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P08799

- MYS2_DICDI

UniProt

P08799 - MYS2_DICDI

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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

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 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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP08799.
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

        10         20         30         40         50
MNPIHDRTSD YHKYLKVKQG DSDLFKLTVS DKRYIWYNPD PKERDSYECG
60 70 80 90 100
EIVSETSDSF TFKTVDGQDR QVKKDDANQR NPIKFDGVED MSELSYLNEP
110 120 130 140 150
AVFHNLRVRY NQDLIYTYSG LFLVAVNPFK RIPIYTQEMV DIFKGRRRNE
160 170 180 190 200
VAPHIFAISD VAYRSMLDDR QNQSLLITGE SGAGKTENTK KVIQYLASVA
210 220 230 240 250
GRNQANGSGV LEQQILQANP ILEAFGNAKT TRNNNSSRFG KFIEIQFNSA
260 270 280 290 300
GFISGASIQS YLLEKSRVVF QSETERNYHI FYQLLAGATA EEKKALHLAG
310 320 330 340 350
PESFNYLNQS GCVDIKGVSD SEEFKITRQA MDIVGFSQEE QMSIFKIIAG
360 370 380 390 400
ILHLGNIKFE KGAGEGAVLK DKTALNAAST VFGVNPSVLE KALMEPRILA
410 420 430 440 450
GRDLVAQHLN VEKSSSSRDA LVKALYGRLF LWLVKKINNV LCQERKAYFI
460 470 480 490 500
GVLDISGFEI FKVNSFEQLC INYTNEKLQQ FFNHHMFKLE QEEYLKEKIN
510 520 530 540 550
WTFIDFGLDS QATIDLIDGR QPPGILALLD EQSVFPNATD NTLITKLHSH
560 570 580 590 600
FSKKNAKYEE PRFSKTEFGV THYAGQVMYE IQDWLEKNKD PLQQDLELCF
610 620 630 640 650
KDSSDNVVTK LFNDPNIASR AKKGANFITV AAQYKEQLAS LMATLETTNP
660 670 680 690 700
HFVRCIIPNN KQLPAKLEDK VVLDQLRCNG VLEGIRITRK GFPNRIIYAD
710 720 730 740 750
FVKRYYLLAP NVPRDAEDSQ KATDAVLKHL NIDPEQYRFG ITKIFFRAGQ
760 770 780 790 800
LARIEEAREQ RISEIIKAIQ AATRGWIARK VYKQAREHTV AARIIQQNLR
810 820 830 840 850
AYIDFKSWPW WKLFSKARPL LKRRNFEKEI KEKEREILEL KSNLTDSTTQ
860 870 880 890 900
KDKLEKSLKD TESNVLDLQR QLKAEKETLK AMYDSKDALE AQKRELEIRV
910 920 930 940 950
EDMESELDEK KLALENLQNQ KRSVEEKVRD LEEELQEEQK LRNTLEKLKK
960 970 980 990 1000
KYEEELEEMK RVNDGQSDTI SRLEKIKDEL QKEVEELTES FSEESKDKGV
1010 1020 1030 1040 1050
LEKTRVRLQS ELDDLTVRLD SETKDKSELL RQKKKLEEEL KQVQEALAAE
1060 1070 1080 1090 1100
TAAKLAQEAA NKKLQGEYTE LNEKFNSEVT ARSNVEKSKK TLESQLVAVN
1110 1120 1130 1140 1150
NELDEEKKNR DALEKKKKAL DAMLEEMKDQ LESTGGEKKS LYDLKVKQES
1160 1170 1180 1190 1200
DMEALRNQIS ELQSTIAKLE KIKSTLEGEV ARLQGELEAE QLAKSNVEKQ
1210 1220 1230 1240 1250
KKKVELDLED KSAQLAEETA AKQALDKLKK KLEQELSEVQ TQLSEANNKN
1260 1270 1280 1290 1300
VNSDSTNKHL ETSFNNLKLE LEAEQKAKQA LEKKRLGLES ELKHVNEQLE
1310 1320 1330 1340 1350
EEKKQKESNE KRKVDLEKEV SELKDQIEEE VASKKAVTEA KNKKESELDE
1360 1370 1380 1390 1400
IKRQYADVVS SRDKSVEQLK TLQAKNEELR NTAEEAEGQL DRAERSKKKA
1410 1420 1430 1440 1450
EFDLEEAVKN LEEETAKKVK AEKAMKKAET DYRSTKSELD DAKNVSSEQY
1460 1470 1480 1490 1500
VQIKRLNEEL SELRSVLEEA DERCNSAIKA KKTAESALES LKDEIDAANN
1510 1520 1530 1540 1550
AKAKAERKSK ELEVRVAELE ESLEDKSGTV NVEFIRKKDA EIDDLRARLD
1560 1570 1580 1590 1600
RETESRIKSD EDKKNTRKQF ADLEAKVEEA QREVVTIDRL KKKLESDIID
1610 1620 1630 1640 1650
LSTQLDTETK SRIKIEKSKK KLEQTLAERR AAEEGSSKAA DEEIRKQVWQ
1660 1670 1680 1690 1700
EVDELRAQLD SERAALNASE KKIKSLVAEV DEVKEQLEDE ILAKDKLVKA
1710 1720 1730 1740 1750
KRALEVELEE VRDQLEEEED SRSELEDSKR RLTTEVEDIK KKYDAEVEQN
1760 1770 1780 1790 1800
TKLDEAKKKL TDDVDTLKKQ LEDEKKKLNE SERAKKRLES ENEDFLAKLD
1810 1820 1830 1840 1850
AEVKNRSRAE KDRKKYEKDL KDTKYKLNDE AATKTQTEIG AAKLEDQIDE
1860 1870 1880 1890 1900
LRSKLEQEQA KATQADKSKK TLEGEIDNLR AQIEDEGKIK MRLEKEKRAL
1910 1920 1930 1940 1950
EGELEELRET VEEAEDSKSE AEQSKRLVEL ELEDARRNLQ KEIDAKEIAE
1960 1970 1980 1990 2000
DAKSNLQREI VEAKGRLEEE SIARTNSDRS RKRLEAEIDA LTAQVDAEQK
2010 2020 2030 2040 2050
AKNQQIKENK KIETELKEYR KKFGESEKTK TKEFLVVEKL ETDYKRAKKE
2060 2070 2080 2090 2100
AADEQQQRLT VENDLRKHLS EISLLKDAID KLQRDHDKTK RELETETASK
2110
IEMQRKMADF FGGFKA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P08799.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 145 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