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P53281

- LSB1_YEAST

UniProt

P53281 - LSB1_YEAST

Protein

LAS seventeen-binding protein 1

Gene

LSB1

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 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in resistance to EDTA.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-30842-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LAS seventeen-binding protein 1
    Short name:
    LAS17-binding protein 1
    Gene namesi
    Name:LSB1
    Ordered Locus Names:YGR136W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR136w.
    SGDiS000003368. LSB1.

    Subcellular locationi

    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
    Mutagenesisi90 – 901W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 241240LAS seventeen-binding protein 1PRO_0000202825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Cross-linki41 – 41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei48 – 481Phosphoserine1 Publication
    Cross-linki79 – 79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei114 – 1141Phosphoserine1 Publication
    Modified residuei116 – 1161Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated by RSP5.4 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP53281.
    PaxDbiP53281.
    PeptideAtlasiP53281.

    Expressioni

    Gene expression databases

    GenevestigatoriP53281.

    Interactioni

    Subunit structurei

    Interacts with LAS17, RSP5 and SUP35.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACF2Q121684EBI-23329,EBI-32973
    AIM21P405635EBI-23329,EBI-25376
    AIM3P382663EBI-23329,EBI-21584
    APP1P539334EBI-23329,EBI-28798
    GYL1Q043222EBI-23329,EBI-27427

    Protein-protein interaction databases

    BioGridi33384. 32 interactions.
    DIPiDIP-1863N.
    IntActiP53281. 29 interactions.
    MINTiMINT-375073.
    STRINGi4932.YGR136W.

    Structurei

    3D structure databases

    ProteinModelPortaliP53281.
    SMRiP53281. Positions 56-111.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 11260SH3PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi135 – 1384PY motif

    Domaini

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

    Sequence similaritiesi

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

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG136033.
    GeneTreeiENSGT00510000054224.
    HOGENOMiHOG000195703.
    OMAiSQTKQNV.
    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.

    P53281-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSASLVNRSL KNIRNELEFL KESNVISGDI FELINSKLPE KWDGNQRSPQ    50
    NADTEEYVEA LYDFEAQQDG DLSLKTGDKI QVLEKISPDW YRGKSNNKIG 100
    IFPANYVKPA FTRSASPKSA EAASSSTVSR PSVPPPSYEP AASQYPSQQV 150
    SAPYAPPAGY MQAPPPQQQQ APLPYPPPFT NYYQQPQQQY APPSQQAPVE 200
    AQPQQSSGAS SAFKSFGSKL GNAAIFGAGS AIGSDIVNSI F 241
    Length:241
    Mass (Da):26,139
    Last modified:October 1, 1996 - v1
    Checksum:i5F0B1361AF84AA79
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72921 Genomic DNA. Translation: CAA97149.1.
    BK006941 Genomic DNA. Translation: DAA08229.1.
    PIRiS64445.
    RefSeqiNP_011652.1. NM_001181265.1.

    Genome annotation databases

    EnsemblFungiiYGR136W; YGR136W; YGR136W.
    GeneIDi853037.
    KEGGisce:YGR136W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72921 Genomic DNA. Translation: CAA97149.1 .
    BK006941 Genomic DNA. Translation: DAA08229.1 .
    PIRi S64445.
    RefSeqi NP_011652.1. NM_001181265.1.

    3D structure databases

    ProteinModelPortali P53281.
    SMRi P53281. Positions 56-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33384. 32 interactions.
    DIPi DIP-1863N.
    IntActi P53281. 29 interactions.
    MINTi MINT-375073.
    STRINGi 4932.YGR136W.

    Proteomic databases

    MaxQBi P53281.
    PaxDbi P53281.
    PeptideAtlasi P53281.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR136W ; YGR136W ; YGR136W .
    GeneIDi 853037.
    KEGGi sce:YGR136W.

    Organism-specific databases

    CYGDi YGR136w.
    SGDi S000003368. LSB1.

    Phylogenomic databases

    eggNOGi NOG136033.
    GeneTreei ENSGT00510000054224.
    HOGENOMi HOG000195703.
    OMAi SQTKQNV.
    OrthoDBi EOG75MW70.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30842-MONOMER.

    Miscellaneous databases

    NextBioi 972938.

    Gene expression databases

    Genevestigatori P53281.

    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 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.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "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.
    4. Cited for: FUNCTION.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79.
      Strain: SUB592.
    7. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79.
    8. "Ubiquitination screen using protein microarrays for comprehensive identification of Rsp5 substrates in yeast."
      Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N.J., Parkinson J., Rotin D.
      Mol. Syst. Biol. 3:116-116(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY RSP5.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: UBIQUITINATION BY RSP5, INTERACTION WITH RSP5.
    12. "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: SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-90, INTERACTION WITH LAS17 AND SUP35.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    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 nameiLSB1_YEAST
    AccessioniPrimary (citable) accession number: P53281
    Secondary accession number(s): D6VUR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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