Loading...
*  Histone H2B type F-M (P0C1H6) | InterPro | EMBL-EBI
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
http://www.ebi.ac.uk/interpro/protein/P0C1H6
*  Histone-lysine N-methyltransferase PRDM9 (Q96EQ9) | InterPro | EMBL-EBI
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
http://www.ebi.ac.uk/interpro/protein/Q96EQ9
*  Histone H2A (IPR002119) | InterPro | EMBL-EBI
Histone H2A (IPR002119). Short name: Histone_H2A Family relationships *Histone H2A (IPR002119) *Core histone macro-H2A ( ... Histone H2A is a small, highly conserved nuclear protein that, together with two molecules each of histones H2B, H3 and H4, ... In the mouse, histone H2A can be replaced by histone H2A-like 1 [PMID: 17261847]. ... Phylogenetic analysis of the core histones H2A, H2B, H3, and H4.. Nucleic Acids Res. 22 174-9 1994 ...
http://www.ebi.ac.uk/interpro/entry/IPR002119
*  Histone-binding protein RBBP4, N-terminal (IPR022052) | InterPro | EMBL-EBI
Histone-binding protein RBBP4, N-terminal (IPR022052). Short name: Histone-bd_RBBP4_N ... Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46.. Structure 16 1077-85 2008 ... RBBP7 folds into the beta-propeller and binds histone H4 in a groove formed between this N-terminal helix and an extended loop ... The CAF-1 complex is a conserved heterotrimeric protein complex that promotes histone H3 and H4 deposition onto newly ...
http://www.ebi.ac.uk/interpro/entry/IPR022052
*  Literature: Histone-lysine N-methyltransferase, SET2, plant (IPR025787) | InterPro | EMBL-EBI
Literature: Histone-lysine N-methyltransferase, SET2, plant (IPR025787). References used in this entry. The following ...
http://www.ebi.ac.uk/interpro/entry/IPR025787/literature
*  Histone-like protein H-NS, N-terminal (IPR027454) | InterPro | EMBL-EBI
Histone-like protein H-NS, N-terminal (IPR027454). Short name: Histone_HNS_N ... This superfamily represents N-terminal domain of histone-like H-NS proteins that is responsible for dimerisation and involved ...
http://www.ebi.ac.uk/interpro/entry/IPR027454
*  Histone-lysine N-methyltransferase, H3 lysine-79 specific (Q8TEK3) | InterPro | EMBL-EBI
GO:0018024 histone-lysine N-methyltransferase activity GO:0031151 histone methyltransferase activity (H3-K79 specific) ... GO:0034729 histone H3-K79 methylation GO:0051726 regulation of cell cycle ...
http://www.ebi.ac.uk/interpro/protein/Q8TEK3
*  Histone H3-K9 methyltransferase, plant (IPR025794) | InterPro | EMBL-EBI
In general, members of this family methylate 'Lys-9' of histone H3. It also methylates 'Lys-27' of histone H3 [PMID: 15546353] ... Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3.. EMBO J. 23 4286-96 2004 ... Histone H3-K9 methyltransferase, plant (IPR025794). Short name: Hist-Lys_N-MeTrfase_plant ... Pivotal role of AtSUVH2 in heterochromatic histone methylation and gene silencing in Arabidopsis.. EMBO J. 24 1418-29 2005 ...
https://www.ebi.ac.uk/interpro/entry/IPR025794
*  Histone-like protein H-NS, C-terminal domain superfamily (IPR037150) | InterPro | EMBL-EBI
Histone-like protein H-NS, C-terminal domain superfamily (IPR037150). Short name: H-NS_C_dom_sf ...
http://www.ebi.ac.uk/interpro/entry/IPR037150
*  Linker histone H1/H5, domain H15 (IPR005818) | InterPro | EMBL-EBI
The Histone Database: a comprehensive resource for histones and histone fold-containing proteins.. Proteins 62 838-42 2006 ... In addition to the core histones, there is a "linker histone" called H1 (or H5 in avian species). The linker histones present ... The core histone octamer is composed of a central H3-H4 tetramer and two flanking H2A-H2B dimers. Each of the core histone ... Histone H5 performs the same function as histone H1, and replaces H1 in certain cells. The structure of GH5, the globular ...
http://www.ebi.ac.uk/interpro/entry/IPR005818
*  Ureohydrolase domain superfamily (IPR023696) | InterPro | EMBL-EBI
Histone deacetylase family (IPR000286). *Histone deacetylase (IPR003084). *Acetoin utilization protein AcuC (IPR003085) ...
http://www.ebi.ac.uk/interpro/entry/IPR023696
*  Compound Report Card
Histone deacetylase 1 inhibitor Histone deacetylase 1 PubMed PubMed Histone deacetylase 11 inhibitor Histone deacetylase 11 ... Histone deacetylase 2 inhibitor Histone deacetylase 2 PubMed PubMed Histone deacetylase 3 inhibitor Histone deacetylase 3 ... Histone deacetylase 8 inhibitor Histone deacetylase 8 PubMed PubMed Indications MESH Heading. MESH ID. EFO ID. EFO Term. Max ...
https://www.ebi.ac.uk/chembldb/index.php/compound/inspect/ChEMBL272980
*  TATA box binding protein associated factor (TAF) (IPR004823) | InterPro | EMBL-EBI
TFIID is composed of TATA binding protein (TBP)and a number of TBP-associated factors (TAFS). TAF proteins adopt a histone-like ...
http://www.ebi.ac.uk/interpro/entry/IPR004823?q=
*  Transcription activator BRG1 (P51532) | InterPro | EMBL-EBI
GO:0042393 histone binding Cellular Component. GO:0005634 nucleus GO:0016514 SWI/SNF complex ...
http://www.ebi.ac.uk/interpro/protein/P51532
*  Bromodomain-like superfamily (IPR036427) | InterPro | EMBL-EBI
Histone acetyltransferase GCN5/PCAF (IPR016376). *Transcription factor GTE1/GTE6 (IPR017413). *Bromodomain, conserved site ( ...
http://www.ebi.ac.uk/interpro/entry/IPR036427
*  Tyrosine-protein kinase (G5E852) | InterPro | EMBL-EBI
GO:0042393 histone binding Cellular Component. GO:0005856 cytoskeleton GO:0016020 membrane ...
https://www.ebi.ac.uk/interpro/protein/G5E852
*  Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.438 Show More. Calculated Compound Parent Properties. Mol. Weight. Mol. ...
https://www.ebi.ac.uk/chembl/compound/inspect/CHEMBL15841
*  CHEMBL1245 Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.393 CHEMBL5514 Huntingtin Homo sapiens 0.374 ...
https://www.ebi.ac.uk/chembl/compound/inspect/CHEMBL1245
*  Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.839 CHEMBL5514 Huntingtin Homo sapiens 0.819 ...
https://www.ebi.ac.uk/chembldb/index.php/compound/inspect/CHEMBL1599
*  Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.355 CHEMBL2026 Beta-lactamase AmpC Escherichia coli K-12 0.230 ...
https://www.ebi.ac.uk/chembldb/index.php/compound/inspect/CHEMBL83668
*  Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.409 CHEMBL3622 Cytochrome P450 2C19 Homo sapiens 0.396 ...
https://www.ebi.ac.uk/chembldb/index.php/compound/inspect/CHEMBL76370
*  Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.358 CHEMBL2392 DNA polymerase beta Homo sapiens 0.340 ...
https://www.ebi.ac.uk/chembldb/index.php/compound/inspect/CHEMBL1334860
*  CREB-binding protein (Q92793) | InterPro | EMBL-EBI
GO:0004402 histone acetyltransferase activity GO:0005515 protein binding GO:0008270 zinc ion binding ...
http://www.ebi.ac.uk/interpro/protein/Q92793
*  Compound Report Card
Histone-lysine N-methyltransferase MLL Homo sapiens 0.856 CHEMBL4439 TGF-beta receptor type I Homo sapiens 0.644 ...
https://www.ebi.ac.uk/chembl/compound/inspect/CHEMBL502835
*  PDB 5ayf structure summary ‹ Protein Data Bank in Europe (PDBe) ‹ EMBL-EBI
Histone-lysine N-methyltransferase SETD7. '> SET domain * Occurring in:. *Histone-lysine N-methyltransferase SETD7. '> Histone- ... S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. ... Histone-lysine N-methyltransferase SETD7 Chain: A Molecule details › Chain: A. Length: 263 amino acids. Theoretical weight: ...
https://www.ebi.ac.uk/pdbe/entry/pdb/5AYF