Protein detail
MYO10
Unconventional myosin-X (Unconventional myosin-10)
Entry name MYO10 | UniProt ID | EVMP confidence score 0.50 |
Supporting publications (n) 2 | Transmembrane count | Protein classification Plasma proteinsPredicted intracellular proteins |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information11
Protein Names
Unconventional myosin-X (Unconventional myosin-10)
Protein Class (2)
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym (2)
KIAA0799MyoX
Gene Description
Myosin X
Chromosome
5
Position
16661907-16936288
Supporting publications (n)
2
EVMP confidence score
0.50
Fluorescence & Localization3
Tissue SpecifictestisCell SpecificAdipocytes
Function & Pathway8
Protein Function
Predicted intracellular proteins
Cellular Component (12)
- GO:0001726 ruffle
- GO:0005730 nucleolus
- GO:0005829 cytosol
- GO:0005886 plasma membrane
- GO:0005938 cell cortex
- GO:0016459 myosin complex
- GO:0030027 lamellipodium
- GO:0030175 filopodium
- GO:0031527 filopodium membrane
- GO:0032433 filopodium tip
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Molecular Function (8)
Biological Process (3)
KEGG (3)
Reactome (7)
Canonical Pathways (3)
- M56 Pid lpa4 pathway
- M8 Pid endothelin pathway
- M15 Pid lysophospholipid pathway
Mediation Categories (4)
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediation
Relations & Evidence31
Enzyme-Mediated Modification (3)
3 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| MYO10 | EGF | P01133 | S | 962 | phosphorylation | BEL-Large-Corpus_ProtMapperProtMapper | ProtMapper:17081983 |
| MYO10 | EGF | P01133 | S | 965 | phosphorylation | BEL-Large-Corpus_ProtMapperProtMapper | ProtMapper:17081983 |
| MYO10 | EGF | P01133 | S | 969 | phosphorylation | BEL-Large-Corpus_ProtMapperProtMapper | ProtMapper:17081983 |
Ligand-Receptor Signaling (9)
9 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | No | No | No | No | No |
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| ferm_domain | intracellular_intercellular_related | HGNC | Yes | No | No | No | No |
| intracellular_intercellular_related | intracellular_intercellular_related | OmniPath | Yes | No | No | No | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
| transmembrane | transmembrane | OmniPath | No | No | No | No | No |
Regulatory Interaction Network (2)
2 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| MYO10 | Q9HD67 | DCC | P43146 | Yes | Yes | No | SIGNORELMHINTIntActLit-BM-17 | HINT:21642953SIGNOR:17237772Lit-BM-17:21642953ELM:21642953IntAct:21642953 |
| DCC | P43146 | MYO10 | Q9HD67 | Yes | Yes | No | SIGNORELMHINTIntActLit-BM-17 | HINT:21642953SIGNOR:17237772Lit-BM-17:21642953ELM:21642953IntAct:21642953 |
Protein Complex Composition (16)
16 records.
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Sequence, Structure & Domains16
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 (2)
- TRAFAC class myosin-kinesin ATPase superfamily
- Myosin family
Sequence Similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.