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JmjC domain-containing histone demethylation protein 3A; Jumonji domain-containing protein 2A (MJD2A, JHDM3, JMJD2, KDM4A, KIAA0677)
Function:
1) histone demethylase
2) specifically demethylates Lys-9 & Lys-36 residues of histone H3, thus plays a role in histone code
3) does not demethylate histone H3 Lys-4, H3 Lys-27 nor histone H4 Lys-20
4) demethylates trimethylated histone H3 Lys-9 & H3 Lys-36, while it has no activity on mono- & dimethylated residues
5) demethylation of Lys generates formaldehyde & succinate
6) role in transcriptional repression of ASCL2 & E2F-responsive promoters via recruitment of histone deacetylases & NCOR1, respectively
7) interacts with histone deacetylase proteins HDAC1, HDAC2 & HDAC3
8) interacts with RB & NCOR1
Cofactor: binds 1 Fe+2 per subunit
Structure:
- belongs to the JHDM3 histone demethylase family
- contains 1 JmjC domain
- contains 1 JmjN domain
- contains 2 PHD-type zinc fingers
- contains 2 Tudor domains Tudor domains recognize & bind methylated histone H3 Lys-4 Double Tudor domain has an interdigitated structure & the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 Lys-4 is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1 Tudor domains are able to bind trimethylated histone H3 Lys-4, trimethylated histone H3 Lys-9, di- & trimethylated H4 Lys-20
Compartment: nucleus
Expression: ubiquitous
Pathology: interacts with HTLV-1 Tax protein
General
dioxygenase
histone demethylase
JmjC domain-containing protein (JMJD)
phosphoprotein
zinc finger protein
Properties
SIZE: MW = 121 kD
entity length = 1064 aa
COMPARTMENT: cell nucleus
MOTIF: JmjN {14-56}
binding site
SITE: 132-132
FOR-BINDING-OF: Alpha-ketoglutarate
JmjC {142-308}
MOTIF: Iron [Fe]-binding site
SITE: 188-188
Iron [Fe]-binding site
SITE: 190-190
binding site
SITE: 198-198
FOR-BINDING-OF: Alpha-ketoglutarate
binding site
SITE: 206-206
FOR-BINDING-OF: Alpha-ketoglutarate
Zn+2-binding site
SITE: 234-234
Zn+2-binding site
SITE: 240-240
Iron [Fe]-binding site
SITE: 276-276
Zn+2-binding site
SITE: 306-306
Zn+2-binding site
SITE: 308-308
Tyr phosphorylation site {Y547}
interaction with NCOR1 {597-638}
Zn finger PHD-type
NAME: Zn finger PHD-type
SITE: 709-767
EFFECTOR-BOUND: Zn+2
Zn finger PHD-type
NAME: Zn finger PHD-type
SITE: 829-885
EFFECTOR-BOUND: Zn+2
Tudor domain
SITE: 897-954
MOTIF: binding site
SITE: 945-945
FOR-BINDING-OF: Histone H3-K4Me3
Tudor domain
SITE: 955-1011
MOTIF: binding site
SITE: 967-967
FOR-BINDING-OF: Histone H3-K4Me3
binding site
SITE: 973-973
FOR-BINDING-OF: Histone H3-K4Me3
Database Correlations
UniProt O75164
PFAM correlations
References
UniProt :accession O75164