Overview
| Uniprot ID | Q8NB78 |
| Protein Name | Lysine-specific histone demethylase 2 |
| Gene Name | KDM1B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 11 |
PRGRTKKKASFDHSP |
| 33 |
SGRQAKKKATETTDE |
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)
Protein Sequence
10
MATPRGRTKK
20
KASFDHSPDS
30
LPLRSSGRQA
40
KKKATETTDE
50
DEDGGSEKKY
60
RKCEKAGCTA
70
TCPVCFASAS
80
ERCAKNGYTS
90
RWYHLSCGEH
100
FCNECFDHYY
110
RSHKDGYDKY
120
TTWKKIWTSN
130
GKTEPSPKAF
140
MADQQLPYWV
150
QCTKPECRKW
160
RQLTKEIQLT
170
PQIAKTYRCG
180
MKPNTAIKPE
190
TSDHCSLPED
200
LRVLEVSNHW
210
WYSMLILPPL
220
LKDSVAAPLL
230
SAYYPDCVGM
240
SPSCTSTNRA
250
AATGNASPGK
260
LEHSKAALSV
270
HVPGMNRYFQ
280
PFYQPNECGK
290
ALCVRPDVME
300
LDELYEFPEY
310
SRDPTMYLAL
320
RNLILALWYT
330
NCKEALTPQK
340
CIPHIIVRGL
350
VRIRCVQEVE
360
RILYFMTRKG
370
LINTGVLSVG
380
ADQYLLPKDY
390
HNKSVIIIGA
400
GPAGLAAARQ
410
LHNFGIKVTV
420
LEAKDRIGGR
430
VWDDKSFKGV
440
TVGRGAQIVN
450
GCINNPVALM
460
CEQLGISMHK
470
FGERCDLIQE
480
GGRITDPTID
490
KRMDFHFNAL
500
LDVVSEWRKD
510
KTQLQDVPLG
520
EKIEEIYKAF
530
IKESGIQFSE
540
LEGQVLQFHL
550
SNLEYACGSN
560
LHQVSARSWD
570
HNEFFAQFAG
580
DHTLLTPGYS
590
VIIEKLAEGL
600
DIQLKSPVQC
610
IDYSGDEVQV
620
TTTDGTGYSA
630
QKVLVTVPLA
640
LLQKGAIQFN
650
PPLSEKKMKA
660
INSLGAGIIE
670
KIALQFPYRF
680
WDSKVQGADF
690
FGHVPPSASK
700
RGLFAVFYDM
710
DPQKKHSVLM
720
SVIAGEAVAS
730
VRTLDDKQVL
740
QQCMATLREL
750
FKEQEVPDPT
760
KYFVTRWSTD
770
PWIQMAYSFV
780
KTGGSGEAYD
790
IIAEDIQGTV
800
FFAGEATNRH
810
FPQTVTGAYL
820
SGVREASKIA
AF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0000786 |
nucleosome |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0071949 |
FAD binding |
| Molecular Function |
GO:0140682 |
FAD-dependent H3K4me/H3K4me3 demethylase activity |
| Molecular Function |
GO:0042393 |
histone binding |
| Molecular Function |
GO:0032452 |
histone demethylase activity |
| Molecular Function |
GO:0016491 |
oxidoreductase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0071514 |
genomic imprinting |
| Biological Process |
GO:0045815 |
transcription initiation-coupled chromatin remodeling |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.