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Search results 201 to 239 out of 239 for Setd7

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0.024s

Type

Details

Score

UniProt Feature

Begin:	1
Description:	Histone-lysine N-methyltransferase SETD7
Type:	chain
End:	366

•

Publication

31141694 | J:300933

First Author:	Nayak A
Year:	2019
Journal:	Cell Rep
Title:	Regulation of SETD7 Methyltransferase by SENP3 Is Crucial for Sarcomere Organization and Cachexia.
Volume:	27
Issue:	9
Pages:	2725-2736.e4

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Publication

12711597 | -

First Author:	Chakrabarti SK
Year:	2003
Journal:	J Biol Chem
Title:	Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells.
Volume:	278
Issue:	26
Pages:	23617-23

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Allele

Tg(Ttr-SETD7)1Ital | MGI:7451203

Name:	transgene insertion 1, Iannis Talianidis
Allele Type:	Transgenic
Attribute String:	Inserted expressed sequence

•

Strain

MGI:6335558 | STOCK Tg(Ttr-SETD7)1Ital/Flmg

Attribute String:

mutant strain, transgenic

•

Allele

Tg(Ttr-SETD7*H297A)1Ital | MGI:7451205

Name:	transgene insertion 1, Iannis Talianidis
Allele Type:	Transgenic
Attribute String:	Inserted expressed sequence

•

Strain

MGI:6335559 | STOCK Tg(Ttr-SETD7*H297A)1Ital/Flmg

Attribute String:

mutant strain, transgenic

•

Publication

12389038 | -

First Author:	Jacobs SA
Year:	2002
Journal:	Nat Struct Biol
Title:	The active site of the SET domain is constructed on a knot.
Volume:	9
Issue:	11
Pages:	833-8

•

Publication

12514135 | -

First Author:	Kwon T
Year:	2003
Journal:	EMBO J
Title:	Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.
Volume:	22
Issue:	2
Pages:	292-303

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Publication

15525938 | J:345036

First Author:	Chuikov S
Year:	2004
Journal:	Nature
Title:	Regulation of p53 activity through lysine methylation.
Volume:	432
Issue:	7015
Pages:	353-60

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Publication

18391193 | -

First Author:	Zhang X
Year:	2008
Journal:	Proc Natl Acad Sci U S A
Title:	Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases.
Volume:	105
Issue:	15
Pages:	5728-32

•

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

•

Publication

27088648 | -

First Author:	Takemoto Y
Year:	2016
Journal:	J Med Chem
Title:	Identification of Cyproheptadine as an Inhibitor of SET Domain Containing Lysine Methyltransferase 7/9 (Set7/9) That Regulates Estrogen-Dependent Transcription.
Volume:	59
Issue:	8
Pages:	3650-60

•

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 [].

•

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.

•

Publication

12372304 | -

First Author:	Wilson JR
Year:	2002
Journal:	Cell
Title:	Crystal structure and functional analysis of the histone methyltransferase SET7/9.
Volume:	111
Issue:	1
Pages:	105-15

•

Publication

36949755 | J:334295

First Author:	Hernandez JC
Year:	2023
Journal:	iScience
Title:	LIN28 and histone H3K4 methylase induce TLR4 to generate tumor-initiating stem-like cells.
Volume:	26
Issue:	3
Pages:	106254

•

Publication

27736906 | J:254208

First Author:	Papeta N
Year:	2016
Journal:	PLoS One
Title:	Refinement of the HIVAN1 Susceptibility Locus on Chr. 3A1-A3 via Generation of Sub-Congenic Strains.
Volume:	11
Issue:	10
Pages:	e0163860

•

Protein Domain

IPR016858 | Hist_H4-K20_MeTrfase

Type:

Family

Description:

Methyltransferases (EC 2.1.1.-) constitute an important class of enzymespresent in every life form. They transfer a methyl group most frequently fromS-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such asnitrogen, oxygen, sulfur or carbon leading to S-adenosyl-L-homocysteine(AdoHcy) and a methylated molecule. The substrates that are methylated bythese enzymes cover virtually every kind of biomolecules ranging from smallmolecules, to lipids, proteins and nucleic acids. Methyltransferases aretherefore involved in many essential cellular processes includingbiosynthesis, signal transduction, protein repair, chromatin regulation andgene silencing [, , ]. More than 230 different enzymatic reactions ofmethyltransferases have been described so far, of which more than 220 use SAMas the methyl donor [E1]. A review published in 2003 []divides allmethyltransferases into 5 classes based on the structure of their catalyticdomain (fold):class I: Rossmann-like alpha/beta class II: TIM beta/α-barrel alpha/beta class III: tetrapyrrole methylase alpha/betaclass IV: SPOUT alpha/beta class V: SET domainall betaA more recent paper []based on a study of the Saccharomyces cerevisiae methyltransferome argues for four more folds:class VI: transmembrane all alpha class VII: DNA/RNA-binding 3-helical bundle all alpha class VIII: SSo0622-like alpha+beta class IX: thymidylate synthetase alpha+betaThis entry represents the class V proteins, which contain the SET domain usually flanked byother domains forming the so-called pre- and post-SET regions. The enzymesbelonging to this class all N-methylate lysine in proteins. Most of them arehistone methyltransferases (EC 2.1.1.43) like the histone H3-K9methyltransferase dim-5 or the histone H3-K4methyltransferase SETD7 [, ]. Some others methylate thelarge subunit of the enzyme ribulose-bisphosphate-carboxylase/oxygenase(RuBisCO) (EC 2.1.1.127) in plants; in these enzymes the SET domain isinterrupted by a novel domain []. Cytochrome c lysine N-methyltransferases(EC 2.1.1.59) do not possess a SET domain, or at least not a SET domaindetected by any of the detection methods; however they do display a SET-likeregion and for this reason they are also assigned to this class [].

•

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

•

Protein Domain

IPR025785 | SETD3

Type:

Family

Description:

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 [].Methyltransferases (EC [intenz:2.1.1.-]) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [, , ]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM []. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [, , ]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [, , ]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.A review published in 2003 []divides allmethyltransferases into 5 classes based on the structure of their catalyticdomain (fold):class I: Rossmann-like alpha/betaclass II: TIM beta/α-barrel alpha/betaclass III: tetrapyrrole methylase alpha/betaclass IV: SPOUT alpha/beta class V: SET domain all betaA more recent paper []based on a study of the Saccharomyces cerevisiaemethyltransferome argues for four more folds:class VI: transmembrane all alpha class VII: DNA/RNA-binding 3-helical bundle all alphaclass VIII: SSo0622-like alpha betaclass IX: thymidylate synthetase alpha betaClass V proteins contain the SET domain usually flanked byother domains forming the so-called pre- and post-SET regions. Except themembers of the STD3 family which N-methylate histidine in beta-actin (EC2.1.1.85) [, ], enzymes belonging to this class N-methylatelysine in proteins. Most of them are histone methyltransferases (EC 2.1.1.43)like the histone H3-K9 methyltransferase dim-5 or the histoneH3-K4 methyltransferase SETD7 [, ]. Some others methylatethe large subunit of the enzyme ribulose-bisphosphate-carboxylase/oxygenase(RuBisCO) (EC 2.1.1.127) in plants; in these enzymes the SET domain isinterrupted by a novel domain []. Cytochrome c lysine N-methyltransferases(EC 2.1.1.59) do not possess a SET domain, or at least not a SET domaindetected by any of the detection methods; however they do display a SET-likeregion and for this reason they are also assigned to this class [].

•

Publication

17327221 | -

First Author:	Porras-Yakushi TR
Year:	2007
Journal:	J Biol Chem
Title:	Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily: identification of Rpl23ab methylation sites and recognition motifs.
Volume:	282
Issue:	17
Pages:	12368-76

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Protein

Q8C1L9

Organism:	Mus musculus/domesticus
Length:	323
Fragment?:	true

•

Publication

30526847 | -

First Author:	Kwiatkowski S
Year:	2018
Journal:	Elife
Title:	SETD3 protein is the actin-specific histidine N-methyltransferase.
Volume:	7

•

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

Q2YDW7

Organism:	Mus musculus/domesticus
Length:	349
Fragment?:	false

•

Protein

F2Z438

Organism:	Mus musculus/domesticus
Length:	155
Fragment?:	true

•

Protein

A0A0G2JFK5

Organism:	Mus musculus/domesticus
Length:	295
Fragment?:	false

•

Protein

E9QNB8

Organism:	Mus musculus/domesticus
Length:	350
Fragment?:	false

•

Protein

D3YXI6

Organism:	Mus musculus/domesticus
Length:	364
Fragment?:	false

•

Protein

Q91WC0

Organism:	Mus musculus/domesticus
Length:	594
Fragment?:	false

•

Protein

F2Z420

Organism:	Mus musculus/domesticus
Length:	290
Fragment?:	false

•

Publication

16225687 | -

First Author:	Kozbial PZ
Year:	2005
Journal:	BMC Struct Biol
Title:	Natural history of S-adenosylmethionine-binding proteins.
Volume:	5

Pages:	19

•

Publication

21858014 | -

First Author:	Wlodarski T
Year:	2011
Journal:	PLoS One
Title:	Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome.
Volume:	6
Issue:	8
Pages:	e23168

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Publication

12826405 | -

First Author:	Schubert HL
Year:	2003
Journal:	Trends Biochem Sci
Title:	Many paths to methyltransfer: a chronicle of convergence.
Volume:	28
Issue:	6
Pages:	329-35

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Publication

7897657 | -

First Author:	Schluckebier G
Year:	1995
Journal:	J Mol Biol
Title:	Universal catalytic domain structure of AdoMet-dependent methyltransferases.
Volume:	247
Issue:	1
Pages:	16-20

•

Publication

- | J:82809

First Author:	European Mouse Mutant Archive
Year:	2003
Journal:	Unpublished
Title:	Information obtained from the European Mouse Mutant Archive (EMMA)

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

•

Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

•

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