Search Results

Overview

Uniprot IDQ7LBC6
Protein NameLysine-specific demethylase 3B
Gene NameKDM3B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
282 KRESIEGKDGRRRKS
288 GKDGRRRKSASDSGC
301 GCDPASKKLKGDRGE
303 DPASKKLKGDRGEVD
325 EASRGPWKGGNASGE
361 IRFATYTKENGRTLV
449 AAGTVPEKQKGSRSQ
570 SLSSGLCKGRSVLGT
584 TDTKPGSKAGSSVDR
688 ADSASLAKKKPLFIT
689 DSASLAKKKPLFITT
844 IPEHLMGKLGPNGER
859 SAELLLGKSKGKQAP
861 ELLLGKSKGKQAPKG
876 RPRTAPLKVGQSVLK
883 KVGQSVLKDVSKVKK
924 CRLERYRKFKEQEQD

Function

Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity

Protein Sequence

10 MADAAASPVG 20 KRLLLLFADT 30 AASASASAPA 40 AAAASGDPGP 50 ALRTRAWRAG 60 TVRAMSGAVP 70 QDLAIFVEFD 80 GCNWKQHSWV 90 KVHAEEVIVL 100 LLEGSLVWAP 110 REDPVLLQGI 120 RVSIAQWPAL 130 TFTPLVDKLG 140 LGSVVPVEYL 150 LDRELRFLSD 160 ANGLHLFQMG 170 TDSQNQILLE 180 HAALRETVNA 190 LISDQKLQEI 200 FSRGPYSVQG 210 HRVKIYQPEG 220 EEGWLYGVVS 230 HQDSITRLME 240 VSVTESGEIK 250 SVDPRLIHVM 260 LMDNSAPQSE 270 GGTLKAVKSS 280 KGKKKRESIE 290 GKDGRRRKSA 300 SDSGCDPASK 310 KLKGDRGEVD 320 SNGSDGGEAS 330 RGPWKGGNAS 340 GEPGLDQRAK 350 QPPSTFVPQI 360 NRNIRFATYT 370 KENGRTLVVQ 380 DEPVGGDTPA 390 SFTPYSTATG 400 QTPLAPEVGG 410 AENKEAGKTL 420 EQVGQGIVAS 430 AAVVTTASST 440 PNTVRISDTG 450 LAAGTVPEKQ 460 KGSRSQASGE 470 NSRNSILASS 480 GFGAPLPSSS 490 QPLTFGSGRS 500 QSNGVLATEN 510 KPLGFSFGCS 520 SAQEAQKDTD 530 LSKNLFFQCM 540 SQTLPTSNYF 550 TTVSESLADD 560 SSSRDSFKQS 570 LESLSSGLCK 580 GRSVLGTDTK 590 PGSKAGSSVD 600 RKVPAESMPT 610 LTPAFPRSLL 620 NARTPENHEN 630 LFLQPPKLSR 640 EEPSNPFLAF 650 VEKVEHSPFS 660 SFASQASGSS 670 SSATTVTSKV 680 APSWPESHSS 690 ADSASLAKKK 700 PLFITTDSSK 710 LVSGVLGSAL 720 TSGGPSLSAM 730 GNGRSSSPTS 740 SLTQPIEMPT 750 LSSSPTEERP 760 TVGPGQQDNP 770 LLKTFSNVFG 780 RHSGGFLSSP 790 ADFSQENKAP 800 FEAVKRFSLD 810 ERSLACRQDS 820 DSSTNSDLSD 830 LSDSEEQLQA 840 KTGLKGIPEH 850 LMGKLGPNGE 860 RSAELLLGKS 870 KGKQAPKGRP 880 RTAPLKVGQS 890 VLKDVSKVKK 900 LKQSGEPFLQ 910 DGSCINVAPH 920 LHKCRECRLE 930 RYRKFKEQEQ 940 DDSTVACRFF 950 HFRRLIFTRK 960 GVLRVEGFLS 970 PQQSDPDAMN 980 LWIPSSSLAE 990 GIDLETSKYI 1000 LANVGDQFCQ 1010 LVMSEKEAMM 1020 MVEPHQKVAW 1030 KRAVRGVREM 1040 CDVCETTLFN 1050 IHWVCRKCGF 1060 GVCLDCYRLR 1070 KSRPRSETEE 1080 MGDEEVFSWL 1090 KCAKGQSHEP 1100 ENLMPTQIIP 1110 GTALYNIGDM 1120 VHAARGKWGI 1130 KANCPCISRQ 1140 NKSVLRPAVT 1150 NGMSQLPSIN 1160 PSASSGNETT 1170 FSGGGGPAPV 1180 TTPEPDHVPK 1190 ADSTDIRSEE 1200 PLKTDSSASN 1210 SNSELKAIRP 1220 PCPDTAPPSS 1230 ALHWLADLAT 1240 QKAKEETKEA 1250 GSLRSVLNKE 1260 SHSPFGLDSF 1270 NSTAKVSPLT 1280 PKLFNSLLLG 1290 PTASNNKTEG 1300 SSLRDLLHSG 1310 PGKLPQTPLD 1320 TGIPFPPVFS 1330 TSSAGVKSKA 1340 SLPNFLDHII 1350 ASVVENKKTS 1360 DASKRACNLT 1370 DTQKEVKEMV 1380 MGLNVLDPHT 1390 SHSWLCDGRL 1400 LCLHDPSNKN 1410 NWKIFRECWK 1420 QGQPVLVSGV 1430 HKKLKSELWK 1440 PEAFSQEFGD 1450 QDVDLVNCRN 1460 CAIISDVKVR 1470 DFWDGFEIIC 1480 KRLRSEDGQP 1490 MVLKLKDWPP 1500 GEDFRDMMPT 1510 RFEDLMENLP 1520 LPEYTKRDGR 1530 LNLASRLPSY 1540 FVRPDLGPKM 1550 YNAYGLITAE 1560 DRRVGTTNLH 1570 LDVSDAVNVM 1580 VYVGIPIGEG 1590 AHDEEVLKTI 1600 DEGDADEVTK 1610 QRIHDGKEKP 1620 GALWHIYAAK 1630 DAEKIRELLR 1640 KVGEEQGQEN 1650 PPDHDPIHDQ 1660 SWYLDQTLRK 1670 RLYEEYGVQG 1680 WAIVQFLGDA 1690 VFIPAGAPHQ 1700 VHNLYSCIKV 1710 AEDFVSPEHV 1720 KHCFRLTQEF 1730 RHLSNTHTNH 1740 EDKLQVKNII 1750 YHAVKDAVGT 1760 LKAHESKLAR S

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000118 histone deacetylase complex
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0031490 chromatin DNA binding
Molecular Function GO:0032454 histone H3K9 demethylase activity
Molecular Function GO:0140683 histone H3K9me/H3K9me2 demethylase activity
Molecular Function GO:0003712 transcription coregulator activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006357 regulation of transcription by RNA polymerase II

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] 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.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.