ID PAT1_YEAST Reviewed; 796 AA.
AC P25644; D6VR80; Q8NKJ3;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 27-MAR-2024, entry version 189.
DE RecName: Full=DNA topoisomerase 2-associated protein PAT1;
DE AltName: Full=Decapping activator and translational repressor PAT1;
DE AltName: Full=Topoisomerase II-associated protein PAT1;
DE AltName: Full=mRNA turnover protein 1;
GN Name=PAT1; Synonyms=MRT1; OrderedLocusNames=YCR077C; ORFNames=YCR77C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 688.
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 [4]
RP SEQUENCE REVISION, AND CHARACTERIZATION.
RX PubMed=7645349; DOI=10.1002/yea.320110608;
RA Rodriguez-Cousino N., Lill R., Neupert W., Court D.A.;
RT "Identification and initial characterization of the cytosolic protein
RT Ycr77p.";
RL Yeast 11:581-585(1995).
RN [5]
RP FUNCTION.
RX PubMed=8816497; DOI=10.1128/mcb.16.10.5830;
RA Hatfield L., Beelman C.A., Stevens A., Parker R.;
RT "Mutations in trans-acting factors affecting mRNA decapping in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:5830-5838(1996).
RN [6]
RP FUNCTION.
RX PubMed=8972867; DOI=10.1093/nar/24.23.4791;
RA Wang X., Watt P.M., Louis E.J., Borts R.H., Hickson I.D.;
RT "Pat1: a topoisomerase II-associated protein required for faithful
RT chromosome transmission in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 24:4791-4797(1996).
RN [7]
RP FUNCTION.
RX PubMed=10523645; DOI=10.1128/mcb.19.11.7568;
RA Zhang S., Williams C.J., Hagan K., Peltz S.W.;
RT "Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of
RT the decapping enzyme.";
RL Mol. Cell. Biol. 19:7568-7576(1999).
RN [8]
RP FUNCTION.
RX PubMed=10394921; DOI=10.1007/s004380050027;
RA Wang X., Watt P.M., Borts R.H., Louis E.J., Hickson I.D.;
RT "The topoisomerase II-associated protein, Pat1p, is required for
RT maintenance of rDNA locus stability in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 261:831-840(1999).
RN [9]
RP FUNCTION, AND ASSOCIATION WITH THE LSM1-LSM7 COMPLEX.
RX PubMed=10747033; DOI=10.1093/emboj/19.7.1661;
RA Bouveret E., Rigaut G., Shevchenko A., Wilm M., Seraphin B.;
RT "A Sm-like protein complex that participates in mRNA degradation.";
RL EMBO J. 19:1661-1671(2000).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE 40S RIBOSOMAL
RP SUBUNIT.
RX PubMed=10779343; DOI=10.1128/mcb.20.10.3538-3549.2000;
RA Wyers F., Minet M., Dufour M.E., Vo L.T., Lacroute F.;
RT "Deletion of the PAT1 gene affects translation initiation and suppresses a
RT PAB1 gene deletion in yeast.";
RL Mol. Cell. Biol. 20:3538-3549(2000).
RN [11]
RP FUNCTION, AND INTERACTION WITH LSM1.
RX PubMed=10913177; DOI=10.1128/mcb.20.16.5939-5946.2000;
RA Bonnerot C., Boeck R., Lapeyre B.;
RT "The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required
RT for mRNA decay, and are functionally linked to Pab1p.";
RL Mol. Cell. Biol. 20:5939-5946(2000).
RN [12]
RP FUNCTION.
RX PubMed=11027264; DOI=10.1128/mcb.20.21.7933-7942.2000;
RA Schwartz D.C., Parker R.;
RT "mRNA decapping in yeast requires dissociation of the cap binding protein,
RT eukaryotic translation initiation factor 4E.";
RL Mol. Cell. Biol. 20:7933-7942(2000).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LSM1 AND LSM5.
RX PubMed=10761922; DOI=10.1038/35006676;
RA Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R.;
RT "Yeast Sm-like proteins function in mRNA decapping and decay.";
RL Nature 404:515-518(2000).
RN [14]
RP FUNCTION.
RX PubMed=11514438; DOI=10.1093/genetics/158.4.1445;
RA He W., Parker R.;
RT "The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from
RT partial degradation.";
RL Genetics 158:1445-1455(2001).
RN [15]
RP INTERACTION WITH CDC33; PAB1; TIF4631 AND TIF4632, AND MRNA-BINDING.
RX PubMed=11741542; DOI=10.1016/s1097-2765(01)00395-1;
RA Tharun S., Parker R.;
RT "Targeting an mRNA for decapping: displacement of translation factors and
RT association of the Lsm1p-7p complex on deadenylated yeast mRNAs.";
RL Mol. Cell 8:1075-1083(2001).
RN [16]
RP INTERACTION WITH DHH1.
RX PubMed=11780629; DOI=10.1017/s135583820101994x;
RA Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R.;
RT "The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts
RT with both the decapping and deadenylase complexes.";
RL RNA 7:1717-1727(2001).
RN [17]
RP INTERACTION WITH DHH1.
RX PubMed=12032091; DOI=10.1093/emboj/21.11.2788;
RA Fischer N., Weis K.;
RT "The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1.";
RL EMBO J. 21:2788-2797(2002).
RN [18]
RP FUNCTION.
RX PubMed=12773554; DOI=10.1128/mcb.23.12.4094-4106.2003;
RA Noueiry A.O., Diez J., Falk S.P., Chen J., Ahlquist P.;
RT "Yeast Lsm1p-7p/Pat1p deadenylation-dependent mRNA-decapping factors are
RT required for brome mosaic virus genomic RNA translation.";
RL Mol. Cell. Biol. 23:4094-4106(2003).
RN [19]
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 [20]
RP SUBCELLULAR LOCATION.
RX PubMed=12730603; DOI=10.1126/science.1082320;
RA Sheth U., Parker R.;
RT "Decapping and decay of messenger RNA occur in cytoplasmic processing
RT bodies.";
RL Science 300:805-808(2003).
RN [21]
RP FUNCTION.
RX PubMed=16179257; DOI=10.1016/j.cell.2005.07.012;
RA Coller J., Parker R.;
RT "General translational repression by activators of mRNA decapping.";
RL Cell 122:875-886(2005).
RN [22]
RP INTERACTION WITH RPB4.
RX PubMed=16357218; DOI=10.1101/gad.353205;
RA Lotan R., Bar-On V.G., Harel-Sharvit L., Duek L., Melamed D., Choder M.;
RT "The RNA polymerase II subunit Rpb4p mediates decay of a specific class of
RT mRNAs.";
RL Genes Dev. 19:3004-3016(2005).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=15703442; DOI=10.1261/rna.7258505;
RA Teixeira D., Sheth U., Valencia-Sanchez M.A., Brengues M., Parker R.;
RT "Processing bodies require RNA for assembly and contain nontranslating
RT mRNAs.";
RL RNA 11:371-382(2005).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=16777600; DOI=10.1016/j.cell.2006.04.037;
RA Sheth U., Parker R.;
RT "Targeting of aberrant mRNAs to cytoplasmic processing bodies.";
RL Cell 125:1095-1109(2006).
RN [25]
RP FUNCTION, AND INTERACTION WITH RPB7.
RX PubMed=17875743; DOI=10.1083/jcb.200701165;
RA Lotan R., Goler-Baron V., Duek L., Haimovich G., Choder M.;
RT "The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major
RT cytoplasmic mRNA decay mechanisms.";
RL J. Cell Biol. 178:1133-1143(2007).
RN [26]
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 [27]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17429074; DOI=10.1091/mbc.e07-03-0199;
RA Teixeira D., Parker R.;
RT "Analysis of P-body assembly in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 18:2274-2287(2007).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [29]
RP FUNCTION.
RX PubMed=17513695; DOI=10.1261/rna.502507;
RA Chowdhury A., Mukhopadhyay J., Tharun S.;
RT "The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability
RT to distinguish between oligoadenylated and polyadenylated RNAs.";
RL RNA 13:998-1016(2007).
RN [30]
RP ASSOCIATION WITH THE LSM1-LSM7 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19111170; DOI=10.1016/s0076-6879(08)02603-7;
RA Tharun S.;
RT "Purification and analysis of the decapping activator Lsm1p-7p-Pat1p
RT complex from yeast.";
RL Methods Enzymol. 448:41-55(2008).
RN [31]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND RNA-BINDING.
RX PubMed=18086885; DOI=10.1128/mcb.00936-07;
RA Pilkington G.R., Parker R.;
RT "Pat1 contains distinct functional domains that promote P-body assembly and
RT activation of decapping.";
RL Mol. Cell. Biol. 28:1298-1312(2008).
RN [32]
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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-457, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [34]
RP FUNCTION.
RX PubMed=19901074; DOI=10.1128/mcb.00251-09;
RA Checkley M.A., Nagashima K., Lockett S.J., Nyswaner K.M., Garfinkel D.J.;
RT "P-body components are required for Ty1 retrotransposition during assembly
RT of retrotransposition-competent virus-like particles.";
RL Mol. Cell. Biol. 30:382-398(2010).
RN [35]
RP FUNCTION.
RX PubMed=20832728; DOI=10.1016/j.molcel.2010.08.025;
RA Nissan T., Rajyaguru P., She M., Song H., Parker R.;
RT "Decapping activators in Saccharomyces cerevisiae act by multiple
RT mechanisms.";
RL Mol. Cell 39:773-783(2010).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [37]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 456-783 IN COMPLEX WITH THE
RP LSM1-LSM7 COMPLEX, AND SUBUNIT.
RX PubMed=24139796; DOI=10.1016/j.celrep.2013.10.004;
RA Sharif H., Conti E.;
RT "Architecture of the Lsm1-7-Pat1 complex: a conserved assembly in
RT eukaryotic mRNA turnover.";
RL Cell Rep. 5:283-291(2013).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 422-796 IN COMPLEX WITH THE
RP LSM1-LSM7 COMPLEX, FUNCTION, AND SUBUNIT.
RX PubMed=24247251; DOI=10.1038/cr.2013.152;
RA Wu D., Muhlrad D., Bowler M.W., Jiang S., Liu Z., Parker R., Song H.;
RT "Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for
RT decapping activation.";
RL Cell Res. 24:233-246(2014).
CC -!- FUNCTION: Activator of decapping that functions as a general and active
CC mechanism of translational repression and required for P-body
CC formation. First decay factor recruited to mRNA, at a time when the
CC mRNA is still associated with translation factors. Subsequently, PAT1
CC recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In
CC association with the LSM1-LSM7 complex, stabilizes the 3' terminus of
CC mRNAs. This association is also required for mosaic virus genomic RNA
CC translation. Modulates the rates of mRNA-decapping that occur following
CC deadenylation. Might be required for promoting the formation or the
CC stabilization of the preinitiation translation complexes. Required for
CC 40S ribosomal subunit joining to capped and/or polyadenylated mRNA.
CC With other P-body components, enhances the formation of
CC retrotransposition-competent Ty1 virus-like particles. Necessary for
CC accurate chromosome transmission during cell division.
CC {ECO:0000269|PubMed:10394921, ECO:0000269|PubMed:10523645,
CC ECO:0000269|PubMed:10747033, ECO:0000269|PubMed:10761922,
CC ECO:0000269|PubMed:10779343, ECO:0000269|PubMed:10913177,
CC ECO:0000269|PubMed:11027264, ECO:0000269|PubMed:11514438,
CC ECO:0000269|PubMed:12773554, ECO:0000269|PubMed:16179257,
CC ECO:0000269|PubMed:17429074, ECO:0000269|PubMed:17513695,
CC ECO:0000269|PubMed:17875743, ECO:0000269|PubMed:18086885,
CC ECO:0000269|PubMed:19901074, ECO:0000269|PubMed:20832728,
CC ECO:0000269|PubMed:24247251, ECO:0000269|PubMed:8816497,
CC ECO:0000269|PubMed:8972867}.
CC -!- SUBUNIT: Associates with the 40S ribosomal subunit. Associates with the
CC heptameric LSM1-LSM7 complex. Interacts directly with LSM2 and LSM3
CC within the LSM1-LSM7 complex. Interacts with DHH1, LSM1, LSM5, RPB4,
CC RPB7 and with topoisomerase TOP2. Interacts with CDC33, PAB1, TIF4631
CC and TIF4632 in an RNA-dependent manner. Binds mRNAs.
CC {ECO:0000269|PubMed:10761922, ECO:0000269|PubMed:10913177,
CC ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:11780629,
CC ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:16357218,
CC ECO:0000269|PubMed:17875743, ECO:0000269|PubMed:24139796,
CC ECO:0000269|PubMed:24247251}.
CC -!- INTERACTION:
CC P25644; P53550: DCP2; NbExp=3; IntAct=EBI-204, EBI-270;
CC P25644; P39517: DHH1; NbExp=7; IntAct=EBI-204, EBI-158;
CC P25644; P47017: LSM1; NbExp=5; IntAct=EBI-204, EBI-174;
CC P25644; P38203: LSM2; NbExp=5; IntAct=EBI-204, EBI-180;
CC P25644; P40070: LSM4; NbExp=7; IntAct=EBI-204, EBI-188;
CC P25644; P53905: LSM7; NbExp=3; IntAct=EBI-204, EBI-141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body.
CC -!- DOMAIN: The region at residues 254 to 422 is required for stimulation
CC of decapping. The region at residues 422 to 763 is required for PAT1
CC and LSM1 to accumulate in P-bodies and responsible for translation
CC repression and P-body assembly. {ECO:0000269|PubMed:18086885}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PAT1 family. {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; X59720; CAC42990.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07549.2; -; Genomic_DNA.
DR PIR; S53590; S53590.
DR RefSeq; NP_010002.3; NM_001178786.2.
DR PDB; 4BRW; X-ray; 2.80 A; B=5-79.
DR PDB; 4C8Q; X-ray; 3.70 A; H=456-783.
DR PDB; 4N0A; X-ray; 3.15 A; H/I/J=422-796.
DR PDB; 4OGP; X-ray; 2.15 A; A/B=473-796.
DR PDB; 4OJJ; X-ray; 2.32 A; A/B/C=473-796.
DR PDB; 5LM5; X-ray; 2.60 A; A/B=435-796.
DR PDB; 5LMF; X-ray; 2.15 A; A/B=435-796.
DR PDB; 5LMG; X-ray; 1.89 A; A/B=435-796.
DR PDBsum; 4BRW; -.
DR PDBsum; 4C8Q; -.
DR PDBsum; 4N0A; -.
DR PDBsum; 4OGP; -.
DR PDBsum; 4OJJ; -.
DR PDBsum; 5LM5; -.
DR PDBsum; 5LMF; -.
DR PDBsum; 5LMG; -.
DR AlphaFoldDB; P25644; -.
DR SMR; P25644; -.
DR BioGRID; 31052; 1292.
DR ComplexPortal; CPX-112; LSM1-7-PAT1 complex.
DR DIP; DIP-883N; -.
DR IntAct; P25644; 56.
DR MINT; P25644; -.
DR STRING; 4932.YCR077C; -.
DR GlyGen; P25644; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P25644; -.
DR MaxQB; P25644; -.
DR PaxDb; 4932-YCR077C; -.
DR PeptideAtlas; P25644; -.
DR EnsemblFungi; YCR077C_mRNA; YCR077C; YCR077C.
DR GeneID; 850440; -.
DR KEGG; sce:YCR077C; -.
DR AGR; SGD:S000000673; -.
DR SGD; S000000673; PAT1.
DR VEuPathDB; FungiDB:YCR077C; -.
DR eggNOG; KOG4592; Eukaryota.
DR GeneTree; ENSGT00520000055649; -.
DR HOGENOM; CLU_012622_1_0_1; -.
DR InParanoid; P25644; -.
DR OMA; YLEHSGH; -.
DR OrthoDB; 2786412at2759; -.
DR BioCyc; YEAST:G3O-29376-MONOMER; -.
DR Reactome; R-SCE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 850440; 1 hit in 10 CRISPR screens.
DR PRO; PR:P25644; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25644; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:SGD.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:SGD.
DR GO; GO:0033962; P:P-body assembly; IMP:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IMP:SGD.
DR DisProt; DP01825; -.
DR InterPro; IPR039900; Pat1-like.
DR InterPro; IPR019167; PAT1_dom.
DR PANTHER; PTHR21551:SF0; PROTEIN ASSOCIATED WITH TOPO II RELATED-1, ISOFORM A; 1.
DR PANTHER; PTHR21551; TOPOISOMERASE II-ASSOCIATED PROTEIN PAT1; 1.
DR Pfam; PF09770; PAT1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..796
FT /note="DNA topoisomerase 2-associated protein PAT1"
FT /id="PRO_0000058235"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 688
FT /note="D -> V (in Ref. 1; CAC42990)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4BRW"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4BRW"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 475..497
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 505..509
FT /evidence="ECO:0007829|PDB:5LMG"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:4OGP"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 522..526
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 530..541
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 545..557
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:5LMG"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 578..601
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 605..618
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 621..624
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 628..643
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 661..673
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 684..694
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 702..713
FT /evidence="ECO:0007829|PDB:5LMG"
FT HELIX 717..749
FT /evidence="ECO:0007829|PDB:5LMG"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:4OJJ"
FT HELIX 756..782
FT /evidence="ECO:0007829|PDB:5LMG"
FT STRAND 785..788
FT /evidence="ECO:0007829|PDB:5LMG"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:5LMG"
SQ SEQUENCE 796 AA; 88511 MW; 2DBE1210C173E468 CRC64;
MSFFGLENSG NARDGPLDFE ESYKGYGEHE LEENDYLNDE TFGDNVQVGT DFDFGNPHSS
GSSGNAIGGN GVGATARSYV AATAEGISGP RTDGTAAAGP LDLKPMESLW STAPPPAMAP
SPQSTMAPAP APQQMAPLQP ILSMQDLERQ QRQMQQQFMN FHAMGHPQGL PQGPPQQQFP
MQPASGQPGP SQFAPPPPPP GVNVNMNQMP MGPVQVPVQA SPSPIGMSNT PSPGPVVGAT
KMPLQSGRRS KRDLSPEEQR RLQIRHAKVE KILKYSGLMT PRDKDFITRY QLSQIVTEDP
YNEDFYFQVY KIIQRGGITS ESNKGLIARA YLEHSGHRLG GRYKRTDIAL QRMQSQVEKA
VTVAKERPSK LKDQQAAAGN SSQDNKQANT VLGKISSTLN SKNPRRQLQI PRQQPSDPDA
LKDVTDSLTN VDLASSGSSS TGSSAAAVAS KQRRRSSYAF NNGNGATNLN KSGGKKFILE
LIETVYEEIL DLEANLRNGQ QTDSTAMWEA LHIDDSSYDV NPFISMLSFD KGIKIMPRIF
NFLDKQQKLK ILQKIFNELS HLQIIILSSY KTTPKPTLTQ LKKVDLFQMI ILKIIVSFLS
NNSNFIEIMG LLLQLIRNNN VSFLTTSKIG LNLITILISR AALIKQDSSR SNILSSPEIS
TWNEIYDKLF TSLESKIQLI FPPREYNDHI MRLQNDKFMD EAYIWQFLAS LALSGKLNHQ
RIIIDEVRDE IFATINEAET LQKKEKELSV LPQRSQELDT ELKSIIYNKE KLYQDLNLFL
NVMGLVYRDG EISELK
//
