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Protein

DNA topoisomerase 2-associated protein PAT1

Gene

PAT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • chromatin binding Source: SGD
  • mRNA binding Source: SGD
  • RNA binding Source: SGD

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • CENP-A containing chromatin organization Source: SGD
  • chromosome segregation Source: SGD
  • cytoplasmic mRNA processing body assembly Source: SGD
  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  • formation of translation preinitiation complex Source: SGD
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of translational initiation Source: SGD
  • regulation of translational initiation Source: SGD
Complete GO annotation...

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 Componenti: Chromosome III

Organism-specific databases

CYGDiYCR077c.
EuPathDBiFungiDB:YCR077C.
SGDiS000000673. PAT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • cytoplasmic stress granule Source: SGD
  • cytosolic small ribosomal subunit Source: SGD
  • kinetochore Source: SGD
  • Lsm1-7-Pat1 complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

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.

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.

Structurei

Secondary structure

1
796
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 353Combined sources
Helixi38 – 414Combined sources
Helixi475 – 49723Combined sources
Helixi505 – 5106Combined sources
Turni511 – 5144Combined sources
Beta strandi517 – 5204Combined sources
Helixi522 – 5265Combined sources
Helixi530 – 5345Combined sources
Helixi536 – 5416Combined sources
Helixi545 – 55814Combined sources
Helixi559 – 5613Combined sources
Helixi563 – 5686Combined sources
Turni570 – 5723Combined sources
Helixi578 – 59922Combined sources
Beta strandi600 – 6023Combined sources
Helixi605 – 61713Combined sources
Helixi621 – 6255Combined sources
Helixi628 – 64215Combined sources
Turni650 – 6523Combined sources
Helixi656 – 67318Combined sources
Helixi677 – 6804Combined sources
Helixi684 – 69310Combined sources
Helixi702 – 71312Combined sources
Helixi717 – 72610Combined sources
Helixi728 – 74922Combined sources
Beta strandi751 – 7533Combined sources
Helixi756 – 78227Combined sources
Beta strandi785 – 7884Combined sources
Beta strandi791 – 7944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BRWX-ray2.80B5-79[»]
4C8QX-ray3.70H456-783[»]
4N0AX-ray3.15H/I/J422-796[»]
4OGPX-ray2.15A/B473-796[»]
4OJJX-ray2.32A/B/C473-796[»]
ProteinModelPortaliP25644.
SMRiP25644. Positions 25-54, 476-796.
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.
InParanoidiP25644.
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

        10         20         30         40         50
MSFFGLENSG NARDGPLDFE ESYKGYGEHE LEENDYLNDE TFGDNVQVGT
60 70 80 90 100
DFDFGNPHSS GSSGNAIGGN GVGATARSYV AATAEGISGP RTDGTAAAGP
110 120 130 140 150
LDLKPMESLW STAPPPAMAP SPQSTMAPAP APQQMAPLQP ILSMQDLERQ
160 170 180 190 200
QRQMQQQFMN FHAMGHPQGL PQGPPQQQFP MQPASGQPGP SQFAPPPPPP
210 220 230 240 250
GVNVNMNQMP MGPVQVPVQA SPSPIGMSNT PSPGPVVGAT KMPLQSGRRS
260 270 280 290 300
KRDLSPEEQR RLQIRHAKVE KILKYSGLMT PRDKDFITRY QLSQIVTEDP
310 320 330 340 350
YNEDFYFQVY KIIQRGGITS ESNKGLIARA YLEHSGHRLG GRYKRTDIAL
360 370 380 390 400
QRMQSQVEKA VTVAKERPSK LKDQQAAAGN SSQDNKQANT VLGKISSTLN
410 420 430 440 450
SKNPRRQLQI PRQQPSDPDA LKDVTDSLTN VDLASSGSSS TGSSAAAVAS
460 470 480 490 500
KQRRRSSYAF NNGNGATNLN KSGGKKFILE LIETVYEEIL DLEANLRNGQ
510 520 530 540 550
QTDSTAMWEA LHIDDSSYDV NPFISMLSFD KGIKIMPRIF NFLDKQQKLK
560 570 580 590 600
ILQKIFNELS HLQIIILSSY KTTPKPTLTQ LKKVDLFQMI ILKIIVSFLS
610 620 630 640 650
NNSNFIEIMG LLLQLIRNNN VSFLTTSKIG LNLITILISR AALIKQDSSR
660 670 680 690 700
SNILSSPEIS TWNEIYDKLF TSLESKIQLI FPPREYNDHI MRLQNDKFMD
710 720 730 740 750
EAYIWQFLAS LALSGKLNHQ RIIIDEVRDE IFATINEAET LQKKEKELSV
760 770 780 790
LPQRSQELDT ELKSIIYNKE KLYQDLNLFL NVMGLVYRDG EISELK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42990.1.
BK006937 Genomic DNA. Translation: DAA07549.2.
PIRiS53590.
RefSeqiNP_010002.3. NM_001178786.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BRWX-ray2.80B5-79[»]
4C8QX-ray3.70H456-783[»]
4N0AX-ray3.15H/I/J422-796[»]
4OGPX-ray2.15A/B473-796[»]
4OJJX-ray2.32A/B/C473-796[»]
ProteinModelPortaliP25644.
SMRiP25644. Positions 25-54, 476-796.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP25644.
PaxDbiP25644.
PeptideAtlasiP25644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYCR077c.
EuPathDBiFungiDB:YCR077C.
SGDiS000000673. PAT1.

Phylogenomic databases

eggNOGiNOG287050.
HOGENOMiHOG000246501.
InParanoidiP25644.
KOiK12617.
OMAiPHPFIAF.
OrthoDBiEOG72RN6K.

Enzyme and pathway databases

BioCyciYEAST:G3O-29376-MONOMER.

Miscellaneous databases

NextBioi966042.
PROiP25644.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 131 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.