Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
Field | Value |
---|---|
Namespace | Cellular component |
Short description | MLL1 complex |
Full defintion | A protein complex that can methylate lysine-4 of histone H3. MLL1/MLL is the catalytic methyltransferase subunit, and the complex also contains the core components ASH2L, HCFC1/HCF1 WDR5 and RBBP5. |
Subterm of |
The relationship of GO:0071339 with other GO terms.
Relationship type | GO terms |
---|---|
Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0071339, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
---|---|
GOC | sp |
PMID | Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell. 2005 Jun 17; 121 (6): 873–85.PMID: 15960975 A stable complex containing MLL1 and MOF has been immunoaffinity purified from a human cell line that stably expresses an epitope-tagged WDR5 subunit. Stable interactions between MLL1 and MOF were confirmed by reciprocal immunoprecipitation, cosedimentation, and cotransfection analyses, and interaction sites were mapped to MLL1 C-terminal and MOF zinc finger domains. The purified complex has a robust MLL1-mediated histone methyltransferase activity that can effect mono-, di-, and trimethylation of H3 K4 and a MOF-mediated histone acetyltransferase activity that is specific for H4 K16. Importantly, both activities are required for optimal transcription activation on a chromatin template in vitro and on an endogenous MLL1 target gene, Hox a9, in vivo. These results indicate an activator-based mechanism for joint MLL1 and MOF recruitment and targeted methylation and acetylation and provide a molecular explanation for the closely correlated distribution of H3 K4 methylation and H4 K16 acetylation on active genes. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | Forkhead-associated (FHA) domain protein; TAIR: AT3G54350.1 Forkhead-associated (FHA) domain-containing protein; Swiss-Prot: sp|Q96EZ8|MCRS1_HUMAN Microspherule protein 1; TrEMBL-Plants: tr|K7KHS6|K7KHS6_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0424900 | 3 | ||
– | Microspherule protein 1; TAIR: AT3G54350.1 Forkhead-associated (FHA) domain-containing protein; Swiss-Prot: sp|Q96EZ8|MCRS1_HUMAN Microspherule protein 1; TrEMBL-Plants: tr|K7KHS6|K7KHS6_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0424900 | 3 | ||
– | Forkhead-associated (FHA) domain protein; TAIR: AT3G54350.1 Forkhead-associated (FHA) domain-containing protein; Swiss-Prot: sp|Q96EZ8|MCRS1_HUMAN Microspherule protein 1; TrEMBL-Plants: tr|V7CD65|V7CD65_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0124300 | 3 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Cellular component | MLL1 complex | 1 | 33.33 |