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Q9WTI7

- MYO1C_MOUSE

UniProt

Q9WTI7 - MYO1C_MOUSE

Protein

Unconventional myosin-Ic

Gene

Myo1c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    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.
    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei88 – 881ATPBy similarity
    Binding sitei96 – 961ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi139 – 14810ATPBy similarity
    Nucleotide bindingi192 – 1965ATPBy similarity

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. ATP binding Source: UniProtKB
    3. calmodulin binding Source: UniProtKB
    4. motor activity Source: InterPro
    5. phospholipid binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. mRNA transport Source: UniProtKB-KW
    2. positive regulation of cell migration by vascular endothelial growth factor signaling pathway Source: Ensembl
    3. positive regulation of protein targeting to membrane Source: Ensembl
    4. positive regulation of vascular endothelial growth factor signaling pathway Source: Ensembl
    5. protein targeting to membrane Source: Ensembl
    6. regulation of tight junction assembly Source: Ensembl
    7. transport Source: MGI

    Keywords - Molecular functioni

    Motor protein, Myosin

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport

    Keywords - Ligandi

    Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unconventional myosin-Ic
    Alternative name(s):
    Myosin I beta
    Short name:
    MMI-beta
    Short name:
    MMIb
    Gene namesi
    Name:Myo1c
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:106612. Myo1c.

    Subcellular locationi

    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.
    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.By similarity

    GO - Cellular componenti

    1. basal plasma membrane Source: Ensembl
    2. brush border Source: MGI
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: Ensembl
    6. filamentous actin Source: Ensembl
    7. lateral plasma membrane Source: Ensembl
    8. membrane Source: UniProtKB
    9. membrane raft Source: Ensembl
    10. myosin I complex Source: MGI
    11. nuclear pore Source: UniProtKB-SubCell
    12. nucleolus Source: UniProtKB-SubCell
    13. nucleoplasm Source: UniProtKB-SubCell
    14. ruffle Source: UniProtKB-SubCell
    15. stereocilium Source: MGI
    16. stereocilium membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi927 – 9271K → A: Inhibits binding to PIP2 and disrupts membrane binding. 1 Publication
    Mutagenesisi938 – 9381R → A: Inhibits binding to PIP2 and disrupts membrane binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10631063Unconventional myosin-IcPRO_0000123446Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei383 – 3831N6-methyllysineBy similarity
    Modified residuei408 – 4081PhosphoserineBy similarity
    Modified residuei486 – 4861N6-acetyllysine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9WTI7.
    PaxDbiQ9WTI7.
    PRIDEiQ9WTI7.

    PTM databases

    PhosphoSiteiQ9WTI7.

    Expressioni

    Tissue specificityi

    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.4 Publications

    Inductioni

    Up-regulated by serum.1 Publication

    Gene expression databases

    ArrayExpressiQ9WTI7.
    BgeeiQ9WTI7.
    CleanExiMM_MYO1C.
    GenevestigatoriQ9WTI7.

    Interactioni

    Subunit structurei

    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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Plekhb1Q9QYE9-14EBI-777558,EBI-1127141
    Plekhb1Q9QYE9-22EBI-777558,EBI-1127145

    Protein-protein interaction databases

    BioGridi201664. 4 interactions.
    IntActiQ9WTI7. 9 interactions.
    MINTiMINT-4129061.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WTI7.
    SMRiQ9WTI7. Positions 44-755, 772-801.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 731685Myosin motorAdd
    BLAST
    Domaini734 – 75724IQ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini758 – 78629IQ 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni927 – 93812PIP2-binding motifAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 2 IQ domains.PROSITE-ProRule annotation
    Contains 1 myosin motor domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5022.
    GeneTreeiENSGT00750000117217.
    HOVERGENiHBG062373.
    InParanoidiQ3U231.
    KOiK10356.
    OMAiYAETCPA.
    OrthoDBiEOG7V49XQ.
    PhylomeDBiQ9WTI7.
    TreeFamiTF312960.

    Family and domain databases

    InterProiIPR000048. IQ_motif_EF-hand-BS.
    IPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00612. IQ. 2 hits.
    PF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00015. IQ. 2 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS50096. IQ. 2 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9WTI7-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD     50
    FVLLENFTSE AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH 100
    MERYRGVSFY EVPPHLFAVA DTVYRALRTE RRDQAVMISG ESGAGKTEAT 150
    KRLLQFYAET CPAPERGGAV RDRLLQSNPV LEAFGNAKTL RNDNSSRFGK 200
    YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF YQLLEGGEEE 250
    TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE 300
    VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR 350
    EALTHRKIIA KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS 400
    LASKDAESPS WRSTTVLGLL DIYGFEVFQH NSFEQFCINY CNEKLQQLFI 450
    ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC DLVEEKFKGI ISILDEECLR 500
    PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG EFRLLHYAGE 550
    VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV 600
    ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG 650
    LMENLRVRRA GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH 700
    LGYKPEEYKM GRTKIFIRFP KTLFATEDSL EVRRQSLATK IQAAWRGFHW 750
    RQKFLRVKRS AICIQSWWRG TLGRRKAAKR KWAAQTIRRL IRGFILRHSP 800
    RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL REASELLREL 850
    CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 900
    LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KGYKPRPRQL LLTPSAVVIV 950
    EDAKVKQRID YANLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI 1000
    ETLTKTALSA DRVNNININQ GSITFAGGPG RDGIIDFTSG SELLITKAKN 1050
    GHLAVVAPRL NSR 1063

    Note: Gene prediction based on EST data.

    Length:1,063
    Mass (Da):121,944
    Last modified:April 14, 2009 - v2
    Checksum:i494A31B8634A1AF9
    GO
    Isoform 2 (identifier: Q9WTI7-2) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:1,028
    Mass (Da):118,156
    Checksum:i2CF5535D816884DF
    GO
    Isoform 3 (identifier: Q9WTI7-3) [UniParc]FASTAAdd to Basket

    Also known as: Nuclear myosin 1, NM1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MALQVELIPTGEIIRVVHPHRPCKL → MRYRAS

    Show »
    Length:1,044
    Mass (Da):119,877
    Checksum:iCDAB0FF699D041C9
    GO
    Isoform 4 (identifier: Q9WTI7-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:963
    Mass (Da):111,290
    Checksum:iC8CEFAE7FADE5B41
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 702RR → GG in CAA67956. (PubMed:9119401)Curated
    Sequence conflicti97 – 993SRQ → RRK in CAA67956. (PubMed:9119401)Curated
    Sequence conflicti102 – 1021E → G in BAE33311. (PubMed:16141072)Curated
    Sequence conflicti107 – 1071V → I in BAE33311. (PubMed:16141072)Curated
    Sequence conflicti251 – 2511T → A(PubMed:8449986)Curated
    Sequence conflicti272 – 2721C → F(PubMed:8449986)Curated
    Sequence conflicti286 – 2872VM → LL(PubMed:8449986)Curated
    Sequence conflicti388 – 3881R → A(PubMed:8449986)Curated
    Sequence conflicti401 – 4033LAS → VPA(PubMed:8449986)Curated
    Sequence conflicti446 – 4461Q → R(PubMed:8449986)Curated
    Sequence conflicti517 – 5193VKP → IKH(PubMed:8449986)Curated
    Sequence conflicti578 – 5781M → T(PubMed:8449986)Curated
    Sequence conflicti607 – 6071S → G(PubMed:8449986)Curated
    Sequence conflicti735 – 7351Q → R in CAA67956. (PubMed:9119401)Curated
    Sequence conflicti821 – 8211R → G in CAA67956. (PubMed:9119401)Curated
    Sequence conflicti842 – 8421E → D in CAA67956. (PubMed:9119401)Curated
    Sequence conflicti1024 – 10241T → A in BAE33311. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535Missing in isoform 2. 4 PublicationsVSP_036863Add
    BLAST
    Alternative sequencei1 – 2525MALQV…RPCKL → MRYRAS in isoform 3. 2 PublicationsVSP_036864Add
    BLAST
    Alternative sequencei932 – 1063132GYKPR…RLNSR → VTSLAPGSCCSRPVLWSLWR MLKSSRELIMPT in isoform 4. 1 PublicationVSP_003350Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS25054.1. [Q9WTI7-2]
    CCDS36228.1. [Q9WTI7-3]
    PIRiB45438.
    H75634.
    RefSeqiNP_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]
    UniGeneiMm.234502.

    Genome annotation databases

    EnsembliENSMUST00000069057; ENSMUSP00000070388; ENSMUSG00000017774. [Q9WTI7-2]
    ENSMUST00000102504; ENSMUSP00000099562; ENSMUSG00000017774. [Q9WTI7-2]
    ENSMUST00000102505; ENSMUSP00000099563; ENSMUSG00000017774. [Q9WTI7-1]
    ENSMUST00000108431; ENSMUSP00000104069; ENSMUSG00000017774. [Q9WTI7-3]
    GeneIDi17913.
    KEGGimmu:17913.
    UCSCiuc007kem.1. mouse. [Q9WTI7-1]
    uc007keo.1. mouse. [Q9WTI7-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS25054.1. [Q9WTI7-2 ]
    CCDS36228.1. [Q9WTI7-3 ]
    PIRi B45438.
    H75634.
    RefSeqi NP_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 ]
    UniGenei Mm.234502.

    3D structure databases

    ProteinModelPortali Q9WTI7.
    SMRi Q9WTI7. Positions 44-755, 772-801.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201664. 4 interactions.
    IntActi Q9WTI7. 9 interactions.
    MINTi MINT-4129061.

    PTM databases

    PhosphoSitei Q9WTI7.

    Proteomic databases

    MaxQBi Q9WTI7.
    PaxDbi Q9WTI7.
    PRIDEi Q9WTI7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069057 ; ENSMUSP00000070388 ; ENSMUSG00000017774 . [Q9WTI7-2 ]
    ENSMUST00000102504 ; ENSMUSP00000099562 ; ENSMUSG00000017774 . [Q9WTI7-2 ]
    ENSMUST00000102505 ; ENSMUSP00000099563 ; ENSMUSG00000017774 . [Q9WTI7-1 ]
    ENSMUST00000108431 ; ENSMUSP00000104069 ; ENSMUSG00000017774 . [Q9WTI7-3 ]
    GeneIDi 17913.
    KEGGi mmu:17913.
    UCSCi uc007kem.1. mouse. [Q9WTI7-1 ]
    uc007keo.1. mouse. [Q9WTI7-3 ]

    Organism-specific databases

    CTDi 4641.
    MGIi MGI:106612. Myo1c.

    Phylogenomic databases

    eggNOGi COG5022.
    GeneTreei ENSGT00750000117217.
    HOVERGENi HBG062373.
    InParanoidi Q3U231.
    KOi K10356.
    OMAi YAETCPA.
    OrthoDBi EOG7V49XQ.
    PhylomeDBi Q9WTI7.
    TreeFami TF312960.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    ChiTaRSi MYO1C. mouse.
    NextBioi 292757.
    PROi Q9WTI7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WTI7.
    Bgeei Q9WTI7.
    CleanExi MM_MYO1C.
    Genevestigatori Q9WTI7.

    Family and domain databases

    InterProi IPR000048. IQ_motif_EF-hand-BS.
    IPR001609. Myosin_head_motor_dom.
    IPR010926. Myosin_tail_2.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00612. IQ. 2 hits.
    PF00063. Myosin_head. 1 hit.
    PF06017. Myosin_TH1. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00015. IQ. 2 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS50096. IQ. 2 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiMYO1C_MOUSE
    AccessioniPrimary (citable) accession number: Q9WTI7
    Secondary accession number(s): O08571
    , O08834, Q3TBQ4, Q3U231, Q5ND46, Q5ND48, Q5ND49, Q9ERB6, Q9QW54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3