNA methylation (tri-Me) (36, 37)
Ash1 (D. melanogaster) transcriptional activation (30)
Arg17 CARM1 transcriptional activation (18)
Lys27 Ezh2 transcriptional silencing (38)
X inactivation (tri-Me)
G9a transcriptional silencing (34)
Lys36 Set2 transcriptional activation (elongation) (39)
Lys79 Dot1 euchromatin (40)
transcriptional activation (elongation) (41)
checkpoint response (42)
H4 Arg3 PRMT1 transcriptional activation (43)
PRMT5 transcriptional repression (31)
Lys20 PR-Set7 transcriptional silencing (mono-Me) (44)
Suv4-20h heterochromatin (tri-Me) (45)
Ash1 (D. melanogaster) transcriptional activation (30)
Set9 (S. pombe) checkpoint response (46)
Lys59 unknown transcriptional silencing (47)


Histone Site Histone-modifying Enzymes Proposed Function Ref. #
H1 Ser27 unknown transcriptional activation, chromatin decondensation (48, 49)
H2A Ser1 unknown mitosis, chromatin assembly (50)
MSK1 transcriptional repression (51)
Thr119 (D. melanogaster) NHK1 mitosis (52)
Ser122 (S. cerevisiae) unknown DNA repair (53)
Ser129 (S. cerevisiae) Mec1, Tel1 DNA repair (54, 55)
Ser139 (mammalian H2A.X) ATR, ATM, DNA-PK DNA repair (56, 57, 58)
H2B Ser10 (S. cerevisiae) Ste20 apoptosis (59)
Ser14 (vertebrates) Mst1 apoptosis (60)
unknown DNA repair (61)
Ser33 (D. melanogaster) TAF1 transcriptional activation (62)
H3 Thr3 Haspin/Gsg2 mitosis (63)
Ser10 Aurora-B kinase mitosis, meiosis (64, 65)
MSK1, MSK2 immediate-early gene activation (66)
IKK-α transcriptional activation (67)
Snf1 transcriptional activation (68)
Thr11 (mammals) Dlk/Zip mitosis (69)
Ser28 (mammals) Aurora-B kinase mitosis (70)
MSK1, MSK2 immediate-early activation (66, 71)
H4 Ser1 unknown mitosis, chromatin assembly (50)
CK2 DNA repair (72)


Histone Site Histone-modifying Enzymes Proposed Function Ref. #
H2A Lys119 (mammals) Ring2 spermatogenesis (73)
H2B Lys120 (mammals) UbcH6 meiosis (74)
Lys123 (S. cerevisiae) Rad6 transcriptional activation (75)


Histone Site Histone-modifying Enzymes Proposed Function Ref. #
H2A Lys126 (S. cerevisiae) Ubc9 transcriptional repression (76)
H2B Lys6 or Lys7 (S. cerevisiae) Ubc9 transcriptional repression (76)
H4 N-terminal tail (S. cerevisiae) Ubc9 transcriptional repression (77)


Histone Site Histone-modifying Enzymes Proposed Function Ref. #
H2A Lys9 biotinidase unknown (78)
Lys13 biotinidase unknown (78)
H3 Lys4 biotinidase gene expression (79)
Lys9 biotinidase gene expression (79)
Lys18 biotinidase gene expression (79)
H4 Lys12 biotinidase DNA damage response (80, 81)

CST would like to thank Prof. Craig Peterson, University of Massachusetts Medical School, Worcester, Massachusetts, for reviewing this table.


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created May 2007

revised November 2010

Histone Modification Table(ヒストン修飾表)