Q9HD67 (MYO10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-X

Alternative name(s):
Unconventional myosin-10

Gene names

Name:	MYO10
Synonyms:	KIAA0799

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2058 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.12
Subcellular location	Cytoplasm › cytosol. Cell projection › lamellipodium. Cell projection › ruffle. Cytoplasm › cytoskeleton. Cell projection › filopodium tip. Cytoplasm › cell cortex. Cell projection › filopodium 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 a 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 process	Transport
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 positive regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara 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_component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell 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: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2058

2058

Unconventional myosin-X

PRO_0000123473

Regions

Domain

1 – 727

727

Myosin head-like

Domain

742 – 763

22

IQ 1

Domain

764 – 787

24

IQ 2

Domain

788 – 817

30

IQ 3

Domain

1212 – 1310

99

PH 1

Domain

1392 – 1497

106

PH 2

Domain

1547 – 1695

149

MyTH4

Domain

1700 – 2044

345

FERM

Coiled coil

799 – 943

145

Potential

Amino acid modifications

Modified residue

965

1

Phosphoserine Ref.8

Natural variations

Natural variant

32

1

V → I.
Corresponds to variant rs17707947 [ dbSNP | Ensembl ].

VAR_046328

Natural variant

148

1

H → Y. Ref.2
Corresponds to variant rs7737765 [ dbSNP | Ensembl ].

VAR_061366

Natural variant

273

1

E → D.
Corresponds to variant rs6870170 [ dbSNP | Ensembl ].

VAR_046329

Natural variant

324

1

R → W. Ref.1 Ref.3
Corresponds to variant rs11750538 [ dbSNP | Ensembl ].

VAR_046330

Natural variant

700

1

R → Q.
Corresponds to variant rs26740 [ dbSNP | Ensembl ].

VAR_046331

Natural variant

1663

1

S → T. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs25901 [ dbSNP | Ensembl ].

VAR_046332

Experimental info

Mutagenesis

1647

1

K → D: Abolishes interaction with tubulin; when associated with D-1650. Ref.11 Ref.12

Mutagenesis

1650

1

K → D: Abolishes interaction with tubulin; when associated with D-1647. Ref.11 Ref.12

Mutagenesis

1718 – 1719

2

SH → AA: Almost abolishes interaction with DCC. Ref.12

Mutagenesis

2002

1

F → K: Abolishes interaction with DCC. Ref.11 Ref.12

Sequence conflict

98

1

S → P in AAF36524. Ref.3

Sequence conflict

256

1

G → W in AAF68025. Ref.1

Sequence conflict

1186

1

G → C in AAF36524. Ref.3

Secondary structure

1

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2058

Helix Strand Turn

Details...

Helix

885 – 911

27

Helix

915 – 926

12

Helix

1505 – 1514

10

Turn

1515 – 1518

4

Helix

1520 – 1529

10

Helix

1531 – 1533

3

Helix

1554 – 1559

6

Helix

1565 – 1578

14

Helix

1586 – 1598

13

Helix

1602 – 1613

12

Helix

1623 – 1636

14

Helix

1643 – 1659

17

Helix

1664 – 1676

13

Helix

1688 – 1695

8

Beta strand

1700 – 1706

7

Turn

1707 – 1709

3

Beta strand

1711 – 1716

6

Helix

1722 – 1732

11

Beta strand

1740 – 1750

11

Beta strand

1752 – 1754

3

Helix

1761 – 1771

11

Beta strand

1783 – 1790

8

Beta strand

1794 – 1797

4

Helix

1802 – 1816

15

Helix

1824 – 1839

16

Helix

1851 – 1853

3

Helix

1858 – 1866

9

Helix

1906 – 1912

7

Helix

1914 – 1929

16

Turn

1930 – 1933

4

Helix

1936 – 1947

12

Turn

1951 – 1954

4

Beta strand

1956 – 1967

12

Beta strand

1969 – 1975

7

Beta strand

1977 – 1984

8

Beta strand

1991 – 1995

5

Helix

1996 – 1998

3

Beta strand

1999 – 2006

8

Beta strand

2009 – 2014

6

Beta strand

2017 – 2022

6

Helix

2026 – 2044

19

Sequences

	Sequence		Length	Mass (Da)
	Q9HD67 [UniParc]. Last modified September 2, 2008. Version 3. Checksum: 269C9E6566BD6D0B	FASTA	2,058	237,347
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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]	"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.
[12]	"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.

IPI

IPI01018912.

PIR

A59267.

RefSeq

NP_036466.2. NM_012334.2.

UniGene

Hs.481720.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9HD67.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46151N.

IntAct

Q9HD67. 5 interactions.

MINT

MINT-1411122.

STRING

9606.ENSP00000391106.

PTM databases

PhosphoSite

Q9HD67.

Polymorphism databases

DMDM

205371854.

Proteomic databases

PaxDb

Q9HD67.

PRIDE

Q9HD67.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000513610; ENSP00000421280; ENSG00000145555.

GeneID

4651.

KEGG

hsa:4651.

UCSC

uc003jft.4. human.

Organism-specific databases

CTD

4651.

GeneCards

GC05M016718.

H-InvDB

HIX0021772.
HIX0164320.

HGNC

HGNC:7593. MYO10.

HPA

CAB015224.
HPA024223.

MIM

601481. gene.

neXtProt

NX_Q9HD67.

PharmGKB

PA31394.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5022.

HOGENOM

HOG000007044.

HOVERGEN

HBG052553.

InParanoid

Q9HD67.

KO

K12559.

OMA

DKGYTTL.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q9HD67.

Bgee

Q9HD67.

CleanEx

HS_MYO10.

Genevestigator

Q9HD67.

GermOnline

ENSG00000145555. Homo sapiens.

Family and domain databases

Gene3D

1.20.80.10. 2 hits.
2.30.29.30. 4 hits.

InterPro

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.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

Pfam

PF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00295. B41. 1 hit.
SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF52540. SSF52540. 1 hit.

PROSITE

PS00660. FERM_1. False negative.
PS00661. FERM_2. False negative.
PS50057. FERM_3. 1 hit.
PS50096. IQ. 2 hits.
PS51016. MYTH4. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MYO10. human.

EvolutionaryTrace

Q9HD67.

GenomeRNAi

4651.

NextBio

17932.

SOURCE

Search...

Entry information

Entry name

MYO10_HUMAN

Accession

Primary (citable) accession number: Q9HD67
Secondary accession number(s): A7E2D1 , O94893, Q9NYM7, Q9P110, Q9P111, Q9UHF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	September 2, 2008
Last modified:	May 29, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.