Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Unconventional myosin-X

Gene

MYO10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • cytoskeleton-dependent intracellular transport Source: UniProtKB
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • positive regulation of cell-cell adhesion Source: Ensembl
  • regulation of cell shape Source: UniProtKB
  • 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

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-373752. 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
Proteomesi
  • UP000005640 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi795F → A: Abolishes interaction with CALM3. 1 Publication1
Mutagenesisi893L → Q: Abolishes dimerization. 1 Publication1
Mutagenesisi904K → A: Abolishes dimerization. 1 Publication1
Mutagenesisi1647K → D: Abolishes interaction with tubulin; when associated with D-1650. 1 Publication1
Mutagenesisi1650K → D: Abolishes interaction with tubulin; when associated with D-1647. 1 Publication1
Mutagenesisi1718 – 1719SH → AA: Almost abolishes interaction with DCC. 1 Publication2
Mutagenesisi2002F → K: Abolishes interaction with DCC. 1 Publication1

Organism-specific databases

DisGeNETi4651.
OpenTargetsiENSG00000145555.
PharmGKBiPA31394.

Polymorphism and mutation databases

BioMutaiMYO10.
DMDMi205371854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001234731 – 2058Unconventional myosin-XAdd BLAST2058

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei962PhosphoserineBy similarity1
Modified residuei965PhosphoserineCombined sources1
Modified residuei968PhosphoserineBy similarity1
Modified residuei1158PhosphothreonineBy similarity1

Post-translational modificationi

The initiator methionine for isoform Headless is removed.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9HD67.
MaxQBiQ9HD67.
PaxDbiQ9HD67.
PeptideAtlasiQ9HD67.
PRIDEiQ9HD67.

PTM databases

iPTMnetiQ9HD67.
PhosphoSitePlusiQ9HD67.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000145555.
CleanExiHS_MYO10.
ExpressionAtlasiQ9HD67. baseline and differential.
GenevisibleiQ9HD67. HS.

Organism-specific databases

HPAiCAB015224.
HPA024223.

Interactioni

Subunit structurei

Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. 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
CALML3P274823EBI-307061,EBI-747537
DCCP431467EBI-307061,EBI-1222919
ITGB5P180842EBI-307061,EBI-1223434

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • spectrin binding Source: MGI

Protein-protein interaction databases

BioGridi110735. 18 interactors.
DIPiDIP-46151N.
IntActiQ9HD67. 20 interactors.
MINTiMINT-1411122.
STRINGi9606.ENSP00000421280.

Structurei

Secondary structure

12058
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 15Combined sources6
Beta strandi18 – 28Combined sources11
Beta strandi31 – 36Combined sources6
Beta strandi41 – 45Combined sources5
Helixi46 – 48Combined sources3
Turni51 – 53Combined sources3
Beta strandi54 – 56Combined sources3
Helixi68 – 70Combined sources3
Helixi76 – 88Combined sources13
Beta strandi93 – 96Combined sources4
Beta strandi99 – 103Combined sources5
Turni110 – 113Combined sources4
Helixi115 – 122Combined sources8
Beta strandi128 – 130Combined sources3
Helixi133 – 146Combined sources14
Beta strandi147 – 149Combined sources3
Beta strandi151 – 156Combined sources6
Helixi163 – 180Combined sources18
Helixi186 – 190Combined sources5
Helixi193 – 208Combined sources16
Beta strandi209 – 212Combined sources4
Beta strandi215 – 219Combined sources5
Beta strandi221 – 229Combined sources9
Beta strandi235 – 243Combined sources9
Helixi247 – 250Combined sources4
Helixi261 – 269Combined sources9
Helixi272 – 277Combined sources6
Helixi283 – 285Combined sources3
Helixi287 – 290Combined sources4
Helixi302 – 315Combined sources14
Helixi320 – 336Combined sources17
Beta strandi341 – 349Combined sources9
Helixi352 – 362Combined sources11
Helixi366 – 374Combined sources9
Beta strandi375 – 380Combined sources6
Beta strandi383 – 388Combined sources6
Helixi391 – 421Combined sources31
Beta strandi426 – 434Combined sources9
Beta strandi442 – 444Combined sources3
Helixi446 – 466Combined sources21
Helixi468 – 476Combined sources9
Helixi490 – 497Combined sources8
Helixi502 – 510Combined sources9
Helixi517 – 528Combined sources12
Beta strandi543 – 548Combined sources6
Beta strandi551 – 556Combined sources6
Helixi560 – 565Combined sources6
Helixi570 – 577Combined sources8
Helixi582 – 588Combined sources7
Helixi611 – 627Combined sources17
Beta strandi629 – 637Combined sources9
Helixi650 – 659Combined sources10
Helixi662 – 671Combined sources10
Beta strandi675 – 678Combined sources4
Helixi679 – 686Combined sources8
Helixi687 – 690Combined sources4
Helixi699 – 710Combined sources12
Beta strandi716 – 719Combined sources4
Beta strandi721 – 726Combined sources6
Helixi728 – 740Combined sources13
Helixi885 – 911Combined sources27
Helixi915 – 926Combined sources12
Helixi1505 – 1514Combined sources10
Turni1515 – 1518Combined sources4
Helixi1520 – 1529Combined sources10
Helixi1531 – 1533Combined sources3
Helixi1554 – 1559Combined sources6
Helixi1565 – 1578Combined sources14
Helixi1586 – 1598Combined sources13
Helixi1602 – 1613Combined sources12
Helixi1623 – 1636Combined sources14
Helixi1643 – 1659Combined sources17
Helixi1664 – 1676Combined sources13
Helixi1688 – 1695Combined sources8
Beta strandi1700 – 1706Combined sources7
Turni1707 – 1709Combined sources3
Beta strandi1711 – 1716Combined sources6
Helixi1722 – 1732Combined sources11
Beta strandi1740 – 1750Combined sources11
Beta strandi1752 – 1754Combined sources3
Helixi1761 – 1771Combined sources11
Beta strandi1783 – 1790Combined sources8
Beta strandi1794 – 1797Combined sources4
Helixi1802 – 1816Combined sources15
Helixi1824 – 1839Combined sources16
Helixi1851 – 1853Combined sources3
Helixi1858 – 1866Combined sources9
Helixi1906 – 1912Combined sources7
Helixi1914 – 1929Combined sources16
Turni1930 – 1933Combined sources4
Helixi1936 – 1947Combined sources12
Turni1951 – 1954Combined sources4
Beta strandi1956 – 1967Combined sources12
Beta strandi1969 – 1975Combined sources7
Beta strandi1977 – 1984Combined sources8
Beta strandi1991 – 1995Combined sources5
Helixi1996 – 1998Combined sources3
Beta strandi1999 – 2006Combined sources8
Beta strandi2009 – 2014Combined sources6
Beta strandi2017 – 2022Combined sources6
Helixi2026 – 2044Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LW9NMR-A/B883-933[»]
3AU4X-ray1.90A1486-2058[»]
3AU5X-ray2.55A/B1486-2058[»]
3PZDX-ray2.50A1503-2047[»]
5I0HX-ray1.80A/B1-741[»]
5I0IX-ray3.15A/B3-793[»]
5KG8electron microscopy9.10A3-741[»]
ProteinModelPortaliQ9HD67.
SMRiQ9HD67.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HD67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 739Myosin motorAdd BLAST677
Domaini742 – 763IQ 1PROSITE-ProRule annotationAdd BLAST22
Domaini764 – 787IQ 2PROSITE-ProRule annotationAdd BLAST24
Domaini788 – 817IQ 3PROSITE-ProRule annotationAdd BLAST30
Domaini1212 – 1310PH 1PROSITE-ProRule annotationAdd BLAST99
Domaini1392 – 1497PH 2PROSITE-ProRule annotationAdd BLAST106
Domaini1547 – 1695MyTH4PROSITE-ProRule annotationAdd BLAST149
Domaini1700 – 2044FERMPROSITE-ProRule annotationAdd BLAST345

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni815 – 908SAHBy similarityAdd BLAST94
Regioni883 – 933Mediates antiparallel dimerization1 PublicationAdd BLAST51

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.
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. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric; however, in its distal part seems to form a semirigid helical structure which overlaps with a region shown to mediate antiparallel coiled coil-mediated dimerization.By similarity

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

Repeat

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129697.
HOGENOMiHOG000007044.
HOVERGENiHBG052553.
InParanoidiQ9HD67.
KOiK12559.
PhylomeDBiQ9HD67.
TreeFamiTF316834.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 5 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.
IPR031971. MYO10_CC.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF16735. MYO10_CC. 1 hit.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
PF00788. RA. 1 hit.
[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.
SSF50729. SSF50729. 4 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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti98S → P in AAF36524 (Ref. 3) Curated1
Sequence conflicti256G → W in AAF68025 (PubMed:10984435).Curated1
Sequence conflicti1186G → C in AAF36524 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04632832V → I.Corresponds to variant rs17707947dbSNPEnsembl.1
Natural variantiVAR_061366148H → Y.1 PublicationCorresponds to variant rs7737765dbSNPEnsembl.1
Natural variantiVAR_046329273E → D.Corresponds to variant rs6870170dbSNPEnsembl.1
Natural variantiVAR_046330324R → W.2 PublicationsCorresponds to variant rs11750538dbSNPEnsembl.1
Natural variantiVAR_046331700R → Q.Corresponds to variant rs26740dbSNPEnsembl.1
Natural variantiVAR_0463321663S → T.4 PublicationsCorresponds to variant rs25901dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0549751 – 643Missing in isoform Headless. 1 PublicationAdd BLAST643
Alternative sequenceiVSP_05497694 – 97TYIG → VQIG in isoform 2. 1 Publication4
Alternative sequenceiVSP_05497798 – 2058Missing in isoform 2. 1 PublicationAdd BLAST1961

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_005248307.2. [Q9HD67-3]
XP_011512348.1. XM_011514046.2. [Q9HD67-3]
UniGeneiHs.481720.

Genome annotation databases

EnsembliENST00000507288; ENSP00000426664; ENSG00000145555. [Q9HD67-2]
ENST00000513610; ENSP00000421280; ENSG00000145555. [Q9HD67-1]
GeneIDi4651.
KEGGihsa:4651.
UCSCiuc003jft.5. human. [Q9HD67-1]

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.
CCDSiCCDS54834.1. [Q9HD67-1]
PIRiA59267.
RefSeqiNP_036466.2. NM_012334.2. [Q9HD67-1]
XP_005248364.1. XM_005248307.2. [Q9HD67-3]
XP_011512348.1. XM_011514046.2. [Q9HD67-3]
UniGeneiHs.481720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LW9NMR-A/B883-933[»]
3AU4X-ray1.90A1486-2058[»]
3AU5X-ray2.55A/B1486-2058[»]
3PZDX-ray2.50A1503-2047[»]
5I0HX-ray1.80A/B1-741[»]
5I0IX-ray3.15A/B3-793[»]
5KG8electron microscopy9.10A3-741[»]
ProteinModelPortaliQ9HD67.
SMRiQ9HD67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110735. 18 interactors.
DIPiDIP-46151N.
IntActiQ9HD67. 20 interactors.
MINTiMINT-1411122.
STRINGi9606.ENSP00000421280.

PTM databases

iPTMnetiQ9HD67.
PhosphoSitePlusiQ9HD67.

Polymorphism and mutation databases

BioMutaiMYO10.
DMDMi205371854.

Proteomic databases

EPDiQ9HD67.
MaxQBiQ9HD67.
PaxDbiQ9HD67.
PeptideAtlasiQ9HD67.
PRIDEiQ9HD67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000507288; ENSP00000426664; ENSG00000145555. [Q9HD67-2]
ENST00000513610; ENSP00000421280; ENSG00000145555. [Q9HD67-1]
GeneIDi4651.
KEGGihsa:4651.
UCSCiuc003jft.5. human. [Q9HD67-1]

Organism-specific databases

CTDi4651.
DisGeNETi4651.
GeneCardsiMYO10.
H-InvDBHIX0021772.
HIX0164320.
HGNCiHGNC:7593. MYO10.
HPAiCAB015224.
HPA024223.
MIMi601481. gene.
neXtProtiNX_Q9HD67.
OpenTargetsiENSG00000145555.
PharmGKBiPA31394.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129697.
HOGENOMiHOG000007044.
HOVERGENiHBG052553.
InParanoidiQ9HD67.
KOiK12559.
PhylomeDBiQ9HD67.
TreeFamiTF316834.

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-373752. Netrin-1 signaling.

Miscellaneous databases

ChiTaRSiMYO10. human.
EvolutionaryTraceiQ9HD67.
GeneWikiiMYO10.
GenomeRNAii4651.
PROiQ9HD67.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145555.
CleanExiHS_MYO10.
ExpressionAtlasiQ9HD67. baseline and differential.
GenevisibleiQ9HD67. HS.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 5 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.
IPR031971. MYO10_CC.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF16735. MYO10_CC. 1 hit.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
PF00788. RA. 1 hit.
[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.
SSF50729. SSF50729. 4 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]
ProtoNetiSearch...

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 30, 2016
This is version 158 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

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10).Curated
Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.