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Search results 501 to 600 out of 31756 for Set

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Categories

Hits by Pathway

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Hits by Strain

Type Details Score
Gene
502130 | Set-ps14
Type: gene
Organism: rat
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Gene
680925 | Set-ps15
Type: gene
Organism: rat
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Gene
689131 | Set-ps16
Type: gene
Organism: rat
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Gene
690563 | Set-ps17
Type: gene
Organism: rat
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Gene
100362101 | Setd9-ps1
Type: gene
Organism: rat
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Gene
100364836 | Set-ps1
Type: gene
Organism: rat
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Gene
100911876 | Set-ps2
Type: gene
Organism: rat
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Gene
100912224 | Set-ps3
Type: gene
Organism: rat
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Gene
100909716 | Set-ps7
Type: gene
Organism: rat
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Gene
103694185 | Set-ps8
Type: gene
Organism: rat
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Gene
120098471 | Set-ps4
Type: gene
Organism: rat
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Gene
120100895 | Set-ps9
Type: gene
Organism: rat
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Gene
120102466 | Set-ps6
Type: gene
Organism: rat
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Gene
379599 | set.L
Type: gene
Organism: frog, African clawed
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Gene
399349 | set.S
Type: gene
Organism: frog, African clawed
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Publication
12453418 | J:80575
First Author: Milne TA
Year: 2002
Journal: Mol Cell
Title: MLL targets SET domain methyltransferase activity to Hox gene promoters.
Volume: 10
Issue: 5
Pages: 1107-17
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Publication
30626964 | J:270048
First Author: Wilkinson AW
Year: 2019
Journal: Nature
Title: SETD3 is an actin histidine methyltransferase that prevents primary dystocia.
Volume: 565
Issue: 7739
Pages: 372-376
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Protein Coding Gene
MGI:2685139 | Setdb2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2136890 | Setd4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1934229 | Setdb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2446244 | Setd1a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913333 | Setd6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1918177 | Setd2
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
2569445 | J:306535
First Author: Sagai T
Year: 1989
Journal: Immunogenetics
Title: New evidence for trans-species evolution of the H-2 class I polymorphism.
Volume: 30
Issue: 2
Pages: 89-98
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Publication
1477475 | J:3516
First Author: Marshall JD
Year: 1992
Journal: Mamm Genome
Title: The AXB and BXA set of recombinant inbred mouse strains.
Volume: 3
Issue: 12
Pages: 669-80
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Publication
8643801 | J:34431
First Author: Petrie BF
Year: 1995
Journal: Psychol Rep
Title: Learning set spatial navigation performance in three mouse strains.
Volume: 77
Issue: 3 Pt 2
Pages: 1339-42
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Publication
18936165 | J:144550
First Author: Chawla G
Year: 2009
Journal: Mol Cell Biol
Title: Sam68 regulates a set of alternatively spliced exons during neurogenesis.
Volume: 29
Issue: 1
Pages: 201-13
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Publication
29342142 | J:257746
First Author: Caggiano V
Year: 2018
Journal: Nature
Title: Midbrain circuits that set locomotor speed and gait selection.
Volume: 553
Issue: 7689
Pages: 455-460
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Publication
18349142 | J:133391
First Author: Robinson FL
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: Loss of the inactive myotubularin-related phosphatase Mtmr13 leads to a Charcot-Marie-Tooth 4B2-like peripheral neuropathy in mice.
Volume: 105
Issue: 12
Pages: 4916-21
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Publication
- | J:231805
     
First Author: SoRelle J
Year: 2016
Journal: MGI Direct Data Submission
Title: Mutagenetix entry for set
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Publication
12372294 | -
First Author: Yeates TO
Year: 2002
Journal: Cell
Title: Structures of SET domain proteins: protein lysine methyltransferases make their mark.
Volume: 111
Issue: 1
Pages: 5-7
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Protein Domain
IPR044435 | Set3/4_SET
Type: Domain
Description: This entry represents the SET domain found in Set3 and Set4 from fungi. They contain both SET and PHD domains. In budding yeasts, Set3 forms a single complex, Set3C, with Snt1, YIL112w, Sif2, Cpr1, and two putative histone deacetylases, Hos2 and NAD-dependent Hst1. Set3C is the yeast analog of the mammalian HDAC3/SMRT complex [].
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Protein
A0A1D5RMH9
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
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Protein
G3UY46
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
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Protein
D6RCZ0
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Protein
A0A0A0MQL7
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
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Protein
F6SZX1
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Protein
A0A1D5RLQ7
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
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Protein
Q8BMV4
Organism: Mus musculus/domesticus
Length: 69  
Fragment?: false
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Publication
33145806 | -
First Author: Akman B
Year: 2021
Journal: J Leukoc Biol
Title: PRDM1 decreases sensitivity of human NK cells to IL2-induced cell expansion by directly repressing CD25 (IL2RA).
Volume: 109
Issue: 5
Pages: 901-914
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Protein Domain
IPR046341 | SET_dom_sf
Type: Homologous_superfamily
Description: The SET domain is a 130 to 140 amino acid, evolutionary well conserved sequence motif that was initially characterised in the Drosophila proteins Su(var)3-9, Enhancer-of-zeste and Trithorax [, ]. In eukaryotic organisms, it appears in proteins with an important role in regulating chromatin-mediated gene transcriptional activation and silencing. In viruses,bacteria and archaea, its function is not clear yet []. This superfamily includes eukaryotic proteins with histone methyltransferase activity, which requires the combination of the SET domain with the adjacent cysteine-rich regions, one located N-terminally (pre-SET) and the other posterior to the SET domain (post-SET). Post- and pre- SET regions seem then to play a crucial role when it comes to substrate recognition and enzymatic activity [, ]. Other SET domain-containing proteins function as transcription factors (such as PR domain zinc finger protein 1 from humans []). The structure of the SET domain and the two adjacent regions pre-SET and post-SET have been solved [, , ]. The SET domain structure is all-β, but consists only in sets of few short strands composing no more than a couple of small sheets. Consequently the SET structure is mostly defined by turns and loops. An unusual feature is that the SET core is made up of two discontinuous segments of the primary sequence forming an approximate L-shape [, , ]. Two of the most conserved motifs in the SET domain are constituted by a stretch at the C-terminal containing a strictly conserved tyrosine residue and a preceding loop inside which the C-terminal segment passes forming a knot-like structure, but not quite a true knot. These two regions have been proven to be essential for SAM binding and catalysis, particularly the invariant tyrosine where in all likelihood catalysis takes place [, ].
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Protein
Q8VHL1
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
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Publication
16332269 | J:156373
First Author: Chang B
Year: 2005
Journal: Vis Neurosci
Title: Mouse models of ocular diseases.
Volume: 22
Issue: 5
Pages: 587-93
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Protein
Q3TYX3
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Protein
Q8CFT2
Organism: Mus musculus/domesticus
Length: 1985  
Fragment?: false
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Publication
26799706 | -
First Author: Ye X
Year: 2016
Journal: PLoS One
Title: SMYD1, an SRF-Interacting Partner, Is Involved in Angiogenesis.
Volume: 11
Issue: 1
Pages: e0146468
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Publication
21852424 | -
First Author: Just S
Year: 2011
Journal: J Cell Sci
Title: The myosin-interacting protein SMYD1 is essential for sarcomere organization.
Volume: 124
Issue: Pt 18
Pages: 3127-36
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Publication
27066749 | -
First Author: Van Aller GS
Year: 2016
Journal: Structure
Title: Structure-Based Design of a Novel SMYD3 Inhibitor that Bridges the SAM-and MEKK2-Binding Pockets.
Volume: 24
Issue: 5
Pages: 774-781
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Publication
22419068 | -
First Author: Van Aller GS
Year: 2012
Journal: Epigenetics
Title: Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation.
Volume: 7
Issue: 4
Pages: 340-3
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Publication
27554136 | -
 
First Author: Giakountis A
Year: 2017
Journal: Semin Cancer Biol
Title: Smyd3-associated regulatory pathways in cancer.
Volume: 42
Pages: 70-80
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Publication
19383909 | -
First Author: Hu L
Year: 2009
Journal: Cancer Res
Title: Identification of Smyd4 as a potential tumor suppressor gene involved in breast cancer development.
Volume: 69
Issue: 9
Pages: 4067-72
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Publication
27377701 | -
 
First Author: Fujii T
Year: 2016
Journal: Sci Rep
Title: Smyd5 plays pivotal roles in both primitive and definitive hematopoiesis during zebrafish embryogenesis.
Volume: 6
Pages: 29157
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Publication
18292091 | -
First Author: Shirai A
Year: 2008
Journal: J Biol Chem
Title: Global analysis of gel mobility of proteins and its use in target identification.
Volume: 283
Issue: 16
Pages: 10745-52
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Protein Domain
IPR044418 | SMYD1_SET
Type: Domain
Description: This entry represents the SET domain of SET and MYND domain-containing protein 1 (SMYD1). SMYD1 functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organisation, as well as in the regulation of endothelial cells (ECs) [, ]. It is expressed in vascular endothelial cells, it has been shown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation [].The SMYD family consists of five members including SMYD1/2/3/4/5. They contain two highly conserved structural and functional domains, the SET and MYND domains. The SET domain is involved in lysine methylation, while the MYND domain is involved in protein-protein interaction. They are essential in several mammalian developmental pathways [, , , ].
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Protein Domain
IPR044432 | Set10/Efm1_SET
Type: Domain
Description: This entry represents the SET domain found in budding yeast Efm1 and fission yeast Set10. They are S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferases. Efm1 monomethylates elongation factor 1-alpha (TEF1/TEF2) at 'Lys-30' [, ], while Set10 methylates ribosomal protein L23 (rpl23a and rpl23b) [].
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Protein Domain
IPR044421 | SMYD4_SET
Type: Domain
Description: This entry represents the SET domain of SET and MYND domain-containing protein 4 (SMYD4). SMYD4 functions as a potential tumour suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha []. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation [].The SMYD family consists of five members including SMYD1/2/3/4/5. They contain two highly conserved structural and functional domains, the SET and MYND domains. The SET domain is involved in lysine methylation, while the MYND domain is involved in protein-protein interaction. They are essential in several mammalian developmental pathways [, , , ].
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Protein Domain
IPR044422 | SMYD5_SET
Type: Domain
Description: This entry represents the SET domain of SET and MYND domain-containing protein 5 (SMYD5, also termed protein NN8-4AG, or retinoic acid-induced protein 15)). SMYD5 functions as a histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions []. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation []. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis [].The SMYD family consists of five members including SMYD1/2/3/4/5. They contain two highly conserved structural and functional domains, the SET and MYND domains. The SET domain is involved in lysine methylation, while the MYND domain is involved in protein-protein interaction. They are essential in several mammalian developmental pathways [, , , ].
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Protein Domain
IPR044420 | SMYD3_SET
Type: Domain
Description: This entry represents the SET domain of SET and MYND domain-containing protein 3 (SMYD3). SMYD3 functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4 []. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex []. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumours, and has been implicated as an oncogene in human malignancies []. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers [].The SMYD family consists of five members including SMYD1/2/3/4/5. They contain two highly conserved structural and functional domains, the SET and MYND domains. The SET domain is involved in lysine methylation, while the MYND domain is involved in protein-protein interaction. They are essential in several mammalian developmental pathways [, , , ].
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Publication
26315269 | -
First Author: Son J
Year: 2015
Journal: Biochem Biophys Res Commun
Title: Crystal structure of Legionella pneumophila type IV secretion system effector LegAS4.
Volume: 465
Issue: 4
Pages: 817-24
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Protein Domain
IPR044430 | SETD6_SET
Type: Domain
Description: This entry represents the SET domain found in SETD6 and related proteins.SET domain methyltransferases can be involved both in translational and transcriptional roles. N-lysine methyltransferase SETD6 is a SET domain protein that specifically monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulation of NF-kappa-B transcription factor activity []. Homologues in yeast monomethylate 60S ribosomal protein L42 (RPL42A and RPL42B) at 'Lys-55' [, ].
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Protein Domain
IPR044427 | LegAS4-like_SET
Type: Domain
Description: LegAS4 () is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region []. This entry represents the SET domain found in LegAS4 and related proteins.
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Publication
21037105 | -
First Author: Berr A
Year: 2010
Journal: Plant Cell
Title: Arabidopsis SET DOMAIN GROUP2 is required for H3K4 trimethylation and is crucial for both sporophyte and gametophyte development.
Volume: 22
Issue: 10
Pages: 3232-48
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Publication
16096273 | -
First Author: Porras-Yakushi TR
Year: 2005
Journal: J Biol Chem
Title: A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast.
Volume: 280
Issue: 41
Pages: 34590-8
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Protein
Q9CWR2
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein Coding Gene
MGI:1925230 | Sbf1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2652820 | Setd1b
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P97443
Organism: Mus musculus/domesticus
Length: 490  
Fragment?: false
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Protein Domain
IPR044431 | SET_RBCMT
Type: Domain
Description: This entry represents the SET domain found in a group of ribulose-bisphosphate carboxylase]-lysine N-methyltransferases (RBCMTs) and related proteins from plants.In pea (Pisum sativum), the protein-lysine methyltransferase (PsLSMT, also known as RBCMT) catalyses the trimethylation of Lys-14 in the large subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) []. Arabidopsis homologue of RBCMT, LSMT, is a protein-lysine methyltransferase methylating chloroplastic fructose 1,6-bisphosphate aldolases []. The sequence conservation pattern and structure analysis of the SET domain provides clues regarding the possible active site residues of the domain. There are three conserved sequence motifs in most of the SET domain. The N-terminal motif (I) has characteristic glycines. The central motif (II) has a distinct pattern of polar and charged residues (Asn, His). The C-terminal conserved motif (III) has a characteristic dyad of polar residues and the hydrophobic residue tyrosine.
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Publication
26391658 | J:227549
First Author: Gopal S
Year: 2015
Journal: J Cell Biol
Title: Transmembrane proteoglycans control stretch-activated channels to set cytosolic calcium levels.
Volume: 210
Issue: 7
Pages: 1199-211
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Publication
37244931 | J:336186
First Author: Sunadome K
Year: 2023
Journal: Nat Commun
Title: Directionality of developing skeletal muscles is set by mechanical forces.
Volume: 14
Issue: 1
Pages: 3060
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Publication
3243551 | J:9727
First Author: Lathrop M
Year: 1988
Journal: Genomics
Title: A mapped set of genetic markers for human chromosome 9.
Volume: 3
Issue: 4
Pages: 361-6
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Publication
25056707 | J:214613
First Author: Chen Z
Year: 2014
Journal: Nat Rev Cancer
Title: Non-small-cell lung cancers: a heterogeneous set of diseases.
Volume: 14
Issue: 8
Pages: 535-46
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Publication
30655503 | J:298770
First Author: Moore SM
Year: 2019
Journal: Transl Psychiatry
Title: Setd5 haploinsufficiency alters neuronal network connectivity and leads to autistic-like behaviors in mice.
Volume: 9
Issue: 1
Pages: 24
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Publication
11994405 | J:76406
First Author: Firestein R
Year: 2002
Journal: J Clin Invest
Title: Male infertility, impaired spermatogenesis, and azoospermia in mice deficient for the pseudophosphatase Sbf1.
Volume: 109
Issue: 9
Pages: 1165-72
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Publication
14993285 | J:89058
First Author: Dodge JE
Year: 2004
Journal: Mol Cell Biol
Title: Histone H3-K9 methyltransferase ESET is essential for early development.
Volume: 24
Issue: 6
Pages: 2478-86
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Publication
37872881 | J:342950
First Author: Whitlock JH
Year: 2023
Journal: J Cell Mol Med
Title: Cell-type-specific gene expression and regulation in the cerebral cortex and kidney of atypical Setbp1(S858R) Schinzel Giedion Syndrome mice.
Volume: 27
Issue: 22
Pages: 3565-3577
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Publication
32937141 | J:298833
First Author: Nagahama K
Year: 2020
Journal: Cell Rep
Title: Setd1a Insufficiency in Mice Attenuates Excitatory Synaptic Function and Recapitulates Schizophrenia-Related Behavioral Abnormalities.
Volume: 32
Issue: 11
Pages: 108126
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Publication
2761224 | J:24697
First Author: Fernandez JL
Year: 1989
Journal: Lab Anim
Title: CBXC: a set of recombinant inbred strains between CBA/Ca and BALB/c.
Volume: 23
Issue: 3
Pages: 200-2
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Publication
20870719 | -
First Author: Saddic LA
Year: 2010
Journal: J Biol Chem
Title: Methylation of the retinoblastoma tumor suppressor by SMYD2.
Volume: 285
Issue: 48
Pages: 37733-40
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Publication
26826421 | -
 
First Author: Ohtomo-Oda R
Year: 2016
Journal: Hum Pathol
Title: SMYD2 overexpression is associated with tumor cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas.
Volume: 49
Pages: 145-55
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Protein Domain
IPR016852 | SET_MeTrfase
Type: Family
Description: The ribosomal protein L12ab (Rpl12ab) in Saccharomyces cerevisiae is modified by methylation at both arginine and lysine residues. Rkm2 (ribosomal lysine methyltransferase 2) is responsible for the predominant epsilon-trimethylation at lysine 10 of Rpl12ab [].This entry includes Rkm2 and other SET domain proteins that may also be lysine methyltransferases.
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Protein Domain
IPR044419 | SMYD2_SET
Type: Domain
Description: This entry represents the SET domain of SET and MYND domain-containing protein 2 (SMYD2). SMYD2 functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1 [, ]. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). It plays a role in myofilament organisation in both skeletal and cardiac muscles via Hsp90 methylation []. SMYD2 overexpression is associated with tumour cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas []. It regulates leukemia cell growth such that diminished SMYD2 expression upregulates SET7/9, thereby possibly shifting leukemia cells from growth to quiescence state associated with resistance to DNA damage associated with Acute Myeloid Leukemia (AML) [].The SMYD family consists of five members including SMYD1/2/3/4/5. They contain two highly conserved structural and functional domains, the SET and MYND domains. The SET domain is involved in lysine methylation, while the MYND domain is involved in protein-protein interaction. They are essential in several mammalian developmental pathways [, , , ].
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Protein Domain
IPR044433 | SETD5_SET
Type: Domain
Description: This entry represents the SET domain found in SETD5, which is a chromatin regulator required for brain development []. SETD5 is essential for regulating histone acetylation during gene transcription []. Haploinsufficiency of SETD5 is implicated in syndromic autism spectrum disorder (ASD) [].
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Publication
34806773 | J:317835
First Author: Michurina A
Year: 2022
Journal: EMBO J
Title: Postnatal expression of the lysine methyltransferase SETD1B is essential for learning and the regulation of neuron-enriched genes.
Volume: 41
Issue: 1
Pages: e106459
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Protein Domain
IPR024636 | SET_assoc
Type: Domain
Description: The SET domain is a protein-protein interaction domain found in protein lysine methyltransferase enzymes. This entry represents a domain of unknown function which is associated with the SET domain and found in histone lysine methyltransferases [].
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Publication
16618927 | J:109102
First Author: Terranova R
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Histone and DNA methylation defects at Hox genes in mice expressing a SET domain-truncated form of Mll.
Volume: 103
Issue: 17
Pages: 6629-34
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Protein
Q91WC0
Organism: Mus musculus/domesticus
Length: 594  
Fragment?: false
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Protein Domain
IPR044429 | SETD4_SET
Type: Domain
Description: This entry represents the SET domain found in SETD4, which is a cytosolic and nuclear functional lysine methyltransferase that plays a crucial role in breast carcinogenesis []. However, its specific substrates and modification sites remain to be disclosed. Proteins containing this domain also include budding yeast Rkm2, which is a ribosomal protein lysine methyltransferase responsible for trimethylation of the lysine residue at position 3 of Rpl12A and Rpl12B [].
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Protein Domain
IPR044428 | SETD3_SET
Type: Domain
Description: This entry represents the SET domain found in SETD3 and related proteins.SETD3 is a protein-histidine N-methyltransferase that specifically mediates methylation of actin at 'His-73' []. It was initially reported to have histone methyltransferase activity and methylate 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). However, this conclusion was based on mass spectrometry data wherein mass shifts were inconsistent with a bona fide methylation event. In vitro, the protein-lysine methyltransferase activity is weak compared to the protein-histidine methyltransferase activity [].
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Publication
18471979 | -
First Author: Subramanian K
Year: 2008
Journal: Mol Cell
Title: Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase.
Volume: 30
Issue: 3
Pages: 336-47
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Protein Domain
IPR044436 | SETD7_SET
Type: Domain
Description: This entry represents the SET domain found in SETD7, an enzyme that specifically monomethylate Lys-4 of histone H3, thereby creating a specific tag for epigenetic transcriptional activation. Methylation of lysine residues in the N-terminal tails of histones is thought to represent an important component of the mechanism that regulates chromatin structure. SETD7 plays a central role in the transcriptional activation of genes such as collagenase and insulin. It is recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. SETD7 also has methyltransferase activity toward non-histone proteins, including TAF10 and p53/TP53. SETD7 monomethylates Lys-189 of TAF10, which increases the affinity of TAF10 for RNA polymerase II. SETD7 monomethylates Lys-372 of p53/TP53, which stabilises p53/TP53 and increases p53/TP53-mediated transcriptional activation [, ]. SETD7 also methylates non-histone proteins, including estrogen receptor alpha (ERa), suggesting it has a role in diverse biological processes. ERa methylation by Set7/9 stabilises ERa and activates its transcriptional activities, which are involved in the carcinogenesis of breast cancer. In a high-throughput screen, treatment of human breast cancer cells (MCF7 cells) with cyproheptadine, a Set7/9 inhibitor, decreased the expression and transcriptional activity of ERa, thereby inhibiting estrogen-dependent cell growth [, ].These enzymes contain a SET domain, which is necessary but not sufficient for histone methyltransferase activity []. Human SETD7 contains an N-terminal β-sheet domain in addition to the conserved SET domain []. Mutagenesis studies identified two residues in the C terminus of the protein that appear essential for catalytic activity toward lysine-4 of histone H3; cofactor AdoMet binds to this domain [].
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Protein Domain
IPR017155 | Hist-Lys_N-MeTrfase_SET
Type: Family
Description: This entry represents histone-lysine N-methyltransferase (SETD7 or SET7/9) (), which contains a SET domain []. This enzyme specifically monomethylate Lys-4 of histone H3, thereby creating a specific tag for epigenetic transcriptional activation. Methylation of lysine residues in the N-terminal tails of histones is thought to represent an important component of the mechanism that regulates chromatin structure. As such SETD7 plays a central role in the transcriptional activation of genes such as collagenase and insulin. It is recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. SETD7 also has methyltransferase activity toward non-histone proteins, including TAF10 and p53/TP53. SETD7 monomethylates Lys-189 of TAF10, which increases the affinity of TAF10 for RNA polymerase II. SETD7 monomethylates Lys-372 of p53/TP53, which stabilises p53/TP53 and increases p53/TP53-mediated transcriptional activation []. These enzymes contain a SET domain, which is necessary but not sufficient for histone methyltransferase activity []. Human SETD7 contains an N-terminal β-sheet domain in addition to the conserved SET domain []. Mutagenesis studies []identified two residues in the C terminus of the protein that appear essential for catalytic activity toward lysine-4 of histone H3; cofactor AdoMet binds to this domain.
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Publication
31527793 | J:293475
First Author: Diep J
Year: 2019
Journal: Nat Microbiol
Title: Enterovirus pathogenesis requires the host methyltransferase SETD3.
Volume: 4
Issue: 12
Pages: 2523-2537
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Publication
31047779 | J:276037
First Author: Styr B
Year: 2019
Journal: Neuron
Title: Mitochondrial Regulation of the Hippocampal Firing Rate Set Point and Seizure Susceptibility.
Volume: 102
Issue: 5
Pages: 1009-1024.e8
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Publication
25643397 | J:269461
   
First Author: Baeyens N
Year: 2015
Journal: Elife
Title: Vascular remodeling is governed by a VEGFR3-dependent fluid shear stress set point.
Volume: 4
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Publication
32533074 | J:293844
First Author: Leonards K
Year: 2020
Journal: Nat Commun
Title: Nuclear interacting SET domain protein 1 inactivation impairs GATA1-regulated erythroid differentiation and causes erythroleukemia.
Volume: 11
Issue: 1
Pages: 2807
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Protein Domain
IPR044438 | EZH1_SET
Type: Domain
Description: This entry represents the SET domain found in EZH1.The Polycomb Repressive Complex 2 (PRC2) is a chromatin modifying complex that consists of three core components: EED, SUZ12 and one of the two histone H3K27 methyltransferases, EZH1 or EZH2 []. The PRC2 complex catalyses di- and trimethylation of histone H3 lysine 27 (H3K37me2/3), which has a repressive role. Even though EZH1 and EZH2 form similar PRC2 complexes, they exhibit contrasting repressive roles. In terms of their expression in mice, EZH1 is more abundant in nonproliferative adult organs, while EZH2 expression is tightly associated with proliferation [].
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Protein Domain
IPR044439 | EZH2_SET
Type: Domain
Description: This entry represents the SET domain found in EZH2.The Polycomb Repressive Complex 2 (PRC2) is a chromatin modifying complex that consists of three core components: EED, SUZ12 and one of the two histone H3K27 methyltransferases, EZH1 or EZH2 []. The PRC2 complex catalyses di- and trimethylation of histone H3 lysine 27 (H3K37me2/3), which has a repressive role. Even though EZH1 and EZH2 form similar PRC2 complexes, they exhibit contrasting repressive roles. In terms of their expression in mice, EZH1 is more abundant in nonproliferative adult organs, while EZH2 expression is tightly associated with proliferation [].
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Protein Coding Gene
MGI:2142581 | Nsd3
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
12805229 | J:83923
First Author: Rayasam GV
Year: 2003
Journal: EMBO J
Title: NSD1 is essential for early post-implantation development and has a catalytically active SET domain.
Volume: 22
Issue: 12
Pages: 3153-63
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