ID   MSH3_HUMAN              Reviewed;        1137 AA.
AC   P20585; A1L480; A1L482; A6NMM6; Q6PJT5; Q86UQ6; Q92867;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=DNA mismatch repair protein Msh3;
DE            Short=hMSH3;
DE   AltName: Full=Divergent upstream protein;
DE            Short=DUP;
DE   AltName: Full=Mismatch repair protein 1;
DE            Short=MRP1;
GN   Name=MSH3; Synonyms=DUC1, DUG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-79; ARG-949 AND THR-1045.
RX   PubMed=2722860; DOI=10.1016/s0021-9258(18)81766-5;
RA   Fujii H., Shimada T.;
RT   "Isolation and characterization of cDNA clones derived from the divergently
RT   transcribed gene in the region upstream from the human dihydrofolate
RT   reductase gene.";
RL   J. Biol. Chem. 264:10057-10064(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MSH2, AND VARIANTS
RP   57-ALA--ALA-65 DEL; VAL-79 AND ARG-949.
RX   PubMed=8942985; DOI=10.1073/pnas.93.24.13629;
RA   Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S., Marsischky G.T.,
RA   Kolodner R.D., Fishel R.;
RT   "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-79; ARG-949 AND
RP   THR-1045.
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; VAL-79;
RP   LEU-709; ARG-949 AND THR-1045.
RG   NIEHS SNPs program;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS 57-ALA--ALA-65 DEL;
RP   VAL-79; ARG-949 AND THR-1045.
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   POSSIBLE INVOLVEMENT IN ENDMC.
RX   PubMed=8782829; DOI=10.1038/ng0996-102;
RA   Risinger J.I., Umar A., Boyd J., Berchuck A., Kunkel T.A., Barrett J.C.;
RT   "Mutation of MSH3 in endometrial cancer and evidence for its functional
RT   role in heteroduplex repair.";
RL   Nat. Genet. 14:102-105(1996).
RN   [8]
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 exonuclease
RT   I.";
RL   J. Biol. Chem. 276:33011-33018(2001).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1099, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1099, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   IDENTIFICATION IN THE MMR COMPLEX, AND INTERACTION WITH MCM9.
RX   PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
RA   Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
RA   Latreille D., Mechali M.;
RT   "MCM9 Is Required for Mammalian DNA Mismatch Repair.";
RL   Mol. Cell 59:831-839(2015).
RN   [14]
RP   VARIANT ALA-ALA-ALA-62 INS.
RX   PubMed=8851770; DOI=10.1007/bf01900603;
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   [15]
RP   VARIANTS VAL-79 AND THR-1045.
RX   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 and
RT   sporadic colon cancer with microsatellite instability.";
RL   J. Hum. Genet. 45:228-230(2000).
RN   [16]
RP   INVOLVEMENT IN FAP4.
RX   PubMed=27476653; DOI=10.1016/j.ajhg.2016.06.015;
RA   Adam R., Spier I., Zhao B., Kloth M., Marquez J., Hinrichsen I., Kirfel J.,
RA   Tafazzoli A., Horpaopan S., Uhlhaas S., Stienen D., Friedrichs N.,
RA   Altmueller J., Laner A., Holzapfel S., Peters S., Kayser K., Thiele H.,
RA   Holinski-Feder E., Marra G., Kristiansen G., Noethen M.M., Buettner R.,
RA   Moeslein G., Betz R.C., Brieger A., Lifton R.P., Aretz S.;
RT   "Exome Sequencing Identifies Biallelic MSH3 Germline Mutations as a
RT   Recessive Subtype of Colorectal Adenomatous Polyposis.";
RL   Am. J. Hum. Genet. 99:337-351(2016).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC       (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA
CC       mismatches thereby initiating DNA repair. When bound, the MutS beta
CC       heterodimer bends the DNA helix and shields approximately 20 base
CC       pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to
CC       13 nucleotides long. After mismatch binding, forms a ternary complex
CC       with the MutL alpha heterodimer, which is thought to be responsible for
CC       directing the downstream MMR events, including strand discrimination,
CC       excision, and resynthesis.
CC   -!- SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at
CC       least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Heterodimer
CC       consisting of MSH2-MSH3 (MutS beta) (PubMed:8942985). Forms a ternary
CC       complex with MutL alpha (MLH1-PMS1). Interacts with EXO1
CC       (PubMed:11427529). Interacts with MCM9 (PubMed:26300262).
CC       {ECO:0000269|PubMed:11427529, ECO:0000269|PubMed:26300262,
CC       ECO:0000269|PubMed:8942985}.
CC   -!- INTERACTION:
CC       P20585; P40692: MLH1; NbExp=5; IntAct=EBI-1164205, EBI-744248;
CC       P20585; P43246: MSH2; NbExp=12; IntAct=EBI-1164205, EBI-355888;
CC       P20585; P12004: PCNA; NbExp=6; IntAct=EBI-1164205, EBI-358311;
CC   -!- DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of
CC       endometrium, the mucous lining of the uterus. Most endometrial cancers
CC       are adenocarcinomas, cancers that begin in cells that make and release
CC       mucus and other fluids. {ECO:0000305|PubMed:8782829}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Familial adenomatous polyposis 4 (FAP4) [MIM:617100]: A form
CC       of familial adenomatous polyposis, a condition characterized by the
CC       development of multiple colorectal adenomatous polyps, benign neoplasms
CC       derived from glandular epithelium. Some affected individuals may
CC       develop colorectal carcinoma. FAP4 inheritance is autosomal recessive.
CC       {ECO:0000269|PubMed:27476653}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11817.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/341/MSH3";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/msh3/";
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DR   EMBL; J04810; AAB47281.1; -; mRNA.
DR   EMBL; U61981; AAB06045.1; -; mRNA.
DR   EMBL; D61419; BAD27111.1; -; Genomic_DNA.
DR   EMBL; AY275681; AAP13535.1; -; Genomic_DNA.
DR   EMBL; AC008434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011817; AAH11817.1; ALT_SEQ; mRNA.
DR   EMBL; BC130434; AAI30435.1; -; mRNA.
DR   EMBL; BC130436; AAI30437.1; -; mRNA.
DR   CCDS; CCDS34195.1; -.
DR   PIR; A33507; A33507.
DR   RefSeq; NP_002430.3; NM_002439.4.
DR   PDB; 3THW; X-ray; 3.09 A; B=219-1134.
DR   PDB; 3THX; X-ray; 2.70 A; B=219-1134.
DR   PDB; 3THY; X-ray; 2.89 A; B=219-1134.
DR   PDB; 3THZ; X-ray; 4.30 A; B=219-1134.
DR   PDB; 8OLX; EM; 3.10 A; B=1-1137.
DR   PDB; 8OM5; EM; 3.52 A; B=1-1137.
DR   PDB; 8OM9; EM; 3.32 A; B=1-1137.
DR   PDB; 8OMA; EM; 3.29 A; B=1-1137.
DR   PDB; 8OMO; EM; 3.43 A; B=1-1137.
DR   PDB; 8OMQ; EM; 3.11 A; B=1-1137.
DR   PDBsum; 3THW; -.
DR   PDBsum; 3THX; -.
DR   PDBsum; 3THY; -.
DR   PDBsum; 3THZ; -.
DR   PDBsum; 8OLX; -.
DR   PDBsum; 8OM5; -.
DR   PDBsum; 8OM9; -.
DR   PDBsum; 8OMA; -.
DR   PDBsum; 8OMO; -.
DR   PDBsum; 8OMQ; -.
DR   AlphaFoldDB; P20585; -.
DR   EMDB; EMD-16964; -.
DR   EMDB; EMD-16969; -.
DR   EMDB; EMD-16971; -.
DR   EMDB; EMD-16972; -.
DR   EMDB; EMD-16973; -.
DR   EMDB; EMD-16974; -.
DR   SMR; P20585; -.
DR   BioGRID; 110574; 106.
DR   ComplexPortal; CPX-77; DNA mismatch repair MutSbeta complex.
DR   CORUM; P20585; -.
DR   DIP; DIP-35127N; -.
DR   IntAct; P20585; 26.
DR   MINT; P20585; -.
DR   STRING; 9606.ENSP00000265081; -.
DR   iPTMnet; P20585; -.
DR   PhosphoSitePlus; P20585; -.
DR   BioMuta; MSH3; -.
DR   DMDM; 317373576; -.
DR   EPD; P20585; -.
DR   jPOST; P20585; -.
DR   MassIVE; P20585; -.
DR   MaxQB; P20585; -.
DR   PaxDb; 9606-ENSP00000265081; -.
DR   PeptideAtlas; P20585; -.
DR   ProteomicsDB; 53762; -.
DR   Pumba; P20585; -.
DR   Antibodypedia; 24651; 329 antibodies from 32 providers.
DR   CPTC; P20585; 1 antibody.
DR   DNASU; 4437; -.
DR   Ensembl; ENST00000265081.7; ENSP00000265081.6; ENSG00000113318.11.
DR   GeneID; 4437; -.
DR   KEGG; hsa:4437; -.
DR   MANE-Select; ENST00000265081.7; ENSP00000265081.6; NM_002439.5; NP_002430.3.
DR   UCSC; uc003kgz.5; human.
DR   AGR; HGNC:7326; -.
DR   CTD; 4437; -.
DR   DisGeNET; 4437; -.
DR   GeneCards; MSH3; -.
DR   HGNC; HGNC:7326; MSH3.
DR   HPA; ENSG00000113318; Low tissue specificity.
DR   MalaCards; MSH3; -.
DR   MIM; 600887; gene.
DR   MIM; 608089; phenotype.
DR   MIM; 617100; phenotype.
DR   neXtProt; NX_P20585; -.
DR   OpenTargets; ENSG00000113318; -.
DR   Orphanet; 480536; MSH3-related attenuated familial adenomatous polyposis.
DR   PharmGKB; PA31134; -.
DR   VEuPathDB; HostDB:ENSG00000113318; -.
DR   eggNOG; KOG0218; Eukaryota.
DR   GeneTree; ENSGT00550000074949; -.
DR   HOGENOM; CLU_002472_0_1_1; -.
DR   InParanoid; P20585; -.
DR   OMA; HIAPCEL; -.
DR   OrthoDB; 168255at2759; -.
DR   PhylomeDB; P20585; -.
DR   TreeFam; TF300525; -.
DR   PathwayCommons; P20585; -.
DR   Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-HSA-5632927; Defective Mismatch Repair Associated With MSH3.
DR   Reactome; R-HSA-5632928; Defective Mismatch Repair Associated With MSH2.
DR   SignaLink; P20585; -.
DR   BioGRID-ORCS; 4437; 13 hits in 1155 CRISPR screens.
DR   ChiTaRS; MSH3; human.
DR   GeneWiki; MSH3; -.
DR   GenomeRNAi; 4437; -.
DR   Pharos; P20585; Tbio.
DR   PRO; PR:P20585; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P20585; Protein.
DR   Bgee; ENSG00000113318; Expressed in bronchial epithelial cell and 214 other cell types or tissues.
DR   ExpressionAtlas; P20585; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0032302; C:MutSbeta complex; IDA:HGNC-UCL.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IDA:BHF-UCL.
DR   GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:HGNC-UCL.
DR   GO; GO:0006298; P:mismatch repair; IDA:ComplexPortal.
DR   GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IDA:BHF-UCL.
DR   GO; GO:0051096; P:positive regulation of helicase activity; IDA:BHF-UCL.
DR   GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; IBA:GO_Central.
DR   Gene3D; 1.10.1420.10; -; 2.
DR   Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR   Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   IDEAL; IID00612; -.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361:SF122; DNA MISMATCH REPAIR PROTEIN MSH3; 1.
DR   PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR   SUPFAM; SSF53150; DNA repair protein MutS, domain II; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   Genevisible; P20585; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1137
FT                   /note="DNA mismatch repair protein Msh3"
FT                   /id="PRO_0000115192"
FT   REGION          31..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..297
FT                   /note="Interaction with EXO1"
FT                   /evidence="ECO:0000269|PubMed:11427529"
FT   REGION          201..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         896..903
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1099
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   VARIANT         57..65
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8942985"
FT                   /id="VAR_020934"
FT   VARIANT         62
FT                   /note="A -> AAAA"
FT                   /evidence="ECO:0000269|PubMed:8851770"
FT                   /id="VAR_020935"
FT   VARIANT         79
FT                   /note="I -> V (in dbSNP:rs1650697)"
FT                   /evidence="ECO:0000269|PubMed:10944853,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2722860,
FT                   ECO:0000269|PubMed:8942985, ECO:0000269|Ref.3,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_020936"
FT   VARIANT         709
FT                   /note="F -> L (in dbSNP:rs1805354)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_016160"
FT   VARIANT         789
FT                   /note="Y -> F (in dbSNP:rs10067975)"
FT                   /id="VAR_055251"
FT   VARIANT         949
FT                   /note="Q -> R (in dbSNP:rs184967)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2722860, ECO:0000269|PubMed:8942985,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT                   /id="VAR_016161"
FT   VARIANT         1045
FT                   /note="A -> T (in dbSNP:rs26279)"
FT                   /evidence="ECO:0000269|PubMed:10944853,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2722860,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT                   /id="VAR_016162"
FT   VARIANT         1054
FT                   /note="T -> A (in dbSNP:rs1805131)"
FT                   /id="VAR_016163"
FT   CONFLICT        61
FT                   /note="A -> T (in Ref. 6; AAI30435)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622
FT                   /note="E -> G (in Ref. 1; AAB47281 and 3; BAD27111)"
FT                   /evidence="ECO:0000305"
FT   HELIX           231..240
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            241..245
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           260..270
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          280..286
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           287..289
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           290..300
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          304..309
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           313..316
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          328..334
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          368..374
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            382..384
FT                   /evidence="ECO:0007829|PDB:3THW"
FT   STRAND          386..393
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            395..397
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          400..407
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           412..421
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          424..431
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           434..445
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          449..451
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          454..458
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           460..462
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           465..475
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           497..512
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           516..519
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           522..524
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          525..528
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            531..533
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           539..544
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          547..549
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            551..553
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           560..564
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           570..581
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           587..601
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           607..613
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            614..617
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           621..629
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           635..661
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           666..672
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           674..678
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           680..682
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           683..686
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           691..696
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           706..708
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           710..737
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          745..747
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          750..757
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           761..763
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          769..773
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          775..781
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           783..814
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           815..817
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           818..841
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          843..845
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          850..854
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          856..862
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           865..870
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          875..877
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          880..884
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          886..888
FT                   /evidence="ECO:0007829|PDB:3THY"
FT   STRAND          891..896
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           900..917
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          922..930
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          933..938
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           952..965
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          971..976
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            977..980
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           983..999
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          1004..1008
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           1012..1016
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           1017..1020
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            1021..1024
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          1025..1033
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          1055..1062
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            1066..1069
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           1070..1073
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            1074..1077
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           1080..1111
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           1116..1128
FT                   /evidence="ECO:0007829|PDB:3THX"
SQ   SEQUENCE   1137 AA;  127412 MW;  FBAE6B84D3F86032 CRC64;
     MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG AAAAAAAAAA
     AAPPAPPAPA FPPQLPPHIA 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 AADNIYKGQS TFMEELTDTA
     EIIRKATSQS LVILDELGRG TSTHDGIAIA YATLEYFIRD VKSLTLFVTH YPPVCELEKN
     YSHQVGNYHM GFLVSEDESK LDPGAAEQVP DFVTFLYQIT RGIAARSYGL NVAKLADVPG
     EILKKAAHKS KELEGLINTK RKRLKYFAKL WTMHNAQDLQ KWTEEFNMEE TQTSLLH
//