MUS81_HUMAN
ID MUS81_HUMAN Reviewed; 551 AA.
AC Q96NY9; Q9H7D9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Crossover junction endonuclease MUS81;
DE EC=3.1.22.-;
GN Name=MUS81;
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 [MRNA], VARIANTS HIS-37 AND PRO-180, FUNCTION,
RP COFACTOR, INTERACTION WITH CHEK2, SUBCELLULAR LOCATION, INDUCTION, AND
RP MUTAGENESIS OF 306-GLY-ASP-307; 333-GLU-ARG-334 AND 338-ASP-ASP-339.
RC TISSUE=Cerebellum;
RX PubMed=11741546; DOI=10.1016/s1097-2765(01)00375-6;
RA Chen X.-B., Melchionna R., Denis C.-M., Gaillard P.-H.L., Blasina A.,
RA Van de Weyer I., Boddy M.N., Russell P., Vialard J., McGowan C.H.;
RT "Human Mus81-associated endonuclease cleaves Holliday junctions in vitro.";
RL Mol. Cell 8:1117-1127(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-37 AND PRO-180.
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-551, AND VARIANTS HIS-37 AND
RP PRO-180.
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 [4]
RP FUNCTION.
RX PubMed=12374758; DOI=10.1093/emboj/cdf554;
RA Constantinou A., Chen X.-B., McGowan C.H., West S.C.;
RT "Holliday junction resolution in human cells: two junction endonucleases
RT with distinct substrate specificities.";
RL EMBO J. 21:5577-5585(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH EME1.
RX PubMed=12686547; DOI=10.1074/jbc.m302484200;
RA Oegruenc M., Sancar A.;
RT "Identification and characterization of human MUS81-MMS4 structure-specific
RT endonuclease.";
RL J. Biol. Chem. 278:21715-21720(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH EME1.
RX PubMed=12721304; DOI=10.1074/jbc.m302882200;
RA Ciccia A., Constantinou A., West S.C.;
RT "Identification and characterization of the human mus81-eme1
RT endonuclease.";
RL J. Biol. Chem. 278:25172-25178(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14638871; DOI=10.1091/mbc.e03-05-0276;
RA Gao H., Chen X.-B., McGowan C.H.;
RT "Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in
RT human S-phase cells.";
RL Mol. Biol. Cell 14:4826-4834(2003).
RN [8]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EME1, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF 338-ASP-ASP-339.
RX PubMed=14617801; DOI=10.1091/mbc.e03-08-0580;
RA Blais V., Gao H., Elwell C.A., Boddy M.N., Gaillard P.-H.L., Russell P.,
RA McGowan C.H.;
RT "RNA interference inhibition of Mus81 reduces mitotic recombination in
RT human cells.";
RL Mol. Biol. Cell 15:552-562(2004).
RN [9]
RP FUNCTION, INTERACTION WITH BLM, AND SUBCELLULAR LOCATION.
RX PubMed=15805243; DOI=10.1158/0008-5472.can-04-2421;
RA Zhang R., Sengupta S., Yang Q., Linke S.P., Yanaihara N., Bradsher J.,
RA Blais V., McGowan C.H., Harris C.C.;
RT "BLM helicase facilitates Mus81 endonuclease activity in human cells.";
RL Cancer Res. 65:2526-2531(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH EME1 AND EME2.
RX PubMed=17289582; DOI=10.1016/j.molcel.2007.01.003;
RA Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R.,
RA Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.;
RT "Identification of FAAP24, a Fanconi anemia core complex protein that
RT interacts with FANCM.";
RL Mol. Cell 25:331-343(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP INTERACTION WITH DCLRE1B.
RX PubMed=18469862; DOI=10.1038/onc.2008.139;
RA Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X.,
RA Shen X., Li L., Legerski R.J.;
RT "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint
RT activation in response to DNA interstrand cross-links.";
RL Oncogene 27:5045-5056(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP FUNCTION, AND INTERACTION WITH SLX4.
RX PubMed=19595721; DOI=10.1016/j.molcel.2009.06.020;
RA Munoz I.M., Hain K., Declais A.-C., Gardiner M., Toh G.W.,
RA Sanchez-Pulido L., Heuckmann J.M., Toth R., Macartney T., Eppink B.,
RA Kanaar R., Ponting C.P., Lilley D.M.J., Rouse J.;
RT "Coordination of structure-specific nucleases by human SLX4/BTBD12 is
RT required for DNA repair.";
RL Mol. Cell 35:116-127(2009).
RN [15]
RP FUNCTION, AND INTERACTION WITH SLX4.
RX PubMed=19596235; DOI=10.1016/j.cell.2009.06.030;
RA Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P.,
RA Elledge S.J., Harper J.W.;
RT "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is
RT required for DNA repair.";
RL Cell 138:63-77(2009).
RN [16]
RP INTERACTION WITH SLX4.
RX PubMed=19596236; DOI=10.1016/j.cell.2009.06.029;
RA Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S.,
RA Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H.,
RA Gaillard P.-H.L.;
RT "Human SLX4 is a Holliday junction resolvase subunit that binds multiple
RT DNA repair/recombination endonucleases.";
RL Cell 138:78-89(2009).
RN [17]
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-101, AND
RP IDENTIFICATION BY 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 INTERACTION WITH RECQL5.
RX PubMed=28575661; DOI=10.1016/j.molcel.2017.05.006;
RA Di Marco S., Hasanova Z., Kanagaraj R., Chappidi N., Altmannova V.,
RA Menon S., Sedlackova H., Langhoff J., Surendranath K., Huehn D.,
RA Bhowmick R., Marini V., Ferrari S., Hickson I.D., Krejci L., Janscak P.;
RT "RECQ5 Helicase Cooperates with MUS81 Endonuclease in Processing Stalled
RT Replication Forks at Common Fragile Sites during Mitosis.";
RL Mol. Cell 66:658-671.e8(2017).
CC -!- FUNCTION: Interacts with EME1 and EME2 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, replication forks and nicked Holliday junctions. Plays an
CC essential role in mitosis for the processing of stalled or collapsed
CC replication forks (PubMed:28575661). {ECO:0000269|PubMed:11741546,
CC ECO:0000269|PubMed:12374758, ECO:0000269|PubMed:12686547,
CC ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801,
CC ECO:0000269|PubMed:15805243, ECO:0000269|PubMed:17289582,
CC ECO:0000269|PubMed:19595721, ECO:0000269|PubMed:19596235,
CC ECO:0000269|PubMed:28575661}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11741546};
CC -!- SUBUNIT: May self-associate. Interacts with EME1, EME2 and CHEK2.
CC Interacts with BLM, and this interaction may stimulate the endonuclease
CC activity of MUS81. Interacts with SLX4/BTBD12; this interaction is
CC direct and links the MUS81-EME1 complex to SLX4, which may coordinate
CC the action of the structure-specific endonuclease during DNA repair.
CC Interacts with DCLRE1B/Apollo. Interacts with RECQL5; this interaction
CC stimulates mitotic DNA synthesis (PubMed:28575661).
CC {ECO:0000269|PubMed:11741546, ECO:0000269|PubMed:12686547,
CC ECO:0000269|PubMed:12721304, ECO:0000269|PubMed:14617801,
CC ECO:0000269|PubMed:15805243, ECO:0000269|PubMed:17289582,
CC ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:19595721,
CC ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:19596236,
CC ECO:0000269|PubMed:28575661}.
CC -!- INTERACTION:
CC Q96NY9; Q96AY2: EME1; NbExp=9; IntAct=EBI-2370806, EBI-2370825;
CC Q96NY9; A4GXA9: EME2; NbExp=3; IntAct=EBI-2370806, EBI-7838486;
CC Q96NY9; P39748: FEN1; NbExp=5; IntAct=EBI-2370806, EBI-707816;
CC Q96NY9; Q8IY92: SLX4; NbExp=13; IntAct=EBI-2370806, EBI-2370740;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11741546,
CC ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:14638871,
CC ECO:0000269|PubMed:15805243}. Note=Recruited to foci of DNA damage in
CC S-phase cells.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed in S phase and G2 phase.
CC {ECO:0000269|PubMed:14638871}.
CC -!- INDUCTION: Up-regulated in cells treated with agents that damage DNA or
CC block replication. This up-regulation seems to be independent of
CC transcription. {ECO:0000269|PubMed:11741546}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF425646; AAL28065.1; -; mRNA.
DR EMBL; BC009999; AAH09999.2; -; mRNA.
DR EMBL; AK024665; BAB14953.1; ALT_INIT; mRNA.
DR CCDS; CCDS8115.1; -.
DR RefSeq; NP_079404.3; NM_025128.4.
DR RefSeq; XP_011543572.1; XM_011545270.1.
DR PDB; 2MC3; NMR; -; A=127-230.
DR PDB; 2ZIX; X-ray; 3.50 A; A=246-551.
DR PDB; 4P0P; X-ray; 2.80 A; A=246-551.
DR PDB; 4P0Q; X-ray; 2.85 A; A=246-551.
DR PDB; 4P0R; X-ray; 6.50 A; A/C=246-551.
DR PDB; 4P0S; X-ray; 6.00 A; A/C/E/G=246-551.
DR PDB; 6VWB; NMR; -; A=2-90.
DR PDB; 7BU5; X-ray; 1.80 A; A=2-99.
DR PDB; 7F6L; X-ray; 3.20 A; A=246-551.
DR PDBsum; 2MC3; -.
DR PDBsum; 2ZIX; -.
DR PDBsum; 4P0P; -.
DR PDBsum; 4P0Q; -.
DR PDBsum; 4P0R; -.
DR PDBsum; 4P0S; -.
DR PDBsum; 6VWB; -.
DR PDBsum; 7BU5; -.
DR PDBsum; 7F6L; -.
DR AlphaFoldDB; Q96NY9; -.
DR BMRB; Q96NY9; -.
DR SMR; Q96NY9; -.
DR BioGRID; 123170; 107.
DR ComplexPortal; CPX-511; Deoxyribonuclease complex MUS81-EME1.
DR ComplexPortal; CPX-586; Deoxyribonuclease complex MUS81-EME2.
DR CORUM; Q96NY9; -.
DR DIP; DIP-48630N; -.
DR IntAct; Q96NY9; 16.
DR MINT; Q96NY9; -.
DR STRING; 9606.ENSP00000307853; -.
DR iPTMnet; Q96NY9; -.
DR PhosphoSitePlus; Q96NY9; -.
DR BioMuta; MUS81; -.
DR DMDM; 166898077; -.
DR EPD; Q96NY9; -.
DR jPOST; Q96NY9; -.
DR MassIVE; Q96NY9; -.
DR MaxQB; Q96NY9; -.
DR PaxDb; Q96NY9; -.
DR PeptideAtlas; Q96NY9; -.
DR PRIDE; Q96NY9; -.
DR ProteomicsDB; 77579; -.
DR Antibodypedia; 16020; 198 antibodies from 25 providers.
DR DNASU; 80198; -.
DR Ensembl; ENST00000308110.9; ENSP00000307853.4; ENSG00000172732.12.
DR GeneID; 80198; -.
DR KEGG; hsa:80198; -.
DR MANE-Select; ENST00000308110.9; ENSP00000307853.4; NM_025128.5; NP_079404.3.
DR UCSC; uc001ofv.5; human.
DR CTD; 80198; -.
DR DisGeNET; 80198; -.
DR GeneCards; MUS81; -.
DR HGNC; HGNC:29814; MUS81.
DR HPA; ENSG00000172732; Low tissue specificity.
DR MalaCards; MUS81; -.
DR MIM; 606591; gene.
DR neXtProt; NX_Q96NY9; -.
DR OpenTargets; ENSG00000172732; -.
DR PharmGKB; PA134881809; -.
DR VEuPathDB; HostDB:ENSG00000172732; -.
DR eggNOG; KOG2379; Eukaryota.
DR GeneTree; ENSGT00390000005498; -.
DR HOGENOM; CLU_014329_3_0_1; -.
DR InParanoid; Q96NY9; -.
DR OMA; WIKEWLD; -.
DR OrthoDB; 738810at2759; -.
DR PhylomeDB; Q96NY9; -.
DR TreeFam; TF315113; -.
DR BRENDA; 3.1.21.10; 2681.
DR PathwayCommons; Q96NY9; -.
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q96NY9; -.
DR BioGRID-ORCS; 80198; 67 hits in 1082 CRISPR screens.
DR ChiTaRS; MUS81; human.
DR EvolutionaryTrace; Q96NY9; -.
DR GeneWiki; MUS81; -.
DR GenomeRNAi; 80198; -.
DR Pharos; Q96NY9; Tbio.
DR PRO; PR:Q96NY9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96NY9; protein.
DR Bgee; ENSG00000172732; Expressed in body of uterus and 198 other tissues.
DR ExpressionAtlas; Q96NY9; baseline and differential.
DR Genevisible; Q96NY9; HS.
DR GO; GO:1905347; C:endodeoxyribonuclease complex; IPI:ComplexPortal.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR GO; GO:0043596; C:nuclear replication fork; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048257; F:3'-flap endonuclease activity; IMP:UniProtKB.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IDA:ComplexPortal.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033687; P:osteoblast proliferation; IMP:CACAO.
DR GO; GO:0031297; P:replication fork processing; IDA:ComplexPortal.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 1.10.150.670; -; 1.
DR IDEAL; IID00098; -.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033309; Mus81.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR13451; PTHR13451; 1.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Crossover junction endonuclease MUS81"
FT /id="PRO_0000198858"
FT DOMAIN 270..372
FT /note="ERCC4"
FT REGION 84..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..244
FT /note="Interaction with BLM"
FT /evidence="ECO:0000269|PubMed:15805243"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 37
FT /note="R -> H (in dbSNP:rs13817)"
FT /evidence="ECO:0000269|PubMed:11741546,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_025340"
FT VARIANT 115
FT /note="S -> F (in dbSNP:rs34381357)"
FT /id="VAR_061988"
FT VARIANT 180
FT /note="R -> P (in dbSNP:rs545500)"
FT /evidence="ECO:0000269|PubMed:11741546,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_038521"
FT VARIANT 189
FT /note="L -> F (in dbSNP:rs2298447)"
FT /id="VAR_021990"
FT VARIANT 350
FT /note="R -> W (in dbSNP:rs34891773)"
FT /id="VAR_038522"
FT VARIANT 481
FT /note="Q -> H (in dbSNP:rs765593)"
FT /id="VAR_025341"
FT MUTAGEN 306..307
FT /note="GD->AE: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11741546"
FT MUTAGEN 333..334
FT /note="ER->AG: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11741546"
FT MUTAGEN 338..339
FT /note="DD->AA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11741546,
FT ECO:0000269|PubMed:14617801"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:7BU5"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:7BU5"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:7BU5"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:7BU5"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:7BU5"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:2MC3"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2MC3"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2MC3"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:2MC3"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2MC3"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2MC3"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2MC3"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:2MC3"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2MC3"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2MC3"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:2ZIX"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 307..316
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 325..336
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:4P0P"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:2ZIX"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 405..422
FT /evidence="ECO:0007829|PDB:4P0P"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4P0P"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:4P0P"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:2ZIX"
FT HELIX 471..479
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 487..496
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 500..509
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 513..517
FT /evidence="ECO:0007829|PDB:4P0P"
FT TURN 518..522
FT /evidence="ECO:0007829|PDB:4P0P"
FT TURN 526..529
FT /evidence="ECO:0007829|PDB:4P0P"
FT HELIX 535..545
FT /evidence="ECO:0007829|PDB:4P0P"
SQ SEQUENCE 551 AA; 61173 MW; D0F331CC2269D847 CRC64;
MAAPVRLGRK RPLPACPNPL FVRWLTEWRD EATRSRRRTR FVFQKALRSL RRYPLPLRSG
KEAKILQHFG DGLCRMLDER LQRHRTSGGD HAPDSPSGEN SPAPQGRLAE VQDSSMPVPA
QPKAGGSGSY WPARHSGARV ILLVLYREHL NPNGHHFLTK EELLQRCAQK SPRVAPGSAR
PWPALRSLLH RNLVLRTHQP ARYSLTPEGL ELAQKLAESE GLSLLNVGIG PKEPPGEETA
VPGAASAELA SEAGVQQQPL ELRPGEYRVL LCVDIGETRG GGHRPELLRE LQRLHVTHTV
RKLHVGDFVW VAQETNPRDP ANPGELVLDH IVERKRLDDL CSSIIDGRFR EQKFRLKRCG
LERRVYLVEE HGSVHNLSLP ESTLLQAVTN TQVIDGFFVK RTADIKESAA YLALLTRGLQ
RLYQGHTLRS RPWGTPGNPE SGAMTSPNPL CSLLTFSDFN AGAIKNKAQS VREVFARQLM
QVRGVSGEKA AALVDRYSTP ASLLAAYDAC ATPKEQETLL STIKCGRLQR NLGPALSRTL
SQLYCSYGPL T
