| General Information |
| MoonProt ID | 132 |
| First appeared in release | 1.0 |
| Name(s) | Mismatch repair endonuclease PMS2
Mismatch repair endonuclease PMS2
Alternative name(s):
DNA mismatch repair protein PMS2
PMS1 protein homolog 2
Gene names
Name: Pms2 |
| UniProt ID | P54279 (PMS2_MOUSE) Reviewed |
| GO terms | GO:0006200 ATP catabolic process
GO:0006281 DNA repair
GO:0006298 mismatch repair
GO:0006974 cellular response to DNA damage stimulus
GO:0007126 meiotic nuclear division
GO:0007131 reciprocal meiotic recombination
GO:0016446 somatic hypermutation of immunoglobulin genes
GO:0016447 somatic recombination of immunoglobulin gene segments
GO:0090305 nucleic acid phosphodiester bond hydrolysis
GO:0003697 single-stranded DNA binding
GO:0004518 nuclease activity
GO:0004519 endonuclease activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATPase activity
GO:0030983 mismatched DNA binding
GO:0032407 MutSalpha complex binding
GO:0005634 nucleus
GO:0032389 MutLalpha complex |
| Organisms for which functions have been demonstrated | Mus musculus |
| Sequence length | 859 |
| FASTA sequence | >sp|P54279|PMS2_MOUSE Mismatch repair endonuclease PMS2 OS=Mus musculus GN=Pms2 PE=2 SV=1
MEQTEGVSTECAKAIKPIDGKSVHQICSGQVILSLSTAVKELIENSVDAGATTIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHGSASVGTRLVFDHNGKITQKTPYPRPKGTTVSVQHLFYTLPVRYKEFQRNIKKEYSKMVQVLQAYCIISAGVRVSCTNQLGQGKRHAVVCTSGTSGMKENIGSVFGQKQLQSLIPFVQLPPSDAVCEEYGLSTSGRHKTFSTFRASFHSARTAPGGVQQTGSFSSSIRGPVTQQRSLSLSMRFYHMYNRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFDSDANKLNVNQQPLLDVEGNLVKLHTAELEKPVPGKQDNSPSLKSTADEKRVASISRLREAFSLHPTKEIKSRGPETAELTRSFPSEKRGVLSSYPSDVISYRGLRGSQDKLVSPTDSPGDCMDREKIEKDSGLSSTSAGSEEEFSTPEVASSFSSDYNVSSLEDRPSQETINCGDLDCRPPGTGQSLKPEDHGYQCKALPLARLSPTNAKRFKTEERPSNVNISQRLPGPQSTSAAEVDVAIKMNKRIVLLEFSLSSLAKRMKQLQHLKAQNKHELSYRKFRAKICPGENQAAEDELRKEISKSMFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTVLQAQRLITPQTLNLTAVNEAVLIENLEIFRKNGFDFVIDEDAPVTERAKLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCRPSRVRQMFASRACRKSVMIGTALNASEMKKLITHMGEMDHPWNCPHGRPTMRHVANLDVISQN |
| Structure Information |
| PDB ID | closest is human at 80% amino acid sequence identity |
| Quaternary structure | |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-13, 374-600, 625-660, 855-859 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | PMS2 mismatch repair enzyme
introduces single-strand breaks near the mismatch |
| References for function | S.M. Baker, C.E. Bronner, L. Zhang, et al. (1995) Male Mice Defective in the DNA Mismatch Repair Gene PMS2 Exhibit Abnormal Chromosome Synapsis in Meiosis. Cell. 82, 309-319. |
| E.C. number | 3.1.- - |
| Location of functional site(s) | |
| Cellular location of function | nucleus |
| Comments | Protein-DNA binding: Pro14, Pro15, Leu16, Gly37, Asp38, Phe39, Glu41, Leu56, Val57, Ser63, Lys64, Met70, Gly72, Pro74, Arg76, Gly106, Val108, Arg110, Lys439, Asn443, Val445, Thr453, Arg454, Gln468, Leu470, Lys471, Arg473, Arg475.
G. Obmolova, C. Ban, P. Hsieh and W. Yang. (2000) Crystal structure of mismatch repair protein MutS and its complex with a substrate DNA. Nature. 407, 703-710.
Nucleotide binding: Glu41, Asn45, Asp70, Thr155.
A. Guarne, M.S. Junop and W. Yang. (2001) Structure and function of the N-terminal 40kDa fragment of human PMS2: a monomeric GHL ATPase. The EMBO J. 20, 5521-5531.
DNA binding: Tyr868, Gly891.
S. Gupta, M. Gellert and W. Yang. (2012) Mechanism of mismatch recognition revealed by human MutS? bound to unpaired DNA loops. Nature. 19, 72-79.
DNA binding(from E.Coli, with 96% Query Cover and 30% Max Ident compared to human MSH3): Met33, Asp35, Phe36, Glu38.
M.H. Lamers, A. Perrakis, J.H. Enzlin, et al. (2000) Nature. 407, 711-717. |
| Function 2 |
| Function description | Hypermutation of antibody variable chains |
| References for function | D.B. Winter, Q.H. Phung, A Umar, et al. (1998) Altered spectra of hypermutation in antibodies from mice deficient for the DNA mismatch repair protein PMS2. Proc. Natl. Acad. Sci. 95, 6953-6958.
M. Wiesendanger, B. Kneitz, W. Edelmann, and M.D. Scharff. (2000) Somatic Hypermutation in MutS Homologue(MSH)3-, MSH6-, and MSH3/MSH6-deficient Mice Reveals a Role for the MSH2-MSH6 Heterodimer in Modulating the Base Sustitution Pattern. J. Exp. Med. 191, 579-584.
Z. Li, S.J. Scherer, D. Ronai, et al. (2004) Examination of Msh6- and Msh3- deficient Mice in Class Switching Reveals Overlapping and Distinct Roles of MutS Homologues in Antibody Diversification. J. Exp. Med. 200, 47-59.
C.E. Schrader, W. Edelmann, R. Kucherlapati, J. Stavnezer. (1999) Reduced Isotype Switching in Splenic B Cells from Mice Deficient in Mismatch Repair Enzymes. J. Exp. Med. 190, 323-330. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | nucleus |
| Comments | |