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Q9HD67

- MYO10_HUMAN

UniProt

Q9HD67 - MYO10_HUMAN

Protein

Unconventional myosin-X

Gene

MYO10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (02 Sep 2008)
      Previous versions | rss
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    Functioni

    Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts.2 Publications
    Isoform Headless: Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion By similarity.By similarity

    GO - Molecular functioni

    1. actin-dependent ATPase activity Source: UniProtKB
    2. actin filament binding Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW
    4. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    5. plus-end directed microfilament motor activity Source: UniProtKB
    6. protein binding Source: IntAct
    7. spectrin binding Source: MGI

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. axon guidance Source: Reactome
    3. cytoskeleton-dependent intracellular transport Source: UniProtKB
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. innate immune response Source: Reactome
    6. metabolic process Source: GOC
    7. positive regulation of cell-cell adhesion Source: Ensembl
    8. regulation of cell shape Source: UniProtKB
    9. regulation of filopodium assembly Source: UniProtKB

    Keywords - Molecular functioni

    Motor protein, Myosin

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_22237. Netrin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unconventional myosin-X
    Alternative name(s):
    Unconventional myosin-10
    Gene namesi
    Name:MYO10
    Synonyms:KIAA0799
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7593. MYO10.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cell projectionlamellipodium 1 Publication. Cell projectionruffle 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell projectionfilopodium tip 1 Publication. Cytoplasmcell cortex 1 Publication. Cell projectionfilopodium membrane By similarity; Peripheral membrane protein By similarity
    Note: May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Undergoes forward and rearward movements within filopodia. Interacts with microtubules.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. filopodium membrane Source: UniProtKB-SubCell
    5. filopodium tip Source: UniProtKB
    6. lamellipodium Source: UniProtKB-SubCell
    7. myosin complex Source: UniProtKB-KW
    8. neuronal cell body Source: Ensembl
    9. neuron projection Source: Ensembl
    10. nucleolus Source: HPA
    11. plasma membrane Source: HPA
    12. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi795 – 7951F → A: Abolishes interaction with CALM3. 2 Publications
    Mutagenesisi893 – 8931L → Q: Abolishes dimerization. 2 Publications
    Mutagenesisi904 – 9041K → A: Abolishes dimerization. 2 Publications
    Mutagenesisi1647 – 16471K → D: Abolishes interaction with tubulin; when associated with D-1650. 2 Publications
    Mutagenesisi1650 – 16501K → D: Abolishes interaction with tubulin; when associated with D-1647. 2 Publications
    Mutagenesisi1718 – 17192SH → AA: Almost abolishes interaction with DCC. 1 Publication
    Mutagenesisi2002 – 20021F → K: Abolishes interaction with DCC. 2 Publications

    Organism-specific databases

    PharmGKBiPA31394.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20582058Unconventional myosin-XPRO_0000123473Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei965 – 9651Phosphoserine1 Publication

    Post-translational modificationi

    The initiator methionine for isoform Headless is removed.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HD67.
    PaxDbiQ9HD67.
    PRIDEiQ9HD67.

    PTM databases

    PhosphoSiteiQ9HD67.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9HD67.
    BgeeiQ9HD67.
    CleanExiHS_MYO10.
    GenevestigatoriQ9HD67.

    Organism-specific databases

    HPAiCAB015224.
    HPA024223.

    Interactioni

    Subunit structurei

    Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation. Interacts strongly with CALM3 and weakly with CALM, the CALM3 interaction is essential for function in filopodial extension and motility. Interacts with ECM29. Interacts with NEO1. Interacts with ITGB1 and ITGB3. Interacts with VASP By similarity. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CALM3P621582EBI-307061,EBI-397435
    CALML3P274822EBI-307061,EBI-747537
    DCCP431467EBI-307061,EBI-1222919
    ITGB5P180842EBI-307061,EBI-1223434

    Protein-protein interaction databases

    BioGridi110735. 8 interactions.
    DIPiDIP-46151N.
    IntActiQ9HD67. 11 interactions.
    MINTiMINT-1411122.
    STRINGi9606.ENSP00000391106.

    Structurei

    Secondary structure

    1
    2058
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi885 – 91127
    Helixi915 – 92612
    Helixi1505 – 151410
    Turni1515 – 15184
    Helixi1520 – 152910
    Helixi1531 – 15333
    Helixi1554 – 15596
    Helixi1565 – 157814
    Helixi1586 – 159813
    Helixi1602 – 161312
    Helixi1623 – 163614
    Helixi1643 – 165917
    Helixi1664 – 167613
    Helixi1688 – 16958
    Beta strandi1700 – 17067
    Turni1707 – 17093
    Beta strandi1711 – 17166
    Helixi1722 – 173211
    Beta strandi1740 – 175011
    Beta strandi1752 – 17543
    Helixi1761 – 177111
    Beta strandi1783 – 17908
    Beta strandi1794 – 17974
    Helixi1802 – 181615
    Helixi1824 – 183916
    Helixi1851 – 18533
    Helixi1858 – 18669
    Helixi1906 – 19127
    Helixi1914 – 192916
    Turni1930 – 19334
    Helixi1936 – 194712
    Turni1951 – 19544
    Beta strandi1956 – 196712
    Beta strandi1969 – 19757
    Beta strandi1977 – 19848
    Beta strandi1991 – 19955
    Helixi1996 – 19983
    Beta strandi1999 – 20068
    Beta strandi2009 – 20146
    Beta strandi2017 – 20226
    Helixi2026 – 204419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LW9NMR-A/B883-933[»]
    3AU4X-ray1.90A1486-2058[»]
    3AU5X-ray2.55A/B1486-2058[»]
    3PZDX-ray2.50A1503-2047[»]
    ProteinModelPortaliQ9HD67.
    SMRiQ9HD67. Positions 45-940, 1176-1383, 1395-1496, 1501-2046.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HD67.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 739677Myosin motorAdd
    BLAST
    Domaini742 – 76322IQ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini764 – 78724IQ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini788 – 81730IQ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1212 – 131099PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1392 – 1497106PH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1547 – 1695149MyTH4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1700 – 2044345FERMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni883 – 93351Mediates antiparallel dimerizationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili813 – 9621501 PublicationAdd
    BLAST

    Domaini

    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.By similarity
    Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains.By similarity
    IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP.

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 3 IQ domains.PROSITE-ProRule annotation
    Contains 1 myosin motor domain.Curated
    Contains 1 MyTH4 domain.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5022.
    HOGENOMiHOG000007044.
    HOVERGENiHBG052553.
    InParanoidiQ9HD67.
    KOiK12559.
    OMAiDKGYTTL.
    OrthoDBiEOG7Q5HC9.
    PhylomeDBiQ9HD67.
    TreeFamiTF316834.

    Family and domain databases

    Gene3Di1.20.80.10. 2 hits.
    2.30.29.30. 4 hits.
    InterProiIPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR000048. IQ_motif_EF-hand-BS.
    IPR001609. Myosin_head_motor_dom.
    IPR000857. MyTH4_dom.
    IPR027417. P-loop_NTPase.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF00612. IQ. 3 hits.
    PF00063. Myosin_head. 1 hit.
    PF00784. MyTH4. 1 hit.
    PF00169. PH. 2 hits.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00295. B41. 1 hit.
    SM00015. IQ. 3 hits.
    SM00242. MYSc. 1 hit.
    SM00139. MyTH4. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50057. FERM_3. 1 hit.
    PS50096. IQ. 2 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    PS51016. MYTH4. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q9HD67-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDNFFTEGTR VWLRENGQHF PSTVNSCAEG IVVFRTDYGQ VFTYKQSTIT     50
    HQKVTAMHPT NEEGVDDMAS LTELHGGSIM YNLFQRYKRN QIYTYIGSIL 100
    ASVNPYQPIA GLYEPATMEQ YSRRHLGELP PHIFAIANEC YRCLWKRHDN 150
    QCILISGESG AGKTESTKLI LKFLSVISQQ SLELSLKEKT SCVERAILES 200
    SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI VDYLLEKNRV 250
    VRQNPGERNY HIFYALLAGL EHEEREEFYL STPENYHYLN QSGCVEDKTI 300
    SDQESFREVI TAMDVMQFSK EEVREVSRLL AGILHLGNIE FITAGGAQVS 350
    FKTALGRSAE LLGLDPTQLT DALTQRSMFL RGEEILTPLN VQQAVDSRDS 400
    LAMALYACCF EWVIKKINSR IKGNEDFKSI GILDIFGFEN FEVNHFEQFN 450
    INYANEKLQE YFNKHIFSLE QLEYSREGLV WEDIDWIDNG ECLDLIEKKL 500
    GLLALINEES HFPQATDSTL LEKLHSQHAN NHFYVKPRVA VNNFGVKHYA 550
    GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL 600
    KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN MQKMPDQFDQ 650
    AVVLNQLRYS GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNLALPEDVR 700
    GKCTSLLQLY DASNSEWQLG KTKVFLRESL EQKLEKRREE EVSHAAMVIR 750
    AHVLGFLARK QYRKVLYCVV IIQKNYRAFL LRRRFLHLKK AAIVFQKQLR 800
    GQIARRVYRQ LLAEKREQEE KKKQEEEEKK KREEEERERE RERREAELRA 850
    QQEEETRKQQ ELEALQKSQK EAELTRELEK QKENKQVEEI LRLEKEIEDL 900
    QRMKEQQELS LTEASLQKLQ ERRDQELRRL EEEACRAAQE FLESLNFDEI 950
    DECVRNIERS LSVGSEFSSE LAESACEEKP NFNFSQPYPE EEVDEGFEAD 1000
    DDAFKDSPNP SEHGHSDQRT SGIRTSDDSS EEDPYMNDTV VPTSPSADST 1050
    VLLAPSVQDS GSLHNSSSGE STYCMPQNAG DLPSPDGDYD YDQDDYEDGA 1100
    ITSGSSVTFS NSYGSQWSPD YRCSVGTYNS SGAYRFSSEG AQSSFEDSEE 1150
    DFDSRFDTDD ELSYRRDSVY SCVTLPYFHS FLYMKGGLMN SWKRRWCVLK 1200
    DETFLWFRSK QEALKQGWLH KKGGGSSTLS RRNWKKRWFV LRQSKLMYFE 1250
    NDSEEKLKGT VEVRTAKEII DNTTKENGID IIMADRTFHL IAESPEDASQ 1300
    WFSVLSQVHA STDQEIQEMH DEQANPQNAV GTLDVGLIDS VCASDSPDRP 1350
    NSFVIITANR VLHCNADTPE EMHHWITLLQ RSKGDTRVEG QEFIVRGWLH 1400
    KEVKNSPKMS SLKLKKRWFV LTHNSLDYYK SSEKNALKLG TLVLNSLCSV 1450
    VPPDEKIFKE TGYWNVTVYG RKHCYRLYTK LLNEATRWSS AIQNVTDTKA 1500
    PIDTPTQQLI QDIKENCLNS DVVEQIYKRN PILRYTHHPL HSPLLPLPYG 1550
    DINLNLLKDK GYTTLQDEAI KIFNSLQQLE SMSDPIPIIQ GILQTGHDLR 1600
    PLRDELYCQL IKQTNKVPHP GSVGNLYSWQ ILTCLSCTFL PSRGILKYLK 1650
    FHLKRIREQF PGSEMEKYAL FTYESLKKTK CREFVPSRDE IEALIHRQEM 1700
    TSTVYCHGGG SCKITINSHT TAGEVVEKLI RGLAMEDSRN MFALFEYNGH 1750
    VDKAIESRTV VADVLAKFEK LAATSEVGDL PWKFYFKLYC FLDTDNVPKD 1800
    SVEFAFMFEQ AHEAVIHGHH PAPEENLQVL AALRLQYLQG DYTLHAAIPP 1850
    LEEVYSLQRL KARISQSTKT FTPCERLEKR RTSFLEGTLR RSFRTGSVVR 1900
    QKVEEEQMLD MWIKEEVSSA RASIIDKWRK FQGMNQEQAM AKYMALIKEW 1950
    PGYGSTLFDV ECKEGGFPQE LWLGVSADAV SVYKRGEGRP LEVFQYEHIL 2000
    SFGAPLANTY KIVVDERELL FETSEVVDVA KLMKAYISMI VKKRYSTTRS 2050
    ASSQGSSR 2058
    Length:2,058
    Mass (Da):237,347
    Last modified:September 2, 2008 - v3
    Checksum:i269C9E6566BD6D0B
    GO
    Isoform 2 (identifier: Q9HD67-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         94-97: TYIG → VQIG
         98-2058: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:97
    Mass (Da):11,184
    Checksum:iBA4CD8AFA3376564
    GO
    Isoform Headless (identifier: Q9HD67-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-643: Missing.

    Note: Produced by alternative promoter usage.

    Show »
    Length:1,415
    Mass (Da):163,554
    Checksum:i23E2CD27439D8A7E
    GO

    Sequence cautioni

    The sequence BAA34519.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981S → P in AAF36524. 1 PublicationCurated
    Sequence conflicti256 – 2561G → W in AAF68025. (PubMed:10984435)Curated
    Sequence conflicti1186 – 11861G → C in AAF36524. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321V → I.
    Corresponds to variant rs17707947 [ dbSNP | Ensembl ].
    VAR_046328
    Natural varianti148 – 1481H → Y.1 Publication
    Corresponds to variant rs7737765 [ dbSNP | Ensembl ].
    VAR_061366
    Natural varianti273 – 2731E → D.
    Corresponds to variant rs6870170 [ dbSNP | Ensembl ].
    VAR_046329
    Natural varianti324 – 3241R → W.2 Publications
    Corresponds to variant rs11750538 [ dbSNP | Ensembl ].
    VAR_046330
    Natural varianti700 – 7001R → Q.
    Corresponds to variant rs26740 [ dbSNP | Ensembl ].
    VAR_046331
    Natural varianti1663 – 16631S → T.4 Publications
    Corresponds to variant rs25901 [ dbSNP | Ensembl ].
    VAR_046332

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 643643Missing in isoform Headless. 1 PublicationVSP_054975Add
    BLAST
    Alternative sequencei94 – 974TYIG → VQIG in isoform 2. 1 PublicationVSP_054976
    Alternative sequencei98 – 20581961Missing in isoform 2. 1 PublicationVSP_054977Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF247457 mRNA. Translation: AAF68025.2.
    AF234532 mRNA. Translation: AAF37875.1.
    AF132021 mRNA. Translation: AAF36524.1.
    AF132022 mRNA. Translation: AAF36525.1.
    AB018342 mRNA. Translation: BAA34519.2. Different initiation.
    AC010310 Genomic DNA. No translation available.
    AC010607 Genomic DNA. No translation available.
    AC024588 Genomic DNA. No translation available.
    BC041694 mRNA. Translation: AAH41694.1.
    BC050682 mRNA. Translation: AAH50682.1.
    BC108736 mRNA. Translation: AAI08737.1.
    BC137168 mRNA. Translation: AAI37169.1.
    BC150285 mRNA. Translation: AAI50286.1.
    AI878891 mRNA. No translation available.
    AF184153 mRNA. Translation: AAF17363.1.
    CCDSiCCDS54834.1. [Q9HD67-1]
    PIRiA59267.
    RefSeqiNP_036466.2. NM_012334.2.
    UniGeneiHs.481720.

    Genome annotation databases

    EnsembliENST00000274203; ENSP00000274203; ENSG00000145555. [Q9HD67-3]
    ENST00000507288; ENSP00000426664; ENSG00000145555. [Q9HD67-2]
    ENST00000513610; ENSP00000421280; ENSG00000145555. [Q9HD67-1]
    GeneIDi4651.
    KEGGihsa:4651.
    UCSCiuc003jft.4. human. [Q9HD67-1]

    Polymorphism databases

    DMDMi205371854.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF247457 mRNA. Translation: AAF68025.2 .
    AF234532 mRNA. Translation: AAF37875.1 .
    AF132021 mRNA. Translation: AAF36524.1 .
    AF132022 mRNA. Translation: AAF36525.1 .
    AB018342 mRNA. Translation: BAA34519.2 . Different initiation.
    AC010310 Genomic DNA. No translation available.
    AC010607 Genomic DNA. No translation available.
    AC024588 Genomic DNA. No translation available.
    BC041694 mRNA. Translation: AAH41694.1 .
    BC050682 mRNA. Translation: AAH50682.1 .
    BC108736 mRNA. Translation: AAI08737.1 .
    BC137168 mRNA. Translation: AAI37169.1 .
    BC150285 mRNA. Translation: AAI50286.1 .
    AI878891 mRNA. No translation available.
    AF184153 mRNA. Translation: AAF17363.1 .
    CCDSi CCDS54834.1. [Q9HD67-1 ]
    PIRi A59267.
    RefSeqi NP_036466.2. NM_012334.2.
    UniGenei Hs.481720.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LW9 NMR - A/B 883-933 [» ]
    3AU4 X-ray 1.90 A 1486-2058 [» ]
    3AU5 X-ray 2.55 A/B 1486-2058 [» ]
    3PZD X-ray 2.50 A 1503-2047 [» ]
    ProteinModelPortali Q9HD67.
    SMRi Q9HD67. Positions 45-940, 1176-1383, 1395-1496, 1501-2046.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110735. 8 interactions.
    DIPi DIP-46151N.
    IntActi Q9HD67. 11 interactions.
    MINTi MINT-1411122.
    STRINGi 9606.ENSP00000391106.

    PTM databases

    PhosphoSitei Q9HD67.

    Polymorphism databases

    DMDMi 205371854.

    Proteomic databases

    MaxQBi Q9HD67.
    PaxDbi Q9HD67.
    PRIDEi Q9HD67.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274203 ; ENSP00000274203 ; ENSG00000145555 . [Q9HD67-3 ]
    ENST00000507288 ; ENSP00000426664 ; ENSG00000145555 . [Q9HD67-2 ]
    ENST00000513610 ; ENSP00000421280 ; ENSG00000145555 . [Q9HD67-1 ]
    GeneIDi 4651.
    KEGGi hsa:4651.
    UCSCi uc003jft.4. human. [Q9HD67-1 ]

    Organism-specific databases

    CTDi 4651.
    GeneCardsi GC05M016718.
    H-InvDB HIX0021772.
    HIX0164320.
    HGNCi HGNC:7593. MYO10.
    HPAi CAB015224.
    HPA024223.
    MIMi 601481. gene.
    neXtProti NX_Q9HD67.
    PharmGKBi PA31394.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5022.
    HOGENOMi HOG000007044.
    HOVERGENi HBG052553.
    InParanoidi Q9HD67.
    KOi K12559.
    OMAi DKGYTTL.
    OrthoDBi EOG7Q5HC9.
    PhylomeDBi Q9HD67.
    TreeFami TF316834.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_22237. Netrin-1 signaling.

    Miscellaneous databases

    ChiTaRSi MYO10. human.
    EvolutionaryTracei Q9HD67.
    GeneWikii MYO10.
    GenomeRNAii 4651.
    NextBioi 17932.
    PROi Q9HD67.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HD67.
    Bgeei Q9HD67.
    CleanExi HS_MYO10.
    Genevestigatori Q9HD67.

    Family and domain databases

    Gene3Di 1.20.80.10. 2 hits.
    2.30.29.30. 4 hits.
    InterProi IPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR000048. IQ_motif_EF-hand-BS.
    IPR001609. Myosin_head_motor_dom.
    IPR000857. MyTH4_dom.
    IPR027417. P-loop_NTPase.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF00612. IQ. 3 hits.
    PF00063. Myosin_head. 1 hit.
    PF00784. MyTH4. 1 hit.
    PF00169. PH. 2 hits.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00295. B41. 1 hit.
    SM00015. IQ. 3 hits.
    SM00242. MYSc. 1 hit.
    SM00139. MyTH4. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50057. FERM_3. 1 hit.
    PS50096. IQ. 2 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    PS51016. MYTH4. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin."
      Berg J.S., Derfler B.H., Pennisi C.M., Corey D.P., Cheney R.E.
      J. Cell Sci. 113:3439-3451(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS TRP-324 AND THR-1663.
    2. "The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X."
      Rogers M.S., Strehler E.E.
      J. Biol. Chem. 276:12182-12189(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS TYR-148 AND THR-1663, INTERACTION WITH CALM3/CLP.
    3. "Cloning of human myosin X."
      Takada T., O'Farrell T.J., Anderson J.T., Pourmotabbed T.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TRP-324.
      Tissue: Colon adenocarcinoma.
    4. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-1663.
      Tissue: Brain.
    5. Nagase T., Kikuno R., Yamakawa H., Ohara O.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-1663.
      Tissue: Brain and Skin.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126 (ISOFORM HEADLESS).
    9. "Physical map and characterization of transcripts in the candidate interval for familial chondrocalcinosis at chromosome 5p15.1."
      Rojas K., Serrano de la Pena L., Gallardo T., Simmons A., Nyce K., McGrath R., Considine E., Vasko A.J., Peterson E., Grady D., Cox R., Andrew L.J., Lovett M., Overhauser J., Williams C.J.
      Genomics 62:177-183(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-495 (ISOFORM 1).
      Tissue: Skeletal muscle.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Myo10 in brain: developmental regulation, identification of a headless isoform and dynamics in neurons."
      Sousa A.D., Berg J.S., Robertson B.W., Meeker R.B., Cheney R.E.
      J. Cell Sci. 119:184-194(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM HEADLESS).
    12. "Myosin-X is a molecular motor that functions in filopodia formation."
      Bohil A.B., Robertson B.W., Cheney R.E.
      Proc. Natl. Acad. Sci. U.S.A. 103:12411-12416(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF FILOPODIA ASSEMBLY AND REGULATION OF CELL SHAPE.
    13. "Interaction with the IQ3 motif of myosin-10 is required for calmodulin-like protein-dependent filopodial extension."
      Bennett R.D., Caride A.J., Mauer A.S., Strehler E.E.
      FEBS Lett. 582:2377-2381(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IQ3 DOMAIN, MUTAGENESIS OF PHE-795.
    14. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
      Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
      J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECM29.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain."
      Hirano Y., Hatano T., Takahashi A., Toriyama M., Inagaki N., Hakoshima T.
      EMBO J. 30:2734-2747(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1486-2058 IN COMPLEX WITH DCC, INTERACTION WITH DCC; ITGB5 AND TUBULIN, MUTAGENESIS OF LYS-1647; LYS-1650 AND PHE-2002.
    17. "Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain."
      Wei Z., Yan J., Lu Q., Pan L., Zhang M.
      Proc. Natl. Acad. Sci. U.S.A. 108:3572-3577(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1503-2047 IN COMPLEX WITH DCC, INTERACTION WITH DCC, MUTAGENESIS OF 1718-SER-HIS-1719.
    18. "Antiparallel coiled-coil-mediated dimerization of myosin X."
      Lu Q., Ye F., Wei Z., Wen Z., Zhang M.
      Proc. Natl. Acad. Sci. U.S.A. 109:17388-17393(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 883-933, SUBUNIT, COILED-COIL DOMAIN, MUTAGENESIS OF LEU-893 AND LYS-904.

    Entry informationi

    Entry nameiMYO10_HUMAN
    AccessioniPrimary (citable) accession number: Q9HD67
    Secondary accession number(s): A7E2D1
    , O94893, Q8IVX5, Q9NYM7, Q9P110, Q9P111, Q9UHF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 134 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3