Welcome! Click here to login or here to register.
Home
Proteins
DNA damage
Diseases
Homologs
Pathways
Keywords
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

MUS81

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;


NCBI GenPept GI number(s): 156151413
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q96NY9 Q96NY9
PFAM: - Q96NY9 (Link - using uniprot id)
InterPro: - Q96NY9 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MAAPVRLGRKRPLPACPNPLFVRWLTEWRDEATRSRRRTRFVFQKALRSL
RRYPLPLRSGKEAKILQHFGDGLCRMLDERLQRHRTSGGDHAPDSPSGEN
SPAPQGRLAEVQDSSMPVPAQPKAGGSGSYWPARHSGARVILLVLYREHL
NPNGHHFLTKEELLQRCAQKSPRVAPGSARPWPALRSLLHRNLVLRTHQP
ARYSLTPEGLELAQKLAESEGLSLLNVGIGPKEPPGEETAVPGAASAELA
SEAGVQQQPLELRPGEYRVLLCVDIGETRGGGHRPELLRELQRLHVTHTV
RKLHVGDFVWVAQETNPRDPANPGELVLDHIVERKRLDDLCSSIIDGRFR
EQKFRLKRCGLERRVYLVEEHGSVHNLSLPESTLLQAVTNTQVIDGFFVK
RTADIKESAAYLALLTRGLQRLYQGHTLRSRPWGTPGNPESGAMTSPNPL
CSLLTFSDFNAGAIKNKAQSVREVFARQLMQVRGVSGEKAAALVDRYSTP
ASLLAAYDACATPKEQETLLSTIKCGRLQRNLGPALSRTLSQLYCSYGPL
T

MUS81 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Human Mus81-associated endonuclease cleaves Holliday junctions in vitro. Chen XB, Melchionna R, Denis CM, Gaillard PH, Blasina A, Van de Weyer I, Boddy MN, Russell P, Vialard J, McGowan CH Mol Cell Nov. 1, 2001
Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities. Constantinou A, Chen XB, McGowan CH, West SC EMBO J Oct. 15, 2002
Identification and characterization of human MUS81-MMS4 structure-specific endonuclease. Ogrunc M, Sancar A J Biol Chem June 13, 2003
Identification and characterization of the human mus81-eme1 endonuclease. Ciccia A, Constantinou A, West SC J Biol Chem July 4, 2003
Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in human S-phase cells. Gao H, Chen XB, McGowan CH Mol Biol Cell Dec. 1, 2003
RNA interference inhibition of Mus81 reduces mitotic recombination in human cells. Blais V, Gao H, Elwell CA, Boddy MN, Gaillard PH, Russell P, McGowan CH Mol Biol Cell Jan. 1, 2004
Complete sequencing and characterization of 21,243 full-length human cDNAs. 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 Nat Genet Feb. 1, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). 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 Genome Res Oct. 1, 2004
BLM helicase facilitates Mus81 endonuclease activity in human cells. Zhang R, Sengupta S, Yang Q, Linke SP, Yanaihara N, Bradsher J, Blais V, McGowan CH, Harris CC Cancer Res April 1, 2005
Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM. 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 Mol Cell Jan. 9, 2007
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res March 1, 2008
Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair. Svendsen JM, Smogorzewska A, Sowa ME, O'Connell BC, Gygi SP, Elledge SJ, Harper JW Cell July 10, 2009
Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair. 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 Mol Cell July 10, 2009
Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases. 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 Cell July 10, 2009


Last modification of this entry: Oct. 13, 2010.

Add your own comment!

There is no comment yet.
Welcome stranger! Click here to login or here to register.
Valid HTML 4.01! This site is Emacs powered. Made with Django.