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Protein

DNA mismatch repair protein MLH3

Gene

MLH3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA mismatch repair (MMR), correcting insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLbeta heterodimer, which probably forms a ternary complex with the MutSbeta heterodimer that initially recognizes the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in promoting meiotic crossing-over and is involved in maintaining the genetic stability of simple sequence repeats by correction of frameshift intermediates.3 Publications

GO - Molecular functioni

  1. ATPase activity Source: SGD
  2. ATP binding Source: InterPro

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. meiotic mismatch repair Source: SGD
  3. mismatch repair Source: SGD
  4. reciprocal meiotic recombination Source: SGD
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-34060-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA mismatch repair protein MLH3
Alternative name(s):
MutL protein homolog 3
Gene namesi
Name:MLH3
Ordered Locus Names:YPL164C
ORF Names:P2550
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL164c.
SGDiS000006085. MLH3.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. MutLgamma complex Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715DNA mismatch repair protein MLH3PRO_0000245570Add
BLAST

Proteomic databases

MaxQBiQ12083.

Expressioni

Gene expression databases

GenevestigatoriQ12083.

Interactioni

Subunit structurei

Heterodimer of MLH1 and MLH3, called MutLbeta, which is involved in correction of a specific subset of IDLs when associated with MutSbeta. Forms a ternary complex with a SGS1-TOP3 heterodimer during meiosis.

Binary interactionsi

WithEntry#Exp.IntActNotes
MLH1P389204EBI-31634,EBI-11003

Protein-protein interaction databases

BioGridi36019. 10 interactions.
DIPiDIP-2414N.
IntActiQ12083. 3 interactions.
MINTiMINT-678752.
STRINGi4932.YPL164C.

Structurei

3D structure databases

ProteinModelPortaliQ12083.
SMRiQ12083. Positions 26-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0323.
GeneTreeiENSGT00550000074903.
HOGENOMiHOG000113600.
InParanoidiQ12083.
KOiK08739.
OMAiRIRVERY.
OrthoDBiEOG77Q552.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR028830. Mlh3.
IPR014790. MutL_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10073:SF7. PTHR10073:SF7. 1 hit.
PfamiPF08676. MutL_C. 1 hit.
[Graphical view]
SMARTiSM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12083-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQHIRKLDS DVSERLKSQA CTVSLASAVR EIVQNSVDAH ATTIDVMIDL
60 70 80 90 100
PNLSFAVYDD GIGLTRSDLN ILATQNYTSK IRKMNDLVTM KTYGYRGDAL
110 120 130 140 150
YSISNVSNLF VCSKKKDYNS AWMRKFPSKS VMLSENTILP IDPFWKICPW
160 170 180 190 200
SRTKSGTVVI VEDMLYNLPV RRRILKEEPP FKTFNTIKAD MLQILVMHPM
210 220 230 240 250
ISLNVQYTDK LRINTEVLFR SKNITEGLTK HQQMSQVLRN VFGAIIPPDM
260 270 280 290 300
LKKVSLKFNE YQIEGIISKM PVGLKDLQFI YINGRRYADS AFQGYVDSLF
310 320 330 340 350
QAQDFGEKGM SLLKTKSVGK PYRSHPVFIL DVRCPQTIDD LLQDPAKKIV
360 370 380 390 400
KPSHIRTIEP LIVKTIRSFL TFQGYLTPDK SDSSFEIVNC SQKTATLPDS
410 420 430 440 450
RIQISKRNQV LNSKMKIARI NSYIGKPAVN GCRINNSTIN YEKIKNIRID
460 470 480 490 500
GQKSRLRNKL SSRPYDSGFT EDYDSIGKTI TDFSISRSVL AKYEVINQVD
510 520 530 540 550
KKFILIRCLD QSIHNCPLLV LVDQHACDER IRLEELFYSL LTEVVTGTFV
560 570 580 590 600
ARDLKDCCIE VDRTEADLFK HYQSEFKKWG IGYETIEGTM ETSLLEIKTL
610 620 630 640 650
PEMLTSKYNG DKDYLKMVLL QHAHDLKDFK KLPMDLSHFE NYTSVDKLYW
660 670 680 690 700
WKYSSCVPTV FHEILNSKAC RSAVMFGDEL TRQECIILIS KLSRCHNPFE
710
CAHGRPSMVP IAELK
Length:715
Mass (Da):82,001
Last modified:November 1, 1996 - v1
Checksum:i970FD7F57EB6E3B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96770 Genomic DNA. Translation: CAA65557.1.
Z73520 Genomic DNA. Translation: CAA97869.1.
BK006949 Genomic DNA. Translation: DAA11270.1.
PIRiS65175.
RefSeqiNP_015161.1. NM_001183978.1.

Genome annotation databases

EnsemblFungiiYPL164C; YPL164C; YPL164C.
GeneIDi855939.
KEGGisce:YPL164C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96770 Genomic DNA. Translation: CAA65557.1.
Z73520 Genomic DNA. Translation: CAA97869.1.
BK006949 Genomic DNA. Translation: DAA11270.1.
PIRiS65175.
RefSeqiNP_015161.1. NM_001183978.1.

3D structure databases

ProteinModelPortaliQ12083.
SMRiQ12083. Positions 26-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36019. 10 interactions.
DIPiDIP-2414N.
IntActiQ12083. 3 interactions.
MINTiMINT-678752.
STRINGi4932.YPL164C.

Proteomic databases

MaxQBiQ12083.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL164C; YPL164C; YPL164C.
GeneIDi855939.
KEGGisce:YPL164C.

Organism-specific databases

CYGDiYPL164c.
SGDiS000006085. MLH3.

Phylogenomic databases

eggNOGiCOG0323.
GeneTreeiENSGT00550000074903.
HOGENOMiHOG000113600.
InParanoidiQ12083.
KOiK08739.
OMAiRIRVERY.
OrthoDBiEOG77Q552.

Enzyme and pathway databases

BioCyciYEAST:G3O-34060-MONOMER.

Miscellaneous databases

NextBioi980696.
PROiQ12083.

Gene expression databases

GenevestigatoriQ12083.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR003594. HATPase_C.
IPR028830. Mlh3.
IPR014790. MutL_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10073:SF7. PTHR10073:SF7. 1 hit.
PfamiPF08676. MutL_C. 1 hit.
[Graphical view]
SMARTiSM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators."
    Purnelle B., Coster F., Goffeau A.
    Yeast 12:1483-1492(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations."
    Flores-Rozas H., Kolodner R.D.
    Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLH1.
  5. "Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction."
    Wang T.-F., Kleckner N., Hunter N.
    Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MLH1.
  6. "Discrete in vivo roles for the MutL homologs Mlh2p and Mlh3p in the removal of frameshift intermediates in budding yeast."
    Harfe B.D., Minesinger B.K., Jinks-Robertson S.
    Curr. Biol. 10:145-148(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Supercomplex formation between Mlh1-Mlh3 and Sgs1-Top3 heterocomplexes in meiotic yeast cells."
    Wang T.-F., Kung W.M.
    Biochem. Biophys. Res. Commun. 296:949-953(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGS1.

Entry informationi

Entry nameiMLH3_YEAST
AccessioniPrimary (citable) accession number: Q12083
Secondary accession number(s): D6W3K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.