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Information on EC 1.14.18.B1 - 5,6-dihydroxyindole-2-carboxylic acid oxidase and Organism(s) Homo sapiens and UniProt Accession Q9UPP1

for references in articles please use BRENDA:EC1.14.18.B1
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Homo sapiens
UNIPROT: Q9UPP1 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
jmjd3, kdm6b, h3k27 demethylase, jumonji domain-containing protein 3, histone h3k27 demethylase, lysine demethylase 6b, h3k27me3 histone demethylase, kdm6ba, 5,6-dihydroxyindole-2-carboxylic acid oxidase, jmjc domain-containing protein 3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
histone demethylase
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PHD finger protein 8
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histone demethylase
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histone H3K27 demethylase
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JmjC domain-containing protein 3
UniProt
Jumonji domain-containing protein 3
UniProt
lysine demethylase 6B
UniProt
SYSTEMATIC NAME
IUBMB Comments
5,6-dihydroxyindole-2-carboxylic acid:oxygen oxidoreductase
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6-dimethyl-L-lysine27 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine27 + succinate + formaldehyde + CO2
show the reaction diagram
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-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine27 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine27 + succinate + formaldehyde + CO2
show the reaction diagram
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-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6-dimethyl-L-lysine27 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine27 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine27 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine27 + succinate + formaldehyde + CO2
show the reaction diagram
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-
-
?
additional information
?
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enzyme PHF8 binds and stabilizes histone H3 N6,N6,N6-trimethyl-L-lysine4, PHF8 is important in maintaining H3K4me3 levels. PHF8 cooperates with KDM3A
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
epidermal keratinocytes
Manually annotated by BRENDA team
CD4+ cells, expression analysis of enzyme in cells from healthy persons and systemic lupus erythematosus patients: significantly decreased H3K27me3 levels and increased JMJD3 binding are detected within the ITGAL (CD11a) promoter locus in SLE CD4+ T cells compared with those in healthy CD4+ T cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
PHF8 knockout by the CRISPR-Cas9 system attenuates hypoxia signaling in 293T cells. Knockdown or knockout of PHF8 by RNAi or CRISPR-Cas9 system reduces the activation of HIF1alpha and the induction of HIF1alpha target genes including KDM3A. Despite the impaired hypoxia induced stabilization of HIF1alpha protein, the upregulation of KDM3A is only attenuated by PHF8 knockout. PHF8 knockdown elevates H3K9me2 at the 3'UTRs of KDM3A, VEGFA and at the TSS of ENO2 under normoxia. Knockdown of PHF8 increases H3K27me2 at the TSS of ENO2 and decreases H3K27me2 at the 3'UTR of ENO2, respective
physiological function
PHF8 regulates hypoxia inducible genes mainly through sustaining the level of trimethylated histone 3 lysine 4 (H3K4me3), an active mark in transcriptional regulation. The positive role of PHF8 in hypoxia signaling extends to hypoxia-induced neuroendocrine differentiation (NED), wherein PHF8 cooperates with KDM3A to regulate the expression of NED genes. The role of PHF8 in hypoxia signaling is associated with the presence of full-length androgen receptor in CRPC cells. PHF8 is an epigenetic factor in hypoxia signaling, and the underlying regulatory mechanisms likely apply to general cancer development involving HIF1alpha. PHF8 regulates hypoxia inducible genes mainly through sustaining the level of trimethylated histone 3 lysine 4 (H3K4me3), an active mark in transcriptional regulation. PHF8 (PHD finger protein 8) is dynamically regulated during the neuroendocrine differentiation that occurs in prostate cancer, and that the c-MYC-miR-22 axis contributes to the regulation of PHF8 in the context of androgen depletion and interleukin-6 treatment. PHF8 plays a critical role in hypoxia signaling as it positively regulates KDM3A which is a critical coactivator of key transcription factor hypoxia-inducible factor 1-alpha, HIF1alpha, indirectly sustains H3K4me3 levels on select hypoxia-inducible genes, and is required for full activation of HIF1alpha through various mechanisms. In the context of prostate cancer, PHF8 appears to execute its regulatory function during hypoxia signaling in androgen receptor-positive prostate cancer cells
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHF8_HUMAN
1060
0
117864
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene KDM6B or JMJD3, quantitative PCR enzyme expression analysis
overexpression of JMJD3 through the transfection of pcDNA3.1-JMJD3 into healthy donor CD4+ T cells leading to an increase in JMJD3 enrichment, a decrease in H3K27me3 enrichment within the ITGAL (CD11a) promoter, and upregulation of CD11a expression, resulting in T and B cell hyperactivity
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation of histone H3K27 demethylase JMJD3 by long noncoding RNA HOTAIR, i.e. homeobox transcript antisense intergenic RNA, a kind of non-protein coding transcripts longer than 200 nucleotides. HOTAIR is an important promoter in metastasis of renal cell carcinoma and also plays a dual regulatory role in chromatin state by effecting both histone metylation and demethylation at different gene loci. HOTAIR can affect histone H3K27 methylation and its target genes' expression
upregulation of JMJD3 expression in scratch-wounded keratinocytes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maina, P.K.; Shao, P.; Jia, X.; Liu, Q.; Umesalma, S.; Marin, M.; Long, D.; Concepcion-Roman, S.; Qi, H.H.
Histone demethylase PHF8 regulates hypoxia signaling through HIF1alpha and H3K4me3
Biochim. Biophys. Acta
1860
1002-1012
2017
Homo sapiens (Q9UPP1)
Manually annotated by BRENDA team
Na, J.; Lee, K.; Na, W.; Shin, J.; Lee, M.; Yune, T.; Lee, H.; Jung, H.; Kim, W.; Ju, B.
Histone H3K27 demethylase JMJD3 in cooperation with NF-kappaB regulates keratinocyte wound healing
J. Invest. Dermatol.
136
847-858
2016
Homo sapiens (O15054)
-
Manually annotated by BRENDA team
Xia, M.; Yao, L.; Zhang, Q.; Wang, F.; Mei, H.; Guo, X.; Huang, W.
Long noncoding RNA HOTAIR promotes metastasis of renal cell carcinoma by up-regulating histone H3K27 demethylase JMJD3
Oncotarget
8
19795-19802
2017
Homo sapiens (O15054)
-
Manually annotated by BRENDA team
Yin, H.; Wu, H.; Zhao, M.; Zhang, Q.; Long, H.; Fu, S.; Lu, Q.
Histone demethylase JMJD3 regulates CD11a expression through changes in histone H3K27 tri-methylation levels in CD4+ T cells of patients with systemic lupus erythematosus
Oncotarget
8
48938-48947
2017
Homo sapiens (O15054)
-
Manually annotated by BRENDA team