MUS81
entrez
80198
canonical
uniprot
Q96NY9
canonical
ensembl
ENSG00000172732
resolver
ensp
ENSP00000307853
resolver
ensp
ENSP00000577383
resolver
ensp
ENSP00000641562
resolver
ensp
ENSP00000641563
resolver
ensp
ENSP00000652946
resolver
ensp
ENSP00000703351
resolver
enst
ENST00000308110
resolver
enst
ENST00000907324
resolver
enst
ENST00000971503
resolver
genesymbol
MUS81
resolver
hgnc
HGNC:29814
resolver
uniprot
Q53ES5
resolver
uniprot
Q9H7D9
resolver
uniprot_entry
MUS81_HUMAN
resolver
uniprot_entry
Q53ES5_HUMAN
resolver
uniprot_sec
Q9H7D9
resolver
amino_acid_sequence
MAAPVRLGRKRPLPACPNPLFVRWLTEWRDEATRSRRRTRFVFQKALRSLRRYPLPLRSGKEAKILQHFGDGLCRMLDERLQRHRTSGGDHAPDSPSGENSPAPQGRLAEVQDSSMPVPAQPKAGGSGSYWPARHSGARVILLVLYREHLNPNGHHFLTKEELLQRCAQKSPRVAPGSARPWPALRSLLHRNLVLRTHQPARYSLTPEGLELAQKLAESEGLSLLNVGIGPKEPPGEETAVPGAASAELASEAGVQQQPLELRPGEYRVLLCVDIGETRGGGHRPELLRELQRLHVTHTVRKLHVGDFVWVAQETNPRDPANPGELVLDHIVERKRLDDLCSSIIDGRFREQKFRLKRCGLERRVYLVEEHGSVHNLSLPESTLLQAVTNTQVIDGFFVKRTADIKESAAYLALLTRGLQRLYQGHTLRSRPWGTPGNPESGAMTSPNPLCSLLTFSDFNAGAIKNKAQSVREVFARQLMQVRGVSGEKAAALVDRYSTPASLLAAYDACATPKEQETLLSTIKCGRLQRNLGPALSRTLSQLYCSYGPLT
uniprot
proteins
ec_number
3.1.22.-
uniprot
proteins
function
FUNCTION: Catalytic subunit of two functionally distinct, structure-specific, heterodimeric DNA endonucleases MUS81-EME1 and MUS81-EME2 that are involved in the maintenance of genome stability (PubMed:11741546, PubMed:12374758, PubMed:12686547, PubMed:12721304, PubMed:24371268, PubMed:24733841, PubMed:24813886, PubMed:35290797, PubMed:39015284). Both endonucleases have essentially the same substrate specificity though MUS81-EME2 is more active than its MUS81-EME1 counterpart. Both cleave 3'-flaps and nicked Holliday junctions, and exhibit limited endonuclease activity with 5' flaps and nicked double-stranded DNAs (PubMed:24371268, PubMed:24733841, PubMed:35290797). MUS81-EME2 which is active during the replication of DNA is more specifically involved in replication fork processing (PubMed:24813886). Replication forks frequently encounter obstacles to their passage, including DNA base lesions, DNA interstrand cross-links, difficult-to-replicate sequences, transcription bubbles, or tightly bound proteins. One mechanism for the restart of a stalled replication fork involves nucleolytic cleavage mediated by the MUS81-EME2 endonuclease. By acting upon the stalled fork, MUS81-EME2 generates a DNA double-strand break (DSB) that can be repaired by homologous recombination, leading to the restoration of an active fork (PubMed:24813886). MUS81-EME2 could also function in telomere maintenance (PubMed:24813886). MUS81-EME1, on the other hand, is active later in the cell cycle and functions in the resolution of mitotic recombination intermediates including the Holliday junctions, the four-way DNA intermediates that form during homologous recombination (PubMed:11741546, PubMed:12374758, PubMed:14617801, PubMed:15805243, PubMed:24813886). {ECO:0000269|PubMed:11741546, ECO:0000269|PubMed:12374758, ECO:0000269|PubMed:12686547, ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:15805243, ECO:0000269|PubMed:24371268, ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:24813886, ECO:0000269|PubMed:35290797, ECO:0000269|PubMed:39015284}.
uniprot
proteins
mass_dalton
61173
uniprot
proteins
mutagenesis
MUTAGEN 186; /note="R->E: Reduced 5 prime flap and nHJ cleavages but only mild effect on the cleavage of 3 prime flap; when associated with E-191."; /evidence="ECO:0000269|PubMed:35290797"; MUTAGEN 191; /note="R->E: Reduced 5 prime flap and nHJ cleavages but only mild effect on the cleavage of 3 prime flap; when associated with E-186."; /evidence="ECO:0000269|PubMed:35290797"; MUTAGEN 274; /note="D->A: Loss of endonuclease activity."; /evidence="ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:35290797"; MUTAGEN 277; /note="E->A: Loss of endonuclease activity."; /evidence="ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:35290797"; MUTAGEN 306..307; /note="GD->AE: Loss of endonuclease activity."; /evidence="ECO:0000269|PubMed:11741546"; MUTAGEN 307; /note="D->A: Loss of endonuclease activity."; /evidence="ECO:0000269|PubMed:24733841, ECO:0000269|PubMed:35290797"; MUTAGEN 333..334; /note="ER->AG: Loss of endonuclease activity."; /evidence="ECO:0000269|PubMed:11741546"; MUTAGEN 338..339; /note="DD->AA: Loss of endonuclease activity."; /evidence="ECO:0000269|PubMed:11741546, ECO:0000269|PubMed:14617801"; MUTAGEN 344; /note="I->R: Decreased endonuclease activity; when associated R-345."; /evidence="ECO:0000269|PubMed:24733841"; MUTAGEN 345; /note="I->R: Decreased endonuclease activity; when associated R-344."; /evidence="ECO:0000269|PubMed:24733841"; MUTAGEN 348; /note="R->E: Reduced 3 prime flap and nHJ cleavage and loss of 5 prime flap cleavage."; /evidence="ECO:0000269|PubMed:35290797"; MUTAGEN 355; /note="R->E: Reduced 3 prime flap and nHJ cleavage and loss of 5 prime flap cleavage."; /evidence="ECO:0000269|PubMed:35290797"; MUTAGEN 383; /note="T->R: Decreased endonuclease activity; when associated with R-387."; /evidence="ECO:0000269|PubMed:24733841"; MUTAGEN 387; /note="A->R: Decreased endonuclease activity; when associated with R-383."; /evidence="ECO:0000269|PubMed:24733841"; MUTAGEN 483; /note="R->A: Loss of endonuclease activity; when associated with A-489 and A-530."; /evidence="ECO:0000269|PubMed:24733841"; MUTAGEN 489; /note="K->A: Loss of endonuclease activity; when associated with A-483 and A-530."; /evidence="ECO:0000269|PubMed:24733841"; MUTAGEN 530; /note="R->A: Decreased endonuclease activity. Loss of endonuclease activity; when associated with A-483 and A-489."; /evidence="ECO:0000269|PubMed:24733841
uniprot
proteins
protein_family
XPF family
uniprot
proteins
pubmed
11741546
uniprot
proteins
pubmed
12374758
uniprot
proteins
pubmed
12686547
uniprot
proteins
pubmed
12721304
uniprot
proteins
pubmed
14617801
uniprot
proteins
pubmed
14638871
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15805243
uniprot
proteins
pubmed
17289582
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18469862
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19595721
uniprot
proteins
pubmed
19596235
uniprot
proteins
pubmed
19596236
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24371268
uniprot
proteins
pubmed
24733841
uniprot
proteins
pubmed
24813886
uniprot
proteins
pubmed
28575661
uniprot
proteins
pubmed
35290797
uniprot
proteins
pubmed
39015284
uniprot
proteins
sequence_length
551
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11741546, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:14638871, ECO:0000269|PubMed:15805243}. Note=Recruited to foci of DNA damage in S-phase cells. {ECO:0000269|PubMed:14638871}.
uniprot
proteins