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Q9WTI7 (MYO1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-Ic
Alternative name(s):
Myosin I beta
Short name=MMI-beta
Short name=MMIb
Gene names
Name:Myo1c
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1063 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. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.22

Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.22

Subunit structure

Interacts (via its IQ motifs) with CALM; this precludes interaction with YWHAB. Interacts with YWHAB; this precludes interaction with CALM. Interacts with RPS6 By similarity. Interacts with actin filaments. Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent. Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and CALM. Interacts with POLR1A and POLR2A. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with GLUT4. Ref.2 Ref.14 Ref.16 Ref.17 Ref.21 Ref.22

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionstereocilium membrane. Cytoplasmic vesicle. Cell projectionruffle. Note: Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 at actin-based membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm. Ref.2 Ref.11 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22

Isoform 3: Nucleusnucleolus. Nucleusnucleoplasm By similarity. Nucleusnuclear pore complex By similarity. Note: In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles. Colocalizes with RPS6 at the nuclear pore level By similarity. Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli. Ref.2 Ref.11 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22

Tissue specificity

Isoform 3 is expressed in small intestine, pancreas, brain, kidney, skin, heart muscle, testis, striated muscle, spleen, liver and lung (at protein level). Expressed in brain, testis, adrenal glands, thymus, spleen, kidney, lung, heart, cochlea and vestibule. Expressed in sensory hair cells of the inner ear. Expressed in adipocytes. Ref.7 Ref.11 Ref.15 Ref.20

Induction

Up-regulated by serum. Ref.20

Domain

Binds directly to large unilamellar vesicles (LUVs) containing phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site corresponds to a putative PH domain present in its tail domain.

Post-translational modification

Isoform 2 contains a N-acetylmethionine at position 1 By similarity.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 2 IQ domains.

Contains 1 myosin motor domain.

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell migration by vascular endothelial growth factor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein targeting to membrane

Inferred from electronic annotation. Source: Ensembl

positive regulation of vascular endothelial growth factor signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein targeting to membrane

Inferred from electronic annotation. Source: Ensembl

regulation of tight junction assembly

Inferred from electronic annotation. Source: Ensembl

transport

Inferred from direct assay Ref.11. Source: MGI

   Cellular_componentbasal plasma membrane

Inferred from electronic annotation. Source: Ensembl

brush border

Inferred from direct assay PubMed 15758024. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

filamentous actin

Inferred from electronic annotation. Source: Ensembl

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Traceable author statement Ref.14. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

myosin I complex

Inferred from direct assay Ref.11. Source: MGI

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

stereocilium

Inferred from direct assay PubMed 17050716. Source: MGI

stereocilium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Non-traceable author statement Ref.14. Source: UniProtKB

actin binding

Non-traceable author statement Ref.14. Source: UniProtKB

calmodulin binding

Non-traceable author statement Ref.14. Source: UniProtKB

motor activity

Inferred from electronic annotation. Source: InterPro

phospholipid binding

Traceable author statement Ref.14. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Plekhb1Q9QYE9-14EBI-777558,EBI-1127141
Plekhb1Q9QYE9-22EBI-777558,EBI-1127145

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WTI7-1)

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.
Note: Gene prediction based on EST data.
Isoform 2 (identifier: Q9WTI7-2)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.
Note: Contains a N-acetylmethionine at position 1 (By similarity).
Isoform 3 (identifier: Q9WTI7-3)

Also known as: Nuclear myosin 1; NM1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MALQVELIPTGEIIRVVHPHRPCKL → MRYRAS
Isoform 4 (identifier: Q9WTI7-4)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     932-1063: GYKPRPRQLL...AVVAPRLNSR → VTSLAPGSCCSRPVLWSLWRMLKSSRELIMPT
Note: No experimental confirmation available. May be due to a frameshift.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10631063Unconventional myosin-Ic
PRO_0000123446

Regions

Domain47 – 731685Myosin motor
Domain734 – 75724IQ 1
Domain758 – 78629IQ 2
Nucleotide binding139 – 14810ATP By similarity
Nucleotide binding192 – 1965ATP By similarity
Region927 – 93812PIP2-binding motif

Sites

Binding site881ATP By similarity
Binding site961ATP By similarity

Amino acid modifications

Modified residue3831N6-methyllysine By similarity
Modified residue4081Phosphoserine By similarity
Modified residue4861N6-acetyllysine Ref.23

Natural variations

Alternative sequence1 – 3535Missing in isoform 2.
VSP_036863
Alternative sequence1 – 2525MALQV…RPCKL → MRYRAS in isoform 3.
VSP_036864
Alternative sequence932 – 1063132GYKPR…RLNSR → VTSLAPGSCCSRPVLWSLWR MLKSSRELIMPT in isoform 4.
VSP_003350

Experimental info

Mutagenesis9271K → A: Inhibits binding to PIP2 and disrupts membrane binding. Ref.18
Mutagenesis9381R → A: Inhibits binding to PIP2 and disrupts membrane binding. Ref.18
Sequence conflict69 – 702RR → GG in CAA67956. Ref.7
Sequence conflict97 – 993SRQ → RRK in CAA67956. Ref.7
Sequence conflict1021E → G in BAE33311. Ref.3
Sequence conflict1071V → I in BAE33311. Ref.3
Sequence conflict2511T → A Ref.9
Sequence conflict2721C → F Ref.9
Sequence conflict286 – 2872VM → LL Ref.9
Sequence conflict3881R → A Ref.9
Sequence conflict401 – 4033LAS → VPA Ref.9
Sequence conflict4461Q → R Ref.9
Sequence conflict517 – 5193VKP → IKH Ref.9
Sequence conflict5781M → T Ref.9
Sequence conflict6071S → G Ref.9
Sequence conflict7351Q → R in CAA67956. Ref.7
Sequence conflict8211R → G in CAA67956. Ref.7
Sequence conflict8421E → D in CAA67956. Ref.7
Sequence conflict10241T → A in BAE33311. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 2.
Checksum: 494A31B8634A1AF9

FASTA1,063121,944
        10         20         30         40         50         60 
MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE 

        70         80         90        100        110        120 
AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA 

       130        140        150        160        170        180 
DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV 

       190        200        210        220        230        240 
LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF 

       250        260        270        280        290        300 
YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE 

       310        320        330        340        350        360 
VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR EALTHRKIIA 

       370        380        390        400        410        420 
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS LASKDAESPS WRSTTVLGLL 

       430        440        450        460        470        480 
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC 

       490        500        510        520        530        540 
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG 

       550        560        570        580        590        600 
EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV 

       610        620        630        640        650        660 
ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG LMENLRVRRA 

       670        680        690        700        710        720 
GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP 

       730        740        750        760        770        780 
KTLFATEDSL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR 

       790        800        810        820        830        840 
KWAAQTIRRL IRGFILRHSP RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL 

       850        860        870        880        890        900 
REASELLREL CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 

       910        920        930        940        950        960 
LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KGYKPRPRQL LLTPSAVVIV EDAKVKQRID 

       970        980        990       1000       1010       1020 
YANLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI ETLTKTALSA DRVNNININQ 

      1030       1040       1050       1060 
GSITFAGGPG RDGIIDFTSG SELLITKAKN GHLAVVAPRL NSR 

« Hide

Isoform 2 (A) [UniParc].

Checksum: 2CF5535D816884DF
Show »

FASTA1,028118,156
Isoform 3 (Nuclear myosin 1) (NM1) [UniParc].

Checksum: CDAB0FF699D041C9
Show »

FASTA1,044119,877
Isoform 4 (B) [UniParc].

Checksum: C8CEFAE7FADE5B41
Show »

FASTA963111,290

References

« Hide 'large scale' references
[1]"The vibrator mutation causes neurodegeneration via reduced expression of PITP alpha: positional complementation cloning and extragenic suppression."
Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T., van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L., Hawkins T.L., Rubin E.M., Lander E.S.
Neuron 18:711-722(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 4).
Strain: DBA/2J.
Tissue: Brain.
[2]"A myosin I isoform in the nucleus."
Pestic-Dragovich L., Stojiljkovic L., Philimonenko A.A., Nowak G., Ke Y., Settlage R.E., Shabanowitz J., Hunt D.F., Hozak P., de Lanerolle P.
Science 290:337-341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH POLR2A, SUBCELLULAR LOCATION.
Tissue: Embryo.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Lung.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 2).
Strain: FVB/N.
Tissue: Mammary gland.
[7]"Cloning of the genes encoding two murine and human cochlear unconventional type I myosins."
Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P., Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D., Pujol R., Petit C.
Genomics 40:332-341(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-842 (ISOFORM 2), TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Cochlea.
[8]Gerhard D.S.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-34 (ISOFORM 1).
Tissue: Placenta.
[9]"Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family."
Sherr E.H., Joyce M.P., Greene L.A.
J. Cell Biol. 120:1405-1416(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-628 (ISOFORM 1/2/3/4).
[10]"A chemical-genetic strategy implicates myosin-1c in adaptation by hair cells."
Holt J.R., Gillespie S.K., Provance D.W., Shah K., Shokat K.M., Corey D.P., Mercer J.A., Gillespie P.G.
Cell 108:371-381(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c."
Bose A., Guilherme A., Robida S.I., Nicoloro S.M., Zhou Q.L., Jiang Z.Y., Pomerleau D.P., Czech M.P.
Nature 420:821-824(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"Myo1c is designed for the adaptation response in the inner ear."
Batters C., Arthur C.P., Lin A., Porter J., Geeves M.A., Milligan R.A., Molloy J.E., Coluccio L.M.
EMBO J. 23:1433-1440(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"An actin-myosin complex on actively transcribing genes."
Fomproix N., Percipalle P.
Exp. Cell Res. 294:140-148(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"PHR1, an integral membrane protein of the inner ear sensory cells, directly interacts with myosin 1c and myosin VIIa."
Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., Pezeron G., Michalski N., Daviet L., Hardelin J.-P., Legrain P., Petit C.
J. Cell Sci. 118:2891-2899(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEKHB1.
[15]"Fast adaptation in vestibular hair cells requires myosin-1c activity."
Stauffer E.A., Scarborough J.D., Hirono M., Miller E.D., Shah K., Mercer J.A., Holt J.R., Gillespie P.G.
Neuron 47:541-553(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[16]"The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription."
Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.
EMBO Rep. 7:525-530(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAZ1B, POLR1A AND SMARCA5, SUBCELLULAR LOCATION.
[17]"Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II."
Hofmann W.A., Vargas G.M., Ramchandran R., Stojiljkovic L., Goodrich J.A., de Lanerolle P.
J. Cell. Biochem. 99:1001-1009(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POLR2A.
[18]"Myo1c binds phosphoinositides through a putative pleckstrin homology domain."
Hokanson D.E., Laakso J.M., Lin T., Sept D., Ostap E.M.
Mol. Biol. Cell 17:4856-4865(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-927 AND ARG-938.
[19]"Myo1c binds tightly and specifically to phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate."
Hokanson D.E., Ostap E.M.
Proc. Natl. Acad. Sci. U.S.A. 103:3118-3123(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]"Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates."
Kahle M., Pridalova J., Spacek M., Dzijak R., Hozak P.
Histochem. Cell Biol. 127:139-148(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[21]"CIB1 and CaBP1 bind to the myo1c regulatory domain."
Tang N., Lin T., Yang J., Foskett J.K., Ostap E.M.
J. Muscle Res. Cell Motil. 28:285-291(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1 AND CIB1, SUBCELLULAR LOCATION.
[22]"Myo1c binding to submembrane actin mediates insulin-induced tethering of GLUT4 vesicles."
Boguslavsky S., Chiu T., Foley K.P., Osorio-Fuentealba C., Antonescu C.N., Bayer K.U., Bilan P.J., Klip A.
Mol. Biol. Cell 23:4065-4078(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLUT4, ACTIN-BINDING.
[23]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96723 mRNA. Translation: AAC53264.1.
U96726 Genomic DNA. Translation: AAC60758.1.
AY007255 mRNA. Translation: AAG02570.1.
AK004743 mRNA. Translation: BAB23524.1.
AK154294 mRNA. Translation: BAE32495.1.
AK155530 mRNA. Translation: BAE33311.1.
AK171107 mRNA. Translation: BAE42253.1.
AL591440 Genomic DNA. Translation: CAI24085.1.
AL591440 Genomic DNA. Translation: CAI24086.2.
AL591440 Genomic DNA. Translation: CAI24088.2.
CH466596 Genomic DNA. Translation: EDL12832.1.
CH466596 Genomic DNA. Translation: EDL12833.1.
BC021481 mRNA. Translation: AAH21481.1.
X99638 mRNA. Translation: CAA67956.1.
CF615767 mRNA. No translation available.
CCDSCCDS25054.1. [Q9WTI7-2]
CCDS36228.1. [Q9WTI7-3]
PIRB45438.
H75634.
RefSeqNP_001074243.1. NM_001080774.1. [Q9WTI7-2]
NP_001074244.1. NM_001080775.1. [Q9WTI7-3]
NP_032685.1. NM_008659.3. [Q9WTI7-2]
XP_006532492.1. XM_006532429.1. [Q9WTI7-1]
UniGeneMm.234502.

3D structure databases

ProteinModelPortalQ9WTI7.
SMRQ9WTI7. Positions 44-755, 772-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201664. 4 interactions.
IntActQ9WTI7. 9 interactions.
MINTMINT-4129061.

PTM databases

PhosphoSiteQ9WTI7.

Proteomic databases

MaxQBQ9WTI7.
PaxDbQ9WTI7.
PRIDEQ9WTI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069057; ENSMUSP00000070388; ENSMUSG00000017774. [Q9WTI7-2]
ENSMUST00000102504; ENSMUSP00000099562; ENSMUSG00000017774. [Q9WTI7-2]
ENSMUST00000102505; ENSMUSP00000099563; ENSMUSG00000017774. [Q9WTI7-1]
ENSMUST00000108431; ENSMUSP00000104069; ENSMUSG00000017774. [Q9WTI7-3]
GeneID17913.
KEGGmmu:17913.
UCSCuc007kem.1. mouse. [Q9WTI7-1]
uc007keo.1. mouse. [Q9WTI7-3]

Organism-specific databases

CTD4641.
MGIMGI:106612. Myo1c.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00750000117217.
HOVERGENHBG062373.
InParanoidQ3U231.
KOK10356.
OMAYAETCPA.
OrthoDBEOG7V49XQ.
PhylomeDBQ9WTI7.
TreeFamTF312960.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_209837. Membrane Trafficking.

Gene expression databases

ArrayExpressQ9WTI7.
BgeeQ9WTI7.
CleanExMM_MYO1C.
GenevestigatorQ9WTI7.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_tail_2.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00612. IQ. 2 hits.
PF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 2 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO1C. mouse.
NextBio292757.
PROQ9WTI7.
SOURCESearch...

Entry information

Entry nameMYO1C_MOUSE
AccessionPrimary (citable) accession number: Q9WTI7
Secondary accession number(s): O08571 expand/collapse secondary AC list , O08834, Q3TBQ4, Q3U231, Q5ND46, Q5ND48, Q5ND49, Q9ERB6, Q9QW54
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot