SUV39H1

SUV39H1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3MTS
Identifiers
Aliases	SUV39H1 , H3-K9-HMTase 1, KMT1A, MG44, SUV39H, suppressor of variegation 3-9 homolog 1, SUV39H1 histone lysine methyltransferase
External IDs	OMIM: 300254; MGI: 1099440; HomoloGene: 2388; GeneCards: SUV39H1; OMA:SUV39H1 - orthologs
Gene location (Human) Chr. X chromosome (human) [1] Band Xp11.23 Start 48,695,554 bp [1] End 48,709,016 bp [1]
Gene location (Mouse) Chr. X chromosome (mouse) [2] Band X A1.1|X 3.64 cM Start 7,927,410 bp [2] End 7,940,999 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad granulocyte ventricular zone apex of heart mucosa of transverse colon testicle epithelium of esophagus tibialis anterior muscle ganglionic eminence gastrocnemius muscle Top expressed in abdominal wall fetal liver hematopoietic progenitor cell yolk sac ventricular zone maxillary prominence mandibular prominence thymus epiblast tail of embryo primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity transferase activity histone methyltransferase activity histone methyltransferase activity (H3-K9 specific) S-adenosylmethionine-dependent methyltransferase activity protein N-terminus binding zinc ion binding chromatin binding transcription cis-regulatory region binding metal ion binding protein binding histone-lysine N-methyltransferase activity Cellular component nuclear lamina nucleoplasm chromosome heterochromatin condensed nuclear chromosome rDNA heterochromatin chromatin silencing complex chromosome, centromeric region nucleus Biological process cell differentiation regulation of transcription, DNA-templated histone H3-K9 dimethylation rhythmic process negative regulation of circadian rhythm negative regulation of transcription by RNA polymerase II transcription, DNA-templated histone H3-K9 trimethylation cellular response to DNA damage stimulus methylation rDNA heterochromatin assembly rRNA processing histone lysine methylation cell cycle viral process negative regulation of transcription, DNA-templated cellular response to hypoxia chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6839 20937 Ensembl ENSG00000101945 ENSMUSG00000039231 UniProt O43463 O54864 RefSeq (mRNA) NM_003173 NM_001282166 NM_001290716 NM_011514 NM_001358237 RefSeq (protein) NP_001269095 NP_003164 NP_001277645 NP_035644 NP_001345166 Location (UCSC) Chr X: 48.7 – 48.71 Mb Chr X: 7.93 – 7.94 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene. ^[5]

Function

This gene is a member of the suppressor of variegation 3-9 homolog family and encodes a protein with a chromodomain and a C-terminal SET domain. This nuclear protein moves to the centromeres during mitosis and functions as a histone methyltransferase, methylating lysine-9 of histone H3. Overall, it plays a vital role in heterochromatin organization, chromosome segregation, and mitotic progression. ^[6] In mouse embryonic stem cells, Suv39h1 expression is repressed by OCT4 protein through the induction of an antisense long non-coding RNA. ^[7]

Interactions

SUV39H1 has been shown to interact with:

• CBX1, ^[5]
• CBX5, ^{[8] [9] [10]}
• DNMT3A, ^[11]
• HDAC1, ^[12]
• HDAC3, ^[12]
• HDAC9, ^[8]
• Histone deacetylase 2, ^[12]
• MBD1, ^[9]
• RUNX1, ^[13]
• Retinoblastoma protein, ^{[14] [15]} and
• SBF1. ^[16]

• PIN1 ^[17]

References

1. GRCh38: Ensembl release 89: ENSG00000101945 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039231 – 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. Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB, Reuter G, Jenuwein T (June 1999). "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31". EMBO J. 18 (7): 1923–38. doi:10.1093/emboj/18.7.1923. PMC   1171278 . PMID   10202156.
6. "Entrez Gene: SUV39H1 suppressor of variegation 3-9 homolog 1 (Drosophila)".
7. Bernard LD, Dubois A, Heurtier V, Fischer V, Gonzalez I, Chervova A, Tachtsidi A, Gil N, Owens N, Bates LE, Vandormael-Pournin S, Silva JC, Ulitsky I, Cohen-Tannoudji M, Navarro P (28 June 2022). "OCT4 activates a Suv39h1-repressive antisense lncRNA to couple histone H3 Lysine 9 methylation to pluripotency". Nucleic Acids Research. 50 (13): 7367–7379. doi:10.1093/nar/gkac550. PMC   9303268 . PMID   35762231.
8. Zhang CL, McKinsey TA, Olson EN (October 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/mcb.22.20.7302-7312.2002. PMC   139799 . PMID   12242305.
9. Fujita N, Watanabe S, Ichimura T, Tsuruzoe S, Shinkai Y, Tachibana M, Chiba T, Nakao M (June 2003). "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression". J. Biol. Chem. 278 (26): 24132–8. doi: 10.1074/jbc.M302283200 . PMID   12711603.
10. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
11. Fuks F, Hurd PJ, Deplus R, Kouzarides T (May 2003). "The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase". Nucleic Acids Res. 31 (9): 2305–12. doi:10.1093/nar/gkg332. PMC   154218 . PMID   12711675.
12. Vaute O, Nicolas E, Vandel L, Trouche D (January 2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. doi:10.1093/nar/30.2.475. PMC   99834 . PMID   11788710.
13. Chakraborty S, Sinha KK, Senyuk V, Nucifora G (August 2003). "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo". Oncogene. 22 (34): 5229–37. doi: 10.1038/sj.onc.1206600 . PMID   12917624.
14. Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera RE, Kouzarides T (August 2001). "Rb targets histone H3 methylation and HP1 to promoters". Nature. 412 (6846): 561–5. Bibcode:2001Natur.412..561N. doi:10.1038/35087620. PMID   11484059. S2CID   4378296.
15. Vandel L, Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (October 2001). "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. 21 (19): 6484–94. doi:10.1128/mcb.21.19.6484-6494.2001. PMC   99795 . PMID   11533237.
16. Firestein R, Cui X, Huie P, Cleary ML (July 2000). "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9". Mol. Cell. Biol. 20 (13): 4900–9. doi:10.1128/mcb.20.13.4900-4909.2000. PMC   85941 . PMID   10848615.
17. Khanal P, Kim G, Lim SC, Yun HJ, Lee KY, Choi HK, Choi HS (2013). "Prolyl isomerase Pin1 negatively regulates the stability of SUV39H1 to promote tumorigenesis in breast cancer". The FASEB Journal. 27 (11): 4606–4618. doi: 10.1096/fj.13-236851 . PMID   23934277. S2CID   5259616.

Further reading

• Schotta G, Ebert A, Reuter G (2003). "SU(VAR)3-9 is a conserved key function in heterochromatic gene silencing". Genetica. 117 (2–3): 149–58. doi:10.1023/A:1022923508198. PMID   12723694. S2CID   39517859.
• Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R (1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Mol. Cell. Biol. 15 (6): 3082–9. doi:10.1128/mcb.15.6.3082. PMC   230539 . PMID   7760804.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Aagaard L, Schmid M, Warburton P, Jenuwein T (2000). "Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres". J. Cell Sci. 113 (5): 817–29. doi:10.1242/jcs.113.5.817. PMID   10671371.
• Melcher M, Schmid M, Aagaard L, Selenko P, Laible G, Jenuwein T (2000). "Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression". Mol. Cell. Biol. 20 (10): 3728–41. doi:10.1128/MCB.20.10.3728-3741.2000. PMC   85674 . PMID   10779362.
• Firestein R, Cui X, Huie P, Cleary ML (2000). "Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9". Mol. Cell. Biol. 20 (13): 4900–9. doi:10.1128/MCB.20.13.4900-4909.2000. PMC   85941 . PMID   10848615.
• Fraser ME, James MN, Bridger WA, Wolodko WT (2000). "Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase". J. Mol. Biol. 299 (5): 1325–39. doi:10.1006/jmbi.2000.3807. PMID   10873456.
• Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T (2000). "Regulation of chromatin structure by site-specific histone H3 methyltransferases". Nature. 406 (6796): 593–9. Bibcode:2000Natur.406..593R. doi:10.1038/35020506. PMID   10949293. S2CID   205008015.
• Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116–20. Bibcode:2001Natur.410..116L. doi:10.1038/35065132. PMID   11242053. S2CID   4331863.
• Vandel L, Trouche D (2001). "Physical association between the histone acetyl transferase CBP and a histone methyl transferase". EMBO Rep. 2 (1): 21–6. doi:10.1093/embo-reports/kve002. PMC   1083799 . PMID   11252719.
• Nielsen SJ, Schneider R, Bauer UM, Bannister AJ, Morrison A, O'Carroll D, Firestein R, Cleary M, Jenuwein T, Herrera RE, Kouzarides T (2001). "Rb targets histone H3 methylation and HP1 to promoters". Nature. 412 (6846): 561–5. Bibcode:2001Natur.412..561N. doi:10.1038/35087620. PMID   11484059. S2CID   4378296.
• Vandel L, Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D (2001). "Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase". Mol. Cell. Biol. 21 (19): 6484–94. doi:10.1128/MCB.21.19.6484-6494.2001. PMC   99795 . PMID   11533237.
• Vaute O, Nicolas E, Vandel L, Trouche D (2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–81. doi:10.1093/nar/30.2.475. PMC   99834 . PMID   11788710.
• Schotta G, Ebert A, Krauss V, Fischer A, Hoffmann J, Rea S, Jenuwein T, Dorn R, Reuter G (2002). "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation and heterochromatic gene silencing". EMBO J. 21 (5): 1121–31. doi:10.1093/emboj/21.5.1121. PMC   125909 . PMID   11867540.
• Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T, Melcher M, Schweizer D, Jenuwein T, Otte AP (2002). "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins". Mol. Cell. Biol. 22 (15): 5539–53. doi:10.1128/MCB.22.15.5539-5553.2002. PMC   133945 . PMID   12101246.
• Zhang CL, McKinsey TA, Olson EN (2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/MCB.22.20.7302-7312.2002. PMC   139799 . PMID   12242305.
• Yamamoto K, Sonoda M (2003). "Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1". Biochem. Biophys. Res. Commun. 301 (2): 287–92. doi:10.1016/S0006-291X(02)03021-8. PMID   12565857.