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 27-MAR-2024, entry version 187. 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 RC 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, ATCC 24657 / RC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 383. 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 GlyGen; P40850; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; P40850; -. DR MaxQB; P40850; -. DR PaxDb; 4932-YNL085W; -. DR PeptideAtlas; P40850; -. DR EnsemblFungi; YNL085W_mRNA; YNL085W; YNL085W. DR GeneID; 855639; -. DR KEGG; sce:YNL085W; -. DR AGR; SGD:S000005029; -. 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 OrthoDB; 6876at2759; -. DR BioCyc; YEAST:G3O-33114-MONOMER; -. DR BioGRID-ORCS; 855639; 0 hits in 10 CRISPR screens. 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:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000932; C:P-body; IDA:SGD. DR GO; GO:0005844; C:polysome; IPI:ComplexPortal. DR GO; GO:0004520; F:DNA endonuclease activity; ISS:SGD. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central. DR GO; GO:0006974; P:DNA damage response; IMP:SGD. DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB. DR GO; GO:0031494; P:regulation of mating type switching; NAS:ComplexPortal. DR GO; GO:0006417; P:regulation of translation; NAS:ComplexPortal. DR CDD; cd09902; H3TH_MKT1; 1. DR CDD; cd09858; PIN_MKT1; 1. DR Gene3D; 3.40.50.1010; 5'-nuclease; 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; FLAP ENDONUCLEASE FAMILY MEMBER; 1. DR PANTHER; PTHR11081:SF32; POST-TRANSCRIPTIONAL REGULATOR MKT1; 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; PIN domain-like; 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 //