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Q06449

- PIN3_YEAST

UniProt

Q06449 - PIN3_YEAST

Protein

[PSI+] inducibility protein 3

Gene

PIN3

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 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Overproduction promotes the de novo induction of the [PSI+] prion form of SUP35. The prion-inducing effect depends on the association with the actin cytoskeleton. Also implicated in prion maintenance during heat stress.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. negative regulation of Arp2/3 complex-mediated actin nucleation Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34285-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [PSI+] inducibility protein 3
    Alternative name(s):
    LAS seventeen-binding protein 2
    Short name:
    LAS17-binding protein 2
    Gene namesi
    Name:PIN3
    Synonyms:LSB2
    Ordered Locus Names:YPR154W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPR154w.
    SGDiS000006358. PIN3.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmcytoskeletonactin patch
    Note: When overexpressed, localizes to punctate structures which are reminiscent of cortical actin patches. Transiently colocalizes with SUP35 aggregates during prionogenesis.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. cytoplasm Source: SGD
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801K → R: Abolishes formation of ubiquitinated protein forms. 1 Publication
    Mutagenesisi91 – 911W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin, aggregation, and prion-inducing ability. 1 Publication
    Mutagenesisi124 – 1252PP → AA: Abolishes RSP5 binding site and consequently ubiquitination.
    Mutagenesisi174 – 1752QQ → AA: Reduces, but does not abolish the ability to promote [PSI+] induction.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 215214[PSI+] inducibility protein 3PRO_0000268696Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei52 – 521Phosphoserine1 Publication
    Modified residuei55 – 551Phosphoserine1 Publication
    Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Ubiquitinated by RSP5. Ubiquitination reduces the protein abundance and its prion-inducing ability.3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ06449.
    PaxDbiQ06449.
    PeptideAtlasiQ06449.

    Expressioni

    Inductioni

    By heat shock. Can thereby reach physiological protein levels high enough to promote prion-formation.1 Publication

    Gene expression databases

    GenevestigatoriQ06449.

    Interactioni

    Subunit structurei

    Interacts with LAS17, RSP5 and SUP35.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APP1P539334EBI-35523,EBI-28798
    LAS17Q124464EBI-35523,EBI-10022
    VTC4P470752EBI-35523,EBI-25789
    YIL108WP404833EBI-35523,EBI-25176

    Protein-protein interaction databases

    BioGridi36321. 51 interactions.
    DIPiDIP-6257N.
    IntActiQ06449. 45 interactions.
    MINTiMINT-374980.
    STRINGi4932.YPR154W.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi58 – 614
    Beta strandi80 – 867
    Beta strandi88 – 969
    Beta strandi99 – 1046
    Helixi105 – 1073
    Beta strandi108 – 1103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YNZX-ray2.20A57-112[»]
    1ZX6X-ray1.60A57-112[»]
    ProteinModelPortaliQ06449.
    SMRiQ06449. Positions 57-112.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06449.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 11360SH3PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi124 – 1274PY motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi122 – 1254Poly-Pro
    Compositional biasi126 – 18156Asn/Gln-richAdd
    BLAST

    Domaini

    The PY motif is recognized directly by the WW domains of RSP5.

    Sequence similaritiesi

    Belongs to the LSB1 family.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG298780.
    GeneTreeiENSGT00510000054224.
    HOGENOMiHOG000195703.
    OMAiYVKPAFS.
    OrthoDBiEOG75MW70.

    Family and domain databases

    InterProiIPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q06449-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSASLINRSL TNIRTELDFL KGSNVISNDV YDQINKSLPA KWDPANAPRN    50
    ASPASLEYVE ALYQFDPQQD GDLGLKPGDK VQLLEKLSPE WYKGSCNGRT 100
    GIFPANYVKP AFSGSNGPSN LPPPPQYKAQ ELQQIPTQNS AASSYQQQPF 150
    PPPSTNYYQQ PQQQPQQAPP PQQQQQQQQH QSSHSHLKSF GSKLGNAAIF 200
    GAGASIGSDI VNNIF 215
    Length:215
    Mass (Da):23,539
    Last modified:November 1, 1996 - v1
    Checksum:i37C95425B02FB284
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28371 Genomic DNA. Translation: AAB68051.1.
    AY692989 Genomic DNA. Translation: AAT93008.1.
    BK006949 Genomic DNA. Translation: DAA11566.1.
    PIRiS61138.
    RefSeqiNP_015480.1. NM_001184251.1.

    Genome annotation databases

    EnsemblFungiiYPR154W; YPR154W; YPR154W.
    GeneIDi856277.
    KEGGisce:YPR154W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28371 Genomic DNA. Translation: AAB68051.1 .
    AY692989 Genomic DNA. Translation: AAT93008.1 .
    BK006949 Genomic DNA. Translation: DAA11566.1 .
    PIRi S61138.
    RefSeqi NP_015480.1. NM_001184251.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YNZ X-ray 2.20 A 57-112 [» ]
    1ZX6 X-ray 1.60 A 57-112 [» ]
    ProteinModelPortali Q06449.
    SMRi Q06449. Positions 57-112.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36321. 51 interactions.
    DIPi DIP-6257N.
    IntActi Q06449. 45 interactions.
    MINTi MINT-374980.
    STRINGi 4932.YPR154W.

    Proteomic databases

    MaxQBi Q06449.
    PaxDbi Q06449.
    PeptideAtlasi Q06449.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPR154W ; YPR154W ; YPR154W .
    GeneIDi 856277.
    KEGGi sce:YPR154W.

    Organism-specific databases

    CYGDi YPR154w.
    SGDi S000006358. PIN3.

    Phylogenomic databases

    eggNOGi NOG298780.
    GeneTreei ENSGT00510000054224.
    HOGENOMi HOG000195703.
    OMAi YVKPAFS.
    OrthoDBi EOG75MW70.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34285-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q06449.
    NextBioi 981592.

    Gene expression databases

    Genevestigatori Q06449.

    Family and domain databases

    InterProi IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex."
      Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C., Soulard A., Moreau V., Winsor B.
      Mol. Biol. Cell 10:3521-3538(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LAS17.
    5. "Prions affect the appearance of other prions: the story of [PIN(+)]."
      Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.
      Cell 106:171-182(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION FORMATION.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-80.
      Strain: SUB592.
    9. "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-52 AND SER-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: UBIQUITINATION BY RSP5, INTERACTION WITH RSP5.
    11. "Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton."
      Chernova T.A., Romanyuk A.V., Karpova T.S., Shanks J.R., Ali M., Moffatt N., Howie R.L., O'Dell A., McNally J.G., Liebman S.W., Chernoff Y.O., Wilkinson K.D.
      Mol. Cell 43:242-252(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION BY RSP5, MUTAGENESIS OF LYS-80; TRP-91; 124-PRO-PRO-125 AND 174-GLN-GLN-175, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH LAS17 AND SUP35.
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "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].
    14. "Structural genomics of yeast SH3 domains."
      Kursula P., Kursula I., Lehmann F., Zou P., Song Y.H., Wilmanns M.
      Submitted (JUN-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 57-112.

    Entry informationi

    Entry nameiPIN3_YEAST
    AccessioniPrimary (citable) accession number: Q06449
    Secondary accession number(s): D6W4F0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 110 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 2190 molecules/cell in log phase SD medium.1 Publication
    Although this protein promotes prion formation and it has a Asn/Gln-rich prion-like domain, it does not seem to have a prion form by itself.

    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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3