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P25644

- PAT1_YEAST

UniProt

P25644 - PAT1_YEAST

Protein

DNA topoisomerase 2-associated protein PAT1

Gene

PAT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.19 Publications

    GO - Molecular functioni

    1. chromatin binding Source: SGD
    2. mRNA binding Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. cytoplasmic mRNA processing body assembly Source: SGD
    4. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
    5. formation of translation preinitiation complex Source: SGD
    6. mRNA processing Source: UniProtKB-KW
    7. negative regulation of translational initiation Source: SGD
    8. regulation of translational initiation Source: SGD

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Cell cycle, Cell division, mRNA processing, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29376-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA topoisomerase 2-associated protein PAT1
    Alternative name(s):
    Decapping activator and translational repressor PAT1
    Topoisomerase II-associated protein PAT1
    mRNA turnover protein 1
    Gene namesi
    Name:PAT1
    Synonyms:MRT1
    Ordered Locus Names:YCR077C
    ORF Names:YCR77C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR077c.
    SGDiS000000673. PAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytoplasmic mRNA processing body Source: SGD
    3. cytoplasmic stress granule Source: SGD
    4. cytosolic small ribosomal subunit Source: SGD
    5. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 796795DNA topoisomerase 2-associated protein PAT1PRO_0000058235Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei456 – 4561Phosphoserine1 Publication
    Modified residuei457 – 4571Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP25644.
    PaxDbiP25644.
    PeptideAtlasiP25644.

    Expressioni

    Gene expression databases

    GenevestigatoriP25644.

    Interactioni

    Subunit structurei

    Associates with the 40S ribosomal subunit. Associates with the heptameric LSM1-LSM7 complex. Interacts directly with LSM2 and LSM3 within the LSM1-LSM7 complex. Interacts with DHH1, LSM1, LSM5, RPB4, RPB7 and with topoisomerase TOP2. Interacts with CDC33, PAB1, TIF4631 and TIF4632 in an RNA-dependent manner. Binds mRNAs.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHH1P395174EBI-204,EBI-158
    LSM1P470175EBI-204,EBI-174
    LSM2P382034EBI-204,EBI-180
    LSM4P400704EBI-204,EBI-188
    LSM5P400893EBI-204,EBI-10236
    LSM7P539053EBI-204,EBI-141

    Protein-protein interaction databases

    BioGridi31052. 795 interactions.
    DIPiDIP-883N.
    IntActiP25644. 44 interactions.
    MINTiMINT-414364.
    STRINGi4932.YCR077C.

    Structurei

    Secondary structure

    1
    796
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 353
    Helixi38 – 414
    Helixi475 – 49723
    Helixi505 – 5084
    Beta strandi517 – 5204
    Helixi522 – 5265
    Helixi530 – 5345
    Helixi536 – 5405
    Helixi546 – 55712
    Turni559 – 5613
    Helixi563 – 5675
    Turni570 – 5723
    Helixi578 – 59114
    Helixi593 – 6008
    Helixi605 – 61814
    Helixi621 – 6244
    Helixi628 – 64518
    Helixi648 – 6503
    Helixi656 – 67318
    Helixi677 – 6804
    Helixi686 – 6916
    Turni692 – 6954
    Helixi702 – 71312
    Helixi718 – 7269
    Helixi728 – 73912
    Helixi742 – 7454
    Helixi761 – 78020
    Turni787 – 7904

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BRWX-ray2.80B5-79[»]
    4C8QX-ray3.70H456-783[»]
    4N0AX-ray3.15H/I/J422-796[»]
    ProteinModelPortaliP25644.
    SMRiP25644. Positions 25-54, 470-794.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi114 – 235122Pro-richAdd
    BLAST
    Compositional biasi133 – 19260Gln-richAdd
    BLAST

    Domaini

    The region at residues 254 to 422 is required for stimulation of decapping. The region at residues 422 to 763 is required for PAT1 and LSM1 to accumulate in P-bodies and responsible for translation repression and P-body assembly.1 Publication

    Sequence similaritiesi

    Belongs to the PAT1 family.Curated

    Phylogenomic databases

    eggNOGiNOG287050.
    HOGENOMiHOG000246501.
    KOiK12617.
    OMAiPHPFIAF.
    OrthoDBiEOG72RN6K.

    Family and domain databases

    InterProiIPR019167. Topo_II-assoc_PAT1.
    [Graphical view]
    PfamiPF09770. PAT1. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25644-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFFGLENSG NARDGPLDFE ESYKGYGEHE LEENDYLNDE TFGDNVQVGT    50
    DFDFGNPHSS GSSGNAIGGN GVGATARSYV AATAEGISGP RTDGTAAAGP 100
    LDLKPMESLW STAPPPAMAP SPQSTMAPAP APQQMAPLQP ILSMQDLERQ 150
    QRQMQQQFMN FHAMGHPQGL PQGPPQQQFP MQPASGQPGP SQFAPPPPPP 200
    GVNVNMNQMP MGPVQVPVQA SPSPIGMSNT PSPGPVVGAT KMPLQSGRRS 250
    KRDLSPEEQR RLQIRHAKVE KILKYSGLMT PRDKDFITRY QLSQIVTEDP 300
    YNEDFYFQVY KIIQRGGITS ESNKGLIARA YLEHSGHRLG GRYKRTDIAL 350
    QRMQSQVEKA VTVAKERPSK LKDQQAAAGN SSQDNKQANT VLGKISSTLN 400
    SKNPRRQLQI PRQQPSDPDA LKDVTDSLTN VDLASSGSSS TGSSAAAVAS 450
    KQRRRSSYAF NNGNGATNLN KSGGKKFILE LIETVYEEIL DLEANLRNGQ 500
    QTDSTAMWEA LHIDDSSYDV NPFISMLSFD KGIKIMPRIF NFLDKQQKLK 550
    ILQKIFNELS HLQIIILSSY KTTPKPTLTQ LKKVDLFQMI ILKIIVSFLS 600
    NNSNFIEIMG LLLQLIRNNN VSFLTTSKIG LNLITILISR AALIKQDSSR 650
    SNILSSPEIS TWNEIYDKLF TSLESKIQLI FPPREYNDHI MRLQNDKFMD 700
    EAYIWQFLAS LALSGKLNHQ RIIIDEVRDE IFATINEAET LQKKEKELSV 750
    LPQRSQELDT ELKSIIYNKE KLYQDLNLFL NVMGLVYRDG EISELK 796
    Length:796
    Mass (Da):88,511
    Last modified:July 27, 2011 - v4
    Checksum:i2DBE1210C173E468
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti688 – 6881D → V in CAC42990. (PubMed:1574125)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAC42990.1.
    BK006937 Genomic DNA. Translation: DAA07549.2.
    PIRiS53590.
    RefSeqiNP_010002.3. NM_001178786.2.

    Genome annotation databases

    EnsemblFungiiYCR077C; YCR077C; YCR077C.
    GeneIDi850440.
    KEGGisce:YCR077C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAC42990.1 .
    BK006937 Genomic DNA. Translation: DAA07549.2 .
    PIRi S53590.
    RefSeqi NP_010002.3. NM_001178786.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BRW X-ray 2.80 B 5-79 [» ]
    4C8Q X-ray 3.70 H 456-783 [» ]
    4N0A X-ray 3.15 H/I/J 422-796 [» ]
    ProteinModelPortali P25644.
    SMRi P25644. Positions 25-54, 470-794.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31052. 795 interactions.
    DIPi DIP-883N.
    IntActi P25644. 44 interactions.
    MINTi MINT-414364.
    STRINGi 4932.YCR077C.

    Proteomic databases

    MaxQBi P25644.
    PaxDbi P25644.
    PeptideAtlasi P25644.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR077C ; YCR077C ; YCR077C .
    GeneIDi 850440.
    KEGGi sce:YCR077C.

    Organism-specific databases

    CYGDi YCR077c.
    SGDi S000000673. PAT1.

    Phylogenomic databases

    eggNOGi NOG287050.
    HOGENOMi HOG000246501.
    KOi K12617.
    OMAi PHPFIAF.
    OrthoDBi EOG72RN6K.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29376-MONOMER.

    Miscellaneous databases

    NextBioi 966042.
    PROi P25644.

    Gene expression databases

    Genevestigatori P25644.

    Family and domain databases

    InterProi IPR019167. Topo_II-assoc_PAT1.
    [Graphical view ]
    Pfami PF09770. PAT1. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Valles G., Volckaerts G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 688.
      Strain: ATCC 204508 / S288c.
    4. "Identification and initial characterization of the cytosolic protein Ycr77p."
      Rodriguez-Cousino N., Lill R., Neupert W., Court D.A.
      Yeast 11:581-585(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION, CHARACTERIZATION.
    5. "Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae."
      Hatfield L., Beelman C.A., Stevens A., Parker R.
      Mol. Cell. Biol. 16:5830-5838(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Pat1: a topoisomerase II-associated protein required for faithful chromosome transmission in Saccharomyces cerevisiae."
      Wang X., Watt P.M., Louis E.J., Borts R.H., Hickson I.D.
      Nucleic Acids Res. 24:4791-4797(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of the decapping enzyme."
      Zhang S., Williams C.J., Hagan K., Peltz S.W.
      Mol. Cell. Biol. 19:7568-7576(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The topoisomerase II-associated protein, Pat1p, is required for maintenance of rDNA locus stability in Saccharomyces cerevisiae."
      Wang X., Watt P.M., Borts R.H., Louis E.J., Hickson I.D.
      Mol. Gen. Genet. 261:831-840(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "A Sm-like protein complex that participates in mRNA degradation."
      Bouveret E., Rigaut G., Shevchenko A., Wilm M., Seraphin B.
      EMBO J. 19:1661-1671(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE LSM1-LSM7 COMPLEX.
    10. "Deletion of the PAT1 gene affects translation initiation and suppresses a PAB1 gene deletion in yeast."
      Wyers F., Minet M., Dufour M.E., Vo L.T., Lacroute F.
      Mol. Cell. Biol. 20:3538-3549(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE 40S RIBOSOMAL SUBUNIT.
    11. "The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p."
      Bonnerot C., Boeck R., Lapeyre B.
      Mol. Cell. Biol. 20:5939-5946(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LSM1.
    12. "mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E."
      Schwartz D.C., Parker R.
      Mol. Cell. Biol. 20:7933-7942(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Yeast Sm-like proteins function in mRNA decapping and decay."
      Tharun S., He W., Mayes A.E., Lennertz P., Beggs J.D., Parker R.
      Nature 404:515-518(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LSM1 AND LSM5.
    14. "The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation."
      He W., Parker R.
      Genetics 158:1445-1455(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
      Tharun S., Parker R.
      Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC33; PAB1; TIF4631 AND TIF4632, MRNA-BINDING.
    16. "The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes."
      Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R.
      RNA 7:1717-1727(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DHH1.
    17. "The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1."
      Fischer N., Weis K.
      EMBO J. 21:2788-2797(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DHH1.
    18. "Yeast Lsm1p-7p/Pat1p deadenylation-dependent mRNA-decapping factors are required for brome mosaic virus genomic RNA translation."
      Noueiry A.O., Diez J., Falk S.P., Chen J., Ahlquist P.
      Mol. Cell. Biol. 23:4094-4106(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    20. "Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
      Sheth U., Parker R.
      Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    21. "General translational repression by activators of mRNA decapping."
      Coller J., Parker R.
      Cell 122:875-886(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "The RNA polymerase II subunit Rpb4p mediates decay of a specific class of mRNAs."
      Lotan R., Bar-On V.G., Harel-Sharvit L., Duek L., Melamed D., Choder M.
      Genes Dev. 19:3004-3016(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPB4.
    23. "Processing bodies require RNA for assembly and contain nontranslating mRNAs."
      Teixeira D., Sheth U., Valencia-Sanchez M.A., Brengues M., Parker R.
      RNA 11:371-382(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    24. "Targeting of aberrant mRNAs to cytoplasmic processing bodies."
      Sheth U., Parker R.
      Cell 125:1095-1109(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    25. "The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major cytoplasmic mRNA decay mechanisms."
      Lotan R., Goler-Baron V., Duek L., Haimovich G., Choder M.
      J. Cell Biol. 178:1133-1143(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPB7.
    26. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    27. "Analysis of P-body assembly in Saccharomyces cerevisiae."
      Teixeira D., Parker R.
      Mol. Biol. Cell 18:2274-2287(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    28. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs."
      Chowdhury A., Mukhopadhyay J., Tharun S.
      RNA 13:998-1016(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "Purification and analysis of the decapping activator Lsm1p-7p-Pat1p complex from yeast."
      Tharun S.
      Methods Enzymol. 448:41-55(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE LSM1-LSM7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    31. "Pat1 contains distinct functional domains that promote P-body assembly and activation of decapping."
      Pilkington G.R., Parker R.
      Mol. Cell. Biol. 28:1298-1312(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, RNA-BINDING.
    32. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "P-body components are required for Ty1 retrotransposition during assembly of retrotransposition-competent virus-like particles."
      Checkley M.A., Nagashima K., Lockett S.J., Nyswaner K.M., Garfinkel D.J.
      Mol. Cell. Biol. 30:382-398(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    35. "Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms."
      Nissan T., Rajyaguru P., She M., Song H., Parker R.
      Mol. Cell 39:773-783(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    36. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    37. "Architecture of the Lsm1-7-Pat1 complex: a conserved assembly in eukaryotic mRNA turnover."
      Sharif H., Conti E.
      Cell Rep. 5:283-291(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 456-783 IN COMPLEX WITH THE LSM1-LSM7 COMPLEX, SUBUNIT.
    38. "Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation."
      Wu D., Muhlrad D., Bowler M.W., Jiang S., Liu Z., Parker R., Song H.
      Cell Res. 24:233-246(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 422-796 IN COMPLEX WITH THE LSM1-LSM7 COMPLEX, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiPAT1_YEAST
    AccessioniPrimary (citable) accession number: P25644
    Secondary accession number(s): D6VR80, Q8NKJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 123 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 656 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3