Protein detail

MYO10

Unconventional myosin-X (Unconventional myosin-10)

Protein symbol MYO10	UniProt ID Q9HD67	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

Ensembl

ENSG00000145555

Entrez Gene Symbol

MYO10

Gene Synonym

KIAA0799MyoX

Gene Description

Myosin X

Chromosome

Position

16661907-16936288

Frequency

EVMP Score

0.50

Fluorescence & Localization

Tissue SpecifictestisCell SpecificAdipocytes

Function & Pathway

Protein Function

Predicted intracellular proteins

Cellular Component

Molecular Function

Biological Process

KEGG

Reactome

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 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 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 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:21642953 SIGNOR:17237772 Lit-BM-17:21642953 ELM:21642953 IntAct:21642953
DCC	P43146	MYO10	Q9HD67	Yes	Yes	No	SIGNORELMHINTIntActLit-BM-17	HINT:21642953 SIGNOR:17237772 Lit-BM-17:21642953 ELM:21642953 IntAct:21642953

Protein Complex Composition

16 records.

Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs
CALM1 MYO10	P0DP23 Q9HD67	4:2	PDB	PDB:5i0i
DCC MYO10	P43146 Q9HD67	1:1	PDB	PDB:3au4
ARHGAP29 GCC1 JPH3 JPH4 MYO10 UBE2O	Q52LW3 Q8WXH2 Q96CN9 Q96JJ6 Q9C0C9 Q9HD67	0:0:0:0:0:0	hu.MAP2
ARHGAP29 GCC1 JPH3 JPH4 MYO10	Q52LW3 Q8WXH2 Q96CN9 Q96JJ6 Q9HD67	0:0:0:0:0	hu.MAP2
ARHGAP29 JPH3 JPH4 MYO10 UBE2O	Q52LW3 Q8WXH2 Q96JJ6 Q9C0C9 Q9HD67	0:0:0:0:0	hu.MAP2
MYO10	Q9HD67	2	PDB	PDB:3au5PDB:2lw9PDB:5i0h

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Isolation & Detection Technology

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential UltracentrifugationSize Exclusion Chromatography	Mass spectrometryWestern blottingFlow cytometry	3	27894104 38321535 29148239

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

Antibody

CAB015224 HPA024223