KDM1B
entrez
221656
canonical
uniprot
Q8NB78
canonical
ensembl
ENSG00000165097
resolver
ensp
ENSP00000297792
resolver
ensp
ENSP00000405669
resolver
ensp
ENSP00000499208
resolver
ensp
ENSP00000567607
resolver
ensp
ENSP00000567609
resolver
ensp
ENSP00000659275
resolver
ensp
ENSP00000659276
resolver
ensp
ENSP00000659278
resolver
ensp
ENSP00000659279
resolver
ensp
ENSP00000659280
resolver
ensp
ENSP00000659281
resolver
enst
ENST00000449850
resolver
enst
ENST00000897550
resolver
genesymbol
KDM1B
resolver
genesymbol_syn
AOF1
resolver
genesymbol_syn
C6orf193
resolver
genesymbol_syn
LSD2
resolver
hgnc
HGNC:21577
resolver
uniprot
A2A2C5
resolver
uniprot
A2A2C6
resolver
uniprot
H0Y6H0
resolver
uniprot
Q5TGV3
resolver
uniprot
Q6AI15
resolver
uniprot
Q6ZUU4
resolver
uniprot
Q8N258
resolver
uniprot
Q96EL7
resolver
uniprot_entry
H0Y6H0_HUMAN
resolver
uniprot_entry
KDM1B_HUMAN
resolver
uniprot_sec
A2A2C5
resolver
uniprot_sec
A2A2C6
resolver
uniprot_sec
Q5TGV3
resolver
uniprot_sec
Q6AI15
resolver
uniprot_sec
Q6ZUU4
resolver
uniprot_sec
Q8N258
resolver
uniprot_sec
Q96EL7
resolver
activity_regulation
ACTIVITY REGULATION: Histone H3K4me1 and H3K4me2 demethylase activity is inhibited by DNA, this inhibition is released in complex with GLYR1. {ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:30970244}.
uniprot
proteins
amino_acid_sequence
MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF
uniprot
proteins
ec_number
1.14.99.66
uniprot
proteins
function
FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of GLYR1 to achieve such activity, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes (PubMed:30970244). {ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244}.
uniprot
proteins
mass_dalton
92098
uniprot
proteins
mutagenesis
MUTAGEN 48..49; /note="KK->AA: Normal demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 51..52; /note="RK->AA: Reduced demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 53; /note="C->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 82; /note="W->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 84; /note="H->A: Loss of demethylase activity. Defective in the binding of FAD."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 90; /note="H->A: Loss of demethylase activity. Defective in the binding of FAD."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 101; /note="R->A: Reduced demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 103; /note="H->D: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 104; /note="K->E: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 109; /note="K->E: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 114..115; /note="KK->AA: Reduced demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 114; /note="K->E: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 115; /note="K->E: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 122; /note="K->E: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 139; /note="W->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 150; /note="W->A: Loss of demethylase activity. Defective in the binding of FAD."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 151; /note="R->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 185; /note="C->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 273..278; /note="YQPNEC->GSGSGS: Strongly reduced demethylase activity. Loss of enzymatic activity; when associated with 285-A--A-287."; /evidence="ECO:0000269|PubMed:23357850"; MUTAGEN 285..287; /note="RPD->APA: Strongly reduced demethylase activity. Loss of enzymatic activity; when associated with 273-G--S-278."; /evidence="ECO:0000269|PubMed:23357850"; MUTAGEN 302; /note="R->D: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 318..319; /note="WY->AA: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 340..341; /note="LV->AA: Loss of demethylase activity. Defective in the binding of FAD."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 361..362; /note="LI->AA: Loss of demethylase activity. Defective in the binding of FAD."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 443..444; /note="IN->GG: Loss of demethylase activity. Defective in the binding of FAD."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 481..482; /note="KR->ED: No effect on DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:30970244"; MUTAGEN 542; /note="N->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 543; /note="L->A: Reduced demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 547; /note="C->A: Reduced demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 559; /note="W->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887"; MUTAGEN 563; /note="E->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23357850"; MUTAGEN 661; /note="K->A: Normal demethylase activity."; /evidence="ECO:0000269|PubMed:23357850"; MUTAGEN 767; /note="Y->A: Loss of demethylase activity."; /evidence="ECO:0000269|PubMed:23266887
uniprot
proteins
protein_family
Flavin monoamine oxidase family
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23260659
uniprot
proteins
pubmed
23266887
uniprot
proteins
pubmed
23357850
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
30664650
uniprot
proteins
pubmed
30970244
uniprot
proteins
sequence_length
822
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30664650}. Chromosome {ECO:0000269|PubMed:30664650}. Note=Found in actively RNAPolII-transcribed gene bodies. {ECO:0000305|PubMed:30970244}.
uniprot
proteins