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P36006

- MYO3_YEAST

UniProt

P36006 - MYO3_YEAST

Protein

Myosin-3

Gene

MYO3

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 138 (01 Oct 2014)
      Sequence version 4 (21 Sep 2011)
      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 STE2.7 Publications

    Regions

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

    GO - Molecular functioni

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

    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. response to osmotic stress Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Motor protein, Myosin

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31910-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin-3
    Alternative name(s):
    Actin-dependent myosin-I MYO3
    Class I unconventional myosin MYO3
    Type I myosin MYO3
    Gene namesi
    Name:MYO3
    Ordered Locus Names:YKL129C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001612. MYO3.

    Subcellular locationi

    Cytoplasmcytoskeletonactin patch 1 Publication
    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
    Mutagenesisi132 – 1321G → R: Loss of function. 1 Publication
    Mutagenesisi357 – 3571S → A: Loss of function. 2 Publications
    Mutagenesisi357 – 3571S → D: Has a constitutive higher activity in actin assembly. 2 Publications
    Mutagenesisi1158 – 11581W → S: Abolishes interaction with LAS17 and causes severe mislocalization of the protein.
    Mutagenesisi1272 – 12721Missing: Abolishes interaction with ARC40.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12721272Myosin-3PRO_0000123490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei357 – 3571Phosphoserine4 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 By similarity. Ser-357 is phosphorylated by CLA4 and STE20 in vitro.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP36006.
    PaxDbiP36006.
    PeptideAtlasiP36006.

    Expressioni

    Gene expression databases

    GenevestigatoriP36006.

    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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIM21P405633EBI-11670,EBI-25376
    BBC1P470685EBI-11670,EBI-3437
    BCK1Q013896EBI-11670,EBI-3470
    BNI1P418323EBI-11670,EBI-3692
    BNR1P404506EBI-11670,EBI-3711
    LAS17Q124463EBI-11670,EBI-10022
    OSH2Q124513EBI-11670,EBI-12621
    PRP8P333344EBI-11670,EBI-465
    SAP1P399553EBI-11670,EBI-16463
    STE20Q034973EBI-11670,EBI-18285
    UBP7P404533EBI-11670,EBI-19857
    VRP1P3737011EBI-11670,EBI-20502
    YOR389WQ089122EBI-11670,EBI-38289

    Protein-protein interaction databases

    BioGridi34006. 66 interactions.
    DIPiDIP-2221N.
    IntActiP36006. 57 interactions.
    MINTiMINT-382399.
    STRINGi4932.YKL129C.

    Structurei

    Secondary structure

    1
    1272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1123 – 11297
    Beta strandi1137 – 11393
    Beta strandi1147 – 11537
    Beta strandi1157 – 11637
    Beta strandi1169 – 11735
    Helixi1174 – 11763
    Beta strandi1177 – 11793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RUWX-ray1.80A1121-1189[»]
    1VA7X-ray2.90A/B/C/D1121-1189[»]
    2BTTNMR-A1121-1189[»]
    ProteinModelPortaliP36006.
    SMRiP36006. Positions 37-715, 736-764, 1121-1189.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36006.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 715680Myosin motorAdd
    BLAST
    Domaini719 – 73921IQ 1Add
    BLAST
    Domaini740 – 76526IQ 2Add
    BLAST
    Domaini1120 – 118263SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni404 – 48683Actin-bindingBy similarityAdd
    BLAST
    Regioni759 – 961203Basic, putative membrane-binding regionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1003 – 1123121Ala/Pro-richAdd
    BLAST
    Compositional biasi1109 – 11168Poly-Pro
    Compositional biasi1259 – 127113Asp-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.
    GeneTreeiENSGT00750000117217.
    HOGENOMiHOG000260265.
    KOiK10356.
    OMAiAGAPMMK.
    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.

    P36006-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE     50
    SINENLKKRF KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE 100
    VPPHVFAIAE SMYYNLKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS 150
    NSHSESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNSQF 200
    EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT YKQMFGVQMP 250
    EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI 300
    LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS 350
    HGMKRGSVYH VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG 400
    ADKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKAEQETYE 450
    REKIKWTPIK YFDNKVVCDL IEAKNPPGIL AAMNDSIATA HADSNAADQA 500
    FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK NKDQLQKDLI 550
    ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP 600
    SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK 650
    FVERFYLLSP DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF 700
    IKTPESLFAL EDMRDKYWYN MAARIQRAWR RFLQRRIDAA IKIQRTIREK 750
    KGGNKYVKLR DYGTKLLAGK KERRSMSLLG YRAFMGDYLS CNESKTKGSY 800
    IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK TFYIIGQTRE 850
    QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT 900
    ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS 950
    STIYVRRGHP ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH 1000
    RDAAKKQPLP SQKPVNPLSL AATAAQAAYN PKPDKTVPIK SSAIPAAKVS 1050
    SKHSSKPSSK EKVAVKKASS SHKSSSAKQN QVSMPPSKGV EKNKEPLKET 1100
    TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL PLKKGDIVFI 1150
    SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN 1200
    QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA 1250
    NKMRAESADD DDNDDGDDDD DW 1272
    Length:1,272
    Mass (Da):142,451
    Last modified:September 21, 2011 - v4
    Checksum:i6CB13AD3CD669600
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951G → RK in AAB34124. (PubMed:7728870)Curated
    Sequence conflicti168 – 1692NP → T in AAB34124. (PubMed:7728870)Curated
    Sequence conflicti263 – 2708TADTIDDV → SADQLMR in CAA81970. (PubMed:8196765)Curated
    Sequence conflicti917 – 9182VG → RLV in AAB34124. (PubMed:7728870)Curated
    Sequence conflicti1021 – 10211A → R in CAA81970. (PubMed:8196765)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S76960 Genomic DNA. Translation: AAB34124.1.
    Z28129 Genomic DNA. Translation: CAA81970.1.
    BK006944 Genomic DNA. Translation: DAA09032.2.
    PIRiS37958.
    RefSeqiNP_012793.2. NM_001179695.2.

    Genome annotation databases

    EnsemblFungiiYKL129C; YKL129C; YKL129C.
    GeneIDi853729.
    KEGGisce:YKL129C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S76960 Genomic DNA. Translation: AAB34124.1 .
    Z28129 Genomic DNA. Translation: CAA81970.1 .
    BK006944 Genomic DNA. Translation: DAA09032.2 .
    PIRi S37958.
    RefSeqi NP_012793.2. NM_001179695.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RUW X-ray 1.80 A 1121-1189 [» ]
    1VA7 X-ray 2.90 A/B/C/D 1121-1189 [» ]
    2BTT NMR - A 1121-1189 [» ]
    ProteinModelPortali P36006.
    SMRi P36006. Positions 37-715, 736-764, 1121-1189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34006. 66 interactions.
    DIPi DIP-2221N.
    IntActi P36006. 57 interactions.
    MINTi MINT-382399.
    STRINGi 4932.YKL129C.

    Proteomic databases

    MaxQBi P36006.
    PaxDbi P36006.
    PeptideAtlasi P36006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL129C ; YKL129C ; YKL129C .
    GeneIDi 853729.
    KEGGi sce:YKL129C.

    Organism-specific databases

    SGDi S000001612. MYO3.

    Phylogenomic databases

    eggNOGi COG5022.
    GeneTreei ENSGT00750000117217.
    HOGENOMi HOG000260265.
    KOi K10356.
    OMAi AGAPMMK.
    OrthoDBi EOG7VDXXK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31910-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P36006.
    NextBioi 974764.

    Gene expression databases

    Genevestigatori P36006.

    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. "Identification and molecular characterization of a yeast myosin I."
      Goodson H.V., Spudich J.A.
      Cell Motil. Cytoskeleton 30:73-84(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CRY3.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 263-270 AND 1021.
      Strain: ATCC 204508 / S288c.
    4. "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: FUNCTION IN ACTIN CYTOSKELETON ORGANIZATION.
    5. "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.
    6. "The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast."
      Wu C., Lytvyn V., Thomas D.Y., Leberer E.
      J. Biol. Chem. 272:30623-30626(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-357 BY CLA4 AND STE20, MUTAGENESIS OF SER-357.
    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; ARC40; LAS17 AND VRP1.
    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 ARP2 AND LAS17, MUTAGENESIS OF GLY-132 AND SER-357.
    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.
    10. "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.
    11. "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.
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    14. "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.
    15. "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].
    16. "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-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S.cerevisiae."
      Musi V., Birdsall B., Fernandez-Ballester G., Guerrini R., Salvatori S., Serrano L., Pastore A.
      Protein Sci. 15:795-807(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1123-1191.
    18. "Crystal structure of the SH3 domain from S.cerevisiae Myo3."
      Kursula P., Kursula I., Lehmann F., Song Y.H., Wilmanns M.
      Submitted (MAR-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1123-1191.
    19. "High-throughput structural genomics of yeast SH3 domains."
      Kursula P., Lehmann F., Song Y.H., Wilmanns M.
      Submitted (JUN-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1123-1191.

    Entry informationi

    Entry nameiMYO3_YEAST
    AccessioniPrimary (citable) accession number: P36006
    Secondary accession number(s): D6VX66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 155 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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3