General Information of Target

Target ID LDTP05005
Target Name Histone H2B type 1-C/E/F/G/I (H2BC4; H2BC6; H2BC7; H2BC8; H2BC10)
Gene Name H2BC4; H2BC6; H2BC7; H2BC8; H2BC10
Gene ID 3017
Synonyms
H2BFL; HIST1H2BC; H2BFH; HIST1H2BE; H2BFG; HIST1H2BF; H2BFA; HIST1H2BG; H2BFK; HIST1H2BI; Histone H2B type 1-C/E/F/G/I; Histone H2B.1 A; Histone H2B.a; H2B/a; Histone H2B.g; H2B/g; Histone H2B.h; H2B/h; Histone H2B.k; H2B/k; Histone H2B.l; H2B/l
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAM
GIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT
KYTSSK
Target Bioclass
Other
Family
Histone H2B family
Subcellular location
Nucleus
Function
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.; Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.
Uniprot ID
P62807
Ensemble ID
ENST00000314332.5
HGNC ID
HGNC:4756

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 6 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
DBIA
 Probe Info 
C73(1.50)  LDD2245  [1]
HHS-475
 Probe Info 
Y84(1.13)  LDD0264  [2]
HHS-465
 Probe Info 
Y84(2.95)  LDD2237  [3]
W1
 Probe Info 
K86(0.59); K47(0.92); K109(0.99); K58(1.16)  LDD0237  [4]
AMP probe
 Probe Info 
N.A.  LDD0200  [5]
ATP probe
 Probe Info 
K47(0.00); K109(0.00); K117(0.00); K35(0.00)  LDD0199  [5]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0116  HHS-0101 DM93 Y84(1.13)  LDD0264  [2]
 LDCM0117  HHS-0201 DM93 Y84(1.00)  LDD0265  [2]
 LDCM0118  HHS-0301 DM93 Y84(1.27)  LDD0266  [2]
 LDCM0119  HHS-0401 DM93 Y84(1.26)  LDD0267  [2]
 LDCM0120  HHS-0701 DM93 Y84(1.74)  LDD0268  [2]
 LDCM0022  KB02 697 C73(1.50)  LDD2245  [1]
 LDCM0023  KB03 AN3-CA C43(1.55)  LDD2681  [1]
 LDCM0024  KB05 AN3-CA C43(1.76)  LDD3098  [1]
 LDCM0110  W12 Hep-G2 K86(0.59); K47(0.92); K109(0.99); K58(1.16)  LDD0237  [4]
 LDCM0111  W14 Hep-G2 E114(0.59); K47(0.95); K58(1.16); K109(1.27)  LDD0238  [4]
 LDCM0113  W17 Hep-G2 K35(0.68); K109(1.25); K47(1.25); K58(1.35)  LDD0240  [4]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Transporter and channel
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
AP-2 complex subunit mu (AP2M1) Adaptor complexes medium subunit family Q96CW1
Other
Click To Hide/Show 2 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Histone H2B type 1-C/E/F/G/I (H2BC4; H2BC6; H2BC7; H2BC8; H2BC10) Histone H2B family P62807
TP53-binding protein 1 (TP53BP1) . Q12888

The Drug(s) Related To This Target

Approved
Click To Hide/Show 1 Drug(s) Interacting with This Target
Drug Name Drug Type External ID
Copper . DB09130

References

1 DrugMap: A quantitative pan-cancer analysis of cysteine ligandability. Cell. 2024 May 9;187(10):2536-2556.e30. doi: 10.1016/j.cell.2024.03.027. Epub 2024 Apr 22.
Mass spectrometry data entry: PXD047840
2 Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2. Chembiochem. 2021 Jun 15;22(12):2134-2139. doi: 10.1002/cbic.202000879. Epub 2021 Apr 29.
3 Global targeting of functional tyrosines using sulfur-triazole exchange chemistry. Nat Chem Biol. 2020 Feb;16(2):150-159. doi: 10.1038/s41589-019-0404-5. Epub 2019 Nov 25.
4 Oxidant-Induced Bioconjugation for Protein Labeling in Live Cells. ACS Chem Biol. 2023 Jan 20;18(1):112-122. doi: 10.1021/acschembio.2c00740. Epub 2022 Dec 21.
5 Targeted Proteomic Approaches for Proteome-Wide Characterizations of the AMP-Binding Capacities of Kinases. J Proteome Res. 2022 Aug 5;21(8):2063-2070. doi: 10.1021/acs.jproteome.2c00225. Epub 2022 Jul 12.