SUV39H1

Protein-coding gene in the species Homo sapiens
SUV39H1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3MTS

Identifiers
AliasesSUV39H1, H3-K9-HMTase 1, KMT1A, MG44, SUV39H, suppressor of variegation 3-9 homolog 1, SUV39H1 histone lysine methyltransferase
External IDsOMIM: 300254; MGI: 1099440; HomoloGene: 2388; GeneCards: SUV39H1; OMA:SUV39H1 - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for SUV39H1
Genomic location for SUV39H1
BandXp11.23Start48,695,554 bp[1]
End48,709,016 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for SUV39H1
Genomic location for SUV39H1
BandX A1.1|X 3.64 cMStart7,927,410 bp[2]
End7,940,999 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr X: 7.93 – 7.94 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101945 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b c 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.