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DNA mismatch repair protein MLH1 (MutL protein homolog 1) (Post meiotic segregation protein 2)

 MLH1_YEAST              Reviewed;         769 AA.
P38920; D6VZY9; Q2I028; Q2I029; Q2I031; Q2I032; Q2I033; Q2I034;
Q2I035; Q2I036; Q2I038; Q2I039; Q2I041;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 171.
RecName: Full=DNA mismatch repair protein MLH1;
AltName: Full=MutL protein homolog 1;
AltName: Full=Post meiotic segregation protein 2;
Name=MLH1; Synonyms=PMS2; OrderedLocusNames=YMR167W;
ORFNames=YM8520.16;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8264608; DOI=10.1128/MCB.14.1.407;
Prolla T.A., Christie D.-M., Liskay R.M.;
"Dual requirement in yeast DNA mismatch repair for MLH1 and PMS1, two
homologs of the bacterial mutL gene.";
Mol. Cell. Biol. 14:407-415(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-240; GLU-242;
PRO-271; LEU-309; ASP-321; LYS-333; THR-375; GLY-452; ASN-465;
SER-470; PHE-607; ASN-678; LEU-703 AND GLY-761.
STRAIN=ATCC 200060 / W303, EAY1066, EAY1068, M2-8, M5-7, M7-8, SK1,
YJM 145, YJM 269, YJM 280, YJM 320, YJM 326, YJM 339, and YJM 627;
PubMed=16492773; DOI=10.1073/pnas.0510998103;
Heck J.A., Argueso J.L., Gemici Z., Reeves R.G., Bernard A.,
Aquadro C.F., Alani E.;
"Negative epistasis between natural variants of the Saccharomyces
cerevisiae MLH1 and PMS1 genes results in a defect in mismatch
repair.";
Proc. Natl. Acad. Sci. U.S.A. 103:3256-3261(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
MUTAGENESIS OF ALA-41; GLY-64; ILE-65; GLU-99; ILE-104; THR-114;
ARG-214; VAL-216; ARG-265; ILE-326; GLN-552; ARG-672 AND ALA-694.
PubMed=11555625; DOI=10.1093/hmg/10.18.1889;
Ellison A.R., Lofing J., Bitter G.A.;
"Functional analysis of human MLH1 and MSH2 missense variants and
hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae.";
Hum. Mol. Genet. 10:1889-1900(2001).
[6]
INTERACTION WITH PMS1, AND MUTAGENESIS OF ALA-41; PHE-96; ARG-97;
GLY-98; LYS-764; PHE-766; GLU-767 AND CYS-769.
PubMed=9234704; DOI=10.1128/MCB.17.8.4465;
Pang Q., Prolla T.A., Liskay R.M.;
"Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p
DNA mismatch repair proteins and their relevance to human hereditary
nonpolyposis colorectal cancer-associated mutations.";
Mol. Cell. Biol. 17:4465-4473(1997).
[7]
FUNCTION, AND SUBUNIT.
PubMed=9545323; DOI=10.1074/jbc.273.16.9837;
Habraken Y., Sung P., Prakash L., Prakash S.;
"ATP-dependent assembly of a ternary complex consisting of a DNA
mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes.";
J. Biol. Chem. 273:9837-9841(1998).
[8]
FUNCTION, AND INTERACTION WITH MLH2; MLH3 AND PMS1.
PubMed=10570173; DOI=10.1073/pnas.96.24.13914;
Wang T.-F., Kleckner N., Hunter N.;
"Functional specificity of MutL homologs in yeast: evidence for three
Mlh1-based heterocomplexes with distinct roles during meiosis in
recombination and mismatch correction.";
Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999).
[9]
INTERACTION WITH PMS1, ATP-BINDING, AND MUTAGENESIS OF GLU-31 AND
GLY-98.
PubMed=10938116; DOI=10.1128/MCB.20.17.6390-6398.2000;
Tran P.T., Liskay R.M.;
"Functional studies on the candidate ATPase domains of Saccharomyces
cerevisiae MutLalpha.";
Mol. Cell. Biol. 20:6390-6398(2000).
[10]
DNA-BINDING.
PubMed=12222686; DOI=10.1515/BC.2002.103;
Drotschmann K., Hall M.C., Shcherbakova P.V., Wang H., Erie D.A.,
Brownewell F.R., Kool E.T., Kunkel T.A.;
"DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1
heterodimers.";
Biol. Chem. 383:969-975(2002).
[11]
ATP-BINDING, MUTAGENESIS OF GLU-31 AND ASN-35, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=11717305; DOI=10.1074/jbc.M106120200;
Hall M.C., Shcherbakova P.V., Kunkel T.A.;
"Differential ATP binding and intrinsic ATP hydrolysis by amino-
terminal domains of the yeast Mlh1 and Pms1 proteins.";
J. Biol. Chem. 277:3673-3679(2002).
[12]
FUNCTION, AND MUTAGENESIS.
PubMed=12529393; DOI=10.1128/MCB.23.3.873-886.2003;
Argueso J.L., Kijas A.W., Sarin S., Heck J.A., Waase M., Alani E.;
"Systematic mutagenesis of the Saccharomyces cerevisiae MLH1 gene
reveals distinct roles for Mlh1p in meiotic crossing over and in
vegetative and meiotic mismatch repair.";
Mol. Cell. Biol. 23:873-886(2003).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[15]
DNA-BINDING, AND MUTAGENESIS OF ARG-273 AND ARG-274.
PubMed=12682353; DOI=10.1093/nar/gkg324;
Hall M.C., Shcherbakova P.V., Fortune J.M., Borchers C.H., Dial J.M.,
Tomer K.B., Kunkel T.A.;
"DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch
repair.";
Nucleic Acids Res. 31:2025-2034(2003).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Required for DNA mismatch repair (MMR), correcting base-
base mismatches and insertion-deletion loops (IDLs) resulting from
DNA replication, DNA damage or from recombination events between
non-identical sequences during meiosis. Component of different
MutL heterodimers that form a ternary complex with the MutS
heterodimers, which initially recognize 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 maintaining the genetic
stability of simple sequence repeats, the repair of heteroduplex
sites present in meiotic recombination intermediates, and the
promotion of meiotic crossing-over. {ECO:0000269|PubMed:10570173,
ECO:0000269|PubMed:12529393, ECO:0000269|PubMed:9545323}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=69 uM for ATP {ECO:0000269|PubMed:11717305};
-!- SUBUNIT: Heterodimer of MLH1 and PMS1, called MutLalpha, which is
the major MMR MutL activity correcting base-base mismatches as
well as IDLs. The heterodimer binds double strand DNA
independently of a mismatch with positive cooperativity and has
more than one DNA binding site. Forms a ternary complex with
either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer
(MutSbeta), which recognize and bind to mismatch DNA. Ternary
complex formation is promoted by ATP binding. Heterodimer of MLH1
and MLH3, called MutLbeta, which is involved in correction of a
specific subset of IDLs when associated with MutSbeta. Heterodimer
of MLH1 and MLH2. {ECO:0000269|PubMed:9545323}.
-!- INTERACTION:
P39875:EXO1; NbExp=3; IntAct=EBI-11003, EBI-6738;
Q07980:MLH2; NbExp=5; IntAct=EBI-11003, EBI-33369;
Q12083:MLH3; NbExp=5; IntAct=EBI-11003, EBI-31634;
Q08214:NTG2; NbExp=3; IntAct=EBI-11003, EBI-12303;
P14242:PMS1; NbExp=12; IntAct=EBI-11003, EBI-13561;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
{ECO:0000305}.
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EMBL; U07187; AAA16835.1; -; Unassigned_DNA.
EMBL; DQ356633; ABC86937.1; -; Genomic_DNA.
EMBL; DQ356634; ABC86938.1; -; Genomic_DNA.
EMBL; DQ356635; ABC86939.1; -; Genomic_DNA.
EMBL; DQ356636; ABC86940.1; -; Genomic_DNA.
EMBL; DQ356637; ABC86941.1; -; Genomic_DNA.
EMBL; DQ356638; ABC86942.1; -; Genomic_DNA.
EMBL; DQ356639; ABC86943.1; -; Genomic_DNA.
EMBL; DQ356640; ABC86944.1; -; Genomic_DNA.
EMBL; DQ356641; ABC86945.1; -; Genomic_DNA.
EMBL; DQ356642; ABC86946.1; -; Genomic_DNA.
EMBL; DQ356643; ABC86947.1; -; Genomic_DNA.
EMBL; DQ356644; ABC86948.1; -; Genomic_DNA.
EMBL; DQ356645; ABC86949.1; -; Genomic_DNA.
EMBL; DQ356646; ABC86950.1; -; Genomic_DNA.
EMBL; Z49705; CAA89803.1; -; Genomic_DNA.
EMBL; BK006946; DAA10063.1; -; Genomic_DNA.
PIR; S54525; S54525.
RefSeq; NP_013890.1; NM_001182671.1.
PDB; 4E4W; X-ray; 2.50 A; A=485-769.
PDB; 4FMN; X-ray; 2.69 A; A=485-769.
PDB; 4FMO; X-ray; 3.04 A; A=485-769.
PDBsum; 4E4W; -.
PDBsum; 4FMN; -.
PDBsum; 4FMO; -.
ProteinModelPortal; P38920; -.
SMR; P38920; -.
BioGrid; 35345; 213.
DIP; DIP-2412N; -.
IntAct; P38920; 17.
MINT; MINT-625234; -.
STRING; 4932.YMR167W; -.
iPTMnet; P38920; -.
MaxQB; P38920; -.
PRIDE; P38920; -.
EnsemblFungi; YMR167W; YMR167W; YMR167W.
GeneID; 855203; -.
KEGG; sce:YMR167W; -.
EuPathDB; FungiDB:YMR167W; -.
SGD; S000004777; MLH1.
GeneTree; ENSGT00800000124177; -.
InParanoid; P38920; -.
KO; K08734; -.
OMA; PWKWTVE; -.
OrthoDB; EOG092C22BC; -.
BioCyc; YEAST:G3O-32857-MONOMER; -.
Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
PRO; PR:P38920; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005712; C:chiasma; IBA:GO_Central.
GO; GO:0032389; C:MutLalpha complex; IPI:SGD.
GO; GO:0097587; C:MutLgamma complex; IPI:SGD.
GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblPlants.
GO; GO:0000795; C:synaptonemal complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IMP:SGD.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
GO; GO:0000713; P:meiotic heteroduplex formation; IMP:SGD.
GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
GO; GO:0006298; P:mismatch repair; IMP:SGD.
GO; GO:0006312; P:mitotic recombination; IEA:EnsemblPlants.
GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR013507; DNA_mismatch_repair_C.
InterPro; IPR014762; DNA_mismatch_repair_CS.
InterPro; IPR002099; DNA_mismatch_repair_fam.
InterPro; IPR011186; DNA_mismatch_repair_MLH1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR032189; Mlh1_C.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR10073:SF40; PTHR10073:SF40; 1.
Pfam; PF01119; DNA_mis_repair; 1.
Pfam; PF16413; Mlh1_C; 1.
SMART; SM01340; DNA_mis_repair; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
TIGRFAMs; TIGR00585; mutl; 1.
PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA damage; DNA repair; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 769 DNA mismatch repair protein MLH1.
/FTId=PRO_0000178008.
REGION 1 335 DNA- and ATP-binding.
REGION 501 756 Interaction with PMS1.
MOD_RES 441 441 Phosphoserine; by ATM or ATR.
{ECO:0000244|PubMed:18407956}.
VARIANT 240 240 S -> R (in strain: SK1).
{ECO:0000269|PubMed:16492773}.
VARIANT 242 242 D -> E (in strain: YJM326 and YJM339).
{ECO:0000269|PubMed:16492773}.
VARIANT 271 271 L -> P (in strain: EAY1066, EAY1068, M2-
8, M7-8, M5-7, SK1, YJM269, YJM280,
YJM320, YJM326, YJM339 and YJM627).
{ECO:0000269|PubMed:16492773}.
VARIANT 309 309 P -> L (in strain: M2-8).
{ECO:0000269|PubMed:16492773}.
VARIANT 321 321 E -> D (in strain: EAY1066).
{ECO:0000269|PubMed:16492773}.
VARIANT 333 333 E -> K (in strain: SK1).
{ECO:0000269|PubMed:16492773}.
VARIANT 375 375 A -> T (in strain: YJM339).
{ECO:0000269|PubMed:16492773}.
VARIANT 452 452 S -> G (in strain: EAY1068, M2-8, M7-8,
M5-7, YJM269 and YJM627).
{ECO:0000269|PubMed:16492773}.
VARIANT 465 465 D -> N (in strain: EAY1066 and YJM280).
{ECO:0000269|PubMed:16492773}.
VARIANT 470 470 P -> S (in strain: YJM339).
{ECO:0000269|PubMed:16492773}.
VARIANT 607 607 L -> F (in strain: EAY1068, M2-8, M7-8,
M5-7 and YJM627).
{ECO:0000269|PubMed:16492773}.
VARIANT 678 678 D -> N (in strain: SK1, YJM320 and
YJM339). {ECO:0000269|PubMed:16492773}.
VARIANT 703 703 P -> L (in strain: SK1, YJM320 and
YJM339). {ECO:0000269|PubMed:16492773}.
VARIANT 761 761 D -> G (in strain: EAY1066, EAY1068, M2-
8, M7-8, M5-7, SK1, YJM145, YJM269,
YJM320, YJM339 and YJM627; forms a non-
functional heterodimer with PMS1 from
strain S288c, resulting in an
accumulation of mutations in spore
progeny of crosses between these
strains). {ECO:0000269|PubMed:16492773}.
MUTAGEN 31 31 E->A: Reduces ATPase activity by 98%.
Displays 3300-fold increase in
spontaneous mutation accumulation.
{ECO:0000269|PubMed:10938116,
ECO:0000269|PubMed:11717305}.
MUTAGEN 35 35 N->A: Abolishes ATP binding, reducing
ATPase activity by 95%. Displays 9800-
fold increase in spontaneous mutation
accumulation.
{ECO:0000269|PubMed:11717305}.
MUTAGEN 41 41 A->F: Defective in a mismatch repair
assay. Abolishes heterodimer formation.
Displays an increases spontaneous
mutation accumulation.
{ECO:0000269|PubMed:11555625,
ECO:0000269|PubMed:9234704}.
MUTAGEN 41 41 A->G: Reduces heterodimer formation.
Displays an weak increase in spontaneous
mutation accumulation.
{ECO:0000269|PubMed:11555625,
ECO:0000269|PubMed:9234704}.
MUTAGEN 41 41 A->S: Fully functional in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625,
ECO:0000269|PubMed:9234704}.
MUTAGEN 64 64 G->R: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 65 65 I->N: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 96 96 F->A: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 97 97 R->A: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 98 98 G->A: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:10938116,
ECO:0000269|PubMed:9234704}.
MUTAGEN 98 98 G->V: Abolishes heterodimer formation.
Displays an increase in spontaneous
mutation accumulation.
{ECO:0000269|PubMed:10938116,
ECO:0000269|PubMed:9234704}.
MUTAGEN 99 99 E->K: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 104 104 I->R: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 114 114 T->R: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 214 214 R->C: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 216 216 V->I: Fully functional in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 265 265 R->C: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 265 265 R->H: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 273 273 R->E: Strongly reduces DNA-binding and
displays 12000-fold increase in
spontaneous mutation accumulation; when
associated with E-274.
{ECO:0000269|PubMed:12682353}.
MUTAGEN 274 274 R->E: Reduces DNA-binding and displays a
1700-fold increase in spontaneous
mutation accumulation. Strongly reduces
DNA-binding and displays 12000-fold
increase in spontaneous mutation
accumulation; when associated with E-273.
{ECO:0000269|PubMed:12682353}.
MUTAGEN 326 326 I->A: Partially defective in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 326 326 I->V: Fully functional in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 552 552 Q->L: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 672 672 R->P: Defective in a mismatch repair
assay. {ECO:0000269|PubMed:11555625}.
MUTAGEN 694 694 A->T: Fully functional in a mismatch
repair assay.
{ECO:0000269|PubMed:11555625}.
MUTAGEN 764 764 K->E: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 764 764 K->R: No effect.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 766 766 F->A: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 767 767 E->D: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 769 769 C->A: No effect.
{ECO:0000269|PubMed:9234704}.
MUTAGEN 769 769 C->S: Displays an increase in spontaneous
mutation accumulation. Does not impair
heterodimer formation.
{ECO:0000269|PubMed:9234704}.
CONFLICT 258 258 P -> L (in Ref. 1; AAA16835).
{ECO:0000305}.
CONFLICT 288 288 N -> F (in Ref. 1; AAA16835).
{ECO:0000305}.
CONFLICT 708 708 S -> L (in Ref. 1; AAA16835).
{ECO:0000305}.
HELIX 512 524 {ECO:0000244|PDB:4E4W}.
HELIX 527 534 {ECO:0000244|PDB:4E4W}.
STRAND 537 543 {ECO:0000244|PDB:4E4W}.
TURN 544 547 {ECO:0000244|PDB:4E4W}.
STRAND 548 553 {ECO:0000244|PDB:4E4W}.
STRAND 556 561 {ECO:0000244|PDB:4E4W}.
HELIX 562 577 {ECO:0000244|PDB:4E4W}.
STRAND 582 585 {ECO:0000244|PDB:4E4W}.
HELIX 591 593 {ECO:0000244|PDB:4E4W}.
HELIX 597 601 {ECO:0000244|PDB:4E4W}.
HELIX 610 622 {ECO:0000244|PDB:4E4W}.
HELIX 624 631 {ECO:0000244|PDB:4E4W}.
STRAND 634 639 {ECO:0000244|PDB:4E4W}.
HELIX 644 646 {ECO:0000244|PDB:4E4W}.
STRAND 647 654 {ECO:0000244|PDB:4E4W}.
HELIX 666 675 {ECO:0000244|PDB:4E4W}.
HELIX 682 697 {ECO:0000244|PDB:4E4W}.
HELIX 714 733 {ECO:0000244|PDB:4E4W}.
HELIX 735 742 {ECO:0000244|PDB:4E4W}.
HELIX 747 752 {ECO:0000244|PDB:4E4W}.
STRAND 753 758 {ECO:0000244|PDB:4E4W}.
HELIX 759 765 {ECO:0000244|PDB:4E4W}.
SEQUENCE 769 AA; 87062 MW; B2DBB31DE3943171 CRC64;
MSLRIKALDA SVVNKIAAGE IIISPVNALK EMMENSIDAN ATMIDILVKE GGIKVLQITD
NGSGINKADL PILCERFTTS KLQKFEDLSQ IQTYGFRGEA LASISHVARV TVTTKVKEDR
CAWRVSYAEG KMLESPKPVA GKDGTTILVE DLFFNIPSRL RALRSHNDEY SKILDVVGRY
AIHSKDIGFS CKKFGDSNYS LSVKPSYTVQ DRIRTVFNKS VASNLITFHI SKVEDLNLES
VDGKVCNLNF ISKKSISPIF FINNRLVTCD LLRRALNSVY SNYLPKGNRP FIYLGIVIDP
AAVDVNVHPT KREVRFLSQD EIIEKIANQL HAELSAIDTS RTFKASSIST NKPESLIPFN
DTIESDRNRK SLRQAQVVEN SYTTANSQLR KAKRQENKLV RIDASQAKIT SFLSSSQQFN
FEGSSTKRQL SEPKVTNVSH SQEAEKLTLN ESEQPRDANT INDNDLKDQP KKKQKLGDYK
VPSIADDEKN ALPISKDGYI RVPKERVNVN LTSIKKLREK VDDSIHRELT DIFANLNYVG
VVDEERRLAA IQHDLKLFLI DYGSVCYELF YQIGLTDFAN FGKINLQSTN VSDDIVLYNL
LSEFDELNDD ASKEKIISKI WDMSSMLNEY YSIELVNDGL DNDLKSVKLK SLPLLLKGYI
PSLVKLPFFI YRLGKEVDWE DEQECLDGIL REIALLYIPD MVPKVDTSDA SLSEDEKAQF
INRKEHISSL LEHVLFPCIK RRFLAPRHIL KDVVEIANLP DLYKVFERC


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