Protein detail

MYO10

Unconventional myosin-X (Unconventional myosin-10)

Protein symbol
MYO10
UniProt ID
EVMP score
0.50
Frequency
2
Transmembrane count
Protein classification
Plasma proteinsPredicted intracellular proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Unconventional myosin-X (Unconventional myosin-10)
Protein Class
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym
KIAA0799MyoX
Gene Description
Myosin X
Chromosome
5
Position
16661907-16936288
Frequency
2
EVMP Score
0.50
Fluorescence & Localization
Tissue SpecifictestisCell SpecificAdipocytes
Function & Pathway
Protein Function
Predicted intracellular proteins
Canonical Pathways
  • M56 Pid lpa4 pathway
  • M8 Pid endothelin pathway
  • M15 Pid lysophospholipid pathway
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediation
Relations & Evidence

Enzyme-Mediated Modification

3 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
MYO10EGFP01133S962phosphorylationBEL-Large-Corpus_ProtMapperProtMapperProtMapper:17081983
MYO10EGFP01133S965phosphorylationBEL-Large-Corpus_ProtMapperProtMapperProtMapper:17081983
MYO10EGFP01133S969phosphorylationBEL-Large-Corpus_ProtMapperProtMapperProtMapper:17081983

Ligand-Receptor Signaling

9 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
ferm_domainintracellular_intercellular_relatedHGNCYesNoNoNoNo
intracellular_intercellular_relatedintracellular_intercellular_relatedOmniPathYesNoNoNoNo
transmembranetransmembraneRamilowski_locationNoNoNoNoNo
transmembranetransmembraneOmniPathNoNoNoNoNo

Regulatory Interaction Network

2 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
MYO10Q9HD67DCCP43146YesYesNoSIGNORELMHINTIntActLit-BM-17HINT:21642953SIGNOR:17237772Lit-BM-17:21642953ELM:21642953IntAct:21642953
DCCP43146MYO10Q9HD67YesYesNoSIGNORELMHINTIntActLit-BM-17HINT:21642953SIGNOR:17237772Lit-BM-17:21642953ELM:21642953IntAct:21642953

Protein Complex Composition

16 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ACTA1MCCC1MYH7BMYL1MYO10PPIFTNNC1TPM3TRAP1UBCUNC45AA7E2Y1P05976P06753P0CG48P30405P63316P68133Q12931Q96RQ3Q9H3U1Q9HD671:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC6361
DYNC1H1DYNC1I1DYNLL1DYNLL2MYO10MYO5AUBCO14576P0CG48P63167Q14204Q96FJ2Q9HD67Q9Y4I11:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8148
ACTA1CALM3MYH8MYL1MYO10MYO6PPIASOD2UBCUNC45AP04179P05976P0CG48P0DP25P13535P62937P68133Q9H3U1Q9HD67Q9UM541:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC3907
ACTA1CALM3ERCC1MYH8MYL6MYO10PPIASOD2UBCUNC45AP04179P07992P0CG48P0DP25P13535P60660P62937P68133Q9H3U1Q9HD671:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC3839
ACTA1CALM3CDC42BPBMARK4MYL1MYO10MYO18APPIAUBCUNC45AP05976P0CG48P0DP25P62937P68133Q92614Q96L34Q9H3U1Q9HD67Q9Y5S21:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC6153
ACTBCALM3HSP90AA1MYH3MYL12AMYL3MYO10PPIAUBCUNC45AYWHAZP07900P08590P0CG48P0DP25P11055P19105P60709P62937P63104Q9H3U1Q9HD671:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC9502
ACTBCALM3HSP90AA1MYL12AMYL6MYO10MYO18AMYO6RIPK3UBCUNC45AP07900P0CG48P0DP25P19105P60660P60709Q92614Q9H3U1Q9HD67Q9UM54Q9Y5721:1:3:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC7009
ACTBCALM3HSP90AA1MYL6MYO10MYO18BMYO6RIPK3UBCUNC45AP07900P0CG48P0DP25P60660P60709Q8IUG5Q9H3U1Q9HD67Q9UM54Q9Y5721:1:3:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8276
ACTBCALM3CORO1AMCM5MYH3MYL3MYO10PPIAUBCUNC45AYWHAZP08590P0CG48P0DP25P11055P31146P33992P60709P62937P63104Q9H3U1Q9HD671:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC3943
DYNC1H1DYNC1I2DYNLL1MYO10UBCP0CG48P63167Q13409Q14204Q9HD671:1:1:1:1NetworkBlastCompleatCompleat:HC6103
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Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometryWestern blottingFlow cytometry3278941043832153529148239
Sequence, Structure & Domains

Sequences

Length
2,058
Mass
237,347
Sequence
MDNFFTEGTRVWLRENGQHFPSTVNSCAEGIVVFRTDYGQVFTYKQSTITHQKVTAMHPTNEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVERAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMDVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYACCFEWVIKKINSRIKGNEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNDTVVPTSPSADSTVLLAPSVQDSGSLHNSSSGESTYCMPQNAGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTTKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIQEMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGSEMEKYALFTYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTVVADVLAKFEKLAATSEVGDLPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHHPAPEENLQVLAALRLQYLQGDYTLHAAIPPLEEVYSLQRLKARISQSTKTFTPCERLEKRRTSFLEGTLRRSFRTGSVVRQKVEEEQMLDMWIKEEVSSARASIIDKWRKFQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSASSQGSSR
Alternative Products
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3; Name=1; IsoId=Q9HD67-1; Sequence=Displayed; Name=2; IsoId=Q9HD67-2; Sequence=VSP_054976, VSP_054977; Name=Headless; IsoId=Q9HD67-3; Sequence=VSP_054975
Alternative Sequence
1..643; Missing (in isoform Headless); 94..97; TYIG -> VQIG (in isoform 2); 98..2058; Missing (in isoform 2)

3D Structural Models

Turn
51..53; 110..113; 1515..1518; 1707..1709; 1930..1933; 1951..1954
Helix
46..48; 68..70; 76..88; 115..122; 133..146; 163..180; 186..190; 193..208; 247..250; 261..269; 272..277; 283..285; 287..290; 302..315; 320..336; 352..362; 366..374; 391..421; 446..466; 468..476; 490..497; 502..510; 517..528; 560..565; 570..577; 582..588; 611..627; 650..659; 662..671; 679..686; 687..690; 699..710; 728..740; 885..911; 915..926; 1505..1514; 1520..1529; 1531..1533; 1554..1559; 1565..1578; 1586..1598; 1602..1613; 1623..1636; 1643..1659; 1664..1676; 1688..1695; 1722..1732; 1761..1771; 1802..1816; 1824..1839; 1851..1853; 1858..1866; 1906..1912; 1914..1929; 1936..1947; 1996..1998; 2026..2044
Beta Strand
10..15; 18..28; 31..36; 41..45; 54..56; 93..96; 99..103; 128..130; 147..149; 151..156; 209..212; 215..219; 221..229; 235..243; 341..349; 375..380; 383..388; 426..434; 442..444; 543..548; 551..556; 629..637; 675..678; 716..719; 721..726; 1700..1706; 1711..1716; 1740..1750; 1752..1754; 1783..1790; 1794..1797; 1956..1967; 1969..1975; 1977..1984; 1991..1995; 1999..2006; 2009..2014; 2017..2022
3D Structure
Electron microscopy (1); NMR spectroscopy (1); X-ray crystallography (5)

Domain & Motif Annotations

Compositional Bias
847..861; Basic and acidic residues; 989..1003; Acidic residues; 1040..1049; Polar residues; 1060..1071; Low complexity
Coiled Coil
884..934
Domain (CC)
Interaction between the motor domain and the tail leads to an inactive, monomeric conformation. Phospholipid binding via the PH domains leads to the formation of the active, dimeric form of the protein and strongly increases actin-dependent ATPase activity and motor activity (By similarity).; DOMAIN: Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains.; DOMAIN: IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP.; DOMAIN: The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds (By similarity). It can refold after extension suggesting an in vivo force-dependent function (By similarity). An anti-parallel coiled coil is located C-terminal to the SAH domain and mediates dimerization (PubMed:23012428).
Domain (FT)
63..739; Myosin motor; 742..763; IQ 1; 764..787; IQ 2; 788..817; IQ 3; 1212..1310; PH 1; 1392..1497; PH 2; 1547..1695; MyTH4; 1700..2044; FERM
Region
619..641; Actin-binding; 814..883; SAH; 819..840; Disordered; 847..866; Disordered; 964..1090; Disordered
Protein Families
  • TRAFAC class myosin-kinesin ATPase superfamily
  • Myosin family
Sequence Similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Clinical Relevance