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JmjC domain-containing histone demethylation protein 3B; Jumonji domain-containing protein 2B (JMJD2B, JHDM3B, KDM4B, KIAA0876)
Function:
1) histone demethylase
2) specifically demethylates Lys-9 of histone H3, thus plays a role in histone code
3) does not demethylate histone H3 Lys-4, H3 Lys-27, H3 Lys-36 nor H4 Lys-20
4) only able to demethylate trimethylated H3 Lys-9, with weaker activity than JMJD2A, JMJD2C & JMJD2D
5) demethylation of Lys generates formaldehyde & succinate
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
- 2 Tudor domains recognize & bind methylated histones double Tudor domain has an interdigitated structure unusual fold is required for its ability to bind methylated histone tails
Compartment: nucleus
Alternative splicing: named isoforms=2
General
dioxygenase
histone demethylase
JmjC domain-containing protein (JMJD)
phosphoprotein
zinc finger protein
Properties
SIZE: MW = 122 kD
entity length = 1096 aa
COMPARTMENT: cell nucleus
MOTIF: JmjN {15-57}
binding site
SITE: 133-133
FOR-BINDING-OF: Alpha-ketoglutarate
JmjC {146-309}
MOTIF: Iron [Fe]-binding site
SITE: 189-189
Iron [Fe]-binding site
SITE: 191-191
binding site
SITE: 199-199
FOR-BINDING-OF: Alpha-ketoglutarate
binding site
SITE: 207-207
FOR-BINDING-OF: Alpha-ketoglutarate
Zn+2-binding site
SITE: 235-235
Zn+2-binding site
SITE: 241-241
Iron [Fe]-binding site
SITE: 277-277
Zn+2-binding site
SITE: 307-307
Zn+2-binding site
SITE: 309-309
proline-rich region
SITE: 463-535
MOTIF: proline residue (SEVERAL)
Ser phosphorylation site {S566}
Ser phosphorylation site {S622}
Zn finger PHD-type
NAME: Zn finger PHD-type
SITE: 731-789
EFFECTOR-BOUND: Zn+2
Zn finger PHD-type
NAME: Zn finger PHD-type
SITE: 851-907
EFFECTOR-BOUND: Zn+2
Tudor domain
SITE: 917-974
Tudor domain
SITE: 975-1031
Database Correlations
UniProt O94953
PFAM correlations
References
UniProt :accession O94953