Hmdb loader
Identification
HMDB Protein ID HMDBP09036
Secondary Accession Numbers
  • 14778
Name Histone-lysine N-methyltransferase SETMAR
Synonyms
  1. Histone-lysine N-methyltransferase
  2. HsMar1
  3. Mariner transposase Hsmar1
  4. Metnase
  5. SET domain and mariner transposase fusion gene-containing protein
Gene Name SETMAR
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 'Lys-36'. Has sequence-specific DNA-binding activity and recognizes the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element. Has DNA nicking activity. Has in vivo end joining activity and may mediate genomic integration of foreign DNA.
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
DNA double-strand break processing
DNA integration
DNA catabolic process, endonucleolytic
negative regulation of chromosome organization
positive regulation of double-strand break repair via nonhomologous end joining
transposition, DNA-mediated
negative regulation of cell cycle arrest
Cellular Component
chromosome
nucleus
Component
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
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
nucleic acid binding
dna binding
transposase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
Molecular Function
histone-lysine N-methyltransferase activity
metal ion binding
endonuclease activity
zinc ion binding
structure-specific DNA binding
transposase activity
Process
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
dna metabolic process
dna recombination
cellular process
cellular component organization at cellular level
organelle organization
chromosome organization
chromatin organization
chromatin modification
dna integration
transposition, dna-mediated
Cellular Location
  1. Nucleus (Probable)
  2. Chromosome (Probable)
Gene Properties
Chromosome Location 3
Locus 3p26.1
SNPs SETMAR
Gene Sequence
>2016 bp
ATGGCGGAGTTTAAGGAGAAGCCTGAGGCCCCGACTGAGCAGCTGGATGTCGCGTGCGGC
CAGGAAAACTTGCCGGTGGGCGCGTGGCCCCCGGGGGCCGCGCCGGCGCCCTTCCAGTAC
ACTCCTGATCATGTAGTTGGACCTGGAGCAGACATTGATCCCACTCAAATAACCTTTCCC
GGATGCATTTGTGTCAAAACTCCCTGCCTCCCTGGCACTTGCTCCTGTCTCCGCCATGGA
GAGAACTATGATGATAACTCATGCCTTAGAGATATAGGATCTGGAGGAAAGTATGCAGAG
CCTGTTTTTGAATGCAATGTCCTGTGCCGATGCAGTGACCACTGCAGAAACAGAGTGGTC
CAGAAAGGTCTACAGTTCCACTTCCAAGTGTTCAAGACGCATAAAAAAGGCTGGGGACTT
CGTACCTTGGAATTTATACCGAAAGGAAGGTTTGTCTGTGAATATGCTGGTGAGGTTTTA
GGATTCTCTGAAGTTCAGAGAAGAATTCACTTACAAACAAAATCCGACTCCAATTACATT
ATAGCCATCAGGGAACATGTTTATAATGGGCAGGTAATGGAAACATTTGTTGACCCTACT
TATATAGGAAATATTGGAAGATTCCTTAATCATTCTTGTGAGCCAAACCTTTTGATGATT
CCTGTCCGAATTGACTCAATGGTACCTAAGTTGGCACTTTTTGCAGCCAAAGATATTGTG
CCAGAAGAAGAACTCTCTTATGATTATTCAGGAAGATATCTTAATCTAACAGTCAGTGAA
GACAAAGAAAGGCTAGATCATGGGAAACTAAGGAAACCTTGTTACTGTGGTGCCAAATCA
TGTACTGCTTTCCTGCCTTTTGACAGTTCTCTGTACTGCCCCGTAGAAAAGTCGAACATC
AGTTGTGGAAATGAGAAGGAACCCAGCATGTGTGGCTCAGCCCCTTCTGTGTTCCCCTCC
TGCAAGCGATTGACCCTTGAGACTATGAAAATGATGTTAGACAAAAAGCAAATTCGAGCA
ATTTTCTTATTCGAGTTCAAAATGGGTCGTAAAGCAGCAGAAACAACTCGCAACATCAAC
AATGCATTTGGCCCAGGAACTGCTAACGAACGTACAGTGCAGTGGTGGTTCAAGAAGTTT
TGCAAAGGAGATGAGAGCCTTGAAGATGAGGAGCGTAGTGGCCGGCCATCAGAAGTTGAC
AACGACCAGTTGAGAGCAATCATCGAAGCTGATCCCCTTACAACTACACGAGAAGTTGCT
GAAGAACTCAATGTCAACCATTCTACGGTCGTTCGACATTTGAAGCAAATTGGAAAGGTG
AAAAAGCTCGATAAGTGGGTGCCTCATGAGCTGACTGAAAATCAAAAAAATCGTCGTTTT
GAAGTGTCATCTTCTCTTATTCTACGCAACCACAACGAACCATTTCTCGATCGGATTGTG
ACGTGTGATGAAAAGTGGATTTTATATGACAACCGGCGACGATCAGCTCAGTGGTTGGAT
CAAGAAGAAGCTCCAAAGCACTTCCCAAAGCCAATCTTGCACCCAAAAAAGGTCATGGTC
ACTATTTGGTGGTCTGCTGCTGGTCTGATCCACTACAGCTTTCTGAATCCCGGTGAAACC
ATTACATCTGAGAAGTATGCTCAGGAAATCGATGAGATGAACCAAAAACTGCAACGCCTG
CAGCTGGCATTGGTCAACAGAAAGGGCCCAATTCTTCTCCACGACAATGCCCGACCGCAT
GTTGCACAACCCACACTTCAAAAGTTGAATGAATTGGGCTATGAAGTTTTGCCTCATCCA
CCGTATTCACCTGACCTCTTGCCAACCAACTACCACGTCTTTAAGCATCTCAACAACTTT
TTGCAGGGAAAACGCTTCCACAACCAGCAGGATGCAGAAAATGCTTTCCAAGAGTTCGTC
GAATCCCAAAGCACGGATTTTTACGCTACAGGAATAAACCAACTTATTTCTCGTTGGCAA
AAATGTGTTGATTGTAATGGTTCCTATTTTGATTAA
Protein Properties
Number of Residues 671
Molecular Weight 62123.24
Theoretical pI 7.435
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Histone-lysine N-methyltransferase SETMAR
MAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFP
GCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVV
QKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYI
IAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIV
PEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNI
SCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNIN
NAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVA
EELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIV
TCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGET
ITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHP
PYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQ
KCVDCNGSYFD
GenBank ID Protein 62897027
UniProtKB/Swiss-Prot ID Q53H47
UniProtKB/Swiss-Prot Entry Name SETMR_HUMAN
PDB IDs
GenBank Gene ID AK222734
GeneCard ID SETMAR
GenAtlas ID SETMAR
HGNC ID HGNC:10762
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed:16641997 ]
  4. Lee SH, Oshige M, Durant ST, Rasila KK, Williamson EA, Ramsey H, Kwan L, Nickoloff JA, Hromas R: The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair. Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):18075-80. Epub 2005 Dec 6. [PubMed:16332963 ]
  5. Cordaux R, Udit S, Batzer MA, Feschotte C: Birth of a chimeric primate gene by capture of the transposase gene from a mobile element. Proc Natl Acad Sci U S A. 2006 May 23;103(21):8101-6. Epub 2006 May 3. [PubMed:16672366 ]
  6. Robertson HM, Zumpano KL: Molecular evolution of an ancient mariner transposon, Hsmar1, in the human genome. Gene. 1997 Dec 31;205(1-2):203-17. [PubMed:9461395 ]
  7. Roman Y, Oshige M, Lee YJ, Goodwin K, Georgiadis MM, Hromas RA, Lee SH: Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity. Biochemistry. 2007 Oct 9;46(40):11369-76. Epub 2007 Sep 18. [PubMed:17877369 ]
  8. Miskey C, Papp B, Mates L, Sinzelle L, Keller H, Izsvak Z, Ivics Z: The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends. Mol Cell Biol. 2007 Jun;27(12):4589-600. Epub 2007 Apr 2. [PubMed:17403897 ]