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lysine-specific demethylase 5C; histone demethylase JARID1C; Jumonji/ARID domain-containing protein 1C; protein SmcX; protein Xe169 (KDM5C, DXS1272E, JARID1C, SMCX, XE169)

Function: - histone demethylase - specifically demethylates Lys-4 of histone H3, thus playing a central role in histone cod - does not demethylate histone H3 Lys-9, H3 Lys-27, H3 Lys-36, H3 Lys-79 or H4 Lys-20 - demethylates trimethylated & dimethylated but not monomethylated H3 Lys-4 - participates in transcriptional repression of neuronal genes by recruiting histone deacetylases & REST at neuron- restrictive silencer elements - part of two distinct complexes, one containing E2F6, & the other containing REST Cofactor: alpha-ketoglutarate, Fe+2 Structure: - the 1st PHD-type Zn+2 finger domain recognizes & binds H3-K9Me3 - both the JmjC domain & the JmjN domain are required for enzymatic activity - belongs to the JARID1 histone demethylase family - contains 1 ARID domain - contains 1 JmjC domain - contains 1 JmjN domain - contains 2 PHD-type Zn+2 fingers Compartment: nucleus Alternative splicing: named isoforms=3 Expression: - expressed in all tissues examined - highest levels found in brain & skeletal muscle Pathology: - defects in KDM5C are the cause of mental retardation syndromic X-linked JARID1C-related Notes: escapes X-inactivation

General

histone demethylase JmjC domain-containing protein (JMJD) phosphoprotein zinc finger protein

Properties

SIZE: entity length = 1560 aa MW = 176 kD COMPARTMENT: cell nucleus MOTIF: JmjN {14-55} ARID {79-169} Ser phosphorylation site {S317} Zn finger PHD-type NAME: Zn finger PHD-type SITE: 326-372 EFFECTOR-BOUND: Zn+2 JmjC {468-634} Zn finger PHD-type NAME: Zn finger PHD-type SITE: 1187-1248 EFFECTOR-BOUND: Zn+2 Ser phosphorylation site {S1359}

Database Correlations

OMIM correlations UniProt P41229 PFAM correlations Entrez Gene 8242 Kegg hsa:8242

References

  1. UniProt :accession P41229
  2. GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/JARID1C