SETMAR
entrez
6419
canonical
uniprot
Q53H47
canonical
ensembl
ENSG00000170364
resolver
ensp
ENSP00000373354
resolver
ensp
ENSP00000403000
resolver
ensp
ENSP00000403145
resolver
ensp
ENSP00000535046
resolver
genesymbol
SETMAR
resolver
hgnc
HGNC:10762
resolver
uniprot
B4DND2
resolver
uniprot
B4DY74
resolver
uniprot
E7EN68
resolver
uniprot
Q13579
resolver
uniprot
Q1G668
resolver
uniprot
Q96F41
resolver
uniprot
Q96H41
resolver
uniprot_entry
B4DND2_HUMAN
resolver
uniprot_entry
Q96H41_HUMAN
resolver
uniprot_entry
SETMR_HUMAN
resolver
uniprot_sec
B4DY74
resolver
uniprot_sec
E7EN68
resolver
uniprot_sec
Q13579
resolver
uniprot_sec
Q1G668
resolver
uniprot_sec
Q96F41
resolver
amino_acid_sequence
MFAEAAKTTRPCGMAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFPGCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVVQKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYIIAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIVPEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNISCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNINNAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVAEELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIVTCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGETITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHPPYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQKCVDCNGSYFD
uniprot
proteins
ec_number
2.1.1.357
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
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. Also has 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:17403897, PubMed:17877369, PubMed:18263876, PubMed:20521842, PubMed:22231448, PubMed:24573677). 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}.
uniprot
proteins
mass_dalton
78034
uniprot
proteins
mutagenesis
MUTAGEN 223; /note="N->S: Reduces activity in double-strand break repair."; /evidence="ECO:0000269|PubMed:16332963"; MUTAGEN 261; /note="D->S: Reduces activity in double-strand break repair."; /evidence="ECO:0000269|PubMed:16332963"; MUTAGEN 445; /note="R->A: Abolishes TIR-specific DNA-binding."; /evidence="ECO:0000269|PubMed:17877369"; MUTAGEN 473; /note="F->K: Abolishes homodimerization and DNA-binding and reduces cleavage of single-stranded DNA."; /evidence="ECO:0000269|PubMed:20521842"; MUTAGEN 496; /note="D->A: Abolishes DNA cleavage."; /evidence="ECO:0000269|PubMed:17877369"; MUTAGEN 503; /note="D->S: Reduces activity in double-strand break repair."; /evidence="ECO:0000269|PubMed:16332963"; MUTAGEN 508; /note="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."; /evidence="ECO:0000269|PubMed:22231448"; MUTAGEN 623; /note="N->D,E: Loss of function in DNA repair. Altered DNA-binding properties."; /evidence="ECO:0000269|PubMed:24573677
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily; Mariner transposase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16332963
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16672366
uniprot
proteins
pubmed
17403897
uniprot
proteins
pubmed
17877369
uniprot
proteins
pubmed
18263876
uniprot
proteins
pubmed
18790802
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20457750
uniprot
proteins
pubmed
20521842
uniprot
proteins
pubmed
21187428
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22231448
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24573677
uniprot
proteins
pubmed
9461395
uniprot
proteins
sequence_length
684
uniprot
proteins
subcellular_location
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}.
uniprot
proteins