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Entry
EC 1.14.11.27               Enzyme                                 

Name
[histone-H3]-lysine-36 demethylase;
JHDM1A;
JmjC domain-containing histone demethylase 1A;
H3-K36-specific demethylase;
histone-lysine (H3-K36) demethylase;
histone demethylase;
protein-6-N,6-N-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy
Sysname
protein-N6,N6-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase
Reaction(IUBMB)
protein N6,N6-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O2 = protein L-lysine + 2 succinate + 2 formaldehyde + 2 CO2 (overall reaction) [RN:R10056];
(1a) protein N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N6-methyl-L-lysine + succinate + formaldehyde + CO2 [RN:R09510];
(1b) protein N6-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2 [RN:R09511]
Reaction(KEGG)
Substrate
protein N6,N6-dimethyl-L-lysine [CPD:C05545];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007];
protein N6-methyl-L-lysine [CPD:C05544]
Product
protein L-lysine;
succinate [CPD:C00042];
formaldehyde [CPD:C00067];
CO2 [CPD:C00011];
protein N6-methyl-L-lysine [CPD:C05544]
Comment
Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys-36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. It can also demethylate the monomethyl- but not the trimethyl form of Lys-36.
History
EC 1.14.11.27 created 2006
Orthology
K10276  
F-box and leucine-rich repeat protein 10/11
K16914  
bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
Genes
HSA: 
22992(KDM2A) 79697(C14orf169) 84678(KDM2B)
PTR: 
451362(KDM2A) 465184(KDM2B)
PPS: 
100983162(KDM2A) 100988129(KDM2B)
GGO: 
101134785(C14H14orf169) 101140212(KDM2A) 101154151(KDM2B)
PON: 
NLE: 
100579905(KDM2B) 100601545(KDM2A)
MCC: 
696773(C7H14orf169) 699938(KDM2B) 712907(KDM2A)
MCF: 
102125851(KDM2B) 102135352(C7H14orf169) 102142242(KDM2A)
CJC: 
100397900(KDM2B) 100403232(KDM2A) 100404196(C10H14orf169)
MMU: 
225876(Kdm2a) 30841(Kdm2b) 71952(2410016O06Rik)
RNO: 
304495(Kdm2b) 314300(RGD1307704) 361700(Kdm2a)
CGE: 
NGI: 
HGL: 
OCU: 
100349603(KDM2B) 100352993(KDM2A) 103351690(C20H14orf169)
TUP: 
CFA: 
102155553(C8H14orf169) 483702(KDM2A) 486262(KDM2B)
AML: 
UMR: 
FCA: 
101090549(KDM2A) 101094455(KDM2B) 102900260(CB3H14orf169)
PTG: 
BTA: 
511031(NO66) 540141(KDM2A) 614487(KDM2B)
BOM: 
PHD: 
CHX: 
102173094(C10H14orf169) 102180467(KDM2A) 102180525(KDM2B)
OAS: 
101103759(KDM2B) 101108003(KDM2A)
SSC: 
100294703(KDM2A) 100512074(KDM2B) 100523074(C7H14orf169)
CFR: 
BACU: 
LVE: 
ECB: 
100052955(KDM2A) 100059690(KDM2B) 100146448(C24H14orf169)
MYB: 
MYD: 
PALE: 
MDO: 
100015947 100024523(C1H14orf169) 100029240(KDM2A)
SHR: 
OAA: 
GGA: 
416844(KDM2B) 423249(C5H14ORF169) 425999(KDM2A)
MGP: 
APLA: 
TGU: 
100218907(KDM2B) 100219109(C5H14orf169) 100230512(KDM2A)
FAB: 
101813982(KDM2B) 101818982(KDM2A) 101819482(C5H14orf169)
PHI: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
100555582(kdm2a) 100557128(kdm2b) 100557464(c1h14orf169)
PBI: 
XLA: 
444267(kdm2b)
XTR: 
DRE: 
560815(im:7141580) 562643(kdm2bb) 799441(kdm2a)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
100179691 778852(zf(cxxc)-1)
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
410848(GB19015) 411568(GB19248)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_T26A5.5(jhdm-1) CELE_T28F2.4(jmjc-1)
CBR: 
BMY: 
LOA: 
HRO: 
LGI: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
OBR: 
BDI: 
SBI: 
SORBI_06g031470(SORBIDRAFT_06g031470)
SITA: 
PPP: 
OLU: 
OTA: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
YER051W(JHD1)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
TPF: 
TPHA_0C01220(TPHA0C01220)
TDL: 
TDEL_0H02210(TDEL0H02210)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
YLI: 
CLU: 
ANI: 
AFM: 
AOR: 
AOR_1_1284164(AO090001000714)
ANG: 
ANI_1_3330024(An02g14310)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
DSQ: 
PCO: 
SHS: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT53452(AGABI1DRAFT_53452)
ABV: 
AGABI2DRAFT183418(AGABI2DRAFT_183418)
CPUT: 
SLA: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
MBR: 
DDI: 
DPP: 
DFA: 
DFA_11703(jcdG)
ACAN: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:16362057]
  Authors
Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y.
  Title
Histone demethylation by a family of JmjC domain-containing proteins.
  Journal
Nature. 439 (2006) 811-6.
  Sequence
[hsa:22992 84678] [sce:YER051W]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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