MKT1_YEAST
ID MKT1_YEAST Reviewed; 830 AA.
AC P40850; D6W194; Q45T81; Q8TF89;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Post-transcriptional regulator MKT1 {ECO:0000305};
DE AltName: Full=Inactive endonuclease MKT1 {ECO:0000305};
GN Name=MKT1; OrderedLocusNames=YNL085W; ORFNames=N2302;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2574;
RX PubMed=7532890; DOI=10.1002/yea.320101111;
RA Vermut M., Widner W.R., Dinman J.D., Wickner R.B.;
RT "Sequence of MKT1, needed for propagation of M2 satellite dsRNA of the L-A
RT virus of Saccharomyces cerevisiae.";
RL Yeast 10:1477-1479(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303, S96, YJM 1129, YJM 270, YJM 627, and YJM 789;
RX PubMed=11907579; DOI=10.1038/416326a;
RA Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
RA McCusker J.H., Davis R.W.;
RT "Dissecting the architecture of a quantitative trait locus in yeast.";
RL Nature 416:326-330(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c, ATCC 204626 / S288c / A364A,
RC ATCC 24657 / D273-10B, and Sigma 1278B;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740422;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT frames.";
RL Yeast 12:485-491(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, INTERACTION WITH PBP1, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-32.
RX PubMed=15082763; DOI=10.1128/mcb.24.9.3670-3681.2004;
RA Tadauchi T., Inada T., Matsumoto K., Irie K.;
RT "Posttranscriptional regulation of HO expression by the Mkt1-Pbp1
RT complex.";
RL Mol. Cell. Biol. 24:3670-3681(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-362 AND SER-371, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in 3'-UTR mediated RNA regulation (PubMed:15082763).
CC Binds to RNA-binding and RNA regulatory proteins (PubMed:15082763).
CC Complexes with PAB1-binding protein to promote mRNA interactions with
CC poly(A)-binding protein (PubMed:15082763). Promotes mating-type
CC switching in mother cells by positively regulating HO expression
CC (PubMed:15082763). {ECO:0000269|PubMed:15082763}.
CC -!- SUBUNIT: Interacts (via C-terminus) with PBP1 (via C-terminus).
CC {ECO:0000269|PubMed:15082763}.
CC -!- INTERACTION:
CC P40850; P53297: PBP1; NbExp=3; IntAct=EBI-10983, EBI-12961;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15082763}.
CC Note=Localizes to polysomes in a PBP1-dependent manner.
CC {ECO:0000269|PubMed:15082763}.
CC -!- DISRUPTION PHENOTYPE: Normal vegetative cell population growth rate and
CC morphology (PubMed:15082763). Decreases expression from the HO locus
CC (PubMed:15082763). {ECO:0000269|PubMed:15082763}.
CC -!- MISCELLANEOUS: Present with 3430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the XPG/RAD2 endonuclease family, only
CC two of the seven Asp residues involved in Mg(2+) binding are conserved
CC suggesting that it has no nuclease activity. {ECO:0000305}.
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DR EMBL; U09129; AAC49470.1; -; Genomic_DNA.
DR EMBL; AF458969; AAM00519.1; -; Genomic_DNA.
DR EMBL; AF458975; AAM00555.1; -; Genomic_DNA.
DR EMBL; AF458977; AAM00567.1; -; Genomic_DNA.
DR EMBL; AF458978; AAM00573.1; -; Genomic_DNA.
DR EMBL; AF458980; AAM00585.1; -; Genomic_DNA.
DR EMBL; AF458981; AAM00591.1; -; Genomic_DNA.
DR EMBL; DQ116825; AAZ23277.1; -; Genomic_DNA.
DR EMBL; DQ116826; AAZ23278.1; -; Genomic_DNA.
DR EMBL; DQ116827; AAZ23279.1; -; Genomic_DNA.
DR EMBL; DQ116828; AAZ23280.1; -; Genomic_DNA.
DR EMBL; X89016; CAA61425.1; -; Genomic_DNA.
DR EMBL; Z71361; CAA95961.1; -; Genomic_DNA.
DR EMBL; Z71360; CAA95960.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10460.1; -; Genomic_DNA.
DR PIR; S57537; S57537.
DR RefSeq; NP_014314.3; NM_001182923.3.
DR AlphaFoldDB; P40850; -.
DR BioGRID; 35738; 349.
DR ComplexPortal; CPX-1295; MKT1-PBP1 translation regulation complex.
DR DIP; DIP-6530N; -.
DR IntAct; P40850; 30.
DR MINT; P40850; -.
DR STRING; 4932.YNL085W; -.
DR iPTMnet; P40850; -.
DR MaxQB; P40850; -.
DR PaxDb; P40850; -.
DR PRIDE; P40850; -.
DR EnsemblFungi; YNL085W_mRNA; YNL085W; YNL085W.
DR GeneID; 855639; -.
DR KEGG; sce:YNL085W; -.
DR SGD; S000005029; MKT1.
DR VEuPathDB; FungiDB:YNL085W; -.
DR eggNOG; ENOG502QVHA; Eukaryota.
DR HOGENOM; CLU_378548_0_0_1; -.
DR InParanoid; P40850; -.
DR OMA; FYQTKVI; -.
DR BioCyc; YEAST:G3O-33114-MON; -.
DR PRO; PR:P40850; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40850; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISS:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0031494; P:regulation of mating type switching; IC:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR CDD; cd09902; H3TH_MKT1; 1.
DR InterPro; IPR022039; MKT1_C.
DR InterPro; IPR037314; MKT1_H3TH.
DR InterPro; IPR022040; MKT1_N.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR Pfam; PF12246; MKT1_C; 1.
DR Pfam; PF12247; MKT1_N; 1.
DR Pfam; PF00752; XPG_N; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..830
FT /note="Post-transcriptional regulator MKT1"
FT /id="PRO_0000096495"
FT REGION 130..380
FT /note="Interaction with PBP1"
FT /evidence="ECO:0000269|PubMed:15082763"
FT REGION 347..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 30
FT /note="D -> G (in strain: 2574, ATCC 24657 / D273-10B, ATCC
FT 200060 / W303, Sigma 1278B, YJM 1129, YJM 270, YJM 627 and
FT YJM 789)"
FT VARIANT 453
FT /note="K -> R (in strain: ATCC 24657 / D273-10B, ATCC
FT 200060 / W303, Sigma 1278B, YJM 1129, YJM 270, YJM 627 and
FT YJM 789)"
FT MUTAGEN 32
FT /note="D->A: Decreases gene expression from the ho locus."
FT /evidence="ECO:0000269|PubMed:15082763"
FT MUTAGEN 130..380
FT /note="Missing: In mkt1-19; HO gene expression is
FT decreased."
FT /evidence="ECO:0000269|PubMed:15082763"
FT CONFLICT 809..830
FT /note="IDENVFKLFTKAVEFTTTALSS -> TMKTCLNYH (in Ref. 1;
FT AAC49470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 94495 MW; BD976D8387E4F708 CRC64;
MAIKSLESFL FERGLVGSYA IEALNNCTLD IDVNHYVSRL LTNKREQYLD AIGGFPTSLK
MYLESDLKIF KDFNITPIFV FNGGLTYNQL EASGHFTAAS ASASISSTTT SSSGTNATTR
SNTESVLLQR SRGWTQWNNL ISSNQNSYID QPIQPQEPFR HNTTIDSKAY QNDLIAYFIE
HGYMYQVAPY SSWFQLAYLL NSAYIDAIYG PTDCLMLDCV DRFILGMEFP NKEFRFIDRS
RVMKDLGCTH EEFIDIAMAV GNDLQPTTLP PLQIYPVPQL FDIALEMVLN TGTNFYAYQL
STTLQNDSKE NIQNYQRGIS ALRYMPVLKD TGKVELFVQE IVVSEEDSEK NNKDGKKSNL
SSPSSASSSA SPATTVTKNA SEKLTYEKSS TKEVRKPRDI PNDVHDFIGQ MLPHEYYFYR
SIGLVTGKLF DAIVTGVYPE EPPLGGGSST SYKKLVSKSV EIFKNKEINL LTQPINRYYQ
IKQIKQVKWY AANEPTTLTN RMSPSMFETI NHLIVKTETS DEKEFSISEF ITTINGSSNM
AKDFISEKVI FPNSVPIESK LNSPFNLLST NFLRLLVLLE FFTFDFKEKL LEPTRWGEVF
LKLNELNIDS KYHESVIIFL VFLKCDVLKL DEEVQPPAPS ALSQATLRSY PEESLYVLLI
TRVLTLFQVD QKPSNYHGPI DKKTLIFRDH LSFIKENLNE LFEAVLISSL TSGEFNRLSL
DNFGWARKIV RYLPFKLDSP NTIMAMMWEF FLQKYLHNGN AKNDALSLVA TEFNTYKSTP
NLDEQFVESH RFLLEISKVM QELNAAKLID ENVFKLFTKA VEFTTTALSS
