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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: SETMR_HUMAN B4DND2_HUMAN
LinkDB: SETMR_HUMAN B4DND2_HUMAN
Original site: SETMR_HUMAN B4DND2_HUMAN 
ID   SETMR_HUMAN             Reviewed;         684 AA.
AC   Q53H47; B4DY74; E7EN68; Q13579; Q1G668; Q96F41;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Histone-lysine N-methyltransferase SETMAR {ECO:0000305};
DE   AltName: Full=SET domain and mariner transposase fusion protein {ECO:0000305};
DE            Short=Metnase {ECO:0000303|PubMed:16332963};
DE   Includes:
DE     RecName: Full=Histone-lysine N-methyltransferase {ECO:0000305};
DE              EC=2.1.1.357 {ECO:0000269|PubMed:16332963};
DE   Includes:
DE     RecName: Full=Transposon Hsmar1 transposase {ECO:0000303|PubMed:9461395};
DE              EC=3.1.-.- {ECO:0000269|PubMed:16332963};
GN   Name=SETMAR {ECO:0000312|HGNC:HGNC:10762};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-684 (ISOFORM 2).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-684 (ISOFORM 1), FUNCTION, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASN-223; ASP-261 AND
RP   ASP-503.
RX   PubMed=16332963; DOI=10.1073/pnas.0503676102;
RA   Lee S.-H., Oshige M., Durant S.T., Rasila K.K., Williamson E.A., Ramsey H.,
RA   Kwan L., Nickoloff J.A., Hromas R.;
RT   "The SET domain protein Metnase mediates foreign DNA integration and links
RT   integration to nonhomologous end-joining repair.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18075-18080(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-684, FUNCTION, AND DNA-BINDING.
RX   PubMed=16672366; DOI=10.1073/pnas.0601161103;
RA   Cordaux R., Udit S., Batzer M.A., Feschotte C.;
RT   "Birth of a chimeric primate gene by capture of the transposase gene from a
RT   mobile element.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8101-8106(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-684.
RX   PubMed=9461395; DOI=10.1016/s0378-1119(97)00472-1;
RA   Robertson H.M., Zumpano K.L.;
RT   "Molecular evolution of an ancient mariner transposon, Hsmar1, in the human
RT   genome.";
RL   Gene 205:203-217(1997).
RN   [7]
RP   FUNCTION, DNA CLEAVAGE ACTIVITY, AND MUTAGENESIS OF ARG-445 AND ASP-496.
RX   PubMed=17877369; DOI=10.1021/bi7005477;
RA   Roman Y., Oshige M., Lee Y.J., Goodwin K., Georgiadis M.M., Hromas R.A.,
RA   Lee S.H.;
RT   "Biochemical characterization of a SET and transposase fusion protein,
RT   Metnase: its DNA binding and DNA cleavage activity.";
RL   Biochemistry 46:11369-11376(2007).
RN   [8]
RP   FUNCTION, LACK OF TRANSPOSASE ACTIVITY, AND DOMAIN.
RX   PubMed=17403897; DOI=10.1128/mcb.02027-06;
RA   Miskey C., Papp B., Mates L., Sinzelle L., Keller H., Izsvak Z., Ivics Z.;
RT   "The ancient mariner sails again: transposition of the human Hsmar1 element
RT   by a reconstructed transposase and activities of the SETMAR protein on
RT   transposon ends.";
RL   Mol. Cell. Biol. 27:4589-4600(2007).
RN   [9]
RP   FUNCTION, INTERACTION WITH PRPF19, AND SUBCELLULAR LOCATION.
RX   PubMed=18263876; DOI=10.1074/jbc.m800150200;
RA   Beck B.D., Park S.J., Lee Y.J., Roman Y., Hromas R.A., Lee S.H.;
RT   "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase
RT   function in DNA repair.";
RL   J. Biol. Chem. 283:9023-9030(2008).
RN   [10]
RP   FUNCTION, INTERACTION WITH TOP2A, METHYLATION AT LYS-498, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=18790802; DOI=10.1093/nar/gkn560;
RA   Williamson E.A., Rasila K.K., Corwin L.K., Wray J., Beck B.D., Severns V.,
RA   Mobarak C., Lee S.H., Nickoloff J.A., Hromas R.;
RT   "The SET and transposase domain protein Metnase enhances chromosome
RT   decatenation: regulation by automethylation.";
RL   Nucleic Acids Res. 36:5822-5831(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH PCNA; RAD9A; RAD9B AND TOP2A.
RX   PubMed=20457750; DOI=10.1093/nar/gkq339;
RA   De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L.,
RA   Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.;
RT   "Metnase promotes restart and repair of stalled and collapsed replication
RT   forks.";
RL   Nucleic Acids Res. 38:5681-5691(2010).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
RP   FUNCTION.
RX   PubMed=21187428; DOI=10.1073/pnas.1013571108;
RA   Fnu S., Williamson E.A., De Haro L.P., Brenneman M., Wray J., Shaheen M.,
RA   Radhakrishnan K., Lee S.H., Nickoloff J.A., Hromas R.;
RT   "Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous
RT   end-joining.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:540-545(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [17]
RP   FUNCTION, PHOSPHORYLATION AT SER-508 BY CHEK1, DEPHOSPHORYLATION BY PP2A,
RP   MUTAGENESIS OF SER-508, AND SUBCELLULAR LOCATION.
RX   PubMed=22231448; DOI=10.1038/onc.2011.586;
RA   Hromas R., Williamson E.A., Fnu S., Lee Y.J., Park S.J., Beck B.D.,
RA   You J.S., Leitao A., Laitao A., Nickoloff J.A., Lee S.H.;
RT   "Chk1 phosphorylation of Metnase enhances DNA repair but inhibits
RT   replication fork restart.";
RL   Oncogene 31:4245-4254(2012).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [19]
RP   FUNCTION, AND MUTAGENESIS OF ASN-623.
RX   PubMed=24573677; DOI=10.1074/jbc.m113.533216;
RA   Kim H.S., Chen Q., Kim S.K., Nickoloff J.A., Hromas R., Georgiadis M.M.,
RA   Lee S.H.;
RT   "The DDN catalytic motif is required for Metnase functions in non-
RT   homologous end joining (NHEJ) repair and replication restart.";
RL   J. Biol. Chem. 289:10930-10938(2014).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 15-303, AND X-RAY CRYSTALLOGRAPHY
RP   (1.59 ANGSTROMS) OF 459-684 IN COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE;
RP   ZINC AND MAGNESIUM IONS.
RG   Structural genomics consortium (SGC);
RT   "The crystal structure of transposase domain of human histone-lysine N-
RT   methyltransferase SETMAR.";
RL   Submitted (AUG-2009) to the PDB data bank.
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 446-684, FUNCTION, SUBUNIT, AND
RP   MUTAGENESIS OF PHE-473.
RX   PubMed=20521842; DOI=10.1021/bi100171x;
RA   Goodwin K.D., He H., Imasaki T., Lee S.H., Georgiadis M.M.;
RT   "Crystal structure of the human Hsmar1-derived transposase domain in the
RT   DNA repair enzyme Metnase.";
RL   Biochemistry 49:5705-5713(2010).
CC   -!- FUNCTION: Protein derived from the fusion of a methylase with the
CC       transposase of an Hsmar1 transposon that plays a role in DNA double-
CC       strand break repair, stalled replication fork restart and DNA
CC       integration. DNA-binding protein, it is indirectly recruited to sites
CC       of DNA damage through protein-protein interactions. Has also kept a
CC       sequence-specific DNA-binding activity recognizing the 19-mer core of
CC       the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and
CC       displays a DNA nicking and end joining activity (PubMed:16332963,
CC       PubMed:16672366, PubMed:17877369, PubMed:17403897, PubMed:18263876,
CC       PubMed:22231448, PubMed:24573677, PubMed:20521842). In parallel, has a
CC       histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36'
CC       of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at
CC       sites of DNA double-strand break and may recruit proteins required for
CC       efficient DSB repair through non-homologous end-joining
CC       (PubMed:16332963, PubMed:21187428, PubMed:22231448). Also regulates
CC       replication fork processing, promoting replication fork restart and
CC       regulating DNA decatenation through stimulation of the topoisomerase
CC       activity of TOP2A (PubMed:18790802, PubMed:20457750).
CC       {ECO:0000269|PubMed:16332963, ECO:0000269|PubMed:16672366,
CC       ECO:0000269|PubMed:17403897, ECO:0000269|PubMed:17877369,
CC       ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:20457750,
CC       ECO:0000269|PubMed:20521842, ECO:0000269|PubMed:21187428,
CC       ECO:0000269|PubMed:22231448, ECO:0000269|PubMed:24573677,
CC       ECO:0000303|PubMed:18263876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+)
CC         + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357;
CC         Evidence={ECO:0000269|PubMed:16332963};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- SUBUNIT: Homodimer (PubMed:20521842). Interacts with PRPF19; required
CC       for SETMAR recruitment to damaged DNA sites (PubMed:18263876).
CC       Interacts with PCNA (PubMed:20457750). Interacts with TOP2A; stimulates
CC       TOP2A topoisomerase activity (PubMed:18790802, PubMed:20457750). May
CC       interact with RAD9A and/or RAD9B (PubMed:20457750).
CC       {ECO:0000269|PubMed:18263876, ECO:0000269|PubMed:18790802,
CC       ECO:0000269|PubMed:20457750, ECO:0000269|PubMed:20521842}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18263876}. Chromosome
CC       {ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22231448}.
CC       Note=Recruited on damaged DNA at sites of double-strand breaks.
CC       {ECO:0000269|PubMed:18263876}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q53H47-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q53H47-2; Sequence=VSP_021440, VSP_021441;
CC       Name=3;
CC         IsoId=Q53H47-3; Sequence=VSP_054089;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC       placenta and ovary and lowest expression in skeletal muscle.
CC       {ECO:0000269|PubMed:16332963}.
CC   -!- DOMAIN: The mariner transposase Hsmar1 region mediates DNA-binding. It
CC       has retained some of the nucleases activity but has lost its
CC       transposase activity because the active site contains an Asn in
CC       position 610 instead of an Asp residue. {ECO:0000269|PubMed:17403897}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC       arranged in a triangular cluster; some of these Cys residues contribute
CC       to the binding of two zinc ions within the cluster.
CC   -!- PTM: Methylated. Methylation regulates activity in DNA decatenation.
CC       {ECO:0000269|PubMed:18790802}.
CC   -!- PTM: Phosphorylated at Ser-508 by CHEK1 and dephosphorylated by protein
CC       phosphatase 2A/PP2A. Phosphorylation at Ser-508 is enhanced by DNA
CC       damage and promotes recruitment to damaged DNA. It stimulates DNA
CC       repair and impairs replication fork restart.
CC       {ECO:0000269|PubMed:22231448}.
CC   -!- MISCELLANEOUS: The mariner transposase region in only present in
CC       primates and appeared 40-58 million years ago, after the insertion of a
CC       transposon downstream of a preexisting SET gene, followed by the de
CC       novo exonization of previously non-coding sequence and the creation of
CC       a new intron.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class V-like SAM-
CC       binding methyltransferase superfamily. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the mariner
CC       transposase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11635.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAY29570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD96454.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Taming genes - Issue 167 of
CC       February 2015;
CC       URL="https://web.expasy.org/spotlight/back_issues/167/";
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DR   EMBL; AK222734; BAD96454.1; ALT_INIT; mRNA.
DR   EMBL; AK302296; BAG63636.1; -; mRNA.
DR   EMBL; AC023483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC034191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011635; AAH11635.1; ALT_INIT; mRNA.
DR   EMBL; AY952295; AAY29570.1; ALT_INIT; mRNA.
DR   EMBL; DQ341316; ABC72087.1; -; Genomic_DNA.
DR   EMBL; U52077; AAC52010.1; -; Genomic_DNA.
DR   CCDS; CCDS2563.2; -. [Q53H47-1]
DR   CCDS; CCDS58814.1; -. [Q53H47-3]
DR   CCDS; CCDS63528.1; -. [Q53H47-2]
DR   RefSeq; NP_001230652.1; NM_001243723.1. [Q53H47-3]
DR   RefSeq; NP_001263254.1; NM_001276325.1. [Q53H47-2]
DR   RefSeq; NP_001307606.1; NM_001320677.1.
DR   RefSeq; NP_001307607.1; NM_001320678.1.
DR   RefSeq; NP_006506.3; NM_006515.3. [Q53H47-1]
DR   PDB; 3BO5; X-ray; 1.59 A; A=15-303.
DR   PDB; 3F2K; X-ray; 1.85 A; A/B=459-684.
DR   PDB; 3K9J; X-ray; 1.90 A; A/B=446-684.
DR   PDB; 3K9K; X-ray; 2.55 A; A/B=446-684.
DR   PDB; 7S03; X-ray; 2.37 A; A=343-453.
DR   PDBsum; 3BO5; -.
DR   PDBsum; 3F2K; -.
DR   PDBsum; 3K9J; -.
DR   PDBsum; 3K9K; -.
DR   PDBsum; 7S03; -.
DR   AlphaFoldDB; Q53H47; -.
DR   SMR; Q53H47; -.
DR   BioGRID; 112317; 24.
DR   IntAct; Q53H47; 15.
DR   MINT; Q53H47; -.
DR   STRING; 9606.ENSP00000373354; -.
DR   BindingDB; Q53H47; -.
DR   ChEMBL; CHEMBL2189111; -.
DR   iPTMnet; Q53H47; -.
DR   PhosphoSitePlus; Q53H47; -.
DR   BioMuta; SETMAR; -.
DR   DMDM; 74740552; -.
DR   EPD; Q53H47; -.
DR   jPOST; Q53H47; -.
DR   MassIVE; Q53H47; -.
DR   MaxQB; Q53H47; -.
DR   PaxDb; 9606-ENSP00000373354; -.
DR   PeptideAtlas; Q53H47; -.
DR   ProteomicsDB; 17093; -.
DR   ProteomicsDB; 62493; -. [Q53H47-1]
DR   ProteomicsDB; 62494; -. [Q53H47-2]
DR   Pumba; Q53H47; -.
DR   ABCD; Q53H47; 1 sequenced antibody.
DR   Antibodypedia; 25143; 212 antibodies from 33 providers.
DR   DNASU; 6419; -.
DR   Ensembl; ENST00000358065.5; ENSP00000373354.3; ENSG00000170364.13. [Q53H47-1]
DR   Ensembl; ENST00000425863.5; ENSP00000403145.1; ENSG00000170364.13. [Q53H47-3]
DR   Ensembl; ENST00000430981.1; ENSP00000403000.1; ENSG00000170364.13. [Q53H47-2]
DR   GeneID; 6419; -.
DR   KEGG; hsa:6419; -.
DR   MANE-Select; ENST00000358065.5; ENSP00000373354.3; NM_006515.4; NP_006506.3.
DR   UCSC; uc003bpw.6; human. [Q53H47-1]
DR   AGR; HGNC:10762; -.
DR   CTD; 6419; -.
DR   DisGeNET; 6419; -.
DR   GeneCards; SETMAR; -.
DR   HGNC; HGNC:10762; SETMAR.
DR   HPA; ENSG00000170364; Low tissue specificity.
DR   MIM; 609834; gene.
DR   neXtProt; NX_Q53H47; -.
DR   OpenTargets; ENSG00000170364; -.
DR   PharmGKB; PA35680; -.
DR   VEuPathDB; HostDB:ENSG00000170364; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   GeneTree; ENSGT00440000033232; -.
DR   HOGENOM; CLU_020840_3_3_1; -.
DR   InParanoid; Q53H47; -.
DR   OMA; CNGAYFD; -.
DR   OrthoDB; 5481936at2759; -.
DR   PhylomeDB; Q53H47; -.
DR   TreeFam; TF352220; -.
DR   BioCyc; MetaCyc:HS10111-MONOMER; -.
DR   BRENDA; 2.1.1.357; 2681.
DR   BRENDA; 2.7.7.B22; 2681.
DR   PathwayCommons; Q53H47; -.
DR   SignaLink; Q53H47; -.
DR   SIGNOR; Q53H47; -.
DR   BioGRID-ORCS; 6419; 14 hits in 1169 CRISPR screens.
DR   EvolutionaryTrace; Q53H47; -.
DR   GeneWiki; SETMAR; -.
DR   GenomeRNAi; 6419; -.
DR   Pharos; Q53H47; Tbio.
DR   PRO; PR:Q53H47; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q53H47; Protein.
DR   Bgee; ENSG00000170364; Expressed in body of uterus and 168 other cell types or tissues.
DR   ExpressionAtlas; Q53H47; baseline and differential.
DR   Genevisible; Q53H47; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0044547; F:DNA topoisomerase binding; IPI:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IMP:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0140954; F:histone H3K36 dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IMP:UniProtKB.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0006308; P:DNA catabolic process; IDA:UniProtKB.
DR   GO; GO:0000729; P:DNA double-strand break processing; IDA:UniProtKB.
DR   GO; GO:0015074; P:DNA integration; IMP:UniProtKB.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:2001251; P:negative regulation of chromosome organization; IDA:UniProtKB.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IMP:UniProtKB.
DR   GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; IDA:UniProtKB.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR   CDD; cd10544; SET_SETMAR; 1.
DR   Gene3D; 1.10.10.1450; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR041426; Mos1_HTH.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR001888; Transposase_1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR46060:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR; 1.
DR   PANTHER; PTHR46060; MARINER MOS1 TRANSPOSASE-LIKE PROTEIN; 1.
DR   Pfam; PF17906; HTH_48; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF01359; Transposase_1; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Methylation; Methyltransferase; Multifunctional enzyme;
KW   Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN           1..684
FT                   /note="Histone-lysine N-methyltransferase SETMAR"
FT                   /id="PRO_0000259526"
FT   DOMAIN          73..136
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          139..263
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          283..299
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   DNA_BIND        364..395
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   DNA_BIND        428..448
FT                   /note="H-T-H motif"
FT   REGION          1..345
FT                   /note="Histone-lysine N-methyltransferase"
FT   REGION          346..684
FT                   /note="Mariner transposase Hsmar1"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         149..151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         192
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         220
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         223..224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT   BINDING         496
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         588
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   MOD_RES         498
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:18790802"
FT   MOD_RES         508
FT                   /note="Phosphoserine; by CHEK1"
FT                   /evidence="ECO:0000269|PubMed:22231448,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         163..301
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054089"
FT   VAR_SEQ         341..365
FT                   /note="TMKMMLDKKQIRAIFLFEFKMGRKA -> VSLFSDKQLAPPYSGRQWLASFT
FT                   SA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021440"
FT   VAR_SEQ         366..684
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021441"
FT   MUTAGEN         223
FT                   /note="N->S: Reduces activity in double-strand break
FT                   repair."
FT                   /evidence="ECO:0000269|PubMed:16332963"
FT   MUTAGEN         261
FT                   /note="D->S: Reduces activity in double-strand break
FT                   repair."
FT                   /evidence="ECO:0000269|PubMed:16332963"
FT   MUTAGEN         445
FT                   /note="R->A: Abolishes TIR-specific DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:17877369"
FT   MUTAGEN         473
FT                   /note="F->K: Abolishes homodimerization and DNA-binding and
FT                   reduces cleavage of single-stranded DNA."
FT                   /evidence="ECO:0000269|PubMed:20521842"
FT   MUTAGEN         496
FT                   /note="D->A: Abolishes DNA cleavage."
FT                   /evidence="ECO:0000269|PubMed:17877369"
FT   MUTAGEN         503
FT                   /note="D->S: Reduces activity in double-strand break
FT                   repair."
FT                   /evidence="ECO:0000269|PubMed:16332963"
FT   MUTAGEN         508
FT                   /note="S->A: Prevents phosphorylation. Impairs recruitment
FT                   to damaged DNA and double-strand break repair. Impairs
FT                   interaction with histone H3 and its methylation. Allows
FT                   replication fork restart."
FT                   /evidence="ECO:0000269|PubMed:22231448"
FT   MUTAGEN         623
FT                   /note="N->D,E: Loss of function in DNA repair. Altered DNA-
FT                   binding properties."
FT                   /evidence="ECO:0000269|PubMed:24573677"
FT   CONFLICT        91
FT                   /note="R -> H (in Ref. 1; BAG63636)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="K -> E (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="N -> D (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="T -> S (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        484
FT                   /note="H -> N (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="S -> P (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514
FT                   /note="Q -> R (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525
FT                   /note="I -> N (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        528
FT                   /note="P -> Q (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="I -> V (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="E -> Q (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        567..568
FT                   /note="NQ -> HR (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="L -> P (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="L -> S (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        623
FT                   /note="N -> D (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        626
FT                   /note="V -> F (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        631
FT                   /note="N -> D (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        656
FT                   /note="Q -> R (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        667
FT                   /note="Q -> K (in Ref. 6; AAC52010)"
FT                   /evidence="ECO:0000305"
FT   TURN            30..33
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          147..157
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          164..167
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   HELIX           175..182
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          206..216
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          229..241
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          243..250
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          257..260
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   STRAND          270..279
FT                   /evidence="ECO:0007829|PDB:3BO5"
FT   HELIX           348..360
FT                   /evidence="ECO:0007829|PDB:7S03"
FT   HELIX           365..376
FT                   /evidence="ECO:0007829|PDB:7S03"
FT   HELIX           383..394
FT                   /evidence="ECO:0007829|PDB:7S03"
FT   HELIX           414..423
FT                   /evidence="ECO:0007829|PDB:7S03"
FT   HELIX           429..436
FT                   /evidence="ECO:0007829|PDB:7S03"
FT   HELIX           440..449
FT                   /evidence="ECO:0007829|PDB:7S03"
FT   HELIX           466..485
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           489..491
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   STRAND          492..503
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   STRAND          530..538
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   STRAND          541..547
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           556..573
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           574..576
FT                   /evidence="ECO:0007829|PDB:3K9J"
FT   STRAND          584..586
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           591..594
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           598..605
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           617..619
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           621..624
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           626..634
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           642..654
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           660..666
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   HELIX           668..677
FT                   /evidence="ECO:0007829|PDB:3F2K"
FT   TURN            678..680
FT                   /evidence="ECO:0007829|PDB:3F2K"
SQ   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
//
ID   B4DND2_HUMAN            Unreviewed;       428 AA.
AC   B4DND2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   22-FEB-2023, entry version 62.
DE   SubName: Full=cDNA FLJ54643, highly similar to Homo sapiens SET domain and mariner transposase fusion gene (SETMAR), mRNA {ECO:0000313|EMBL:BAG60194.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG60194.1};
RN   [1] {ECO:0000313|EMBL:BAG60194.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart {ECO:0000313|EMBL:BAG60194.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK297865; BAG60194.1; -; mRNA.
DR   RefSeq; NP_001307606.1; NM_001320677.1.
DR   RefSeq; XP_006713357.1; XM_006713294.3.
DR   AlphaFoldDB; B4DND2; -.
DR   SMR; B4DND2; -.
DR   PeptideAtlas; B4DND2; -.
DR   DNASU; 6419; -.
DR   GeneID; 6419; -.
DR   CTD; 6419; -.
DR   OrthoDB; 5481936at2759; -.
DR   BioGRID-ORCS; 6419; 14 hits in 1169 CRISPR screens.
DR   GenomeRNAi; 6419; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 1.10.10.1450; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR041426; Mos1_HTH.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR001888; Transposase_1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR46060:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR; 1.
DR   PANTHER; PTHR46060; MARINER MOS1 TRANSPOSASE-LIKE PROTEIN; 1.
DR   Pfam; PF17906; HTH_48; 1.
DR   Pfam; PF01359; Transposase_1; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN          92..141
FT                   /note="Mos1 transposase HTH"
FT                   /evidence="ECO:0000259|Pfam:PF17906"
SQ   SEQUENCE   428 AA;  49667 MW;  61D2D24D22E896C4 CRC64;
     MQSLFLNAMS CADAVTTAET EWSRKVYSST SKCSRRIKKA GDFVPWNLYR KEEKSNISCG
     NEKEPSMCGS APSVFPSCKR LTLETMKMML DKKQIRAIFL FEFKMGRKAA ETTRNINNAF
     GPGTANERTV QWWFKKFCKG DESLEDEERS GRPSEVDNDQ LRAIIEADPL TTTREVAEEL
     NVNHSTVVRH LKQIGKVKKL DKWVPHELTE NQKNRRFEVS SSLILRNHNE PFLDRIVTCD
     EKWILYDNRR RSAQWLDQEE APKHFPKPIL HPKKVMVTIW WSAAGLIHYS FLNPGETITS
     EKYAQEIDEM NQKLQRLQLA LVNRKGPILL HDNARPHVAQ PTLQKLNELG YEVLPHPPYS
     PDLLPTNYHV FKHLNNFLQG KRFHNQQDAE NAFQEFVESQ STDFYATGIN QLISRWQKCV
     DCNGSYFD
//
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