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P47068

- BBC1_YEAST

UniProt

P47068 - BBC1_YEAST

Protein

Myosin tail region-interacting protein MTI1

Gene

BBC1

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 125 (01 Oct 2014)
      Sequence version 2 (17 Jan 2003)
      Previous versions | rss
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    Functioni

    Involved in the regulation of actin cytoskeleton.1 Publication

    GO - Molecular functioni

    1. myosin I binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: SGD
    2. cytoskeleton organization Source: UniProtKB

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31492-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin tail region-interacting protein MTI1
    Alternative name(s):
    Protein BBC1
    Gene namesi
    Name:BBC1
    Synonyms:MTI1
    Ordered Locus Names:YJL020C
    ORF Names:J1286, J1305, YJL021C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL020c.
    SGDiS000003557. BBC1.

    Subcellular locationi

    Cytoplasmcytoskeletonactin patch 1 Publication
    Note: Colocalizes with cortical actin patches.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11571157Myosin tail region-interacting protein MTI1PRO_0000064839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031Phosphoserine4 Publications
    Modified residuei158 – 1581Phosphoserine3 Publications
    Modified residuei166 – 1661Phosphoserine3 Publications
    Modified residuei565 – 5651Phosphoserine3 Publications
    Modified residuei621 – 6211Phosphoserine2 Publications
    Modified residuei631 – 6311Phosphoserine3 Publications
    Modified residuei634 – 6341Phosphoserine2 Publications
    Modified residuei636 – 6361Phosphothreonine1 Publication
    Modified residuei638 – 6381Phosphoserine3 Publications
    Modified residuei647 – 6471Phosphoserine2 Publications
    Modified residuei850 – 8501Phosphothreonine1 Publication
    Modified residuei889 – 8891Phosphoserine1 Publication
    Modified residuei894 – 8941Phosphothreonine2 Publications
    Modified residuei895 – 8951Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP47068.
    PaxDbiP47068.
    PeptideAtlasiP47068.

    Expressioni

    Gene expression databases

    GenevestigatoriP47068.

    Interactioni

    Subunit structurei

    Binds to the SH3 domains of the type I myosins MYO3 and MYO5.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIM21P405638EBI-3437,EBI-25376
    APP1P539333EBI-3437,EBI-28798
    MYO3P360065EBI-3437,EBI-11670
    MYO5Q044396EBI-3437,EBI-11687
    YPR091CQ068332EBI-3437,EBI-37290

    Protein-protein interaction databases

    BioGridi33738. 128 interactions.
    DIPiDIP-2614N.
    DIP-6279N.
    IntActiP47068. 71 interactions.
    MINTiMINT-553243.

    Structurei

    Secondary structure

    1
    1157
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 149
    Beta strandi21 – 233
    Beta strandi31 – 377
    Beta strandi39 – 4810
    Beta strandi54 – 607
    Helixi61 – 633
    Beta strandi64 – 663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TG0X-ray0.97A1-68[»]
    1WDXX-ray2.50A/B/C/D1-68[»]
    1ZUKX-ray1.90A/B1-68[»]
    2DYFNMR-B796-802[»]
    ProteinModelPortaliP47068.
    SMRiP47068. Positions 3-68.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47068.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 6965SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili234 – 30168Sequence AnalysisAdd
    BLAST
    Coiled coili356 – 43075Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi278 – 412135Glu-richAdd
    BLAST
    Compositional biasi674 – 830157Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG12793.
    OMAiRTESHEE.
    OrthoDBiEOG7FBRS6.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P47068-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEPEVPFKV VAQFPYKSDY EDDLNFEKDQ EIIVTSVEDA EWYFGEYQDS     50
    NGDVIEGIFP KSFVAVQGSE VGKEAESSPN TGSTEQRTIQ PEVEQKDLPE 100
    PISPETKKET LSGPVPVPAA TVPVPAATVP VPAATAVSAQ VQHDSSSGNG 150
    ERKVPMDSPK LKARLSMFNQ DITEQVPLPK STHLDLENIP VKKTIVADAP 200
    KYYVPPGIPT NDTSNLERKK SLKENEKKIV PEPINRAQVE SGRIETENDQ 250
    LKKDLPQMSL KERIALLQEQ QRLQAAREEE LLRKKAKLEQ EHERSAVNKN 300
    EPYTETEEAE ENEKTEPKPE FTPETEHNEE PQMELLAHKE ITKTSREADE 350
    GTNDIEKEQF LDEYTKENQK VEESQADEAR GENVAEESEI GYGHEDREGD 400
    NDEEKEEEDS EENRRAALRE RMAKLSGASR FGAPVGFNPF GMASGVGNKP 450
    SEEPKKKQHK EKEEEEPEQL QELPRAIPVM PFVDPSSNPF FRKSNLSEKN 500
    QPTETKTLDP HATTEHEQKQ EHGTHAYHNL AAVDNAHPEY SDHDSDEDTD 550
    DHEFEDANDG LRKHSMVEQA FQIGNNESEN VNSGEKIYPQ EPPISHRTAE 600
    VSHDIENSSQ NTTGNVLPVS SPQTRVARNG SINSLTKSIS GENRRKSINE 650
    YHDTVSTNSS ALTETAQDIS MAAPAAPVLS KVSHPEDKVP PHPVPSAPSA 700
    PPVPSAPSVP SAPPVPPAPP ALSAPSVPPV PPVPPVSSAP PALSAPSIPP 750
    VPPTPPAPPA PPAPLALPKH NEVEEHVKSS APLPPVSEEY HPMPNTAPPL 800
    PRAPPVPPAT FEFDSEPTAT HSHTAPSPPP HQNVTASTPS MMSTQQRVPT 850
    SVLSGAEKES RTLPPHVPSL TNRPVDSFHE SDTTPKVASI RRSTTHDVGE 900
    ISNNVKIEFN AQERWWINKS APPAISNLKL NFLMEIDDHF ISKRLHQKWV 950
    VRDFYFLFEN YSQLRFSLTF NSTSPEKTVT TLQERFPSPV ETQSARILDE 1000
    YAQRFNAKVV EKSHSLINSH IGAKNFVSQI VSEFKDEVIQ PIGARTFGAT 1050
    ILSYKPEEGI EQLMKSLQKI KPGDILVIRK AKFEAHKKIG KNEIINVGMD 1100
    SAAPYSSVVT DYDFTKNKFR VIENHEGKII QNSYKLSHMK SGKLKVFRIV 1150
    ARGYVGW 1157
    Length:1,157
    Mass (Da):128,297
    Last modified:January 17, 2003 - v2
    Checksum:i88A5899B89CCE8ED
    GO

    Sequence cautioni

    The sequence CAA89311.1 differs from that shown. Reason: Frameshift at positions 729 and 732.
    The sequence CAA89312.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49295 Genomic DNA. Translation: CAA89311.1. Frameshift.
    Z49296 Genomic DNA. Translation: CAA89312.1. Different initiation.
    AF373805 Genomic DNA. Translation: AAL57239.1.
    BK006943 Genomic DNA. Translation: DAA08776.1.
    PIRiS56791.
    S56792.
    RefSeqiNP_012514.2. NM_001181454.1.

    Genome annotation databases

    EnsemblFungiiYJL020C; YJL020C; YJL020C.
    GeneIDi853433.
    KEGGisce:YJL020C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49295 Genomic DNA. Translation: CAA89311.1 . Frameshift.
    Z49296 Genomic DNA. Translation: CAA89312.1 . Different initiation.
    AF373805 Genomic DNA. Translation: AAL57239.1 .
    BK006943 Genomic DNA. Translation: DAA08776.1 .
    PIRi S56791.
    S56792.
    RefSeqi NP_012514.2. NM_001181454.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TG0 X-ray 0.97 A 1-68 [» ]
    1WDX X-ray 2.50 A/B/C/D 1-68 [» ]
    1ZUK X-ray 1.90 A/B 1-68 [» ]
    2DYF NMR - B 796-802 [» ]
    ProteinModelPortali P47068.
    SMRi P47068. Positions 3-68.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33738. 128 interactions.
    DIPi DIP-2614N.
    DIP-6279N.
    IntActi P47068. 71 interactions.
    MINTi MINT-553243.

    Proteomic databases

    MaxQBi P47068.
    PaxDbi P47068.
    PeptideAtlasi P47068.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL020C ; YJL020C ; YJL020C .
    GeneIDi 853433.
    KEGGi sce:YJL020C.

    Organism-specific databases

    CYGDi YJL020c.
    SGDi S000003557. BBC1.

    Phylogenomic databases

    eggNOGi NOG12793.
    OMAi RTESHEE.
    OrthoDBi EOG7FBRS6.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31492-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P47068.
    NextBioi 973976.
    PROi P47068.

    Gene expression databases

    Genevestigatori P47068.

    Family and domain databases

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

    Publicationsi

    1. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [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 novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich syndrome protein-interacting protein (WIP), may antagonistically regulate type I myosins in Saccharomyces cerevisiae."
      Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.
      Genetics 160:923-934(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 699-765, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    4. Pohl T.M., Aljinovic G.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1157.
    5. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    6. "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-103; SER-158; SER-166; SER-565; SER-621; SER-631; SER-634; SER-638; THR-894 AND THR-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "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-103; SER-158 AND SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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-103; SER-166; SER-565 AND SER-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-103; SER-158; SER-166; SER-565; SER-621; SER-631; SER-634; THR-636; SER-638; SER-647; THR-850; THR-894 AND THR-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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 nameiBBC1_YEAST
    AccessioniPrimary (citable) accession number: P47068
    Secondary accession number(s): D6VWG0, P47067, Q8X1F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 17, 2003
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

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

    External Data

    Dasty 3