JARID2

Also known as JMJ, jumonji and AT-rich interaction domain containing 2

Protein Jumonji is a protein that in humans is encoded by the JARID2 gene. JARID2 is a member of the alpha-ketoglutarate-dependent hydroxylase superfamily.

Gene data

JARID2

Name: jumonji and AT-rich interaction domain containing 2
Type: protein-coding
Aliases: DIDDF, JMJ

This gene encodes a Jumonji- and AT-rich interaction domain (ARID)-domain-containing protein. The encoded protein is a DNA-binding protein that functions as a transcriptional repressor. This protein interacts with the Polycomb repressive complex 2 (PRC2) which plays an essential role in regulating gene expression during embryonic development. This protein facilitates the recruitment of the PRC2 complex to target genes. Alternate splicing results in multiple transcript variants. Mutations in this gene are associated with chronic myeloid malignancies. [provided by RefSeq, May 2012].

via MyGene.info

Gene · Ensembl

jumonji and AT-rich interaction domain containing 2

Symbol: JARID2
Biotype: Protein coding
Organism: Homo sapiens
Location: 6:15,244,937-15,522,042
Strand: Forward (+)
Assembly: GRCh38

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via Ensembl · EMBL-EBI

Wikidata facts

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HomoloGene ID: 31279
exact match: identifiers.org/ncbigene/3720
genomic end: 15522042
genomic start: 15246069
cytogenetic location: 6p22.3

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Protein Jumonji is a protein that in humans is encoded by the JARID2 gene. JARID2 is a member of the alpha-ketoglutarate-dependent hydroxylase superfamily.

Jarid2 (jumonji, AT rich interactive domain 2) is a protein coding gene that functions as a putative transcription factor. Distinguished as a nuclear protein necessary for mouse embryogenesis, Jarid2 is a member of the jumonji family that contains a DNA binding domain known as the AT-rich interaction domain (ARID). In vitro studies of Jarid2 reveal that ARID along with other functional domains are involved in DNA binding, nuclear localization, transcriptional repression, and recruitment of Polycomb-repressive complex 2 (PRC2). Intracellular mechanisms underlying these interactions remain largely unknown.