SETD7

Protein-coding gene in the species Homo sapiens

SETD7

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

1H3I, 1MT6, 1MUF, 1N6A, 1N6C, 1O9S, 1XQH, 2F69, 3CBM, 3CBO, 3CBP, 3M53, 3M54, 3M55, 3M56, 3M57, 3M58, 3M59, 3M5A, 3OS5, 3VUZ, 3VV0, 4E47, 4J7F, 4J8O, 4JDS, 4JLG, 5EG2, 5AYF

Identifiers
Aliases| SETD7, KMT7, SET7, SET7/9, SET9, SET domain containing lysine methyltransferase 7, SET domain containing 7, histone lysine methyltransferase
External IDs| OMIM: 606594; MGI: 1920501; HomoloGene: 12741; GeneCards: SETD7; OMA:SETD7 - orthologs
| Gene location (Human)

Chr.| Chromosome 4 (human)[1]

Band| 4q31.1| Start| 139,495,941 bp[1]
End| 139,606,699 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 3 (mouse)[2]

Band| 3|3 C| Start| 51,422,740 bp[2]
End| 51,468,300 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* tibialis anterior muscle

* deltoid muscle

* cardiac muscle tissue of right atrium

* myocardium of left ventricle

* skin of arm

* quadriceps femoris muscle

* Skeletal muscle tissue of rectus abdominis

* biceps brachii

* vastus lateralis muscle

* Skeletal muscle tissue of biceps brachii

| Top expressed in

* triceps brachii muscle

* temporal muscle

* sternocleidomastoid muscle

* ciliary body

* digastric muscle

* lobe of cerebellum

* cerebellar vermis

* ankle

* lateral geniculate nucleus

* epithelium of lens

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* methyltransferase activity
* transferase activity
* p53 binding
* chromatin binding
* protein-lysine N-methyltransferase activity
* protein binding
* histone-lysine N-methyltransferase activity

Cellular component|

* nucleoplasm
* chromosome
* nucleolus
* nucleus

Biological process|

* regulation of transcription, DNA-templated
* peptidyl-lysine monomethylation
* transcription, DNA-templated
* cellular response to DNA damage stimulus
* positive regulation of transcription, DNA-templated
* peptidyl-lysine methylation
* methylation
* heterochromatin organization
* peptidyl-lysine dimethylation
* histone lysine methylation
* response to ethanol
* regulation of histone H3-K9 methylation
* chromatin organization

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

80854

73251

Ensembl| |

ENSG00000145391

ENSMUSG00000037111

UniProt| |

Q8WTS6

Q8VHL1

RefSeq (mRNA)| |

NM_001306199
NM_001306200
NM_030648

NM_080793

RefSeq (protein)| |

NP_001293128
NP_001293129
NP_085151

NP_542983

Location (UCSC)| Chr 4: 139.5 – 139.61 Mb| Chr 3: 51.42 – 51.47 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.[5][6][7]

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000145391 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037111 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ 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.
6. ^ 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. S2CID 37879139.
7. ^ "SETD7 SET domain containing 7, histone lysine methyltransferase [ Homo sapiens (human) ]".

## Further reading

[edit]

* 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. S2CID 14727763.
* 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. S2CID 28718612.
* 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\. Bibcode:2002PNAS...9916899M. 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" (PDF). Nature. 421 (6923): 652–6\. Bibcode:2003Natur.421..652X. doi:10.1038/nature01378. PMID 12540855. S2CID 4423407.
* 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\. CiteSeerX 10.1.1.320.8454. 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\. Bibcode:2004Natur.432..353C. doi:10.1038/nature03117. PMID 15525938. S2CID 4398310.
* 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. S2CID 38483056.
* 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. S2CID 10003129.

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PDB gallery

* 1h3i: CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9

* 1mt6: Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy

* 1muf: Structure of histone H3 K4-specific methyltransferase SET7/9

* 1n6a: Structure of SET7/9

* 1n6c: Structure of SET7/9

* 1o9s: CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF THE HUMAN HISTONE METHYLTRANSFERASE SET7/9

* 1xqh: Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH

* 2f69: Ternary complex of SET7/9 bound to AdoHcy and a TAF10 peptide

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