Search
JmjC domain-containing histone demethylation protein 1B; [histone-H3]-lysine-36 demethylase 1B; F-box/LRR-repeat protein 10; F-box & leucine-rich repeat protein 10; F-box protein FBL10; protein JEMMA; Jumonji domain-containing EMSY-interactor methyltransferase motif protein; CXXC-type zinc finger protein 2; protein-containing CXXC domain 2 (FBXL10, KDM2B, CXXC2, FBL10, JHDM1B, PCCX2)
Function:
1) histone demethylase
2) specifically demethylates Lys-36 of histone H3, thus role in histone code
3) weak or no activity for mono- & tri-methylated H3 Lys-36
4) substrate-recognition component of the SCF-type* E3 ubiquitin ligase complex
5) interacts with SKP1A & CUL1
6) JmjC domain mediates the demethylation activity
* SCF: SKP1-CUL1-F-box protein
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
protein 6-N-methyl-L-lysine + succinate + formaldehyde + CO2
Cofactor: binds 1 Fe+2 ion per subunit
Structure:
- belongs to the JHDM1 histone demethylase family
- contains 1 CXXC-type zinc finger
- contains 1 F-box domain
- contains 1 JmjC domain
- contains 4 LRR repeats (leucine-rich repeats)
- contains 1 PHD-type zinc finger
Compartment: nucleus
Alternative splicing: named isoforms=3
General
dioxygenase
histone demethylase
JmjC domain-containing protein (JMJD)
phosphoprotein
zinc finger protein
Properties
SIZE: MW = 153 kD
entity length = 1336 aa
COMPARTMENT: cell nucleus
MOTIF: JmjC {178-346}
MOTIF: binding site
SITE: 239-239
FOR-BINDING-OF: Substrate
Iron [Fe]-binding site
SITE: 242-242
Iron [Fe]-binding site
SITE: 244-244
binding site
SITE: 259-259
FOR-BINDING-OF: Substrate
Iron [Fe]-binding site
SITE: 314-314
glutamate-rich region {409-430}
MOTIF: glutamate residue (SEVERAL)
Ser phosphorylation site {S474}
Ser phosphorylation site {S497}
Zinc finger
NAME: Zinc finger
SITE: 606-652
EFFECTOR-BOUND: Zn+2
Zn finger PHD-type
NAME: Zn finger PHD-type
SITE: 659-725
EFFECTOR-BOUND: Zn+2
coiled coil {943-971}
proline-rich region
SITE: 1014-1056
MOTIF: proline residue (SEVERAL)
F-box domain {1059-1105}
leucine-rich repeat
SITE: 1148-1171
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 1217-1242
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 1269-1293
MOTIF: leucine residue (SEVERAL)
leucine-rich repeat
SITE: 1294-1336
MOTIF: leucine residue (SEVERAL)
Database Correlations
UniProt Q8NHM5
PFAM correlations
ENZYME 1.14.11.27
References
UniProt :accession Q8NHM5