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Description:
DNA mismatch repair protein Msh3 (Divergent upstream protein) (DUP)(Mismatch repair protein 1) (MRP1).
Molecular weight: 1274
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) mismatch repair( GO:0006298 )
Important dates:
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
07-FEB-2006, entry version 44.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein MSH3_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | J04810 | AAB47281.1 | - |
| EMBL | U61981 | AAB06045.1 | - |
| EMBL | D61419 | BAD27111.1 | - |
| EMBL | AY275681 | AAP13535.1 | - |
| EMBL | BC011817 | AAH11817.1 | ALT_TERM |
| PIR | A33507 | A33507. | |
| HSSP | P23909 | 1NG9 | |
| Ensembl | ENSG00000113318 | Homo sapiens.1 | |
| HGNC | HGNC:7326 | MSH3.1 | |
| MIM | 600887 | gene. | |
| MIM | 608089 | phenotype. | |
| GO | GO:0006298 | P:mismatch repair | TAS. |
| InterPro | IPR000432 | MutS_C. | |
| InterPro | IPR007860 | MutS_II. | |
| InterPro | IPR007696 | MutS_III. | |
| InterPro | IPR007695 | MutS_N. | |
| Pfam | PF01624 | MutS_I | 1. |
| Pfam | PF05188 | MutS_II | 1. |
| Pfam | PF05192 | MutS_III | 1. |
| Pfam | PF00488 | MutS_V | 1. |
| ProDom | PD001263 | MutS_C | 1. |
| SMART | SM00534 | MUTSac | 1. |
| SMART | SM00533 | MUTSd | 1. |
| PROSITE | PS00486 | DNA_MISMATCH_REPAIR_2 | 1. |
Keywords:
ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding; Polymorphism.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX MEDLINE=89255490; PubMed=2722860;
RA Fujii H., Shimada T.;
RT "Isolation and characterization of cDNA clones derived from the
RT divergently transcribed gene in the region upstream from the human
RT dihydrofolate reductase gene.";
RL J. Biol. Chem. 264:10057-10064(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS 57-ALA--ALA-65 DEL AND
RP ALA-1045.
RX MEDLINE=97098445; PubMed=8942985; DOI=10.1073/pnas.93.24.13629;
RA Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S.,
RA Marsischky G.T., Kolodner R.D., Fishel R.;
RT "hMSH2 forms specific mispair-binding complexes with hMSH3 and
RT hMSH6.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shimada T., Ikejima M., Watanabe A., Orimo H.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-ALA-ALA-62 INS;
RP ILE-79; LEU-709; GLN-949 AND ALA-1045.
RA Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W.,
RA Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D.,
RA Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-852, AND VARIANT
RP 57-ALA--ALA-65 DEL.
RC TISSUE=Muscle;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [6]
RP INTERACTION WITH EXO1.
RX PubMed=11427529; DOI=10.1074/jbc.M102670200;
RA Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R.;
RT "The interaction of DNA mismatch repair proteins with human
RT exonuclease I.";
RL J. Biol. Chem. 276:33011-33018(2001).
RN [7]
RP VARIANT ALA-ALA-ALA-62 INS.
RX MEDLINE=97004459; PubMed=8851770;
RA Nakajima E., Orimo H., Ikejima M., Shimada T.;
RT "Nine-bp repeat polymorphism in exon 1 of the hMSH3 gene.";
RL Jpn. J. Hum. Genet. 40:343-345(1995).
RN [8]
RP VARIANTS ILE-79 AND ALA-1045.
RX MEDLINE=20401150; PubMed=10944853; DOI=10.1007/s100380070031;
RA Orimo H., Nakajima E., Yamamoto M., Ikejima M., Emi M., Shimada T.;
RT "Association between single nucleotide polymorphisms in the hMSH3 gene
RT and sporadic colon cancer with microsatellite instability.";
RL J. Hum. Genet. 45:228-230(2000).
Feature:
CHAIN 1 1137 DNA mismatch repair protein Msh3.
/FTId=PRO_0000115192.
NP_BIND 896 903 ATP (Potential).
REGION 75 297 Interaction with EXO1.
COMPBIAS 51 62 Poly-Ala.
VARIANT 57 65 Missing.
/FTId=VAR_020934.
VARIANT 62 62 A -> AAAA.
/FTId=VAR_020935.
VARIANT 79 79 V -> I.
/FTId=VAR_020936.
VARIANT 709 709 F -> L (in dbSNP:1805354).
/FTId=VAR_016160.
VARIANT 949 949 R -> Q (in dbSNP:184967).
/FTId=VAR_016161.
VARIANT 1045 1045 T -> A (in dbSNP:26279).
/FTId=VAR_016162.
VARIANT 1054 1054 T -> A (in dbSNP:1805131).
/FTId=VAR_016163.
CONFLICT 622 622 E -> G (in Ref. 1 and 3).
Comments:
-!- FUNCTION: Probable DNA-repair protein.
-!- SUBUNIT: Interacts with EXO1.
-!- DISEASE: Defects in MSH3 are a cause of susceptibility to
endometrial cancer [MIM:608089].
-!- SIMILARITY: Belongs to the DNA mismatch repair mutS family.
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Sequence length: 1137
MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG AAAAAAAAAA
AAPPAPPAPA FPPQLPPHVA TEIDRRKKRP LENDGPVKKK VKKVQQKEGG SDLGMSGNSE
PKKCLRTRNV SKSLEKLKEF CCDSALPQSR VQTESLQERF AVLPKCTDFD DISLLHAKNA
VSSEDSKRQI NQKDTTLFDL SQFGSSNTSH ENLQKTASKS ANKRSKSIYT PLELQYIEMK
QQHKDAVLCV ECGYKYRFFG EDAEIAAREL NIYCHLDHNF MTASIPTHRL FVHVRRLVAK
GYKVGVVKQT ETAALKAIGD NRSSLFSRKL TALYTKSTLI GEDVNPLIKL DDAVNVDEIM
TDTSTSYLLC ISENKENVRD KKKGNIFIGI VGVQPATGEV VFDSFQDSAS RSELETRMSS
LQPVELLLPS ALSEQTEALI HRATSVSVQD DRIRVERMDN IYFEYSHAFQ AVTEFYAKDT
VDIKGSQIIS GIVNLEKPVI CSLAAIIKYL KEFNLEKMLS KPENFKQLSS KMEFMTINGT
TLRNLEILQN QTDMKTKGSL LWVLDHTKTS FGRRKLKKWV TQPLLKLREI NARLDAVSEV
LHSESSVFGQ IENHLRKLPD IERGLCSIYH KKCSTQEFFL IVKTLYHLKS EFQAIIPAVN
SHIQSDLLRT VILEIPELLS PVEHYLKILN EQAAKVGDKT ELFKDLSDFP LIKKRKDEIQ
GVIDEIRMHL QEIRKILKNP SAQYVTVSGQ EFMIEIKNSA VSCIPTDWVK VGSTKAVSRF
HSPFIVENYR HLNQLREQLV LDCSAEWLDF LEKFSEHYHS LCKAVHHLAT VDCIFSLAKV
AKQGDYCRPT VQEERKIVIK NGRHPVIDVL LGEQDQYVPN NTDLSEDSER VMIITGPNMG
GKSSYIKQVA LITIMAQIGS YVPAEEATIG IVDGIFTRMG AADNIYKGRS TFMEELTDTA
EIIRKATSQS LVILDELGRG TSTHDGIAIA YATLEYFIRD VKSLTLFVTH YPPVCELEKN
YSHQVGNYHM GFLVSEDESK LDPGTAEQVP DFVTFLYQIT RGIAARSYGL NVAKLADVPG
EILKKAAHKS KELEGLINTK RKRLKYFAKL WTMHNAQDLQ KWTEEFNMEE TQTSLLH