Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UM54 (MYO6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-VI
Alternative name(s):
Unconventional myosin-6
Gene names
Name:MYO6
Synonyms:KIAA0389
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1294 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. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells By similarity. Ref.9 Ref.10 Ref.14 Ref.15

Subunit structure

Homodimer. Binding to calmodulin through a unique insert, not found in other myosins, located in the neck region between the motor domain and the IQ domain appears to contribute to the directionality reversal. This interaction occurs only if the C-terminal lobe of calmodulin is occupied by calcium. Interaction with F-actin/ACTN1 occurs only at the apical brush border domain of the proximal tubule cells By similarity. Interacts with DAB2. In vitro, the C-terminal globular tail binds a C-terminal region of DAB2. Interacts with CFTR. Forms a complex with CFTR and DAB2 in the apical membrane of epithelial cells. Interacts with OPTN By similarity. Ref.11 Ref.12 Ref.13

Subcellular location

Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein. Golgi apparatus By similarity. Nucleus. Cytoplasmperinuclear region. Membraneclathrin-coated pit. Cell projectionruffle membrane; Peripheral membrane protein. Note: Also present in endocyctic vesicles, and membrane ruffles. Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with DAB2 in clathrin-coated pits/vesicles. Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane By similarity. Ref.10 Ref.15

Isoform 3: Cytoplasmic vesicleclathrin-coated vesicle membrane.

Isoform 4: Cytoplasmic vesicleclathrin-coated vesicle membrane. Cell projectionruffle membrane Ref.10 Ref.15.

Tissue specificity

Expressed in most tissues examined including heart, brain, placenta, pancreas, spleen, thymus, prostate, testis, ovary, small intestine and colon. Highest levels in brain, pancreas, testis and small intestine. Also expressed in fetal brain and cochlea. Isoform 1 and isoform 2, containing the small insert, and isoform 4, containing neither insert, are expressed in unpolarized epithelial cells. Ref.1

Domain

Divided into three regions: a N-terminal motor (head) domain, followed by a neck domain consisting of a calmodulin-binding linker domain and a single IQ motif, and a C-terminal tail region with a coiled-coil and a unique globular domain required for interaction with other proteins.

Post-translational modification

Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK) By similarity.

Involvement in disease

Deafness, autosomal dominant, 22 (DFNA22) [MIM:606346]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA22 is progressive and postlingual, with onset during childhood. By the age of approximately 50 years, affected individuals invariably have profound sensorineural deafness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Deafness, autosomal recessive, 37 (DFNB37) [MIM:607821]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Deafness, sensorineural, with hypertrophic cardiomyopathy (DFNHCM) [MIM:606346]: An autosomal dominant sensorineural deafness associated with hypertrophic cardiomyopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-6 (MYH6).

Sequence caution

The sequence BAA20843.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processEndocytosis
Hearing
Protein transport
Transport
   Cellular componentCell membrane
Cell projection
Coated pit
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Disease mutation
Non-syndromic deafness
   DomainCoiled coil
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from direct assay Ref.15. Source: UniProtKB

actin filament-based movement

Inferred from sequence or structural similarity. Source: UniProtKB

auditory receptor cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

dendrite development

Inferred from electronic annotation. Source: Ensembl

endocytosis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

glutamate secretion

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

membrane organization

Traceable author statement. Source: Reactome

metabolic process

Inferred from sequence or structural similarity. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.14. Source: UniProtKB

protein targeting

Inferred from electronic annotation. Source: Ensembl

regulation of secretion

Inferred from mutant phenotype PubMed 15837803. Source: UniProtKB

regulation of synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: UniProtKB-KW

synapse assembly

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase II, holoenzyme

Inferred from direct assay Ref.14. Source: UniProtKB

Golgi apparatus

Inferred from direct assay Ref.15. Source: UniProtKB

apical part of cell

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

clathrin-coated vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.15Ref.14PubMed 9852149. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from direct assay Ref.15. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

filamentous actin

Inferred from direct assay PubMed 9852149. Source: UniProtKB

lysosomal membrane

Traceable author statement. Source: Reactome

microvillus

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from direct assay Ref.15. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 16948370. Source: UniProtKB

nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 9852149. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

ruffle

Inferred from direct assay Ref.15PubMed 9852149. Source: UniProtKB

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

unconventional myosin complex

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionADP binding

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin binding

Traceable author statement Ref.9. Source: UniProtKB

actin filament binding

Inferred from direct assay PubMed 9852149. Source: UniProtKB

calmodulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

minus-end directed microfilament motor activity

Non-traceable author statement Ref.9. Source: UniProtKB

motor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DAB2P980823EBI-350606,EBI-1171238
Dab2P980784EBI-350606,EBI-1391846From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q9UM54-3)

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.
Isoform 1 (identifier: Q9UM54-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1037-1045: Missing.
Isoform 2 (identifier: Q9UM54-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1037-1068: Missing.
Isoform 4 (identifier: Q9UM54-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1155: Missing.
Isoform 5 (identifier: Q9UM54-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1037-1068: Missing.
     1147-1155: Missing.
Isoform 6 (identifier: Q9UM54-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1156: DFAPFLNNSP → A

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12941294Unconventional myosin-VI
PRO_0000123464

Regions

Domain1 – 759759Myosin head-like
Domain814 – 83421IQ
Nucleotide binding151 – 1588ATP Potential
Region273 – 31745Responsible for slow ATPase activity By similarity
Region665 – 6728Actin-binding Potential
Region782 – 81029Required for binding calmodulin By similarity
Region1116 – 11183Interaction with OPTN
Coiled coil864 – 1023160 Potential
Compositional bias920 – 1027108Glu-rich

Amino acid modifications

Modified residue4051Phosphothreonine By similarity

Natural variations

Alternative sequence1037 – 106832Missing in isoform 2 and isoform 5.
VSP_007985
Alternative sequence1037 – 10459Missing in isoform 1.
VSP_022332
Alternative sequence1147 – 115610DFAPFLNNSP → A in isoform 6.
VSP_042208
Alternative sequence1147 – 11559Missing in isoform 4 and isoform 5.
VSP_022333
Natural variant2161E → V in DFNB37. Ref.18
Corresponds to variant rs28936390 [ dbSNP | Ensembl ].
VAR_016209
Natural variant2461H → R in DFNHCM. Ref.19
Corresponds to variant rs28936391 [ dbSNP | Ensembl ].
VAR_029988
Natural variant4421C → Y in DFNA22. Ref.17
VAR_012110

Experimental info

Sequence conflict11561P → A in CAI42826. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified January 9, 2007. Version 4.
Checksum: 3A8966E6864B8576

FASTA1,294149,691
        10         20         30         40         50         60 
MEDGKPVWAP HPTDGFQMGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE 

        70         80         90        100        110        120 
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSE AIKSYQGKSL 

       130        140        150        160        170        180 
GTRPPHVFAI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFVLRYLTE SYGTGQDIDD 

       190        200        210        220        230        240 
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK 

       250        260        270        280        290        300 
EERNYHIFYR LCAGASEDIR EKLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY 

       310        320        330        340        350        360 
LKAGSMKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG 

       370        380        390        400        410        420 
GCNLKNKSAQ SLEYCAELLG LDQDDLRVSL TTRVMLTTAG GTKGTVIKVP LKVEQANNAR 

       430        440        450        460        470        480 
DALAKTVYSH LFDHVVNRVN QCFPFETSSY FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL 

       490        500        510        520        530        540 
QQFFNERILK EEQELYQKEG LGVNEVHYVD NQDCIDLIEA KLVGILDILD EENRLPQPSD 

       550        560        570        580        590        600 
QHFTSAVHQK HKDHFRLTIP RKSKLAVHRN IRDDEGFIIR HFAGAVCYET TQFVEKNNDA 

       610        620        630        640        650        660 
LHMSLESLIC ESRDKFIREL FESSTNNNKD TKQKAGKLSF ISVGNKFKTQ LNLLLDKLRS 

       670        680        690        700        710        720 
TGASFIRCIK PNLKMTSHHF EGAQILSQLQ CSGMVSVLDL MQGGYPSRAS FHELYNMYKK 

       730        740        750        760        770        780 
YMPDKLARLD PRLFCKALFK ALGLNENDYK FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL 

       790        800        810        820        830        840 
VKRVNHWLTC SRWKKVQWCS LSVIKLKNKI KYRAEACIKM QKTIRMWLCK RRHKPRIDGL 

       850        860        870        880        890        900 
VKVGTLKKRL DKFNEVVSVL KDGKPEMNKQ IKNLEISIDT LMAKIKSTMM TQEQIQKEYD 

       910        920        930        940        950        960 
ALVKSSEELL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEDEKRRRKE EEERRMKLEM 

       970        980        990       1000       1010       1020 
EAKRKQEEEE RKKREDDEKR IQAEVEAQLA RQKEEESQQQ AVLEQERRDR ELALRIAQSE 

      1030       1040       1050       1060       1070       1080 
AELISDEAQA DLALRRSLDS YPVSKNDGTR PKMTPEQMAK EMSEFLSRGP AVLATKAAAG 

      1090       1100       1110       1120       1130       1140 
TKKYDLSKWK YAELRDTINT SCDIELLAAC REEFHRRLKV YHAWKSKNKK RNTETEQRAP 

      1150       1160       1170       1180       1190       1200 
KSVTDYDFAP FLNNSPQQNP AAQIPARQRE IEMNRQQRFF RIPFIRPADQ YKDPQSKKKG 

      1210       1220       1230       1240       1250       1260 
WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL EETGLTRKRG AEILPRQFEE 

      1270       1280       1290 
IWERCGGIQY LQNAIESRQA RPTYATAMLQ SLLK 

« Hide

Isoform 1 [UniParc].

Checksum: BCB4FDFE920712CD
Show »

FASTA1,285148,714
Isoform 2 [UniParc].

Checksum: CF1FA35796FC1C60
Show »

FASTA1,262146,048
Isoform 4 [UniParc].

Checksum: F68A79F74AB9170C
Show »

FASTA1,285148,685
Isoform 5 [UniParc].

Checksum: DD739BA2DD557EEF
Show »

FASTA1,253145,042
Isoform 6 [UniParc].

Checksum: EAE6008E2FAC170C
Show »

FASTA1,285148,659

References

« Hide 'large scale' references
[1]"Characterization of unconventional MYO6, the human homologue of the gene responsible for deafness in Snell's waltzer mice."
Avraham K.B., Hasson T., Sobe T., Balsara B., Testa J.R., Skvorak A.B., Morton C.C., Copeland N.G., Jenkins N.A.
Hum. Mol. Genet. 6:1225-1231(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Brain.
[2]Avraham K.B.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Genomic organization of the human myosin VI gene (MYO6), a candidate gene for neurosensory and storage disorders."
Kuehn M.H., Hageman G.S.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 5).
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
[8]"Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes."
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R. expand/collapse author list , Kanda K., Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.
Genome Res. 16:55-65(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1102-1294 (ISOFORM 6).
Tissue: Salivary gland.
[9]"Myosin VI is an actin-based motor that moves backwards."
Wells A.L., Lin A.W., Chen L.-Q., Safer D., Cain S.M., Hasson T., Carragher B.O., Milligan R.A., Sweeney H.L.
Nature 401:505-508(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis."
Buss F., Arden S.D., Lindsay M., Luzio J.P., Kendrick-Jones J.
EMBO J. 20:3676-3684(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTOSIS, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
[11]"Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton."
Morris S.M., Arden S.D., Roberts R.C., Kendrick-Jones J., Cooper J.A., Luzio J.P., Buss F.
Traffic 3:331-341(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2.
[12]"Myosin VI regulates endocytosis of the cystic fibrosis transmembrane conductance regulator."
Swiatecka-Urban A., Boyd C., Coutermarsh B., Karlson K.H., Barnaby R., Aschenbrenner L., Langford G.M., Hasson T., Stanton B.A.
J. Biol. Chem. 279:38025-38031(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CFTR.
[13]"A monomeric myosin VI with a large working stroke."
Lister I., Schmitz S., Walker M., Trinick J., Buss F., Veigel C., Kendrick-Jones J.
EMBO J. 23:1729-1738(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[14]"Nuclear myosin VI enhances RNA polymerase II-dependent transcription."
Vreugde S., Ferrai C., Miluzio A., Hauben E., Marchisio P.C., Crippa M.P., Bussi M., Biffo S.
Mol. Cell 23:749-755(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Myosin VI is a mediator of the p53-dependent cell survival pathway."
Jung E.J., Liu G., Zhou W., Chen X.
Mol. Cell. Biol. 26:2175-2186(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"MYO6, the human homologue of the gene responsible for deafness in Snell's waltzer mice, is mutated in autosomal dominant nonsyndromic hearing loss."
Melchionda S., Ahituv N., Bisceglia L., Sobe T., Glaser F., Rabionet R., Arbones M.L., Notarangelo A., Di Iorio E., Carella M., Zelante L., Estivill X., Avraham K.B., Gasparini P.
Am. J. Hum. Genet. 69:635-640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA22 TYR-442.
[18]"Mutations of MYO6 are associated with recessive deafness, DFNB37."
Ahmed Z.M., Morell R.J., Riazuddin S., Gropman A., Shaukat S., Ahmad M.M., Mohiddin S.A., Fananapazir L., Caruso R.C., Husnain T., Khan S.N., Riazuddin S., Griffith A.J., Friedman T.B., Wilcox E.R.
Am. J. Hum. Genet. 72:1315-1322(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNB37 VAL-216.
[19]"Novel association of hypertrophic cardiomyopathy, sensorineural deafness, and a mutation in unconventional myosin VI (MYO6)."
Mohiddin S.A., Ahmed Z.M., Griffith A.J., Tripodi D., Friedman T.B., Fananapazir L., Morell R.J.
J. Med. Genet. 41:309-314(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNHCM ARG-246.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90236 mRNA. Translation: AAC51654.2.
AF229111 expand/collapse EMBL AC list , AF229082, AF229083, AF229084, AF229085, AF229086, AF229087, AF229088, AF229089, AF229090, AF229091, AF229092, AF229093, AF229094, AF229095, AF229096, AF229097, AF229098, AF229099, AF229100, AF229101, AF229102, AF229103, AF229104, AF229105, AF229106, AF229107, AF229108, AF229109, AF229110 Genomic DNA. Translation: AAK00229.1.
AL109897, AL136093 Genomic DNA. Translation: CAI19520.1.
AL109897, AL136093 Genomic DNA. Translation: CAI19521.1.
AL109897, AL136093 Genomic DNA. Translation: CAI19522.1.
AL136093, AL109897 Genomic DNA. Translation: CAI42824.1.
AL136093, AL109897 Genomic DNA. Translation: CAI42825.1.
AL136093, AL109897 Genomic DNA. Translation: CAI42826.1.
AB002387 mRNA. Translation: BAA20843.2. Different initiation.
CH471051 Genomic DNA. Translation: EAW48730.1.
CH471051 Genomic DNA. Translation: EAW48731.1.
BC146764 mRNA. Translation: AAI46765.1.
BP333853 mRNA. No translation available.
RefSeqNP_004990.3. NM_004999.3.
XP_005248782.1. XM_005248725.1.
UniGeneHs.149387.

3D structure databases

ProteinModelPortalQ9UM54.
SMRQ9UM54. Positions 2-922, 1175-1277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110730. 29 interactions.
DIPDIP-33123N.
IntActQ9UM54. 15 interactions.
MINTMINT-239443.
STRING9606.ENSP00000358994.

PTM databases

PhosphoSiteQ9UM54.

Polymorphism databases

DMDM122065628.

Proteomic databases

PaxDbQ9UM54.
PRIDEQ9UM54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369977; ENSP00000358994; ENSG00000196586. [Q9UM54-1]
ENST00000369985; ENSP00000359002; ENSG00000196586. [Q9UM54-2]
GeneID4646.
KEGGhsa:4646.
UCSCuc003pig.1. human. [Q9UM54-5]
uc003pih.1. human. [Q9UM54-1]
uc003pii.1. human. [Q9UM54-2]

Organism-specific databases

CTD4646.
GeneCardsGC06P076515.
HGNCHGNC:7605. MYO6.
HPACAB010762.
MIM600970. gene.
606346. phenotype.
607821. phenotype.
neXtProtNX_Q9UM54.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
228012. Progressive sensorineural hearing loss - hypertrophic cardiomyopathy.
PharmGKBPA31410.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5022.
HOVERGENHBG003523.
InParanoidQ9UM54.
KOK10358.
OrthoDBEOG7TQTZZ.
PhylomeDBQ9UM54.
TreeFamTF351449.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ9UM54.
BgeeQ9UM54.
CleanExHS_MYO6.
GenevestigatorQ9UM54.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSMYO6. human.
GeneWikiMYO6.
GenomeRNAi4646.
NextBio17908.
PROQ9UM54.
SOURCESearch...

Entry information

Entry nameMYO6_HUMAN
AccessionPrimary (citable) accession number: Q9UM54
Secondary accession number(s): A6H8V4 expand/collapse secondary AC list , E1P540, Q5TEM5, Q5TEM6, Q5TEM7, Q9BZZ7, Q9UEG2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 143 of the entry and version 4 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM