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Database: UniProt
Entry: P40562
LinkDB: P40562
Original site: P40562 
ID   MPH1_YEAST              Reviewed;         993 AA.
AC   P40562; D6VVT2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-OCT-2019, entry version 174.
DE   RecName: Full=ATP-dependent DNA helicase MPH1 {ECO:0000305};
DE            EC=3.6.4.12 {ECO:0000269|PubMed:15634678};
DE   AltName: Full=FANCM-like protein 1 {ECO:0000250|UniProtKB:Q9UT23};
DE   AltName: Full=Mutator phenotype protein 1 {ECO:0000303|PubMed:10628851};
GN   Name=MPH1 {ECO:0000303|PubMed:10628851};
GN   OrderedLocusNames=YIR002C {ECO:0000312|SGD:S000001441};
GN   ORFNames=YIB2C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7762303; DOI=10.1002/yea.320110109;
RA   Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA   Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT   "Nucleotide sequence and analysis of the centromeric region of yeast
RT   chromosome IX.";
RL   Yeast 11:61-78(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
RA   Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
RA   Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
RA   Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   GENE NAME.
RX   PubMed=10628851; DOI=10.1007/pl00013817;
RA   Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA   Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G.,
RA   Kramer W., Klein S., Koetter P., Kricke J., Launhardt H.,
RA   Mannhaupt G., Maierl A., Meyer P., Mewes W., Munder T.,
RA   Niedenthal R.K., Ramezani Rad M., Roehmer A., Roemer A., Rose M.,
RA   Schaefer B., Siegler M.-L., Vetter J., Wilhelm N., Wolf K.,
RA   Zimmermann F.K., Zollner A., Hinnen A.;
RT   "Functional analysis of 150 deletion mutants in Saccharomyces
RT   cerevisiae by a systematic approach.";
RL   Mol. Gen. Genet. 262:683-702(1999).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10880470;
RA   Scheller J., Schuerer K.A., Rudolph C., Hettwer S., Kramer W.;
RT   "MPH1, a yeast gene encoding a DEAH protein, plays a role in
RT   protection of the genome from spontaneous and chemically induced
RT   damage.";
RL   Genetics 155:1069-1081(2000).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=15126389; DOI=10.1534/genetics.166.4.1673;
RA   Schuerer K.A., Rudolph C., Ulrich H.D., Kramer W.;
RT   "Yeast MPH1 gene functions in an error-free DNA damage bypass pathway
RT   that requires genes from homologous recombination, but not from
RT   postreplicative repair.";
RL   Genetics 166:1673-1686(2004).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15634678; DOI=10.1074/jbc.m413898200;
RA   Prakash R., Krejci L., Van Komen S., Schuerer K.A., Kramer W.,
RA   Sung P.;
RT   "Saccharomyces cerevisiae MPH1 gene, required for homologous
RT   recombination-mediated mutation avoidance, encodes a 3' to 5' DNA
RT   helicase.";
RL   J. Biol. Chem. 280:7854-7860(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=16121259; DOI=10.1371/journal.pgen.0010024;
RA   Lee W., St Onge R.P., Proctor M., Flaherty P., Jordan M.I.,
RA   Arkin A.P., Davis R.W., Nislow C., Giaever G.;
RT   "Genome-wide requirements for resistance to functionally distinct DNA-
RT   damaging agents.";
RL   PLoS Genet. 1:235-246(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19136626; DOI=10.1101/gad.1737809;
RA   Prakash R., Satory D., Dray E., Papusha A., Scheller J., Kramer W.,
RA   Krejci L., Klein H., Haber J.E., Sung P., Ira G.;
RT   "Yeast Mph1 helicase dissociates Rad51-made D-loops: implications for
RT   crossover control in mitotic recombination.";
RL   Genes Dev. 23:67-79(2009).
RN   [12]
RP   FUNCTION.
RX   PubMed=20347428; DOI=10.1016/j.molcel.2010.01.039;
RA   Yan Z., Delannoy M., Ling C., Daee D., Osman F., Muniandy P.A.,
RA   Shen X., Oostra A.B., Du H., Steltenpool J., Lin T., Schuster B.,
RA   Decaillet C., Stasiak A., Stasiak A.Z., Stone S., Hoatlin M.E.,
RA   Schindler D., Woodcock C.L., Joenje H., Sen R., de Winter J.P., Li L.,
RA   Seidman M.M., Whitby M.C., Myung K., Constantinousend A., Wang W.;
RT   "A histone-fold complex and FANCM form a conserved DNA-remodeling
RT   complex to maintain genome stability.";
RL   Mol. Cell 37:865-878(2010).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair
CC       by homologous recombination and in genome maintenance
CC       (PubMed:10880470, PubMed:15126389, PubMed:15634678,
CC       PubMed:16121259). Capable of unwinding D-loops. Plays a role in
CC       limiting crossover recombinants during mitotic DNA double-strand
CC       break (DSB) repair (PubMed:19136626). Component of a FANCM-MHF
CC       complex which promotes gene conversion at blocked replication
CC       forks, probably by reversal of the stalled fork (PubMed:20347428).
CC       {ECO:0000269|PubMed:10880470, ECO:0000269|PubMed:15126389,
CC       ECO:0000269|PubMed:15634678, ECO:0000269|PubMed:16121259,
CC       ECO:0000269|PubMed:19136626, ECO:0000305|PubMed:20347428}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000269|PubMed:15634678};
CC   -!- SUBUNIT: Interacts with the MHF histone-fold complex composed of
CC       MHF1 and MHF2 to form the FANCM-MHF complex.
CC       {ECO:0000250|UniProtKB:Q9UT23}.
CC   -!- INTERACTION:
CC       Q08204:SMC5; NbExp=5; IntAct=EBI-25369, EBI-34125;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10880470,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. FANCM sub-subfamily. {ECO:0000305}.
DR   EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z38062; CAA86204.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08548.1; -; Genomic_DNA.
DR   PIR; S48436; S48436.
DR   RefSeq; NP_012267.1; NM_001179524.1.
DR   BioGrid; 34993; 263.
DR   DIP; DIP-5016N; -.
DR   IntAct; P40562; 9.
DR   STRING; 4932.YIR002C; -.
DR   iPTMnet; P40562; -.
DR   MaxQB; P40562; -.
DR   PaxDb; P40562; -.
DR   PRIDE; P40562; -.
DR   EnsemblFungi; YIR002C_mRNA; YIR002C; YIR002C.
DR   GeneID; 854818; -.
DR   KEGG; sce:YIR002C; -.
DR   EuPathDB; FungiDB:YIR002C; -.
DR   SGD; S000001441; MPH1.
DR   HOGENOM; HOG000066122; -.
DR   InParanoid; P40562; -.
DR   KO; K14635; -.
DR   OMA; IRPHIFI; -.
DR   BioCyc; YEAST:G3O-31423-MONOMER; -.
DR   BRENDA; 3.6.4.12; 984.
DR   PRO; PR:P40562; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IDA:SGD.
DR   GO; GO:0070336; F:flap-structured DNA binding; IDA:SGD.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IGI:SGD.
DR   GO; GO:0007535; P:donor selection; IMP:SGD.
DR   GO; GO:0036297; P:interstrand cross-link repair; IGI:SGD.
DR   GO; GO:0060543; P:negative regulation of strand invasion; IDA:SGD.
DR   GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR   InterPro; IPR039686; FANCM/Mph1-like.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR14025:SF20; PTHR14025:SF20; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1    993       ATP-dependent DNA helicase MPH1.
FT                                /FTId=PRO_0000055193.
FT   DOMAIN       94    261       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      507    655       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     107    114       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       209    212       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
SQ   SEQUENCE   993 AA;  114058 MW;  474DDC99C543171F CRC64;
     MASADDYFSD FEDDELDKLY EKAINKSVKE TITRRAVPVQ KDLHDNVLPG QKTVYEEIQR
     DVSFGPTHHE LDYDALSFYV YPTNYEVRDY QYTIVHKSLF QNTLCAIPTG MGKTFIASTV
     MLNYFRWTKK AKIIFTAPTR PLVAQQIKAC LGITGIPSDQ TAILLDKSRK NREEIWANKR
     VFFATPQVVE NDLKRGVLDP KDIVCLVIDE AHRATGSSAY TNVVKFIDRF NSSYRLLALT
     ATPASDLEGV QEVVNNLDIS KIEIRTEESM DIVKYMKKRK KEKIEVPLLL EIEDIIEQLG
     MAVKPVLQQA IELGIYEECD PSQINAFKAM QQSQKIIANP TIPEGIKWRN FFILQLLNNV
     GQMLKRLKIY GIRTFFNYFQ NKCTEFTTKY NLKKSTNKIA AEFYYHPILK NIKNQCENYL
     SDPKFVGHGK LQCVRDELMD FFQKRGSDSR VIIFTELRES ALEIVKFIDS VADDQIRPHI
     FIGQARAKEG FDEVKYTRKH APKGRKKVER LHRQEQEKFL EAERTKRAAN DKLERSARRT
     GSSEEAQISG MNQKMQKEVI HNFKKGEYNV LVCTSIGEEG LDIGEVDLII CYDTTSSPIK
     NIQRMGRTGR KRDGKIVLLF SSNESYKFER AMEDYSTLQA LISKQCIDYK KSDRIIPEDI
     IPECHETLIT INDENEIINE MEDVDEVIRY ATQCMMGKKV KPKKAITKKK RVQENKKPKK
     FFMPDNVETS IVSASTLINK FLVNESGGKQ LVTSNENPSK KRKIFKALDN LENDSTEEAS
     SSLETEDEEV SDDNNVFIAE GQNGCQKDLE TAIIRTGESL TTLKPLHNFE RPNMALFVND
     CGLPTKIEKN VKDIRGNQHN LEKEKSCTVD KNNMVLSLDD WNFFRNRYIP EGVSFDVEPN
     FVQYTKGVKV PHCHKVSKII TLFNDESNDN KKRTIDMNYT KCLARGMLRD EKKFVKVNDK
     SQVDNNSVNH DSSQSFTLSN AELDDILGSD SDF
//
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