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P08799

- MYS2_DICDI

UniProt

P08799 - MYS2_DICDI

Protein

Myosin-2 heavy chain

Gene

mhcA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi179 – 1868ATP

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: dictyBase
    2. actin-dependent ATPase activity Source: dictyBase
    3. actin filament binding Source: dictyBase
    4. adenyl nucleotide binding Source: dictyBase
    5. ATP binding Source: dictyBase
    6. microfilament motor activity Source: dictyBase
    7. motor activity Source: dictyBase
    8. protein binding Source: IntAct
    9. protein homodimerization activity Source: dictyBase

    GO - Biological processi

    1. actin-myosin filament sliding Source: dictyBase
    2. ATP catabolic process Source: GOC
    3. bleb assembly Source: dictyBase
    4. cellular component movement Source: dictyBase
    5. chemotaxis Source: dictyBase
    6. contractile actin filament bundle assembly Source: dictyBase
    7. contractile vacuole organization Source: dictyBase
    8. cortical actin cytoskeleton organization Source: dictyBase
    9. culmination involved in sorocarp development Source: dictyBase
    10. cytoplasmic actin-based contraction involved in forward cell motility Source: dictyBase
    11. filopodium assembly Source: dictyBase
    12. hypotonic response Source: dictyBase
    13. metabolic process Source: GOC
    14. mitotic cytokinesis Source: dictyBase
    15. myosin filament assembly Source: dictyBase
    16. negative regulation of actin filament polymerization Source: dictyBase
    17. protein localization Source: dictyBase
    18. pseudopodium retraction Source: dictyBase
    19. uropod retraction Source: dictyBase

    Keywords - Molecular functioni

    Motor protein, Myosin

    Keywords - Ligandi

    Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin-2 heavy chain
    Alternative name(s):
    Myosin II heavy chain
    Gene namesi
    Name:mhcA
    ORF Names:DDB_G0286355
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 4, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0286355. mhcA.

    Subcellular locationi

    Cytoplasmcell cortex
    Note: Highest concentration in the posterior cell cortex.

    GO - Cellular componenti

    1. actomyosin Source: dictyBase
    2. actomyosin contractile ring Source: dictyBase
    3. apical cortex Source: dictyBase
    4. cell cortex Source: dictyBase
    5. cell trailing edge Source: dictyBase
    6. cytoskeleton Source: dictyBase
    7. cytosol Source: dictyBase
    8. early phagosome Source: dictyBase
    9. myosin filament Source: dictyBase
    10. myosin II complex Source: dictyBase
    11. phagocytic cup base Source: dictyBase
    12. uropod Source: dictyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21162116Myosin-2 heavy chainPRO_0000123373Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301N6,N6-dimethyllysineSequence Analysis
    Modified residuei1823 – 18231Phosphothreonine; by MHCK2 Publications
    Modified residuei1833 – 18331Phosphothreonine; by MHCK2 Publications
    Modified residuei2029 – 20291Phosphothreonine; by MHCK2 Publications

    Post-translational modificationi

    Phosphorylation inhibits thick filament formation and reduces the actin-activated ATPase activity.2 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    PRIDEiP08799.

    Interactioni

    Subunit structurei

    Myosin-2 heavy chain is two-headed. It self-assembles into filaments. Hexamer of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Associates with elmoA.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    elmoAQ54YW12EBI-2928504,EBI-2928498

    Protein-protein interaction databases

    DIPiDIP-46078N.
    IntActiP08799. 1 interaction.
    STRINGi44689.DDB_0191444.

    Structurei

    Secondary structure

    1
    2116
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 53
    Beta strandi6 – 94
    Helixi10 – 156
    Helixi22 – 287
    Beta strandi34 – 374
    Beta strandi39 – 435
    Beta strandi44 – 463
    Beta strandi48 – 558
    Beta strandi57 – 637
    Beta strandi65 – 673
    Beta strandi69 – 735
    Turni74 – 763
    Beta strandi77 – 793
    Helixi83 – 853
    Helixi91 – 933
    Helixi99 – 11113
    Beta strandi116 – 1194
    Beta strandi122 – 1265
    Helixi137 – 1437
    Helixi148 – 1503
    Helixi155 – 16915
    Beta strandi173 – 1786
    Helixi185 – 20016
    Beta strandi204 – 2063
    Helixi207 – 2093
    Helixi210 – 22617
    Beta strandi227 – 2304
    Beta strandi236 – 24712
    Beta strandi249 – 2513
    Beta strandi253 – 2619
    Helixi265 – 2684
    Helixi279 – 2879
    Helixi290 – 2967
    Helixi301 – 3033
    Turni305 – 3073
    Beta strandi308 – 3114
    Helixi320 – 33415
    Helixi338 – 35518
    Beta strandi359 – 3613
    Beta strandi363 – 3686
    Helixi373 – 38210
    Helixi386 – 3949
    Beta strandi397 – 4004
    Beta strandi403 – 4064
    Helixi411 – 44131
    Beta strandi447 – 4548
    Beta strandi462 – 4643
    Helixi466 – 49530
    Turni496 – 4983
    Helixi506 – 5105
    Helixi511 – 5188
    Turni520 – 5234
    Helixi525 – 5339
    Beta strandi534 – 5374
    Helixi540 – 55112
    Turni552 – 5543
    Beta strandi556 – 5594
    Beta strandi565 – 5728
    Beta strandi575 – 5806
    Helixi584 – 5896
    Helixi594 – 6018
    Helixi608 – 6136
    Helixi615 – 6184
    Beta strandi624 – 6263
    Helixi630 – 64617
    Beta strandi648 – 6569
    Helixi669 – 67810
    Helixi681 – 6877
    Helixi688 – 6903
    Beta strandi694 – 6985
    Helixi699 – 7013
    Turni702 – 7043
    Helixi706 – 7083
    Beta strandi709 – 7113
    Helixi719 – 73012
    Helixi734 – 7363
    Beta strandi737 – 7393
    Beta strandi741 – 7466
    Turni748 – 7525
    Beta strandi754 – 7563
    Beta strandi757 – 7604

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D0XX-ray2.00A1-759[»]
    1D0YX-ray2.00A1-759[»]
    1D0ZX-ray2.00A1-759[»]
    1D1AX-ray2.00A1-759[»]
    1D1BX-ray2.00A1-759[»]
    1D1CX-ray2.30A1-759[»]
    1FMVX-ray2.10A1-759[»]
    1FMWX-ray2.15A1-759[»]
    1G8XX-ray2.80A/B1-761[»]
    1JWYX-ray2.30A3-765[»]
    1JX2X-ray2.30A3-765[»]
    1LVKX-ray1.90A1-759[»]
    1MMAX-ray2.10A1-759[»]
    1MMDX-ray2.00A1-759[»]
    1MMGX-ray2.10A1-759[»]
    1MMNX-ray2.10A1-759[»]
    1MNDX-ray2.60A1-759[»]
    1MNEX-ray2.70A1-759[»]
    1Q5Gmodel-A2-765[»]
    1VOMX-ray1.90A1-759[»]
    1W9IX-ray1.75A1-754[»]
    1W9JX-ray2.00A1-758[»]
    1W9KX-ray2.05A1-759[»]
    1W9LX-ray1.95A1-759[»]
    1YV3X-ray2.00A1-762[»]
    2AKAX-ray1.90A2-765[»]
    2JHRX-ray2.80A2-761[»]
    2JJ9X-ray2.30A2-761[»]
    2X9HX-ray2.70A3-696[»]
    2XELX-ray2.50A2-761[»]
    2XO8X-ray2.40A3-761[»]
    2Y0RX-ray2.85X2-759[»]
    2Y8IX-ray3.13X2-759[»]
    2Y9EX-ray3.40X2-759[»]
    3BZ7X-ray2.00A2-759[»]
    3BZ8X-ray2.20A2-759[»]
    3BZ9X-ray2.10A2-759[»]
    3MJXX-ray2.20A2-761[»]
    3MKDX-ray2.40A2-693[»]
    3MNQX-ray2.20A3-761[»]
    3MYHX-ray2.01X2-759[»]
    3MYKX-ray1.84X2-759[»]
    3MYLX-ray2.00X2-759[»]
    4AE3X-ray2.50A2-761[»]
    ProteinModelPortaliP08799.
    SMRiP08799. Positions 2-821.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08799.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 759674Myosin motorAdd
    BLAST
    Domaini762 – 79130IQPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni638 – 66023Actin-bindingAdd
    BLAST
    Regioni738 – 75215Actin-bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili817 – 21161300Sequence AnalysisAdd
    BLAST

    Domaini

    Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). It can be further split into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).
    The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5022.
    KOiK10352.
    OMAiRNEANES.
    PhylomeDBiP08799.

    Family and domain databases

    Gene3Di4.10.270.10. 1 hit.
    InterProiIPR000048. IQ_motif_EF-hand-BS.
    IPR027401. Myosin-like_IQ_dom.
    IPR001609. Myosin_head_motor_dom.
    IPR004009. Myosin_N.
    IPR008989. Myosin_S1_N.
    IPR002928. Myosin_tail.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00063. Myosin_head. 1 hit.
    PF02736. Myosin_N. 1 hit.
    PF01576. Myosin_tail_1. 3 hits.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00015. IQ. 2 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50084. SSF50084. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08799-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPIHDRTSD YHKYLKVKQG DSDLFKLTVS DKRYIWYNPD PKERDSYECG     50
    EIVSETSDSF TFKTVDGQDR QVKKDDANQR NPIKFDGVED MSELSYLNEP 100
    AVFHNLRVRY NQDLIYTYSG LFLVAVNPFK RIPIYTQEMV DIFKGRRRNE 150
    VAPHIFAISD VAYRSMLDDR QNQSLLITGE SGAGKTENTK KVIQYLASVA 200
    GRNQANGSGV LEQQILQANP ILEAFGNAKT TRNNNSSRFG KFIEIQFNSA 250
    GFISGASIQS YLLEKSRVVF QSETERNYHI FYQLLAGATA EEKKALHLAG 300
    PESFNYLNQS GCVDIKGVSD SEEFKITRQA MDIVGFSQEE QMSIFKIIAG 350
    ILHLGNIKFE KGAGEGAVLK DKTALNAAST VFGVNPSVLE KALMEPRILA 400
    GRDLVAQHLN VEKSSSSRDA LVKALYGRLF LWLVKKINNV LCQERKAYFI 450
    GVLDISGFEI FKVNSFEQLC INYTNEKLQQ FFNHHMFKLE QEEYLKEKIN 500
    WTFIDFGLDS QATIDLIDGR QPPGILALLD EQSVFPNATD NTLITKLHSH 550
    FSKKNAKYEE PRFSKTEFGV THYAGQVMYE IQDWLEKNKD PLQQDLELCF 600
    KDSSDNVVTK LFNDPNIASR AKKGANFITV AAQYKEQLAS LMATLETTNP 650
    HFVRCIIPNN KQLPAKLEDK VVLDQLRCNG VLEGIRITRK GFPNRIIYAD 700
    FVKRYYLLAP NVPRDAEDSQ KATDAVLKHL NIDPEQYRFG ITKIFFRAGQ 750
    LARIEEAREQ RISEIIKAIQ AATRGWIARK VYKQAREHTV AARIIQQNLR 800
    AYIDFKSWPW WKLFSKARPL LKRRNFEKEI KEKEREILEL KSNLTDSTTQ 850
    KDKLEKSLKD TESNVLDLQR QLKAEKETLK AMYDSKDALE AQKRELEIRV 900
    EDMESELDEK KLALENLQNQ KRSVEEKVRD LEEELQEEQK LRNTLEKLKK 950
    KYEEELEEMK RVNDGQSDTI SRLEKIKDEL QKEVEELTES FSEESKDKGV 1000
    LEKTRVRLQS ELDDLTVRLD SETKDKSELL RQKKKLEEEL KQVQEALAAE 1050
    TAAKLAQEAA NKKLQGEYTE LNEKFNSEVT ARSNVEKSKK TLESQLVAVN 1100
    NELDEEKKNR DALEKKKKAL DAMLEEMKDQ LESTGGEKKS LYDLKVKQES 1150
    DMEALRNQIS ELQSTIAKLE KIKSTLEGEV ARLQGELEAE QLAKSNVEKQ 1200
    KKKVELDLED KSAQLAEETA AKQALDKLKK KLEQELSEVQ TQLSEANNKN 1250
    VNSDSTNKHL ETSFNNLKLE LEAEQKAKQA LEKKRLGLES ELKHVNEQLE 1300
    EEKKQKESNE KRKVDLEKEV SELKDQIEEE VASKKAVTEA KNKKESELDE 1350
    IKRQYADVVS SRDKSVEQLK TLQAKNEELR NTAEEAEGQL DRAERSKKKA 1400
    EFDLEEAVKN LEEETAKKVK AEKAMKKAET DYRSTKSELD DAKNVSSEQY 1450
    VQIKRLNEEL SELRSVLEEA DERCNSAIKA KKTAESALES LKDEIDAANN 1500
    AKAKAERKSK ELEVRVAELE ESLEDKSGTV NVEFIRKKDA EIDDLRARLD 1550
    RETESRIKSD EDKKNTRKQF ADLEAKVEEA QREVVTIDRL KKKLESDIID 1600
    LSTQLDTETK SRIKIEKSKK KLEQTLAERR AAEEGSSKAA DEEIRKQVWQ 1650
    EVDELRAQLD SERAALNASE KKIKSLVAEV DEVKEQLEDE ILAKDKLVKA 1700
    KRALEVELEE VRDQLEEEED SRSELEDSKR RLTTEVEDIK KKYDAEVEQN 1750
    TKLDEAKKKL TDDVDTLKKQ LEDEKKKLNE SERAKKRLES ENEDFLAKLD 1800
    AEVKNRSRAE KDRKKYEKDL KDTKYKLNDE AATKTQTEIG AAKLEDQIDE 1850
    LRSKLEQEQA KATQADKSKK TLEGEIDNLR AQIEDEGKIK MRLEKEKRAL 1900
    EGELEELRET VEEAEDSKSE AEQSKRLVEL ELEDARRNLQ KEIDAKEIAE 1950
    DAKSNLQREI VEAKGRLEEE SIARTNSDRS RKRLEAEIDA LTAQVDAEQK 2000
    AKNQQIKENK KIETELKEYR KKFGESEKTK TKEFLVVEKL ETDYKRAKKE 2050
    AADEQQQRLT VENDLRKHLS EISLLKDAID KLQRDHDKTK RELETETASK 2100
    IEMQRKMADF FGGFKA 2116
    Length:2,116
    Mass (Da):243,786
    Last modified:March 20, 2007 - v3
    Checksum:i97DE4FB422AD3D56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti249 – 2491S → N in AAA33227. (PubMed:3540939)Curated
    Sequence conflicti312 – 3121C → Y in AAA33227. (PubMed:3540939)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14628 Genomic DNA. Translation: AAA33227.1.
    AAFI02000085 Genomic DNA. Translation: EAL64202.1.
    PIRiA26655.
    RefSeqiXP_637740.1. XM_632648.1.

    Genome annotation databases

    EnsemblProtistsiDDB0191444; DDB0191444; DDB_G0286355.
    GeneIDi8625606.
    KEGGiddi:DDB_G0286355.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14628 Genomic DNA. Translation: AAA33227.1 .
    AAFI02000085 Genomic DNA. Translation: EAL64202.1 .
    PIRi A26655.
    RefSeqi XP_637740.1. XM_632648.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D0X X-ray 2.00 A 1-759 [» ]
    1D0Y X-ray 2.00 A 1-759 [» ]
    1D0Z X-ray 2.00 A 1-759 [» ]
    1D1A X-ray 2.00 A 1-759 [» ]
    1D1B X-ray 2.00 A 1-759 [» ]
    1D1C X-ray 2.30 A 1-759 [» ]
    1FMV X-ray 2.10 A 1-759 [» ]
    1FMW X-ray 2.15 A 1-759 [» ]
    1G8X X-ray 2.80 A/B 1-761 [» ]
    1JWY X-ray 2.30 A 3-765 [» ]
    1JX2 X-ray 2.30 A 3-765 [» ]
    1LVK X-ray 1.90 A 1-759 [» ]
    1MMA X-ray 2.10 A 1-759 [» ]
    1MMD X-ray 2.00 A 1-759 [» ]
    1MMG X-ray 2.10 A 1-759 [» ]
    1MMN X-ray 2.10 A 1-759 [» ]
    1MND X-ray 2.60 A 1-759 [» ]
    1MNE X-ray 2.70 A 1-759 [» ]
    1Q5G model - A 2-765 [» ]
    1VOM X-ray 1.90 A 1-759 [» ]
    1W9I X-ray 1.75 A 1-754 [» ]
    1W9J X-ray 2.00 A 1-758 [» ]
    1W9K X-ray 2.05 A 1-759 [» ]
    1W9L X-ray 1.95 A 1-759 [» ]
    1YV3 X-ray 2.00 A 1-762 [» ]
    2AKA X-ray 1.90 A 2-765 [» ]
    2JHR X-ray 2.80 A 2-761 [» ]
    2JJ9 X-ray 2.30 A 2-761 [» ]
    2X9H X-ray 2.70 A 3-696 [» ]
    2XEL X-ray 2.50 A 2-761 [» ]
    2XO8 X-ray 2.40 A 3-761 [» ]
    2Y0R X-ray 2.85 X 2-759 [» ]
    2Y8I X-ray 3.13 X 2-759 [» ]
    2Y9E X-ray 3.40 X 2-759 [» ]
    3BZ7 X-ray 2.00 A 2-759 [» ]
    3BZ8 X-ray 2.20 A 2-759 [» ]
    3BZ9 X-ray 2.10 A 2-759 [» ]
    3MJX X-ray 2.20 A 2-761 [» ]
    3MKD X-ray 2.40 A 2-693 [» ]
    3MNQ X-ray 2.20 A 3-761 [» ]
    3MYH X-ray 2.01 X 2-759 [» ]
    3MYK X-ray 1.84 X 2-759 [» ]
    3MYL X-ray 2.00 X 2-759 [» ]
    4AE3 X-ray 2.50 A 2-761 [» ]
    ProteinModelPortali P08799.
    SMRi P08799. Positions 2-821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46078N.
    IntActi P08799. 1 interaction.
    STRINGi 44689.DDB_0191444.

    Proteomic databases

    PRIDEi P08799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0191444 ; DDB0191444 ; DDB_G0286355 .
    GeneIDi 8625606.
    KEGGi ddi:DDB_G0286355.

    Organism-specific databases

    dictyBasei DDB_G0286355. mhcA.

    Phylogenomic databases

    eggNOGi COG5022.
    KOi K10352.
    OMAi RNEANES.
    PhylomeDBi P08799.

    Miscellaneous databases

    EvolutionaryTracei P08799.

    Family and domain databases

    Gene3Di 4.10.270.10. 1 hit.
    InterProi IPR000048. IQ_motif_EF-hand-BS.
    IPR027401. Myosin-like_IQ_dom.
    IPR001609. Myosin_head_motor_dom.
    IPR004009. Myosin_N.
    IPR008989. Myosin_S1_N.
    IPR002928. Myosin_tail.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00063. Myosin_head. 1 hit.
    PF02736. Myosin_N. 1 hit.
    PF01576. Myosin_tail_1. 3 hits.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00015. IQ. 2 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50084. SSF50084. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum."
      Warrick H.M., de Lozanne A., Leinwand L.A., Spudich J.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:9433-9437(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "Cloning and characterization of a nonmuscle myosin heavy chain cDNA."
      De Lozanne A., Lewis M., Spudich J.A., Leinwand L.A.
      Proc. Natl. Acad. Sci. U.S.A. 82:6807-6810(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2035-2116.
    4. "Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II."
      Lueck-Vielmeter D., Schleicher M., Grabatin B., Wippler J., Gerisch G.
      FEBS Lett. 269:239-243(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-1823; THR-1833 AND THR-2029, MUTAGENESIS.
      Strain: AX2.
    5. "Phosphorylation of threonine residues on cloned fragments of the Dictyostelium myosin heavy chain."
      Wagle G., Noegel A., Scheel J., Gerisch G.
      FEBS Lett. 227:71-75(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-1823; THR-1833 AND THR-2029.
    6. "Thirteen is enough: the myosins of Dictyostelium discoideum and their light chains."
      Kollmar M.
      BMC Genomics 7:183-183(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    7. "An Elmo-like protein associated with myosin II restricts spurious F-actin events to coordinate phagocytosis and chemotaxis."
      Isik N., Brzostowski J.A., Jin T.
      Dev. Cell 15:590-602(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ELMOA.
    8. "X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-."
      Fisher A.J., Smith C.A., Thoden J.B., Smith R., Sutoh K., Holden H.M., Rayment I.
      Biochemistry 34:8960-8972(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-762.
    9. "X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7-A resolution."
      Smith C.A., Rayment I.
      Biochemistry 34:8973-8981(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-762.
    10. "X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9-A resolution."
      Smith C.A., Rayment I.
      Biochemistry 35:5404-5417(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-762.
    11. "X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain."
      Gulick A.M., Bauer C.B., Thoden J.B., Rayment I.
      Biochemistry 36:11619-11628(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-762.
    12. "X-ray crystal structure and solution fluorescence characterization of Mg.2'(3')-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain."
      Bauer C.B., Kuhlman P.A., Bagshaw C.R., Rayment I.
      J. Mol. Biol. 274:394-407(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-762.
    13. "Structure of a genetically engineered molecular motor."
      Kliche W., Fujita-Becker S., Kollmar M., Manstein D.J., Kull F.J.
      EMBO J. 20:40-46(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-761.

    Entry informationi

    Entry nameiMYS2_DICDI
    AccessioniPrimary (citable) accession number: P08799
    Secondary accession number(s): Q54LU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    Dictyostelium myosin-2 has no K2EDTA ATPase activity, perhaps correlated with the absence of a Cys at the SH-1 position (688).

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3