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MSH3

Protein FULL name:

mutS homolog 3 [Homo sapiens].


MSH3 (Homo sapiens) is product of expression of MSH3 gene.

Human diseases related to this protein:

MSH3 is involved in:

MMR in Homo sapiens
     


Keywords:



FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion- deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis.

SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a ternary complex with MutL alpha (MLH1-PMS1). Interacts with EXO1.

INTERACTION: P43246:MSH2; NbExp=1; IntAct=EBI-1164205, EBI-355888;

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

DISEASE: Defects in MSH3 are a cause of susceptibility to endometrial cancer [MIM:608089].

SIMILARITY: Belongs to the DNA mismatch repair mutS family. MSH3 subfamily.

SEQUENCE CAUTION: Sequence=AAH11817.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;

WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; [LINK]

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 68303635
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P20585 P20585
PFAM: - P20585 (Link - using uniprot id)
InterPro: - P20585 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MSRRKPASGGLAASSSAPARQAVLSRFFQSTGSLKSTSSSTGAADQVDPG
AAAAAAAAAAAAPPAPPAPAFPPQLPPHIATEIDRRKKRPLENDGPVKKK
VKKVQQKEGGSDLGMSGNSEPKKCLRTRNVSKSLEKLKEFCCDSALPQSR
VQTESLQERFAVLPKCTDFDDISLLHAKNAVSSEDSKRQINQKDTTLFDL
SQFGSSNTSHENLQKTASKSANKRSKSIYTPLELQYIEMKQQHKDAVLCV
ECGYKYRFFGEDAEIAARELNIYCHLDHNFMTASIPTHRLFVHVRRLVAK
GYKVGVVKQTETAALKAIGDNRSSLFSRKLTALYTKSTLIGEDVNPLIKL
DDAVNVDEIMTDTSTSYLLCISENKENVRDKKKGNIFIGIVGVQPATGEV
VFDSFQDSASRSELETRMSSLQPVELLLPSALSEQTEALIHRATSVSVQD
DRIRVERMDNIYFEYSHAFQAVTEFYAKDTVDIKGSQIISGIVNLEKPVI
CSLAAIIKYLKEFNLEKMLSKPENFKQLSSKMEFMTINGTTLRNLEILQN
QTDMKTKGSLLWVLDHTKTSFGRRKLKKWVTQPLLKLREINARLDAVSEV
LHSESSVFGQIENHLRKLPDIERGLCSIYHKKCSTQEFFLIVKTLYHLKS
EFQAIIPAVNSHIQSDLLRTVILEIPELLSPVEHYLKILNEQAAKVGDKT
ELFKDLSDFPLIKKRKDEIQGVIDEIRMHLQEIRKILKNPSAQYVTVSGQ
EFMIEIKNSAVSCIPTDWVKVGSTKAVSRFHSPFIVENYRHLNQLREQLV
LDCSAEWLDFLEKFSEHYHSLCKAVHHLATVDCIFSLAKVAKQGDYCRPT
VQEERKIVIKNGRHPVIDVLLGEQDQYVPNNTDLSEDSERVMIITGPNMG
GKSSYIKQVALITIMAQIGSYVPAEEATIGIVDGIFTRMGAADNIYKGRS
TFMEELTDTAEIIRKATSQSLVILDELGRGTSTHDGIAIAYATLEYFIRD
VKSLTLFVTHYPPVCELEKNYSHQVGNYHMGFLVSEDESKLDPGAAEQVP
DFVTFLYQITRGIAARSYGLNVAKLADVPGEILKKAAHKSKELEGLINTK
RKRLKYFAKLWTMHNAQDLQKWTEEFNMEETQTSLLH

MSH3 (Homo sapiens) is able to recognize following damages:
MSH3 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Isolation and characterization of cDNA clones derived from the divergently transcribed gene in the region upstream from the human dihydrofolate reductase gene. Fujii H, Shimada T J Biol Chem June 15, 1989
Nine-bp repeat polymorphism in exon 1 of the hMSH3 gene. Nakajima E, Orimo H, Ikejima M, Shimada T Jpn J Hum Genet Dec. 1, 1995
hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6. Acharya S, Wilson T, Gradia S, Kane MF, Guerrette S, Marsischky GT, Kolodner R, Fishel R Proc Natl Acad Sci U S A Nov. 26, 1996
Association between single nucleotide polymorphisms in the hMSH3 gene and sporadic colon cancer with microsatellite instability. Orimo H, Nakajima E, Yamamoto M, Ikejima M, Emi M, Shimada T J Hum Genet Jan. 1, 2000
The interaction of DNA mismatch repair proteins with human exonuclease I. Schmutte C, Sadoff MM, Shim KS, Acharya S, Fishel R J Biol Chem Aug. 31, 2001
The DNA sequence and comparative analysis of human chromosome 5. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM Nature Sept. 16, 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
Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z EMBO J Nov. 1, 2006
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007


Last modification of this entry: Nov. 11, 2010.

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