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Identification
HMDB Protein ID HMDBP00424
Secondary Accession Numbers
  • 5661
Name Histone-lysine N-methyltransferase SUV39H2
Synonyms
  1. H3-K9-HMTase 2
  2. Histone H3-K9 methyltransferase 2
  3. Lysine N-methyltransferase 1B
  4. Su(var)3-9 homolog 2
  5. Suppressor of variegation 3-9 homolog 2
Gene Name SUV39H2
Protein Type Unknown
Biological Properties
General Function Involved in chromatin binding
Specific Function Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis.
Pathways
  • Lysine degradation
Reactions
S-Adenosylmethionine + L-lysine-[histone] → S-Adenosylhomocysteine + N(6)-methyl-L-lysine-[histone] details
Protein lysine + S-Adenosylmethionine → Protein N6-methyl-L-lysine + S-Adenosylhomocysteine details
S-Adenosylmethionine + Protein N6-methyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6-dimethyl-L-lysine details
S-Adenosylmethionine + Protein N6,N6-dimethyl-L-lysine → S-Adenosylhomocysteine + Protein N6,N6,N6-trimethyl-L-lysine details
GO Classification
Biological Process
chromatin remodeling
chromatin assembly or disassembly
male meiosis
cell differentiation
regulation of transcription, DNA-dependent
transcription, DNA-dependent
Cellular Component
chromosome, centromeric region
chromatin
nuclear heterochromatin
Component
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
organelle part
intracellular organelle part
chromosomal part
chromatin
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
transferase activity
protein methyltransferase activity
protein-lysine n-methyltransferase activity
histone-lysine n-methyltransferase activity
chromatin binding
transferase activity, transferring one-carbon groups
methyltransferase activity
Molecular Function
histone methyltransferase activity (H3-K9 specific)
zinc ion binding
chromatin binding
Process
cellular process
cellular component organization at cellular level
organelle organization
chromosome organization
chromatin organization
chromatin modification
chromatin assembly or disassembly
Cellular Location
  1. Nucleus
  2. Chromosome
  3. centromere
Gene Properties
Chromosome Location 10
Locus 10p13
SNPs SUV39H2
Gene Sequence
>1233 bp
ATGGCGGCGGTCGGGGCCGAGGCGCGAGGAGCTTGGTGTGTGCCTTGCCTAGTTTCACTT
GATACTCTTCAGGAATTATGTAGAAAAGAAAAGCTCACATGTAAATCGATTGGAATCACC
AAAAGGAATCTAAACAATTATGAGGTGGAATACTTGTGTGACTACAAGGTAGTAAAGGAT
ATGGAATATTATCTTGTAAAATGGAAAGGATGGCCAGATTCTACAAATACTTGGGAACCT
TTGCAAAATCTGAAGTGCCCGTTACTGCTTCAGCAATTCTCTAATGACAAGCATAATTAT
TTATCTCAGGTAAAGAAAGGCAAAGCAATAACTCCAAAAGACAATAACAAAACTTTGAAA
CCTGCCATTGCTGAGTACATTGTGAAGAAGGCTAAACAAAGGATAGCTCTGCAGAGATGG
CAAGATGAACTCAACAGAAGAAAGAATCATAAAGGAATGATATTTGTTGAAAATACTGTT
GATTTAGAGGGCCCACCTTCAGACTTCTATTACATTAACGAATACAAACCAGCTCCTGGA
ATCAGCTTAGTCAATGAAGCTACCTTTGGTTGTTCATGCACAGATTGCTTCTTTCAAAAA
TGTTGTCCTGCTGAAGCTGGAGTTCTTTTGGCTTATAATAAAAACCAACAAATTAAAATC
CCACCTGGTACTCCCATCTATGAATGCAACTCAAGGTGTCAGTGTGGTCCTGATTGTCCC
AATAGGATTGTACAAAAAGGCACACAGTATTCGCTTTGCATCTTTCGAACTAGCAATGGA
CGTGGCTGGGGTGTAAAGACCCTTGTGAAGATTAAAAGAATGAGTTTTGTCATGGAATAT
GTTGGAGAGGTAATCACAAGTGAAGAAGCTGAAAGACGAGGACAGTTCTATGACAACAAG
GGAATCACGTATCTCTTTGATCTGGACTATGAGTCTGATGAATTCACAGTGGATGCGGCT
CGATACGGCAATGTGTCTCATTTTGTGAATCACAGCTGTGACCCAAATCTTCAGGTGTTC
AATGTTTTCATTGATAACCTCGATACTCGTCTTCCCCGAATAGCATTGTTTTCCACAAGA
ACCATAAATGCTGGAGAAGAGCTGACTTTTGATTATCAAATGAAAGGTTCTGGAGATATA
TCTTCAGATTCTATTGACCACAGCCCAGCCAAAAAGAGGGTCAGAACAGTATGTAAATGT
GGAGCTGTGACTTGCAGAGGTTACCTCAACTGA
Protein Properties
Number of Residues 410
Molecular Weight 46682.015
Theoretical pI 8.198
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Histone-lysine N-methyltransferase SUV39H2
MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKD
MEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLK
PAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPG
ISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCP
NRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNK
GITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTR
TINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN
GenBank ID Protein 301171588
UniProtKB/Swiss-Prot ID Q9H5I1
UniProtKB/Swiss-Prot Entry Name SUV92_HUMAN
PDB IDs
GenBank Gene ID NM_001193424.1
GeneCard ID SUV39H2
GenAtlas ID SUV39H2
HGNC ID HGNC:17287
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
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  9. Frontelo P, Leader JE, Yoo N, Potocki AC, Crawford M, Kulik M, Lechleider RJ: Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression. Oncogene. 2004 Jul 1;23(30):5242-51. [PubMed:15107829 ]