Type |
Details |
Score |
Protein Domain |
Type: |
Family |
Description: |
Host cell factor 1 (HCFC1) is associated with the activation and repression of gene expression. It is brought to specific promoters by association with DNA-sequence-specific transcription factors such as Sp1, GABP, YY1, Ronin/THAP11, and E2F1 and E2F4 []. HCFC1 recruits and is a part of several different complexes, including the SET1 histone methyltransferase complex (transcription activation), the SIN3 histone deacetylase complex (transcription repression) [], the THAP1/THAP3-HCFC1-OGT complex (required for the regulation of the transcriptional activity of RRM1) [], and the NSL complex (acetylation of nucleosomal histone H4) []. This entry includes mammalian HCFC1 and the Drosophila homologue, dHCF. They undergo a process of proteolytic maturation to produce a heterodimeric complex of HCF-N and HCF-C subunits, by different enzymes, O-GlcNAc transferase and taspase1, respectively [, ]. They share a Kelch domain, regions biased for basic (Basic) or acidic (Acidic) amino acids, fibronectin type 3 repeats, and a nuclear localization signal [].During human herpes simplex virus infection, HCFC1 forms a multiprotein-DNA complex enabling transcription of the virus's early genes []. It is also a co-activator of EGR2/Krox20 []and the GA-binding protein GABP2 [], and represses ZBTB17/Miz-1 []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Rodriguez-Jato S |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
Drosophila melanogaster dHCF interacts with both PcG and TrxG epigenetic regulators. |
Volume: |
6 |
Issue: |
12 |
Pages: |
e27479 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
In animals, histone-lysine N-methyltransferase SETD1A () is a histone methyltransferase that produces mono-, di-, and trimethylated histone H3 at 'Lys-4. However, if 'Lys-9' residue is already methylated, 'Lys-4' will not be. The 'Lys-4' methylation is a tag for epigenetic transcriptional activation [, ]. The SET1 complex contains either SETD1A or SETD1B.The SET1 complex is a methyltransferase that that produces trimethylated histone H3 at Lys(4). It is composed of at least the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 []. In yeast there is only one SET1 complex, but in mammals there are additional H3K4 methylases []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Histone-lysine N-methyltransferase SETD1B () is a histone methyltransferase that produces trimethylated histone H3 at 'Lys-4'. However, if 'Lys-9' residue is already methylated, 'Lys-4' will not be. The 'Lys-4' methylation is a tag for epigenetic transcriptional activation []. The SET1 complex contains either SETD1A or SETD1B.The SET1 complex is a methyltransferase that that produces trimethylated histone H3 at Lys(4). It is composed of at least the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 []. In yeast there is only one SET1 complex, but in mammals there are additional H3K4 methylases []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Li MD |
Year: |
2013 |
Journal: |
Cell Metab |
Title: |
O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination. |
Volume: |
17 |
Issue: |
2 |
Pages: |
303-10 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jínek M |
Year: |
2004 |
Journal: |
Nat Struct Mol Biol |
Title: |
The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. |
Volume: |
11 |
Issue: |
10 |
Pages: |
1001-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Whelan SA |
Year: |
2010 |
Journal: |
J Biol Chem |
Title: |
Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes. |
Volume: |
285 |
Issue: |
8 |
Pages: |
5204-11 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yi W |
Year: |
2012 |
Journal: |
Science |
Title: |
Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. |
Volume: |
337 |
Issue: |
6097 |
Pages: |
975-80 |
|
•
•
•
•
•
|
Publication |
First Author: |
Fujiki R |
Year: |
2011 |
Journal: |
Nature |
Title: |
GlcNAcylation of histone H2B facilitates its monoubiquitination. |
Volume: |
480 |
Issue: |
7378 |
Pages: |
557-60 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase (OGT; ) is a heterotrimer of one 78kDa subunit and two 110kDa subunits. OGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in a protein. Substrate proteins include histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. The consequences of this form of glycosylation are diverse, including insulin resistance in muscle and adipocyte cells (brought about by inhibiting the 'Thr-308' phosphorylation of AKT1) []; regulation of glycolysis by inhibiting PFKL activity []; in the cell cycle O-glycosylation stabilizes ARNTL/BMAL1 and CLOCK, preventing their ubiquitination and subsequent degradation []; glycosylation of HCFC1 and interaction with TET proteins promotes binding of the SET1/COMPASS methyltransferase SETD1A to chromatin []; and H2B GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination []. It is a component of several complexes, including MLL5-L, NSL []and THAP1/THAP3-HCFC1-OGT [].This entry represents the 110kDa subunit which has thirteen tetratricopeptide (TPR) repeats that are required for substrate binding and oligomerization [].The NSL complex is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. The complex is composed of at least MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Badeaux AI |
Year: |
2012 |
Journal: |
J Biol Chem |
Title: |
Loss of the methyl lysine effector protein PHF20 impacts the expression of genes regulated by the lysine acetyltransferase MOF. |
Volume: |
287 |
Issue: |
1 |
Pages: |
429-37 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wysocka J |
Year: |
2003 |
Journal: |
Genes Dev |
Title: |
Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. |
Volume: |
17 |
Issue: |
7 |
Pages: |
896-911 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hughes CM |
Year: |
2004 |
Journal: |
Mol Cell |
Title: |
Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus. |
Volume: |
13 |
Issue: |
4 |
Pages: |
587-97 |
|
•
•
•
•
•
|
Publication |
First Author: |
Xu Z |
Year: |
2009 |
Journal: |
J Cell Biol |
Title: |
A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking. |
Volume: |
186 |
Issue: |
3 |
Pages: |
343-53 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes Sdc1 from yeasts, and its homologues, Dpy-30, from animals. Protein dpy-30 homologue (DPY30) is a component of the MLL1/MLL complex which trimethylates histone H3 at 'Lys-4' as a specific tag for epigenetic transcriptional activation []. DPY30 is also a component in MLL2/3 and MLL4/WBP7 methyltransferase-containing complexes [, ]and the SET1 complex []. DPY30 is found in the nucleus and the trans-Golgi network where it interacts with ARFGEF1 implying a role in endosomal trafficking []. This entry also includes C. elegans dpy-30, which is an essential component of the C. elegans dosage compensation machinery that reduces X chromosome transcript levels in hermaphrodites (XX) [].The SET1 complex is a methyltransferase that that produces trimethylated histone H3 at Lys(4). It is composed of at least the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 []. In yeast there is only one SET1 complex, but in mammals there are additional H3K4 methylases []. |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Publication |
First Author: |
Deplus R |
Year: |
2013 |
Journal: |
EMBO J |
Title: |
TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS. |
Volume: |
32 |
Issue: |
5 |
Pages: |
645-55 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
70
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee JH |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex. |
Volume: |
280 |
Issue: |
50 |
Pages: |
41725-31 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mazars R |
Year: |
2010 |
Journal: |
J Biol Chem |
Title: |
The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias. |
Volume: |
285 |
Issue: |
18 |
Pages: |
13364-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cai Y |
Year: |
2010 |
Journal: |
J Biol Chem |
Title: |
Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. |
Volume: |
285 |
Issue: |
7 |
Pages: |
4268-72 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee JH |
Year: |
2007 |
Journal: |
J Biol Chem |
Title: |
Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex. |
Volume: |
282 |
Issue: |
18 |
Pages: |
13419-28 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
209
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Wu M |
Year: |
2008 |
Journal: |
Mol Cell Biol |
Title: |
Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS. |
Volume: |
28 |
Issue: |
24 |
Pages: |
7337-44 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cho YW |
Year: |
2007 |
Journal: |
J Biol Chem |
Title: |
PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. |
Volume: |
282 |
Issue: |
28 |
Pages: |
20395-406 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gudkova D |
Year: |
2019 |
Journal: |
Nucleic Acids Res |
Title: |
HCF-2 inhibits cell proliferation and activates differentiation-gene expression programs. |
Volume: |
47 |
Issue: |
11 |
Pages: |
5792-5808 |
|
•
•
•
•
•
|
Publication |
First Author: |
Izeta A |
Year: |
2003 |
Journal: |
Gene |
Title: |
Primary structure and compartmentalization of Drosophila melanogaster host cell factor. |
Volume: |
305 |
Issue: |
2 |
Pages: |
175-83 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sabina RL |
Year: |
1989 |
Journal: |
Mol Cell Biol |
Title: |
Expression of three stage-specific transcripts of AMP deaminase during myogenesis. |
Volume: |
9 |
Issue: |
5 |
Pages: |
2244-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Berr A |
Year: |
2009 |
Journal: |
Plant Physiol |
Title: |
SET DOMAIN GROUP25 encodes a histone methyltransferase and is involved in FLOWERING LOCUS C activation and repression of flowering. |
Volume: |
151 |
Issue: |
3 |
Pages: |
1476-85 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes Host cell factor 1 (HCF1) and Host cell factor 2 (HCF2) from humans. They contain an N-terminal kelch domain and a C-terminal FnIII domain. However, HCF2 is smaller than HCF-1, lacking the complete central region including the HCF1 specific repeats and as a result is not subject to proteolytic processing []. This entry also includes their Drosophila melanogaster homologue, dHCF, which is involved in both activation and repression of transcription during fly development []. Host cell factor homologue hcf-1 from C. elegans controls the cell cycle through mitotic histone phosphorylation modulation and negatively regulates responses to environmental stresses [].HCF1 is associated with the activation and repression of gene expression. It is brought to specific promoters by association with DNA-sequence-specific transcription factors such as Sp1, GABP, YY1, Ronin/THAP11, and E2F1 and E2F4 []. HCFC1 recruits and is a part of several different complexes, including the SET1 histone methyltransferase complex (transcription activation), the SIN3 histone deacetylase complex (transcription repression) [], the THAP1/THAP3-HCFC1-OGT complex (required for the regulation of the transcriptional activity of RRM1) [], and the NSL complex (acetylation of nucleosomal histone H4) [].HCF2 is involved in activation of differentiation and morphogenesis gene expression programs, and in parallel in inhibition of cellular growth and metabolism []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The COMPASS complex (complex proteins associated with Set1) is conserved in yeasts and in other eukaryotes up to humans. This entry represents Set1 and its homologues. Set1 is a methyltransferase and the catalytic component of the COMPASS that produces trimethylated histone H3 at Lys(4). The yeast COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation [, , ]. In yeasts, the Set1C complex consists of Set1(2), Bre2(2), Spp1(2), Sdc1(1), Shg1(1), Swd1(1), Swd2(1), and Swd3(1) [, , , ].In animals, SETD1A/B are histone methyltransferases that produce mono-, di-, and trimethylated histone H3 at 'Lys-4. However, if 'Lys-9' residue is already methylated, 'Lys-4' will not be. The 'Lys-4' methylation is a tag for epigenetic transcriptional activation [, ]. The animal COMPASS complex is composed of at least the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 []. ATXR7, the Arabidopsis homologue to Set1, is required for the expression of the flowering repressors FLC and MADS-box genes of the MAF family [, ]. ATXR7 is also involved in the control of seed dormancy and germination []. |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
175
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
99
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
139
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
113
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
177
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
99
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
612
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Hsu DR |
Year: |
1995 |
Journal: |
Development |
Title: |
DPY-30, a nuclear protein essential early in embryogenesis for Caenorhabditis elegans dosage compensation. |
Volume: |
121 |
Issue: |
10 |
Pages: |
3323-34 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2045
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2090
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Vitaliano-Prunier A |
Year: |
2008 |
Journal: |
Nat Cell Biol |
Title: |
Ubiquitylation of the COMPASS component Swd2 links H2B ubiquitylation to H3K4 trimethylation. |
Volume: |
10 |
Issue: |
11 |
Pages: |
1365-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee JS |
Year: |
2007 |
Journal: |
Cell |
Title: |
Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS. |
Volume: |
131 |
Issue: |
6 |
Pages: |
1084-96 |
|
•
•
•
•
•
|
Publication |
First Author: |
Roguev A |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation in budding and fission yeasts. |
Volume: |
278 |
Issue: |
10 |
Pages: |
8487-93 |
|
•
•
•
•
•
|
Publication |
First Author: |
Corda Y |
Year: |
1999 |
Journal: |
Nat Genet |
Title: |
Interaction between Set1p and checkpoint protein Mec3p in DNA repair and telomere functions. |
Volume: |
21 |
Issue: |
2 |
Pages: |
204-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Roguev A |
Year: |
2004 |
Journal: |
Mol Cell Proteomics |
Title: |
A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. |
Volume: |
3 |
Issue: |
2 |
Pages: |
125-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Patel A |
Year: |
2009 |
Journal: |
J Biol Chem |
Title: |
On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. |
Volume: |
284 |
Issue: |
36 |
Pages: |
24242-56 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
182
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
737
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
247
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
196
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
171
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
181
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu Y |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
Identification of the Arabidopsis REDUCED DORMANCY 2 gene uncovers a role for the polymerase associated factor 1 complex in seed dormancy. |
Volume: |
6 |
Issue: |
7 |
Pages: |
e22241 |
|
•
•
•
•
•
|
Publication |
First Author: |
Miller T |
Year: |
2001 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
COMPASS: a complex of proteins associated with a trithorax-related SET domain protein. |
Volume: |
98 |
Issue: |
23 |
Pages: |
12902-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tamada Y |
Year: |
2009 |
Journal: |
Plant Cell |
Title: |
ARABIDOPSIS TRITHORAX-RELATED7 is required for methylation of lysine 4 of histone H3 and for transcriptional activation of FLOWERING LOCUS C. |
Volume: |
21 |
Issue: |
10 |
Pages: |
3257-69 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1046
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
849
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
458
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
316
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1173
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
261
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
87
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
145
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
29
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
365
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1716
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1985
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
722
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1010
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1023
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Dou Y |
Year: |
2005 |
Journal: |
Cell |
Title: |
Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. |
Volume: |
121 |
Issue: |
6 |
Pages: |
873-85 |
|
•
•
•
•
•
|