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P53297

- PBP1_YEAST

UniProt

P53297 - PBP1_YEAST

Protein

PAB1-binding protein 1

Gene

PBP1

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 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Appears to promote proper polyadenylation. In the absence of PBP1, the 3'termini of pre-mRNAs are properly cleaved but lack full-length poly(A) tails. May act to repress the ability of PAB1 to negatively regulate polyadenylation. Negative regulator of poly(A) nuclease (PAN) activity.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. mRNA polyadenylation Source: SGD
    2. positive regulation of translation Source: SGD
    3. stress granule assembly Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30871-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PAB1-binding protein 1
    Gene namesi
    Name:PBP1
    Synonyms:MRS16
    Ordered Locus Names:YGR178C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR178c.
    SGDiS000003410. PBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic stress granule Source: SGD
    2. mitochondrion Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell
    4. polysome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 722722PAB1-binding protein 1PRO_0000058244Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei106 – 1061Phosphoserine3 Publications
    Modified residuei193 – 1931Phosphothreonine1 Publication
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei436 – 4361Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53297.
    PaxDbiP53297.
    PeptideAtlasiP53297.

    Expressioni

    Gene expression databases

    GenevestigatoriP53297.

    Interactioni

    Subunit structurei

    Interacts with FIR1, IGO1, LSM12, PBP4 and PAB1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM12P388286EBI-12961,EBI-24700

    Protein-protein interaction databases

    BioGridi33430. 127 interactions.
    DIPiDIP-2464N.
    IntActiP53297. 23 interactions.
    MINTiMINT-488669.
    STRINGi4932.YGR178C.

    Structurei

    3D structure databases

    ProteinModelPortaliP53297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ataxin-2 family.Curated

    Phylogenomic databases

    eggNOGiCOG5180.
    GeneTreeiENSGT00530000063565.
    HOGENOMiHOG000093792.
    OMAiIEKPYFT.
    OrthoDBiEOG7TF7K9.

    Family and domain databases

    InterProiIPR009604. LsmAD_domain.
    IPR025852. SM_dom_ATX.
    [Graphical view]
    PfamiPF06741. LsmAD. 1 hit.
    PF14438. SM-ATX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53297-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGNFRKRDS STNSRKGGNS DSNYTNGGVP NQNNSSMFYE NPEITRNFDD    50
    RQDYLLANSI GSDVTVTVTS GVKYTGLLVS CNLESTNGID VVLRFPRVAD 100
    SGVSDSVDDL AKTLGETLLI HGEDVAELEL KNIDLSLDEK WENSKAQETT 150
    PARTNIEKER VNGESNEVTK FRTDVDISGS GREIKERKLE KWTPEEGAEH 200
    FDINKGKALE DDSASWDQFA VNEKKFGVKS TFDEHLYTTK INKDDPNYSK 250
    RLQEAERIAK EIESQGTSGN IHIAEDRGII IDDSGLDEED LYSGVDRRGD 300
    ELLAALKSNS KPNSNKGNRY VPPTLRQQPH HMDPAIISSS NSNKNENAVS 350
    TDTSTPAAAG APEGKPPQKT SKNKKSLSSK EAQIEELKKF SEKFKVPYDI 400
    PKDMLEVLKR SSSTLKSNSS LPPKPISKTP SAKTVSPTTQ ISAGKSESRR 450
    SGSNISQGQS STGHTTRSST SLRRRNHGSF FGAKNPHTND AKRVLFGKSF 500
    NMFIKSKEAH DEKKKGDDAS ENMEPFFIEK PYFTAPTWLN TIEESYKTFF 550
    PDEDTAIQEA QTRFQQRQLN SMGNAVPGMN PAMGMNMGGM MGFPMGGPSA 600
    SPNPMMNGFA AGSMGMYMPF QPQPMFYHPS MPQMMPVMGS NGAEEGGGNI 650
    SPHVPAGFMA AGPGAPMGAF GYPGGIPFQG MMGSGPSGMP ANGSAMHSHG 700
    HSRNYHQTSH HGHHNSSTSG HK 722
    Length:722
    Mass (Da):78,781
    Last modified:October 1, 1996 - v1
    Checksum:i92005F3A2346193E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46931 Genomic DNA. Translation: AAB94294.1.
    Z72963 Genomic DNA. Translation: CAA97204.1.
    BK006941 Genomic DNA. Translation: DAA08273.1.
    PIRiS64492.
    RefSeqiNP_011694.3. NM_001181307.3.

    Genome annotation databases

    EnsemblFungiiYGR178C; YGR178C; YGR178C.
    GeneIDi853089.
    KEGGisce:YGR178C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46931 Genomic DNA. Translation: AAB94294.1 .
    Z72963 Genomic DNA. Translation: CAA97204.1 .
    BK006941 Genomic DNA. Translation: DAA08273.1 .
    PIRi S64492.
    RefSeqi NP_011694.3. NM_001181307.3.

    3D structure databases

    ProteinModelPortali P53297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33430. 127 interactions.
    DIPi DIP-2464N.
    IntActi P53297. 23 interactions.
    MINTi MINT-488669.
    STRINGi 4932.YGR178C.

    Proteomic databases

    MaxQBi P53297.
    PaxDbi P53297.
    PeptideAtlasi P53297.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR178C ; YGR178C ; YGR178C .
    GeneIDi 853089.
    KEGGi sce:YGR178C.

    Organism-specific databases

    CYGDi YGR178c.
    SGDi S000003410. PBP1.

    Phylogenomic databases

    eggNOGi COG5180.
    GeneTreei ENSGT00530000063565.
    HOGENOMi HOG000093792.
    OMAi IEKPYFT.
    OrthoDBi EOG7TF7K9.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30871-MONOMER.

    Miscellaneous databases

    NextBioi 973070.

    Gene expression databases

    Genevestigatori P53297.

    Family and domain databases

    InterProi IPR009604. LsmAD_domain.
    IPR025852. SM_dom_ATX.
    [Graphical view ]
    Pfami PF06741. LsmAD. 1 hit.
    PF14438. SM-ATX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing and characterization of a suppressor of the pet- phenotype in a Saccharomyces cerevisiae strain without mitochondrial group II introns."
      Mecklenbrauker I.
      Thesis (1996), Vienna Biocentre, Austria
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 44774 / DBY747.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation."
      Mangus D.A., Amrani N., Jacobson A.
      Mol. Cell. Biol. 18:7383-7396(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAB1.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
      Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
      Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LSM12 AND PBP4, IDENTIFICATION BY MASS SPECTROMETRY.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    9. "Identification of factors regulating poly(A) tail synthesis and maturation."
      Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A.
      Mol. Cell. Biol. 24:4196-4206(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FIR1 AND PBP4.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-215 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-106 AND THR-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Initiation of the TORC1-regulated G0 program requires Igo1/2, which license specific mRNAs to evade degradation via the 5'-3' mRNA decay pathway."
      Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S., Devgan G., Snyder M., Broach J.R., De Virgilio C.
      Mol. Cell 38:345-355(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGO1.
    14. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPBP1_YEAST
    AccessioniPrimary (citable) accession number: P53297
    Secondary accession number(s): D6VUW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2870 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3