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Q9HD67 (MYO10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-X
Alternative name(s):
Unconventional myosin-10
Gene names
Name:MYO10
Synonyms:KIAA0799
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2058 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Plays a role in formation of the podosome belt in osteoclasts By similarity. Ref.9

Subunit structure

Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation. Interacts with CALM. Interacts with ECM29. Interacts with NEO1. Interacts with ITGB1 and ITGB3 By similarity. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Ref.10 Ref.12 Ref.13

Subcellular location

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. Ref.1

Tissue specificity

Ubiquitous. Ref.1

Domain

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.

Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains By similarity.

Sequence similarities

Contains 1 FERM domain.

Contains 3 IQ domains.

Contains 1 myosin head-like domain.

Contains 1 MyTH4 domain.

Contains 2 PH domains.

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10).

Sequence caution

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

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cytoskeleton-dependent intracellular transport

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

metabolic process

Inferred from sequence or structural similarity. Source: GOC

positive regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of filopodium assembly

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

filopodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium tip

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

myosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

actin-dependent ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

plus-end directed microfilament motor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20582058Unconventional myosin-X
PRO_0000123473

Regions

Domain1 – 727727Myosin head-like
Domain742 – 76322IQ 1
Domain764 – 78724IQ 2
Domain788 – 81730IQ 3
Domain1212 – 131099PH 1
Domain1392 – 1497106PH 2
Domain1547 – 1695149MyTH4
Domain1700 – 2044345FERM
Coiled coil799 – 943145 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue9651Phosphoserine Ref.8

Natural variations

Natural variant321V → I.
Corresponds to variant rs17707947 [ dbSNP | Ensembl ].
VAR_046328
Natural variant1481H → Y. Ref.2
Corresponds to variant rs7737765 [ dbSNP | Ensembl ].
VAR_061366
Natural variant2731E → D.
Corresponds to variant rs6870170 [ dbSNP | Ensembl ].
VAR_046329
Natural variant3241R → W. Ref.1 Ref.3
Corresponds to variant rs11750538 [ dbSNP | Ensembl ].
VAR_046330
Natural variant7001R → Q.
Corresponds to variant rs26740 [ dbSNP | Ensembl ].
VAR_046331
Natural variant16631S → T. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs25901 [ dbSNP | Ensembl ].
VAR_046332

Experimental info

Mutagenesis16471K → D: Abolishes interaction with tubulin; when associated with D-1650. Ref.12 Ref.13
Mutagenesis16501K → D: Abolishes interaction with tubulin; when associated with D-1647. Ref.12 Ref.13
Mutagenesis1718 – 17192SH → AA: Almost abolishes interaction with DCC. Ref.13
Mutagenesis20021F → K: Abolishes interaction with DCC. Ref.12 Ref.13
Sequence conflict981S → P in AAF36524. Ref.3
Sequence conflict2561G → W in AAF68025. Ref.1
Sequence conflict11861G → C in AAF36524. Ref.3

Secondary structure

.............................................................................. 2058
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HD67 [UniParc].

Last modified September 2, 2008. Version 3.
Checksum: 269C9E6566BD6D0B

FASTA2,058237,347
        10         20         30         40         50         60 
MDNFFTEGTR VWLRENGQHF PSTVNSCAEG IVVFRTDYGQ VFTYKQSTIT HQKVTAMHPT 

        70         80         90        100        110        120 
NEEGVDDMAS LTELHGGSIM YNLFQRYKRN QIYTYIGSIL ASVNPYQPIA GLYEPATMEQ 

       130        140        150        160        170        180 
YSRRHLGELP PHIFAIANEC YRCLWKRHDN QCILISGESG AGKTESTKLI LKFLSVISQQ 

       190        200        210        220        230        240 
SLELSLKEKT SCVERAILES SPIMEAFGNA KTVYNNNSSR FGKFVQLNIC QKGNIQGGRI 

       250        260        270        280        290        300 
VDYLLEKNRV VRQNPGERNY HIFYALLAGL EHEEREEFYL STPENYHYLN QSGCVEDKTI 

       310        320        330        340        350        360 
SDQESFREVI TAMDVMQFSK EEVREVSRLL AGILHLGNIE FITAGGAQVS FKTALGRSAE 

       370        380        390        400        410        420 
LLGLDPTQLT DALTQRSMFL RGEEILTPLN VQQAVDSRDS LAMALYACCF EWVIKKINSR 

       430        440        450        460        470        480 
IKGNEDFKSI GILDIFGFEN FEVNHFEQFN INYANEKLQE YFNKHIFSLE QLEYSREGLV 

       490        500        510        520        530        540 
WEDIDWIDNG ECLDLIEKKL GLLALINEES HFPQATDSTL LEKLHSQHAN NHFYVKPRVA 

       550        560        570        580        590        600 
VNNFGVKHYA GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL 

       610        620        630        640        650        660 
KCGSKHRRPT VSSQFKDSLH SLMATLSSSN PFFVRCIKPN MQKMPDQFDQ AVVLNQLRYS 

       670        680        690        700        710        720 
GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNLALPEDVR GKCTSLLQLY DASNSEWQLG 

       730        740        750        760        770        780 
KTKVFLRESL EQKLEKRREE EVSHAAMVIR AHVLGFLARK QYRKVLYCVV IIQKNYRAFL 

       790        800        810        820        830        840 
LRRRFLHLKK AAIVFQKQLR GQIARRVYRQ LLAEKREQEE KKKQEEEEKK KREEEERERE 

       850        860        870        880        890        900 
RERREAELRA QQEEETRKQQ ELEALQKSQK EAELTRELEK QKENKQVEEI LRLEKEIEDL 

       910        920        930        940        950        960 
QRMKEQQELS LTEASLQKLQ ERRDQELRRL EEEACRAAQE FLESLNFDEI DECVRNIERS 

       970        980        990       1000       1010       1020 
LSVGSEFSSE LAESACEEKP NFNFSQPYPE EEVDEGFEAD DDAFKDSPNP SEHGHSDQRT 

      1030       1040       1050       1060       1070       1080 
SGIRTSDDSS EEDPYMNDTV VPTSPSADST VLLAPSVQDS GSLHNSSSGE STYCMPQNAG 

      1090       1100       1110       1120       1130       1140 
DLPSPDGDYD YDQDDYEDGA ITSGSSVTFS NSYGSQWSPD YRCSVGTYNS SGAYRFSSEG 

      1150       1160       1170       1180       1190       1200 
AQSSFEDSEE DFDSRFDTDD ELSYRRDSVY SCVTLPYFHS FLYMKGGLMN SWKRRWCVLK 

      1210       1220       1230       1240       1250       1260 
DETFLWFRSK QEALKQGWLH KKGGGSSTLS RRNWKKRWFV LRQSKLMYFE NDSEEKLKGT 

      1270       1280       1290       1300       1310       1320 
VEVRTAKEII DNTTKENGID IIMADRTFHL IAESPEDASQ WFSVLSQVHA STDQEIQEMH 

      1330       1340       1350       1360       1370       1380 
DEQANPQNAV GTLDVGLIDS VCASDSPDRP NSFVIITANR VLHCNADTPE EMHHWITLLQ 

      1390       1400       1410       1420       1430       1440 
RSKGDTRVEG QEFIVRGWLH KEVKNSPKMS SLKLKKRWFV LTHNSLDYYK SSEKNALKLG 

      1450       1460       1470       1480       1490       1500 
TLVLNSLCSV VPPDEKIFKE TGYWNVTVYG RKHCYRLYTK LLNEATRWSS AIQNVTDTKA 

      1510       1520       1530       1540       1550       1560 
PIDTPTQQLI QDIKENCLNS DVVEQIYKRN PILRYTHHPL HSPLLPLPYG DINLNLLKDK 

      1570       1580       1590       1600       1610       1620 
GYTTLQDEAI KIFNSLQQLE SMSDPIPIIQ GILQTGHDLR PLRDELYCQL IKQTNKVPHP 

      1630       1640       1650       1660       1670       1680 
GSVGNLYSWQ ILTCLSCTFL PSRGILKYLK FHLKRIREQF PGSEMEKYAL FTYESLKKTK 

      1690       1700       1710       1720       1730       1740 
CREFVPSRDE IEALIHRQEM TSTVYCHGGG SCKITINSHT TAGEVVEKLI RGLAMEDSRN 

      1750       1760       1770       1780       1790       1800 
MFALFEYNGH VDKAIESRTV VADVLAKFEK LAATSEVGDL PWKFYFKLYC FLDTDNVPKD 

      1810       1820       1830       1840       1850       1860 
SVEFAFMFEQ AHEAVIHGHH PAPEENLQVL AALRLQYLQG DYTLHAAIPP LEEVYSLQRL 

      1870       1880       1890       1900       1910       1920 
KARISQSTKT FTPCERLEKR RTSFLEGTLR RSFRTGSVVR QKVEEEQMLD MWIKEEVSSA 

      1930       1940       1950       1960       1970       1980 
RASIIDKWRK FQGMNQEQAM AKYMALIKEW PGYGSTLFDV ECKEGGFPQE LWLGVSADAV 

      1990       2000       2010       2020       2030       2040 
SVYKRGEGRP LEVFQYEHIL SFGAPLANTY KIVVDERELL FETSEVVDVA KLMKAYISMI 

      2050 
VKKRYSTTRS ASSQGSSR 

« Hide

References

« Hide 'large scale' references
[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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS TRP-324 AND THR-1663.
[2]"Identification of myosin X as a specific binding partner for the tumor sensative calmodulin-like protein."
Rogers M.S., Strehler E.E.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TYR-148 AND THR-1663.
[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], 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], 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 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], VARIANT THR-1663.
Tissue: Brain.
[7]"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.
Tissue: Skeletal muscle.
[8]"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.
[9]"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.
[10]"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.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
BC137168 mRNA. Translation: AAI37169.1.
BC150285 mRNA. Translation: AAI50286.1.
AF184153 mRNA. Translation: AAF17363.1.
PIRA59267.
RefSeqNP_036466.2. NM_012334.2.
UniGeneHs.481720.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LW9NMR-A/B883-933[»]
3AU4X-ray1.90A1486-2058[»]
3AU5X-ray2.55A/B1486-2058[»]
3PZDX-ray2.50A1503-2047[»]
ProteinModelPortalQ9HD67.
SMRQ9HD67. Positions 4-940, 1176-1383, 1415-1495, 1501-2046.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110735. 8 interactions.
DIPDIP-46151N.
IntActQ9HD67. 11 interactions.
MINTMINT-1411122.
STRING9606.ENSP00000391106.

PTM databases

PhosphoSiteQ9HD67.

Polymorphism databases

DMDM205371854.

Proteomic databases

PaxDbQ9HD67.
PRIDEQ9HD67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000513610; ENSP00000421280; ENSG00000145555.
GeneID4651.
KEGGhsa:4651.
UCSCuc003jft.4. human.

Organism-specific databases

CTD4651.
GeneCardsGC05M016718.
H-InvDBHIX0021772.
HIX0164320.
HGNCHGNC:7593. MYO10.
HPACAB015224.
HPA024223.
MIM601481. gene.
neXtProtNX_Q9HD67.
PharmGKBPA31394.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOGENOMHOG000007044.
HOVERGENHBG052553.
InParanoidQ9HD67.
KOK12559.
OMADKGYTTL.
OrthoDBEOG7Q5HC9.
PhylomeDBQ9HD67.
TreeFamTF316834.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9HD67.
BgeeQ9HD67.
CleanExHS_MYO10.
GenevestigatorQ9HD67.

Family and domain databases

Gene3D1.20.80.10. 2 hits.
2.30.29.30. 4 hits.
InterProIPR019749. 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.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00295. B41. 1 hit.
SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMSSF47031. SSF47031. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS50057. FERM_3. 1 hit.
PS50096. IQ. 2 hits.
PS51016. MYTH4. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO10. human.
EvolutionaryTraceQ9HD67.
GeneWikiMYO10.
GenomeRNAi4651.
NextBio17932.
PROQ9HD67.
SOURCESearch...

Entry information

Entry nameMYO10_HUMAN
AccessionPrimary (citable) accession number: Q9HD67
Secondary accession number(s): A7E2D1 expand/collapse secondary AC list , O94893, Q9NYM7, Q9P110, Q9P111, Q9UHF6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM