SETD7: Difference between revisions

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Revision as of 06:10, 11 September 2017

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.^[1]^[2]^[3]

References

↑ Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D (Feb 2002). "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation". Genes Dev. 16 (4): 479–89. doi:10.1101/gad.967202. PMC 155346. PMID 11850410.
↑ Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y (Jan 2002). "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase". Mol Cell. 8 (6): 1207–17. doi:10.1016/S1097-2765(01)00405-1. PMID 11779497.
↑ "Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7".

Nagase T, Kikuno R, Hattori A, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347–55. doi:10.1093/dnares/7.6.347. PMID 11214970.
Wilson JR, Jing C, Walker PA, et al. (2002). "Crystal structure and functional analysis of the histone methyltransferase SET7/9". Cell. 111 (1): 105–15. doi:10.1016/S0092-8674(02)00964-9. PMID 12372304.
Jacobs SA, Harp JM, Devarakonda S, et al. (2002). "The active site of the SET domain is constructed on a knot". Nat. Struct. Biol. 9 (11): 833–8. doi:10.1038/nsb861. PMID 12389038.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Kwon T, Chang JH, Kwak E, et al. (2003). "Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9–AdoMet". EMBO J. 22 (2): 292–303. doi:10.1093/emboj/cdg025. PMC 140100. PMID 12514135.
Xiao B, Jing C, Wilson JR, et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9". Nature. 421 (6923): 652–6. doi:10.1038/nature01378. PMID 12540855.
Wysocka J, Myers MP, Laherty CD, et al. (2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
Kouskouti A, Scheer E, Staub A, et al. (2004). "Gene-specific modulation of TAF10 function by SET9-mediated methylation". Mol. Cell. 14 (2): 175–82. doi:10.1016/S1097-2765(04)00182-0. PMID 15099517.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Chuikov S, Kurash JK, Wilson JR, et al. (2004). "Regulation of p53 activity through lysine methylation". Nature. 432 (7015): 353–60. doi:10.1038/nature03117. PMID 15525938.
Couture JF, Collazo E, Hauk G, Trievel RC (2006). "Structural basis for the methylation site specificity of SET7/9". Nat. Struct. Mol. Biol. 13 (2): 140–6. doi:10.1038/nsmb1045. PMID 16415881.
Hayakawa T, Ohtani Y, Hayakawa N, et al. (2007). "RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation". Genes Cells. 12 (6): 811–26. doi:10.1111/j.1365-2443.2007.01089.x. PMID 17573780.

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

[pmid11850410-1] Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D (Feb 2002). "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation". Genes Dev. 16 (4): 479–89. doi:10.1101/gad.967202. PMC 155346. PMID 11850410.

[pmid11779497-2] Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y (Jan 2002). "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase". Mol Cell. 8 (6): 1207–17. doi:10.1016/S1097-2765(01)00405-1. PMID 11779497.

[entrez-3] "Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7".

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Underlinked|date=June 2016}}
-{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''Histone-lysine N-methyltransferase SETD7''' is an [[enzyme]] that in humans is encoded by the ''SETD7'' [[gene]].<ref name="pmid11850410">{{cite journal | vauthors = Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D | title = Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation | journal = Genes Dev | volume = 16 | issue = 4 | pages = 479–89 |date=Feb 2002 | pmid = 11850410 | pmc = 155346 | doi = 10.1101/gad.967202 }}</ref><ref name="pmid11779497">{{cite journal | vauthors = Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y | title = Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase | journal = Mol Cell | volume = 8 | issue = 6 | pages = 1207–17 |date=Jan 2002 | pmid = 11779497 | pmc =  | doi =10.1016/S1097-2765(01)00405-1  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80854| accessdate = }}</ref>
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-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image = PBB_Protein_SETD7_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h3i.
- | PDB = {{PDB2|1h3i}}, {{PDB2|1mt6}}, {{PDB2|1muf}}, {{PDB2|1n6a}}, {{PDB2|1n6c}}, {{PDB2|1o9s}}, {{PDB2|1xqh}}, {{PDB2|2f69}}
- | Name = SET domain containing (lysine methyltransferase) 7
- | HGNCid = 30412
- | Symbol = SETD7
- | AltSymbols =; SET7; FLJ21193; KIAA1717; SET7/9; SET9
- | OMIM = 606594
- | ECnumber =
- | Homologene = 12741
- | MGIid = 1920501
- | GeneAtlas_image1 = PBB_GE_SETD7_gnf1h04321_at_tn.png
- | GeneAtlas_image2 = PBB_GE_SETD7_gnf1h08582_s_at_tn.png
- | Function = {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0018024 |text = histone-lysine N-methyltransferase activity}}
- | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
- | Process = {{GNF_GO|id=GO:0016568 |text = chromatin modification}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 80854
-    | Hs_Ensembl = ENSG00000145391
-    | Hs_RefseqProtein = NP_085151
-    | Hs_RefseqmRNA = NM_030648
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 4
-    | Hs_GenLoc_start = 140646642
-    | Hs_GenLoc_end = 140697027
-    | Hs_Uniprot = Q8WTS6
-    | Mm_EntrezGene = 73251
-    | Mm_Ensembl = ENSMUSG00000037111
-    | Mm_RefseqmRNA = NM_080793
-    | Mm_RefseqProtein = NP_542983
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 3
-    | Mm_GenLoc_start = 51603247
-    | Mm_GenLoc_end = 51648752
-    | Mm_Uniprot = Q6ZPJ6
-  }}
-}}
-'''SET domain containing (lysine methyltransferase) 7''', also known as '''SETD7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80854| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
@@ Line 56: / Line 10: @@
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Nagase T, Kikuno R, Hattori A, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 6 |pages= 347-55 |year= 2001 |pmid= 11214970 |doi=  }}
+*{{cite journal   |vauthors=Nagase T, Kikuno R, Hattori A, etal |title=Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro |journal=DNA Res. |volume=7 |issue= 6 |pages= 347–55 |year= 2001 |pmid= 11214970 |doi=10.1093/dnares/7.6.347  }}
-*{{cite journal  | author=Wang H, Cao R, Xia L, ''et al.'' |title=Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. |journal=Mol. Cell |volume=8 |issue= 6 |pages= 1207-17 |year= 2002 |pmid= 11779497 |doi=  }}
+*{{cite journal   |vauthors=Wilson JR, Jing C, Walker PA, etal |title=Crystal structure and functional analysis of the histone methyltransferase SET7/9 |journal=Cell |volume=111 |issue= 1 |pages= 105–15 |year= 2002 |pmid= 12372304 |doi=10.1016/S0092-8674(02)00964-9  }}
-*{{cite journal  | author=Nishioka K, Chuikov S, Sarma K, ''et al.'' |title=Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. |journal=Genes Dev. |volume=16 |issue= 4 |pages= 479-89 |year= 2002 |pmid= 11850410 |doi= 10.1101/gad.967202 }}
+*{{cite journal   |vauthors=Jacobs SA, Harp JM, Devarakonda S, etal |title=The active site of the SET domain is constructed on a knot |journal=Nat. Struct. Biol. |volume=9 |issue= 11 |pages= 833–8 |year= 2002 |pmid= 12389038 |doi= 10.1038/nsb861 }}
-*{{cite journal  | author=Wilson JR, Jing C, Walker PA, ''et al.'' |title=Crystal structure and functional analysis of the histone methyltransferase SET7/9. |journal=Cell |volume=111 |issue= 1 |pages= 105-15 |year= 2002 |pmid= 12372304 |doi=  }}
+*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
-*{{cite journal  | author=Jacobs SA, Harp JM, Devarakonda S, ''et al.'' |title=The active site of the SET domain is constructed on a knot. |journal=Nat. Struct. Biol. |volume=9 |issue= 11 |pages= 833-8 |year= 2002 |pmid= 12389038 |doi= 10.1038/nsb861 }}
+*{{cite journal   |vauthors=Kwon T, Chang JH, Kwak E, etal |title=Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9–AdoMet |journal=EMBO J. |volume=22 |issue= 2 |pages= 292–303 |year= 2003 |pmid= 12514135 |doi= 10.1093/emboj/cdg025  | pmc=140100 }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal   |vauthors=Xiao B, Jing C, Wilson JR, etal |title=Structure and catalytic mechanism of the human histone methyltransferase SET7/9 |journal=Nature |volume=421 |issue= 6923 |pages= 652–6 |year= 2003 |pmid= 12540855 |doi= 10.1038/nature01378 }}
-*{{cite journal  | author=Kwon T, Chang JH, Kwak E, ''et al.'' |title=Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. |journal=EMBO J. |volume=22 |issue= 2 |pages= 292-303 |year= 2003 |pmid= 12514135 |doi= 10.1093/emboj/cdg025 }}
+*{{cite journal   |vauthors=Wysocka J, Myers MP, Laherty CD, etal |title=Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 |journal=Genes Dev. |volume=17 |issue= 7 |pages= 896–911 |year= 2003 |pmid= 12670868 |doi= 10.1101/gad.252103  | pmc=196026 }}
-*{{cite journal  | author=Xiao B, Jing C, Wilson JR, ''et al.'' |title=Structure and catalytic mechanism of the human histone methyltransferase SET7/9. |journal=Nature |volume=421 |issue= 6923 |pages= 652-6 |year= 2003 |pmid= 12540855 |doi= 10.1038/nature01378 }}
+*{{cite journal   |vauthors=Kouskouti A, Scheer E, Staub A, etal |title=Gene-specific modulation of TAF10 function by SET9-mediated methylation |journal=Mol. Cell |volume=14 |issue= 2 |pages= 175–82 |year= 2004 |pmid= 15099517 |doi=10.1016/S1097-2765(04)00182-0  }}
-*{{cite journal  | author=Wysocka J, Myers MP, Laherty CD, ''et al.'' |title=Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. |journal=Genes Dev. |volume=17 |issue= 7 |pages= 896-911 |year= 2003 |pmid= 12670868 |doi= 10.1101/gad.252103 }}
+*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
-*{{cite journal  | author=Kouskouti A, Scheer E, Staub A, ''et al.'' |title=Gene-specific modulation of TAF10 function by SET9-mediated methylation. |journal=Mol. Cell |volume=14 |issue= 2 |pages= 175-82 |year= 2004 |pmid= 15099517 |doi=  }}
+*{{cite journal   |vauthors=Chuikov S, Kurash JK, Wilson JR, etal |title=Regulation of p53 activity through lysine methylation |journal=Nature |volume=432 |issue= 7015 |pages= 353–60 |year= 2004 |pmid= 15525938 |doi= 10.1038/nature03117 }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal  | vauthors=Couture JF, Collazo E, Hauk G, Trievel RC |title=Structural basis for the methylation site specificity of SET7/9 |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 2 |pages= 140–6 |year= 2006 |pmid= 16415881 |doi= 10.1038/nsmb1045 }}
-*{{cite journal  | author=Chuikov S, Kurash JK, Wilson JR, ''et al.'' |title=Regulation of p53 activity through lysine methylation. |journal=Nature |volume=432 |issue= 7015 |pages= 353-60 |year= 2004 |pmid= 15525938 |doi= 10.1038/nature03117 }}
+*{{cite journal   |vauthors=Hayakawa T, Ohtani Y, Hayakawa N, etal |title=RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation |journal=Genes Cells |volume=12 |issue= 6 |pages= 811–26 |year= 2007 |pmid= 17573780 |doi= 10.1111/j.1365-2443.2007.01089.x }}
-*{{cite journal  | author=Couture JF, Collazo E, Hauk G, Trievel RC |title=Structural basis for the methylation site specificity of SET7/9. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 2 |pages= 140-6 |year= 2006 |pmid= 16415881 |doi= 10.1038/nsmb1045 }}
-*{{cite journal  | author=Hayakawa T, Ohtani Y, Hayakawa N, ''et al.'' |title=RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation. |journal=Genes Cells |volume=12 |issue= 6 |pages= 811-26 |year= 2007 |pmid= 17573780 |doi= 10.1111/j.1365-2443.2007.01089.x }}
 }}
 {{refend}}
+{{PDB Gallery|geneid=80854}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
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+| update_citations = yes
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-{{protein-stub}}
+{{gene-4-stub}}
-{{WikiDoc Sources}}

SETD7: Difference between revisions

Revision as of 06:10, 11 September 2017

References

Further reading

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