KDM8 report

I. Expression across cell types

Insufficient scRNA-seq data for expression of KDM8 at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of KDM8 at tissue level.

III. Associated gene sets

GO_0001701Biological processin utero embryonic development
GO_0031648Biological processprotein destabilization
GO_0006338Biological processchromatin remodeling
GO_0032922Biological processcircadian regulation of gene expression
GO_0045893Biological processpositive regulation of DNA-templated transcription
GO_0006508Biological processproteolysis
GO_1901796Biological processregulation of signal transduction by p53 class mediator
GO_0048144Biological processfibroblast proliferation
GO_0000086Biological processG2/M transition of mitotic cell cycle
GO_0045892Biological processnegative regulation of DNA-templated transcription
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0005694Cellular componentchromosome
GO_0005634Cellular componentnucleus
GO_0035064Molecular functionmethylated histone binding
GO_0004175Molecular functionendopeptidase activity
GO_0003682Molecular functionchromatin binding
GO_0106157Molecular functionpeptidyl-arginine 3-dioxygenase activity
GO_0002039Molecular functionp53 binding
GO_0046872Molecular functionmetal ion binding
GO_0004177Molecular functionaminopeptidase activity
GO_0005515Molecular functionprotein binding
GO_0051864Molecular functionhistone H3K36 demethylase activity

IV. Literature review

[source]
Gene nameKDM8
Protein nameLysine demethylase 8
Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.73) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8)
SynonymsJMJD5
DescriptionFUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase . Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation . Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity . Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage . Additionally, acts as a Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established . Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation . Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition . Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation . Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition . Regulates the circadian gene expression in the liver (By similarity). Represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a catalytically-independent manner . Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation . .

AccessionsENST00000286096.9 [Q8N371-1]
ENST00000441782.6 [Q8N371-3]
ENST00000569329.1
H3BM39
ENST00000567735.1
H3BPT5
ENST00000562733.1
H3BR76
ENST00000568965.1 [Q8N371-2]
Q8N371