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Q04439

- MYO5_YEAST

UniProt

Q04439 - MYO5_YEAST

Protein

Myosin-5

Gene

MYO5

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 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi129 – 1368ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. microfilament motor activity Source: SGD
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cortical patch localization Source: SGD
    2. bipolar cellular bud site selection Source: SGD
    3. endocytosis Source: SGD
    4. exocytosis Source: SGD
    5. fungal-type cell wall organization Source: SGD
    6. metabolic process Source: GOC
    7. receptor-mediated endocytosis Source: SGD
    8. response to osmotic stress Source: SGD
    9. response to salt stress Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Motor protein, Myosin

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32805-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin-5
    Alternative name(s):
    Actin-dependent myosin-I MYO5
    Class I unconventional myosin MYO5
    Type I myosin MYO5
    Gene namesi
    Name:MYO5
    Ordered Locus Names:YMR109W
    ORF Names:YM9718.08
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR109w.
    SGDiS000004715. MYO5.

    Subcellular locationi

    Cytoplasmcytoskeletonactin patch 4 Publications
    Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. myosin complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1641V → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
    Mutagenesisi168 – 1681N → I: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
    Mutagenesisi209 – 2091N → S: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
    Mutagenesisi357 – 3571S → A: Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2. 1 Publication
    Mutagenesisi357 – 3571S → E: No growth defect, but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2. 1 Publication
    Mutagenesisi377 – 3771K → M: Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization. 1 Publication
    Mutagenesisi472 – 4721E → K in MYO5-1; temperature sensitive loss of function. 1 Publication
    Mutagenesisi1123 – 11231W → S: Abolishes interaction with BBC1 and VRP1. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12191219Myosin-5PRO_0000123492Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei357 – 3571Phosphoserine4 Publications
    Modified residuei359 – 3591Phosphotyrosine1 Publication
    Modified residuei777 – 7771Phosphoserine1 Publication
    Modified residuei992 – 9921Phosphoserine1 Publication
    Modified residuei1205 – 12051Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ04439.
    PaxDbiQ04439.
    PeptideAtlasiQ04439.

    Expressioni

    Gene expression databases

    GenevestigatoriQ04439.

    Interactioni

    Subunit structurei

    Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-11687,EBI-11687
    AIM21P405632EBI-11687,EBI-25376
    APP1P539332EBI-11687,EBI-28798
    ARC40P383283EBI-11687,EBI-2777
    BBC1P470686EBI-11687,EBI-3437
    BCK1Q013896EBI-11687,EBI-3470
    BNR1P404507EBI-11687,EBI-3711
    BZZ1P388225EBI-11687,EBI-3889
    CDC55Q003624EBI-11687,EBI-1942
    CLA4P485623EBI-11687,EBI-4750
    CMD1P067877EBI-11687,EBI-3976
    LAS17Q124467EBI-11687,EBI-10022
    OSH2Q124516EBI-11687,EBI-12621
    PAN1P325212EBI-11687,EBI-12875
    PKH3Q033062EBI-11687,EBI-37683
    PRP8P333344EBI-11687,EBI-465
    RVS167P397433EBI-11687,EBI-14500
    SAP1P399554EBI-11687,EBI-16463
    STE20Q034974EBI-11687,EBI-18285
    UBP7P404534EBI-11687,EBI-19857
    VRP1P3737019EBI-11687,EBI-20502
    YOR389WQ089122EBI-11687,EBI-38289
    ZRG8P400212EBI-11687,EBI-22484

    Protein-protein interaction databases

    BioGridi35285. 116 interactions.
    DIPiDIP-2222N.
    IntActiQ04439. 99 interactions.
    MINTiMINT-593586.
    STRINGi4932.YMR109W.

    Structurei

    Secondary structure

    1
    1219
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1089 – 10946
    Beta strandi1112 – 11187
    Beta strandi1122 – 11309
    Beta strandi1134 – 11385
    Helixi1139 – 11413
    Beta strandi1142 – 11443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YP5X-ray1.68A1088-1145[»]
    1ZUYX-ray1.39A/B1088-1145[»]
    ProteinModelPortaliQ04439.
    SMRiQ04439. Positions 37-715, 1088-1145.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04439.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 715680Myosin motorAdd
    BLAST
    Domaini719 – 73921IQ 1Add
    BLAST
    Domaini740 – 76526IQ 2Add
    BLAST
    Domaini1085 – 114763SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni404 – 48683Actin-bindingBy similarityAdd
    BLAST
    Regioni766 – 961196Basic, putative membrane-binding regionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1000 – 108889Ala/Pro-richAdd
    BLAST
    Compositional biasi1011 – 10166Poly-Pro
    Compositional biasi1060 – 10634Poly-Ala
    Compositional biasi1073 – 10819Poly-Pro
    Compositional biasi1204 – 121815Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.
    The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding domain (TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

    Sequence similaritiesi

    Contains 2 IQ domains.Curated
    Contains 1 myosin motor domain.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG5022.
    GeneTreeiENSGT00750000117868.
    HOGENOMiHOG000260265.
    KOiK10356.
    OMAiLFRVINT.
    OrthoDBiEOG7VDXXK.

    Family and domain databases

    InterProiIPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00242. MYSc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04439-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAILKRGARK KVHQEPAKRS ANIKKATFDS SKKKEVGVSD LTLLSKISDE     50
    AINENLKKRF LNATIYTYIG HVLISVNPFR DLGIYTDAVM NEYKGKNRLE 100
    VPPHVFAIAE SMYYNMKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS 150
    STHTESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNNQF 200
    EPCAGNITNY LLEKQRVVSQ IKNERNFHIF YQFTKGASDA YRQTFGVQKP 250
    EQYVYTAAAG CISAETIDDL QDYQETLKAM RVIGLGQEEQ DQIFRMLAAI 300
    LWIGNVSFIE NEEGNAQVRD TSVTDFVAYL LQIDSQLLIK SLVERIMETN 350
    HGMKRGSVYH VPLNIVQADA VRDALAKAIY NNLFDWIVSR VNKSLQAFPG 400
    AEKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKSEQETYE 450
    REKIQWTPIK YFDNKVVCDL IEARRPPGIF AAMNDSVATA HADSNAADQA 500
    FAQRLNLFTT NPHFDLRSNK FVIKHYAGDV TYDIDGITDK NKDQLQKDLV 550
    ELIGTTTNTF LATIFPDTVD RESKRRPPTA GDKIIKSAND LVETLSKAQP 600
    SYIRTIKPNE TKSPNDYDDR QVLHQIKYLG LQENVRIRRA GFAYRQVFEK 650
    FVERFYLLSP HCSYAGDYTW QGDTLDAVKY ILQDSSIPQQ EYQLGVTSVF 700
    IKTPETLFAL EHMRDRYWHN MAARIQRAWR RFLQRRIDAA TKIQRTIRER 750
    KEGNKYEKLR DYGTKVLGGR KERRSMSLLG YRAFMGDYLS CNESKSKGAY 800
    IKRQVSIKEK VIFSIHGEAL HTKFGRSAQR LKKTFLLTPT TLYIVGQTLV 850
    QNAMTYTQDY KIDVRNIQAV SLTNLQDDWV AIKLASSGQP DPLINTYFKT 900
    ELITHLKRLN DKIQIKIGSA IEYQKKPGKL HSVKCQINES APKYGDIYKS 950
    STISVRRGNP PNSQVHKKPR KKSSISSGYH ASSSQATRRP VSIAAAQHVP 1000
    TAPASRHSKK PAPPPPGMQN KAATRRSVPN PASTLTASQS NARPSPPTAA 1050
    TRATPAATPA AAAMGSGRQA NIPPPPPPPP PSSKPKEPMF EAAYDFPGSG 1100
    SPSELPLKKG DVIYITREEP SGWSLGKLLD GSKEGWVPTA YMKPHSGNNN 1150
    IPTPPQNRDV PKPVLNSVQH DNTSANVIPA AAQASLGDGL ANALAARANK 1200
    MRLESDDEEA NEDEEEDDW 1219
    Length:1,219
    Mass (Da):136,899
    Last modified:November 1, 1997 - v1
    Checksum:iDFFB9EC16B61CD29
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49702 Genomic DNA. Translation: CAA89745.1.
    BK006946 Genomic DNA. Translation: DAA10006.1.
    PIRiS54570.
    RefSeqiNP_013827.1. NM_001182609.1.

    Genome annotation databases

    EnsemblFungiiYMR109W; YMR109W; YMR109W.
    GeneIDi855136.
    KEGGisce:YMR109W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49702 Genomic DNA. Translation: CAA89745.1 .
    BK006946 Genomic DNA. Translation: DAA10006.1 .
    PIRi S54570.
    RefSeqi NP_013827.1. NM_001182609.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YP5 X-ray 1.68 A 1088-1145 [» ]
    1ZUY X-ray 1.39 A/B 1088-1145 [» ]
    ProteinModelPortali Q04439.
    SMRi Q04439. Positions 37-715, 1088-1145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35285. 116 interactions.
    DIPi DIP-2222N.
    IntActi Q04439. 99 interactions.
    MINTi MINT-593586.
    STRINGi 4932.YMR109W.

    Proteomic databases

    MaxQBi Q04439.
    PaxDbi Q04439.
    PeptideAtlasi Q04439.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR109W ; YMR109W ; YMR109W .
    GeneIDi 855136.
    KEGGi sce:YMR109W.

    Organism-specific databases

    CYGDi YMR109w.
    SGDi S000004715. MYO5.

    Phylogenomic databases

    eggNOGi COG5022.
    GeneTreei ENSGT00750000117868.
    HOGENOMi HOG000260265.
    KOi K10356.
    OMAi LFRVINT.
    OrthoDBi EOG7VDXXK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32805-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q04439.
    NextBioi 978516.

    Gene expression databases

    Genevestigatori Q04439.

    Family and domain databases

    InterProi IPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00242. MYSc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS51456. MYOSIN_MOTOR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton."
      Goodson H.V., Anderson B.L., Warrick H.M., Pon L.A., Spudich J.A.
      J. Cell Biol. 133:1277-1291(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Role of type I myosins in receptor-mediated endocytosis in yeast."
      Geli M.I., Riezman H.
      Science 272:533-535(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR ENDOCYTOSIS, MUTAGENESIS OF GLU-472.
    5. "The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization."
      Anderson B.L., Boldogh I., Evangelista M., Boone C., Greene L.A., Pon L.A.
      J. Cell Biol. 141:1357-1370(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VRP1, SUBCELLULAR LOCATION.
    6. "An intact SH3 domain is required for myosin I-induced actin polymerization."
      Geli M.I., Lombardi R., Schmelzl B., Riezman H.
      EMBO J. 19:4281-4291(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VRP1, MUTAGENESIS OF TRP-1123.
    7. "A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex."
      Evangelista M., Klebl B.M., Tong A.H.Y., Webb B.A., Leeuw T., Leberer E., Whiteway M., Thomas D.Y., Boone C.
      J. Cell Biol. 148:353-362(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARC19 AND ARC40.
    8. "Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization."
      Lechler T., Shevchenko A., Li R.
      J. Cell Biol. 148:363-373(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LAS17.
    9. "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: INTERACTION WITH BBC1, MUTAGENESIS OF TRP-1123.
    10. "Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro."
      Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R., Winsor B.
      Mol. Cell. Biol. 22:7889-7906(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BZZ1.
    11. "The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function."
      Wesche S., Arnold M., Jansen R.-P.
      Curr. Biol. 13:715-724(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SHE4.
    12. "She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae."
      Toi H., Fujimura-Kamada K., Irie K., Takai Y., Todo S., Tanaka K.
      Mol. Biol. Cell 14:2237-2249(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SHE4, MUTAGENESIS OF VAL-164; ASN-168; ASN-209 AND LYS-377.
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p."
      Grosshans B.L., Groetsch H., Mukhopadhyay D., Fernandez I.M., Pfannstiel J., Idrissi F.-Z., Lechner J., Riezman H., Geli M.I.
      J. Biol. Chem. 281:11104-11114(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 AND SER-777, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-357, SUBCELLULAR LOCATION, INTERACTION WITH PKH1; PKH2; YPK1 AND YPK2.
    15. "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-357; TYR-359; SER-992 AND SER-1205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    16. "Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis."
      Barker S.L., Lee L., Pierce B.D., Maldonado-Baez L., Drubin D.G., Wendland B.
      Mol. Biol. Cell 18:2893-2903(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAN1, SUBCELLULAR LOCATION.
    17. "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-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-1205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Yeast Myo5 SH3 domain, tetragonal crystal form."
      Gonfloni S., Kursula P., Sacco R., Cesareni G., Wilmanns M.
      Submitted (JAN-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1088-1145.
    21. "High-resolution structure of yeast Myo5 SH3 domain."
      Wilmanns M., Kursula P., Gonfloni S., Ferracuti S., Cesareni G.
      Submitted (OCT-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 1088-1145.

    Entry informationi

    Entry nameiMYO5_YEAST
    AccessioniPrimary (citable) accession number: Q04439
    Secondary accession number(s): D6VZT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 141 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 2280 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3