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Q9HD67

- MYO10_HUMAN

UniProt

Q9HD67 - MYO10_HUMAN

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Protein

Unconventional myosin-X

Gene

MYO10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. filopodium tip Source: UniProtKB
  4. myosin complex Source: UniProtKB-KW
  5. neuronal cell body Source: Ensembl
  6. neuron projection Source: Ensembl
  7. nucleolus Source: HPA
  8. plasma membrane Source: HPA
Complete GO annotation...

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. 1 Publication
Mutagenesisi893 – 8931L → Q: Abolishes dimerization. 1 Publication
Mutagenesisi904 – 9041K → A: Abolishes dimerization. 1 Publication
Mutagenesisi1647 – 16471K → D: Abolishes interaction with tubulin; when associated with D-1650. 1 Publication
Mutagenesisi1650 – 16501K → D: Abolishes interaction with tubulin; when associated with D-1647. 1 Publication
Mutagenesisi1718 – 17192SH → AA: Almost abolishes interaction with DCC. 1 Publication
Mutagenesisi2002 – 20021F → K: Abolishes interaction with DCC. 1 Publication

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

BgeeiQ9HD67.
CleanExiHS_MYO10.
ExpressionAtlasiQ9HD67. baseline and differential.
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 – 91127Combined sources
Helixi915 – 92612Combined sources
Helixi1505 – 151410Combined sources
Turni1515 – 15184Combined sources
Helixi1520 – 152910Combined sources
Helixi1531 – 15333Combined sources
Helixi1554 – 15596Combined sources
Helixi1565 – 157814Combined sources
Helixi1586 – 159813Combined sources
Helixi1602 – 161312Combined sources
Helixi1623 – 163614Combined sources
Helixi1643 – 165917Combined sources
Helixi1664 – 167613Combined sources
Helixi1688 – 16958Combined sources
Beta strandi1700 – 17067Combined sources
Turni1707 – 17093Combined sources
Beta strandi1711 – 17166Combined sources
Helixi1722 – 173211Combined sources
Beta strandi1740 – 175011Combined sources
Beta strandi1752 – 17543Combined sources
Helixi1761 – 177111Combined sources
Beta strandi1783 – 17908Combined sources
Beta strandi1794 – 17974Combined sources
Helixi1802 – 181615Combined sources
Helixi1824 – 183916Combined sources
Helixi1851 – 18533Combined sources
Helixi1858 – 18669Combined sources
Helixi1906 – 19127Combined sources
Helixi1914 – 192916Combined sources
Turni1930 – 19334Combined sources
Helixi1936 – 194712Combined sources
Turni1951 – 19544Combined sources
Beta strandi1956 – 196712Combined sources
Beta strandi1969 – 19757Combined sources
Beta strandi1977 – 19848Combined sources
Beta strandi1991 – 19955Combined sources
Helixi1996 – 19983Combined sources
Beta strandi1999 – 20068Combined sources
Beta strandi2009 – 20146Combined sources
Beta strandi2017 – 20226Combined sources
Helixi2026 – 204419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 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.
GeneTreeiENSGT00770000120520.
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

        10         20         30         40         50
MDNFFTEGTR VWLRENGQHF PSTVNSCAEG IVVFRTDYGQ VFTYKQSTIT
60 70 80 90 100
HQKVTAMHPT NEEGVDDMAS LTELHGGSIM YNLFQRYKRN QIYTYIGSIL
110 120 130 140 150
ASVNPYQPIA GLYEPATMEQ YSRRHLGELP PHIFAIANEC YRCLWKRHDN
160 170 180 190 200
QCILISGESG AGKTESTKLI LKFLSVISQQ SLELSLKEKT SCVERAILES
210 220 230 240 250
SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI VDYLLEKNRV
260 270 280 290 300
VRQNPGERNY HIFYALLAGL EHEEREEFYL STPENYHYLN QSGCVEDKTI
310 320 330 340 350
SDQESFREVI TAMDVMQFSK EEVREVSRLL AGILHLGNIE FITAGGAQVS
360 370 380 390 400
FKTALGRSAE LLGLDPTQLT DALTQRSMFL RGEEILTPLN VQQAVDSRDS
410 420 430 440 450
LAMALYACCF EWVIKKINSR IKGNEDFKSI GILDIFGFEN FEVNHFEQFN
460 470 480 490 500
INYANEKLQE YFNKHIFSLE QLEYSREGLV WEDIDWIDNG ECLDLIEKKL
510 520 530 540 550
GLLALINEES HFPQATDSTL LEKLHSQHAN NHFYVKPRVA VNNFGVKHYA
560 570 580 590 600
GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL
610 620 630 640 650
KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN MQKMPDQFDQ
660 670 680 690 700
AVVLNQLRYS GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNLALPEDVR
710 720 730 740 750
GKCTSLLQLY DASNSEWQLG KTKVFLRESL EQKLEKRREE EVSHAAMVIR
760 770 780 790 800
AHVLGFLARK QYRKVLYCVV IIQKNYRAFL LRRRFLHLKK AAIVFQKQLR
810 820 830 840 850
GQIARRVYRQ LLAEKREQEE KKKQEEEEKK KREEEERERE RERREAELRA
860 870 880 890 900
QQEEETRKQQ ELEALQKSQK EAELTRELEK QKENKQVEEI LRLEKEIEDL
910 920 930 940 950
QRMKEQQELS LTEASLQKLQ ERRDQELRRL EEEACRAAQE FLESLNFDEI
960 970 980 990 1000
DECVRNIERS LSVGSEFSSE LAESACEEKP NFNFSQPYPE EEVDEGFEAD
1010 1020 1030 1040 1050
DDAFKDSPNP SEHGHSDQRT SGIRTSDDSS EEDPYMNDTV VPTSPSADST
1060 1070 1080 1090 1100
VLLAPSVQDS GSLHNSSSGE STYCMPQNAG DLPSPDGDYD YDQDDYEDGA
1110 1120 1130 1140 1150
ITSGSSVTFS NSYGSQWSPD YRCSVGTYNS SGAYRFSSEG AQSSFEDSEE
1160 1170 1180 1190 1200
DFDSRFDTDD ELSYRRDSVY SCVTLPYFHS FLYMKGGLMN SWKRRWCVLK
1210 1220 1230 1240 1250
DETFLWFRSK QEALKQGWLH KKGGGSSTLS RRNWKKRWFV LRQSKLMYFE
1260 1270 1280 1290 1300
NDSEEKLKGT VEVRTAKEII DNTTKENGID IIMADRTFHL IAESPEDASQ
1310 1320 1330 1340 1350
WFSVLSQVHA STDQEIQEMH DEQANPQNAV GTLDVGLIDS VCASDSPDRP
1360 1370 1380 1390 1400
NSFVIITANR VLHCNADTPE EMHHWITLLQ RSKGDTRVEG QEFIVRGWLH
1410 1420 1430 1440 1450
KEVKNSPKMS SLKLKKRWFV LTHNSLDYYK SSEKNALKLG TLVLNSLCSV
1460 1470 1480 1490 1500
VPPDEKIFKE TGYWNVTVYG RKHCYRLYTK LLNEATRWSS AIQNVTDTKA
1510 1520 1530 1540 1550
PIDTPTQQLI QDIKENCLNS DVVEQIYKRN PILRYTHHPL HSPLLPLPYG
1560 1570 1580 1590 1600
DINLNLLKDK GYTTLQDEAI KIFNSLQQLE SMSDPIPIIQ GILQTGHDLR
1610 1620 1630 1640 1650
PLRDELYCQL IKQTNKVPHP GSVGNLYSWQ ILTCLSCTFL PSRGILKYLK
1660 1670 1680 1690 1700
FHLKRIREQF PGSEMEKYAL FTYESLKKTK CREFVPSRDE IEALIHRQEM
1710 1720 1730 1740 1750
TSTVYCHGGG SCKITINSHT TAGEVVEKLI RGLAMEDSRN MFALFEYNGH
1760 1770 1780 1790 1800
VDKAIESRTV VADVLAKFEK LAATSEVGDL PWKFYFKLYC FLDTDNVPKD
1810 1820 1830 1840 1850
SVEFAFMFEQ AHEAVIHGHH PAPEENLQVL AALRLQYLQG DYTLHAAIPP
1860 1870 1880 1890 1900
LEEVYSLQRL KARISQSTKT FTPCERLEKR RTSFLEGTLR RSFRTGSVVR
1910 1920 1930 1940 1950
QKVEEEQMLD MWIKEEVSSA RASIIDKWRK FQGMNQEQAM AKYMALIKEW
1960 1970 1980 1990 2000
PGYGSTLFDV ECKEGGFPQE LWLGVSADAV SVYKRGEGRP LEVFQYEHIL
2010 2020 2030 2040 2050
SFGAPLANTY KIVVDERELL FETSEVVDVA KLMKAYISMI VKKRYSTTRS

ASSQGSSR
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.Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q9HD67-1]
XP_005248364.1. XM_005248307.1. [Q9HD67-3]
UniGeneiHs.481720.

Genome annotation databases

EnsembliENST00000507288; ENSP00000426664; ENSG00000145555. [Q9HD67-2]
ENST00000513610; ENSP00000421280; ENSG00000145555. [Q9HD67-1]
GeneIDi4651.
KEGGihsa:4651.
UCSCiuc003jft.4. human. [Q9HD67-1]
uc003jfv.2. human.

Polymorphism databases

DMDMi205371854.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q9HD67-1 ]
XP_005248364.1. XM_005248307.1. [Q9HD67-3 ]
UniGenei Hs.481720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 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 ENST00000507288 ; ENSP00000426664 ; ENSG00000145555 . [Q9HD67-2 ]
ENST00000513610 ; ENSP00000421280 ; ENSG00000145555 . [Q9HD67-1 ]
GeneIDi 4651.
KEGGi hsa:4651.
UCSCi uc003jft.4. human. [Q9HD67-1 ]
uc003jfv.2. human.

Organism-specific databases

CTDi 4651.
GeneCardsi GC05M016662.
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.
GeneTreei ENSGT00770000120520.
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

Bgeei Q9HD67.
CleanExi HS_MYO10.
ExpressionAtlasi Q9HD67. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 136 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