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Q9HD67

- MYO10_HUMAN

UniProt

Q9HD67 - MYO10_HUMAN

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Protein
Unconventional myosin-X
Gene
MYO10, KIAA0799
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.2 Publications

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. actin filament binding Source: UniProtKB
  3. actin-dependent ATPase activity Source: UniProtKB
  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. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  3. axon guidance Source: Reactome
  4. cytoskeleton-dependent intracellular transport Source: UniProtKB
  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. Cell projectionlamellipodium. Cell projectionruffle. Cytoplasmcytoskeleton. Cell projectionfilopodium tip. Cytoplasmcell cortex. Cell projectionfilopodium membrane; 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.1 Publication

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. neuron projection Source: Ensembl
  9. neuronal cell body Source: Ensembl
  10. nucleolus Source: HPA
  11. plasma membrane Source: HPA
  12. ruffle Source: UniProtKB-SubCell
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. 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-X
PRO_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.5 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9HD67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 739677Myosin motor
Add
BLAST
Domaini742 – 76322IQ 1
Add
BLAST
Domaini764 – 78724IQ 2
Add
BLAST
Domaini788 – 81730IQ 3
Add
BLAST
Domaini1212 – 131099PH 1
Add
BLAST
Domaini1392 – 1497106PH 2
Add
BLAST
Domaini1547 – 1695149MyTH4
Add
BLAST
Domaini1700 – 2044345FERM
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili813 – 9621501 Publication
Add
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.2 Publications
Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains By similarity.2 Publications
IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP.2 Publications

Sequence similaritiesi

Contains 1 FERM domain.
Contains 3 IQ domains.
Contains 1 MyTH4 domain.
Contains 2 PH domains.

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.

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.
VSP_054975Add
BLAST
Alternative sequencei94 – 974TYIG → VQIG in isoform 2.
VSP_054976
Alternative sequencei98 – 20581961Missing in isoform 2.
VSP_054977Add
BLAST

Sequence conflict

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

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

EnsembliENST00000507288; ENSP00000426664; ENSG00000145555.
ENST00000513610; ENSP00000421280; ENSG00000145555.
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 ENST00000507288 ; ENSP00000426664 ; ENSG00000145555 .
ENST00000513610 ; ENSP00000421280 ; ENSG00000145555 .
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.
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Publicationsi

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  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: September 3, 2014
This is version 133 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

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