Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Histone-lysine N-methyltransferase SETMAR (SET domain and mariner transposase fusion protein) (Metnase) [Includes: Histone-lysine N-methyltransferase (EC 2.1.1.43); Transposon Hsmar1 transposase (EC 3.1.-.-)]

 SETMR_HUMAN             Reviewed;         684 AA.
Q53H47; B4DY74; E7EN68; Q13579; Q1G668; Q96F41;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 2.
22-NOV-2017, entry version 120.
RecName: Full=Histone-lysine N-methyltransferase SETMAR {ECO:0000305};
AltName: Full=SET domain and mariner transposase fusion protein {ECO:0000305};
Short=Metnase {ECO:0000303|PubMed:16332963};
Includes:
RecName: Full=Histone-lysine N-methyltransferase {ECO:0000305};
EC=2.1.1.43 {ECO:0000269|PubMed:16332963};
Includes:
RecName: Full=Transposon Hsmar1 transposase {ECO:0000303|PubMed:9461395};
EC=3.1.-.- {ECO:0000269|PubMed:16332963};
Name=SETMAR {ECO:0000312|HGNC:HGNC:10762};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-684 (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-684 (ISOFORM 1), FUNCTION, CATALYTIC
ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASN-223; ASP-261 AND
ASP-503.
PubMed=16332963; DOI=10.1073/pnas.0503676102;
Lee S.-H., Oshige M., Durant S.T., Rasila K.K., Williamson E.A.,
Ramsey H., Kwan L., Nickoloff J.A., 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. 102:18075-18080(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-684, FUNCTION, AND
DNA-BINDING.
PubMed=16672366; DOI=10.1073/pnas.0601161103;
Cordaux R., Udit S., Batzer M.A., 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. 103:8101-8106(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-684.
PubMed=9461395; DOI=10.1016/S0378-1119(97)00472-1;
Robertson H.M., Zumpano K.L.;
"Molecular evolution of an ancient mariner transposon, Hsmar1, in the
human genome.";
Gene 205:203-217(1997).
[7]
FUNCTION, DNA CLEAVAGE ACTIVITY, AND MUTAGENESIS OF ARG-445 AND
ASP-496.
PubMed=17877369; DOI=10.1021/bi7005477;
Roman Y., Oshige M., Lee Y.J., Goodwin K., Georgiadis M.M.,
Hromas R.A., Lee S.H.;
"Biochemical characterization of a SET and transposase fusion protein,
Metnase: its DNA binding and DNA cleavage activity.";
Biochemistry 46:11369-11376(2007).
[8]
FUNCTION, LACK OF TRANSPOSASE ACTIVITY, AND DOMAIN.
PubMed=17403897; DOI=10.1128/MCB.02027-06;
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. 27:4589-4600(2007).
[9]
FUNCTION, INTERACTION WITH PRPF19, AND SUBCELLULAR LOCATION.
PubMed=18263876; DOI=10.1074/jbc.M800150200;
Beck B.D., Park S.J., Lee Y.J., Roman Y., Hromas R.A., Lee S.H.;
"Human Pso4 is a metnase (SETMAR)-binding partner that regulates
metnase function in DNA repair.";
J. Biol. Chem. 283:9023-9030(2008).
[10]
FUNCTION, INTERACTION WITH TOP2A, METHYLATION AT LYS-498, AND
SUBCELLULAR LOCATION.
PubMed=18790802; DOI=10.1093/nar/gkn560;
Williamson E.A., Rasila K.K., Corwin L.K., Wray J., Beck B.D.,
Severns V., Mobarak C., Lee S.H., Nickoloff J.A., Hromas R.;
"The SET and transposase domain protein Metnase enhances chromosome
decatenation: regulation by automethylation.";
Nucleic Acids Res. 36:5822-5831(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
FUNCTION, AND INTERACTION WITH PCNA; RAD9A; RAD9B AND TOP2A.
PubMed=20457750; DOI=10.1093/nar/gkq339;
De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L.,
Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.;
"Metnase promotes restart and repair of stalled and collapsed
replication forks.";
Nucleic Acids Res. 38:5681-5691(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
FUNCTION.
PubMed=21187428; DOI=10.1073/pnas.1013571108;
Fnu S., Williamson E.A., De Haro L.P., Brenneman M., Wray J.,
Shaheen M., Radhakrishnan K., Lee S.H., Nickoloff J.A., Hromas R.;
"Methylation of histone H3 lysine 36 enhances DNA repair by
nonhomologous end-joining.";
Proc. Natl. Acad. Sci. U.S.A. 108:540-545(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
FUNCTION, PHOSPHORYLATION AT SER-508 BY CHEK1, DEPHOSPHORYLATION BY
PP2A, MUTAGENESIS OF SER-508, AND SUBCELLULAR LOCATION.
PubMed=22231448; DOI=10.1038/onc.2011.586;
Hromas R., Williamson E.A., Fnu S., Lee Y.J., Park S.J., Beck B.D.,
You J.S., Leitao A., Laitao A., Nickoloff J.A., Lee S.H.;
"Chk1 phosphorylation of Metnase enhances DNA repair but inhibits
replication fork restart.";
Oncogene 31:4245-4254(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
FUNCTION, AND MUTAGENESIS OF ASN-623.
PubMed=24573677; DOI=10.1074/jbc.M113.533216;
Kim H.S., Chen Q., Kim S.K., Nickoloff J.A., Hromas R.,
Georgiadis M.M., Lee S.H.;
"The DDN catalytic motif is required for Metnase functions in non-
homologous end joining (NHEJ) repair and replication restart.";
J. Biol. Chem. 289:10930-10938(2014).
[20]
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 15-303, AND X-RAY
CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 459-684 IN COMPLEXES WITH
S-ADENOSYL-L-HOMOCYSTEINE; ZINC AND MAGNESIUM IONS.
Structural genomics consortium (SGC);
"The crystal structure of transposase domain of human histone-lysine
N-methyltransferase SETMAR.";
Submitted (AUG-2009) to the PDB data bank.
[21]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 446-684, FUNCTION, SUBUNIT,
AND MUTAGENESIS OF PHE-473.
PubMed=20521842; DOI=10.1021/bi100171x;
Goodwin K.D., He H., Imasaki T., Lee S.H., Georgiadis M.M.;
"Crystal structure of the human Hsmar1-derived transposase domain in
the DNA repair enzyme Metnase.";
Biochemistry 49:5705-5713(2010).
-!- FUNCTION: Protein derived from the fusion of a methylase with the
transposase of an Hsmar1 transposon that plays a role in DNA
double-strand break repair, stalled replication fork restart and
DNA integration. DNA-binding protein, it is indirectly recruited
to sites of DNA damage through protein-protein interactions. Has
also kept a sequence-specific DNA-binding activity recognizing the
19-mer core of the 5'-terminal inverted repeats (TIRs) of the
Hsmar1 element and displays a DNA nicking and end joining activity
(PubMed:16332963, PubMed:16672366, PubMed:17877369,
PubMed:17403897, PubMed:18263876, PubMed:22231448,
PubMed:24573677, PubMed:20521842). In parallel, has a histone
methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of
histone H3. Specifically mediates dimethylation of H3 'Lys-36' at
sites of DNA double-strand break and may recruit proteins required
for efficient DSB repair through non-homologous end-joining
(PubMed:16332963, PubMed:21187428, PubMed:22231448). Also
regulates replication fork processing, promoting replication fork
restart and regulating DNA decatenation through stimulation of the
topoisomerase activity of TOP2A (PubMed:18790802,
PubMed:20457750). {ECO:0000269|PubMed:16332963,
ECO:0000269|PubMed:16672366, ECO:0000269|PubMed:17403897,
ECO:0000269|PubMed:17877369, ECO:0000269|PubMed:18790802,
ECO:0000269|PubMed:20457750, ECO:0000269|PubMed:20521842,
ECO:0000269|PubMed:21187428, ECO:0000269|PubMed:22231448,
ECO:0000269|PubMed:24573677, ECO:0000303|PubMed:18263876}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:16332963}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per subunit.;
-!- SUBUNIT: Homodimer (PubMed:20521842). Interacts with PRPF19;
required for SETMAR recruitment to damaged DNA sites
(PubMed:18263876). Interacts with PCNA (PubMed:20457750).
Interacts with TOP2A; stimulates TOP2A topoisomerase activity
(PubMed:18790802, PubMed:20457750). May interact with RAD9A and/or
RAD9B (PubMed:20457750). {ECO:0000269|PubMed:18263876,
ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:20457750,
ECO:0000269|PubMed:20521842}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18263876}.
Chromosome {ECO:0000269|PubMed:18790802,
ECO:0000269|PubMed:22231448}. Note=Recruited on damaged DNA at
sites of double-strand breaks. {ECO:0000269|PubMed:18263876}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q53H47-1; Sequence=Displayed;
Name=2;
IsoId=Q53H47-2; Sequence=VSP_021440, VSP_021441;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q53H47-3; Sequence=VSP_054089;
-!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
placenta and ovary and lowest expression in skeletal muscle.
{ECO:0000269|PubMed:16332963}.
-!- DOMAIN: The mariner transposase Hsmar1 region mediates DNA-
binding. It has retained some of the nucleases activity but has
lost its transposase activity because the active site contains an
Asn in position 610 instead of an Asp residue.
{ECO:0000269|PubMed:17403897}.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
-!- PTM: Methylated. Methylation regulates activity in DNA
decatenation. {ECO:0000269|PubMed:18790802}.
-!- PTM: Phosphorylated at Ser-508 by CHEK1 and dephosphorylated by
protein phosphatase 2A/PP2A. Phosphorylation at Ser-508 is
enhanced by DNA damage and promotes recruitment to damaged DNA. It
stimulates DNA repair and impairs replication fork restart.
{ECO:0000269|PubMed:22231448}.
-!- MISCELLANEOUS: The mariner transposase region in only present in
primates and appeared 40-58 million years ago, after the insertion
of a transposon downstream of a preexisting SET gene, followed by
the de novo exonization of previously non-coding sequence and the
creation of a new intron.
-!- SIMILARITY: In the N-terminal section; belongs to the class V-like
SAM-binding methyltransferase superfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the mariner
transposase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH11635.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAY29570.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD96454.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Taming genes - Issue
167 of February 2015;
URL="https://web.expasy.org/spotlight/back_issues/167/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK222734; BAD96454.1; ALT_INIT; mRNA.
EMBL; AK302296; BAG63636.1; -; mRNA.
EMBL; AC023483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC034191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011635; AAH11635.1; ALT_INIT; mRNA.
EMBL; AY952295; AAY29570.1; ALT_INIT; mRNA.
EMBL; DQ341316; ABC72087.1; -; Genomic_DNA.
EMBL; U52077; AAC52010.1; -; Genomic_DNA.
CCDS; CCDS2563.2; -. [Q53H47-1]
CCDS; CCDS58814.1; -. [Q53H47-3]
CCDS; CCDS63528.1; -. [Q53H47-2]
RefSeq; NP_001230652.1; NM_001243723.1. [Q53H47-3]
RefSeq; NP_001263254.1; NM_001276325.1. [Q53H47-2]
RefSeq; NP_001307606.1; NM_001320677.1.
RefSeq; NP_001307607.1; NM_001320678.1.
RefSeq; NP_006506.3; NM_006515.3. [Q53H47-1]
UniGene; Hs.475300; -.
PDB; 3BO5; X-ray; 1.59 A; A=15-303.
PDB; 3F2K; X-ray; 1.85 A; A/B=459-684.
PDB; 3K9J; X-ray; 1.90 A; A/B=446-684.
PDB; 3K9K; X-ray; 2.55 A; A/B=446-684.
PDBsum; 3BO5; -.
PDBsum; 3F2K; -.
PDBsum; 3K9J; -.
PDBsum; 3K9K; -.
ProteinModelPortal; Q53H47; -.
SMR; Q53H47; -.
BioGrid; 112317; 18.
IntAct; Q53H47; 3.
MINT; MINT-4826518; -.
STRING; 9606.ENSP00000373354; -.
BindingDB; Q53H47; -.
ChEMBL; CHEMBL2189111; -.
iPTMnet; Q53H47; -.
PhosphoSitePlus; Q53H47; -.
DMDM; 74740552; -.
EPD; Q53H47; -.
MaxQB; Q53H47; -.
PaxDb; Q53H47; -.
PeptideAtlas; Q53H47; -.
PRIDE; Q53H47; -.
Ensembl; ENST00000358065; ENSP00000373354; ENSG00000170364. [Q53H47-1]
Ensembl; ENST00000425863; ENSP00000403145; ENSG00000170364. [Q53H47-3]
Ensembl; ENST00000430981; ENSP00000403000; ENSG00000170364. [Q53H47-2]
GeneID; 6419; -.
KEGG; hsa:6419; -.
UCSC; uc003bpw.6; human. [Q53H47-1]
CTD; 6419; -.
DisGeNET; 6419; -.
EuPathDB; HostDB:ENSG00000170364.12; -.
GeneCards; SETMAR; -.
HGNC; HGNC:10762; SETMAR.
HPA; HPA057999; -.
MIM; 609834; gene.
neXtProt; NX_Q53H47; -.
OpenTargets; ENSG00000170364; -.
PharmGKB; PA35680; -.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00440000033232; -.
HOGENOM; HOG000154295; -.
HOVERGEN; HBG093941; -.
InParanoid; Q53H47; -.
KO; K11433; -.
OMA; ENQKNRR; -.
OrthoDB; EOG091G0Y4N; -.
PhylomeDB; Q53H47; -.
TreeFam; TF352220; -.
EvolutionaryTrace; Q53H47; -.
GeneWiki; SETMAR; -.
GenomeRNAi; 6419; -.
PRO; PR:Q53H47; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000170364; -.
CleanEx; HS_SETMAR; -.
ExpressionAtlas; Q53H47; baseline and differential.
Genevisible; Q53H47; HS.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0044547; F:DNA topoisomerase binding; IPI:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IMP:UniProtKB.
GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IMP:UniProtKB.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IMP:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:UniProtKB.
GO; GO:0000729; P:DNA double-strand break processing; IDA:UniProtKB.
GO; GO:0015074; P:DNA integration; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:0097676; P:histone H3-K36 dimethylation; IMP:UniProtKB.
GO; GO:0010452; P:histone H3-K36 methylation; IDA:UniProtKB.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
GO; GO:0044774; P:mitotic DNA integrity checkpoint; IMP:UniProtKB.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IMP:UniProtKB.
GO; GO:2001251; P:negative regulation of chromosome organization; IDA:UniProtKB.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IMP:UniProtKB.
GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IDA:UniProtKB.
GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR001214; SET_dom.
InterPro; IPR001888; Transposase_1.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
Pfam; PF01359; Transposase_1; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
Complete proteome; DNA damage; DNA repair; DNA-binding; Endonuclease;
Hydrolase; Magnesium; Metal-binding; Methylation; Methyltransferase;
Multifunctional enzyme; Nuclease; Nucleus; Phosphoprotein;
Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
CHAIN 1 684 Histone-lysine N-methyltransferase
SETMAR.
/FTId=PRO_0000259526.
DOMAIN 73 136 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 139 263 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 283 299 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DNA_BIND 364 395 H-T-H motif. {ECO:0000250}.
DNA_BIND 428 448 H-T-H motif.
REGION 1 345 Histone-lysine N-methyltransferase.
REGION 149 151 S-adenosyl-L-methionine binding.
REGION 223 224 S-adenosyl-L-methionine binding.
REGION 346 684 Mariner transposase Hsmar1.
METAL 75 75 Zinc 1.
METAL 75 75 Zinc 2.
METAL 77 77 Zinc 1.
METAL 82 82 Zinc 1.
METAL 82 82 Zinc 3.
METAL 87 87 Zinc 1.
METAL 89 89 Zinc 2.
METAL 118 118 Zinc 2.
METAL 118 118 Zinc 3.
METAL 122 122 Zinc 2.
METAL 124 124 Zinc 3.
METAL 128 128 Zinc 3.
METAL 226 226 Zinc 4.
METAL 287 287 Zinc 4.
METAL 289 289 Zinc 4.
METAL 294 294 Zinc 4.
METAL 496 496 Magnesium.
METAL 588 588 Magnesium.
BINDING 192 192 S-adenosyl-L-methionine.
BINDING 220 220 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 498 498 N6-methyllysine.
{ECO:0000269|PubMed:18790802}.
MOD_RES 508 508 Phosphoserine; by CHEK1.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22231448}.
VAR_SEQ 163 301 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_054089.
VAR_SEQ 341 365 TMKMMLDKKQIRAIFLFEFKMGRKA -> VSLFSDKQLAPP
YSGRQWLASFTSA (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_021440.
VAR_SEQ 366 684 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_021441.
MUTAGEN 223 223 N->S: Reduces activity in double-strand
break repair.
{ECO:0000269|PubMed:16332963}.
MUTAGEN 261 261 D->S: Reduces activity in double-strand
break repair.
{ECO:0000269|PubMed:16332963}.
MUTAGEN 445 445 R->A: Abolishes TIR-specific DNA-binding.
{ECO:0000269|PubMed:17877369}.
MUTAGEN 473 473 F->K: Abolishes homodimerization and DNA-
binding and reduces cleavage of single-
stranded DNA.
{ECO:0000269|PubMed:20521842}.
MUTAGEN 496 496 D->A: Abolishes DNA cleavage.
{ECO:0000269|PubMed:17877369}.
MUTAGEN 503 503 D->S: Reduces activity in double-strand
break repair.
{ECO:0000269|PubMed:16332963}.
MUTAGEN 508 508 S->A: Prevents phosphorylation. Impairs
recruitment to damaged DNA and double-
strand break repair. Impairs interaction
with histone H3 and its methylation.
Allows replication fork restart.
{ECO:0000269|PubMed:22231448}.
MUTAGEN 623 623 N->D,E: Loss of function in DNA repair.
Altered DNA-binding properties.
{ECO:0000269|PubMed:24573677}.
CONFLICT 91 91 R -> H (in Ref. 1; BAG63636).
{ECO:0000305}.
CONFLICT 343 343 K -> E (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 439 439 N -> D (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 465 465 T -> S (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 484 484 H -> N (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 508 508 S -> P (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 514 514 Q -> R (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 525 525 I -> N (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 528 528 P -> Q (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 535 535 I -> V (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 562 562 E -> Q (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 567 568 NQ -> HR (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 575 575 L -> P (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 620 620 L -> S (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 623 623 N -> D (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 626 626 V -> F (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 631 631 N -> D (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 656 656 Q -> R (in Ref. 6; AAC52010).
{ECO:0000305}.
CONFLICT 667 667 Q -> K (in Ref. 6; AAC52010).
{ECO:0000305}.
TURN 30 33 {ECO:0000244|PDB:3BO5}.
STRAND 35 37 {ECO:0000244|PDB:3BO5}.
STRAND 40 43 {ECO:0000244|PDB:3BO5}.
TURN 84 86 {ECO:0000244|PDB:3BO5}.
HELIX 88 90 {ECO:0000244|PDB:3BO5}.
HELIX 133 135 {ECO:0000244|PDB:3BO5}.
STRAND 141 145 {ECO:0000244|PDB:3BO5}.
STRAND 147 157 {ECO:0000244|PDB:3BO5}.
STRAND 164 167 {ECO:0000244|PDB:3BO5}.
STRAND 170 173 {ECO:0000244|PDB:3BO5}.
HELIX 175 182 {ECO:0000244|PDB:3BO5}.
STRAND 194 198 {ECO:0000244|PDB:3BO5}.
STRAND 206 216 {ECO:0000244|PDB:3BO5}.
HELIX 218 221 {ECO:0000244|PDB:3BO5}.
STRAND 229 241 {ECO:0000244|PDB:3BO5}.
STRAND 243 250 {ECO:0000244|PDB:3BO5}.
STRAND 257 260 {ECO:0000244|PDB:3BO5}.
STRAND 270 279 {ECO:0000244|PDB:3BO5}.
HELIX 466 485 {ECO:0000244|PDB:3F2K}.
HELIX 489 491 {ECO:0000244|PDB:3F2K}.
STRAND 492 503 {ECO:0000244|PDB:3F2K}.
STRAND 530 538 {ECO:0000244|PDB:3F2K}.
STRAND 541 547 {ECO:0000244|PDB:3F2K}.
HELIX 556 573 {ECO:0000244|PDB:3F2K}.
HELIX 574 576 {ECO:0000244|PDB:3K9J}.
STRAND 584 586 {ECO:0000244|PDB:3F2K}.
HELIX 591 594 {ECO:0000244|PDB:3F2K}.
HELIX 598 605 {ECO:0000244|PDB:3F2K}.
HELIX 617 619 {ECO:0000244|PDB:3F2K}.
HELIX 621 624 {ECO:0000244|PDB:3F2K}.
HELIX 626 634 {ECO:0000244|PDB:3F2K}.
HELIX 642 654 {ECO:0000244|PDB:3F2K}.
HELIX 660 666 {ECO:0000244|PDB:3F2K}.
HELIX 668 677 {ECO:0000244|PDB:3F2K}.
TURN 678 680 {ECO:0000244|PDB:3F2K}.
SEQUENCE 684 AA; 78034 MW; BB9460455C0BDBFA CRC64;
MFAEAAKTTR PCGMAEFKEK PEAPTEQLDV ACGQENLPVG AWPPGAAPAP FQYTPDHVVG
PGADIDPTQI TFPGCICVKT PCLPGTCSCL RHGENYDDNS CLRDIGSGGK YAEPVFECNV
LCRCSDHCRN RVVQKGLQFH FQVFKTHKKG WGLRTLEFIP KGRFVCEYAG EVLGFSEVQR
RIHLQTKSDS NYIIAIREHV YNGQVMETFV DPTYIGNIGR FLNHSCEPNL LMIPVRIDSM
VPKLALFAAK DIVPEEELSY DYSGRYLNLT VSEDKERLDH GKLRKPCYCG AKSCTAFLPF
DSSLYCPVEK SNISCGNEKE PSMCGSAPSV FPSCKRLTLE TMKMMLDKKQ IRAIFLFEFK
MGRKAAETTR NINNAFGPGT ANERTVQWWF KKFCKGDESL EDEERSGRPS EVDNDQLRAI
IEADPLTTTR EVAEELNVNH STVVRHLKQI GKVKKLDKWV PHELTENQKN RRFEVSSSLI
LRNHNEPFLD RIVTCDEKWI LYDNRRRSAQ WLDQEEAPKH FPKPILHPKK VMVTIWWSAA
GLIHYSFLNP GETITSEKYA QEIDEMNQKL QRLQLALVNR KGPILLHDNA RPHVAQPTLQ
KLNELGYEVL PHPPYSPDLL PTNYHVFKHL NNFLQGKRFH NQQDAENAFQ EFVESQSTDF
YATGINQLIS RWQKCVDCNG SYFD


Related products :

Catalog number Product name Quantity
EIAAB37982 Histone-lysine N-methyltransferase SETMAR,Homo sapiens,HsMar1,Human,Metnase,SET domain and mariner transposase fusion gene-containing protein,SETMAR
EIAAB37981 Histone-lysine N-methyltransferase SETMAR,Rat,Rattus norvegicus,SET domain and mariner transposase fusion gene-containing protein homolog,Setmar
EIAAB37980 Bos taurus,Bovine,Histone-lysine N-methyltransferase SETMAR,SET domain and mariner transposase fusion gene-containing protein homolog,SETMAR
EIAAB37983 Histone-lysine N-methyltransferase SETMAR,Mouse,Mus musculus,SET domain and mariner transposase fusion gene-containing protein homolog,Setmar
EIAAB37955 ERG-associated protein with SET domain,ESET,H3-K9-HMTase 4,Histone H3-K9 methyltransferase 4,Histone-lysine N-methyltransferase SETDB1,Homo sapiens,Human,KIAA0067,KMT1E,Lysine N-methyltransferase 1E,S
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
EIAAB11717 DOT1L,DOT1-like protein,H3-K79-HMTase,Histone H3-K79 methyltransferase,Histone-lysine N-methyltransferase, H3 lysine-79 specific,Homo sapiens,Human,KIAA1814,KMT4,Lysine N-methyltransferase 4
EIAAB12652 Ehmt1,Euchromatic histone-lysine N-methyltransferase 1,Euhmtase1,Eu-HMTase1,G9a-like protein 1,GLP,Glp,GLP1,Histone-lysine N-methyltransferase EHMT1,Kmt1d,Lysine N-methyltransferase 1D,Mouse,Mus muscu
EIAAB37975 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Homo sapiens,Human,KIAA1717,KMT7,Lysine N-methyltransferase 7,SET domain-containing protein 7,SET7,SET
EIAAB37977 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Homo sapiens,Human,KMT5A,Lysine N-methyltransferase 5A,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PRSET7
EIAAB12653 EHMT1,Euchromatic histone-lysine N-methyltransferase 1,EUHMTASE1,Eu-HMTase1,G9a-like protein 1,GLP,GLP,GLP1,H3-K9-HMTase 5,Histone H3-K9 methyltransferase 5,Histone-lysine N-methyltransferase EHMT1,Ho
EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
EIAAB12654 Bat8,Ehmt2,Euchromatic histone-lysine N-methyltransferase 2,G9a,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Mouse,Mus muscul
EIAAB12655 BAT8,C6orf30,EHMT2,Euchromatic histone-lysine N-methyltransferase 2,G9A,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Homo sap
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB37958 C13orf4,Chronic lymphocytic leukemia deletion region gene 8 protein,CLLD8,Histone-lysine N-methyltransferase SETDB2,Homo sapiens,Human,KMT1F,Lysine N-methyltransferase 1F,SET domain bifurcated 2,SETDB
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
CSB-EL021112RA Rat SET domain and mariner transposase fusion gene (SETMAR) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
SETMAR SETMAR Gene SET domain and mariner transposase fusion gene
CSB-EL021112HU Human Histone-lysine N-methyltransferase SETMAR(SETMAR) ELISA kit SpeciesHuman 96T
CSB-EL021112MO Mouse Histone-lysine N-methyltransferase SETMAR(SETMAR) ELISA kit SpeciesMouse 96T
CSB-EL021112BO Bovine Histone-lysine N-methyltransferase SETMAR(SETMAR) ELISA kit SpeciesBovine 96T
CSB-EL021112HU Human Histone-lysine N-methyltransferase SETMAR(SETMAR) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur