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Protein FULL name: crossover junction endonuclease MUS81 [Homo sapiens].
MUS81 (Homo sapiens) is product of expression of
MUS81
gene.
MUS81 is involved in:
HRR in Homo sapiens
Keywords:
FUNCTION: Interacts with EME1 and EME2 to form a DNA structure-
specific endonuclease with substrate preference for branched DNA
structures with a 5'-end at the branch nick. Typical substrates
include 3'-flap structures, replication forks and nicked Holliday
junctions. May be required in mitosis for the processing of
stalled or collapsed replication forks.
COFACTOR: Magnesium.
SUBUNIT: May self-associate. Interacts with EME1, EME2 and CHEK2.
Interacts with BLM, and this interaction may stimulate the
endonuclease activity of MUS81. Interacts with BTBD12/SLX4; this
interaction is direct and links the MUS81-EME1 complex to SLX4,
which may coordinate the action of the structure-specific
endonuclease during DNA repair.
INTERACTION:
Q8IY92:BTBD12; NbExp=3; IntAct=EBI-2370806, EBI-2370740;
SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to foci
of DNA damage in S-phase cells.
TISSUE SPECIFICITY: Widely expressed.
DEVELOPMENTAL STAGE: Expressed in S phase and G2 phase.
INDUCTION: Up-regulated in cells treated with agents that damage
DNA or block replication. This up-regulation seems to be
independent of transcription.
SIMILARITY: Belongs to the XPF family.
SIMILARITY: Contains 1 ERCC4 domain.
SEQUENCE CAUTION:
Sequence=BAB14953.1; Type=Erroneous initiation;
Links to other databases:
Protein sequence:
MAAPVRLGRKRPLPACPNPLFVRWLTEWRDEATRSRRRTRFVFQKALRSL
RRYPLPLRSGKEAKILQHFGDGLCRMLDERLQRHRTSGGDHAPDSPSGEN
SPAPQGRLAEVQDSSMPVPAQPKAGGSGSYWPARHSGARVILLVLYREHL
NPNGHHFLTKEELLQRCAQKSPRVAPGSARPWPALRSLLHRNLVLRTHQP
ARYSLTPEGLELAQKLAESEGLSLLNVGIGPKEPPGEETAVPGAASAELA
SEAGVQQQPLELRPGEYRVLLCVDIGETRGGGHRPELLRELQRLHVTHTV
RKLHVGDFVWVAQETNPRDPANPGELVLDHIVERKRLDDLCSSIIDGRFR
EQKFRLKRCGLERRVYLVEEHGSVHNLSLPESTLLQAVTNTQVIDGFFVK
RTADIKESAAYLALLTRGLQRLYQGHTLRSRPWGTPGNPESGAMTSPNPL
CSLLTFSDFNAGAIKNKAQSVREVFARQLMQVRGVSGEKAAALVDRYSTP
ASLLAAYDACATPKEQETLLSTIKCGRLQRNLGPALSRTLSQLYCSYGPL
T
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MUS81 (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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Human Mus81-associated endonuclease cleaves Holliday junctions in vitro.
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Chen XB, Melchionna R, Denis CM, Gaillard PH, Blasina A, Van de Weyer I, Boddy MN, Russell P, Vialard J, McGowan CH
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Mol Cell
Nov. 1, 2001
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Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities.
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Constantinou A, Chen XB, McGowan CH, West SC
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EMBO J
Oct. 15, 2002
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Identification and characterization of human MUS81-MMS4 structure-specific endonuclease.
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Ogrunc M, Sancar A
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J Biol Chem
June 13, 2003
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Identification and characterization of the human mus81-eme1 endonuclease.
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Ciccia A, Constantinou A, West SC
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J Biol Chem
July 4, 2003
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Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in human S-phase cells.
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Gao H, Chen XB, McGowan CH
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Mol Biol Cell
Dec. 1, 2003
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RNA interference inhibition of Mus81 reduces mitotic recombination in human cells.
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Blais V, Gao H, Elwell CA, Boddy MN, Gaillard PH, Russell P, McGowan CH
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Mol Biol Cell
Jan. 1, 2004
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
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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 TO, 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
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Nat Genet
Feb. 1, 2004
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
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Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J
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Genome Res
Oct. 1, 2004
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BLM helicase facilitates Mus81 endonuclease activity in human cells.
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Zhang R, Sengupta S, Yang Q, Linke SP, Yanaihara N, Bradsher J, Blais V, McGowan CH, Harris CC
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Cancer Res
April 1, 2005
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Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM.
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Ciccia A, Ling C, Coulthard R, Yan Z, Xue Y, Meetei AR, Laghmani el H, Joenje H, McDonald N, de Winter JP, Wang W, West SC
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Mol Cell
Jan. 9, 2007
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Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
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Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd
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J Proteome Res
March 1, 2008
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Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair.
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Svendsen JM, Smogorzewska A, Sowa ME, O'Connell BC, Gygi SP, Elledge SJ, Harper JW
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Cell
July 10, 2009
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Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair.
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Munoz IM, Hain K, Declais AC, Gardiner M, Toh GW, Sanchez-Pulido L, Heuckmann JM, Toth R, Macartney T, Eppink B, Kanaar R, Ponting CP, Lilley DM, Rouse J
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Mol Cell
July 10, 2009
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Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases.
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Fekairi S, Scaglione S, Chahwan C, Taylor ER, Tissier A, Coulon S, Dong MQ, Ruse C, Yates JR 3rd, Russell P, Fuchs RP, McGowan CH, Gaillard PH
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Cell
July 10, 2009
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Last modification of this entry: Oct. 13, 2010.
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