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O00159

- MYO1C_HUMAN

UniProt

O00159 - MYO1C_HUMAN

Protein

Unconventional myosin-Ic

Gene

MYO1C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      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 are presumed to bind to membranous compartments, which would be 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.1 Publication
    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 By similarity.By similarity

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. motor activity Source: InterPro
    3. protein binding Source: UniProtKB
    4. receptor binding Source: UniProtKB

    GO - Biological processi

    1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    2. innate immune response Source: Reactome
    3. membrane organization Source: Reactome
    4. mRNA transport Source: UniProtKB-KW
    5. positive regulation of cell migration Source: UniProtKB
    6. positive regulation of cell migration by vascular endothelial growth factor signaling pathway Source: UniProtKB
    7. positive regulation of protein targeting to membrane Source: UniProtKB
    8. positive regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
    9. protein targeting Source: UniProtKB
    10. protein targeting to membrane Source: UniProtKB
    11. regulation of tight junction assembly Source: UniProtKB

    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_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7597. MYO1C.

    Subcellular locationi

    Isoform 1 : Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Colocalizes with RNA polymerase II. Absent from nucleoli and does not colocalize with RNA polymerase I. Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription.
    Isoform 2 : Cytoplasm. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionstereocilium membrane By similarity. Cell projectionruffle By similarity. Cytoplasmic vesicle By similarity
    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 By similarity.By similarity
    Isoform 3 : Nucleusnucleoplasm. Nucleusnucleolus. Nucleusnuclear pore complex
    Note: Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli By similarity. 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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi736 – 7361S → A: Abolishes interaction with YWHAB. 1 Publication
    Mutagenesisi736 – 7361S → E: Increases affinity for YWHAB. 1 Publication

    Organism-specific databases

    PharmGKBiPA31399.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10631063Unconventional myosin-IcPRO_0000123445Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei383 – 3831N6-methyllysine1 Publication
    Modified residuei408 – 4081Phosphoserine2 Publications
    Modified residuei486 – 4861N6-acetyllysineBy similarity

    Post-translational modificationi

    Isoform 2 contains a N-acetylmethionine at position 1.

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00159.
    PaxDbiO00159.
    PeptideAtlasiO00159.
    PRIDEiO00159.

    PTM databases

    PhosphoSiteiO00159.

    Expressioni

    Gene expression databases

    ArrayExpressiO00159.
    BgeeiO00159.
    CleanExiHS_MYO1C.
    GenevestigatoriO00159.

    Organism-specific databases

    HPAiCAB037023.
    HPA001768.

    Interactioni

    Subunit structurei

    Interacts with GLUT4 By similarity. 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 (via its IQ motifs) with CALM; this precludes interaction with YWHAB. Interacts with YWHAB; this precludes interaction with CALM. Interacts with RPS6 and actin.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi110725. 38 interactions.
    DIPiDIP-33109N.
    IntActiO00159. 16 interactions.
    MINTiMINT-1149702.
    STRINGi9606.ENSP00000352834.

    Structurei

    Secondary structure

    1
    1063
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi51 – 533
    Helixi60 – 7213
    Beta strandi77 – 804
    Beta strandi83 – 875
    Helixi98 – 1047
    Helixi109 – 1113
    Helixi116 – 12914
    Beta strandi134 – 1396
    Helixi146 – 16015
    Helixi170 – 18516
    Beta strandi193 – 1964
    Beta strandi198 – 2069
    Beta strandi212 – 2209
    Helixi225 – 2273
    Helixi238 – 2469
    Helixi249 – 2546
    Helixi261 – 2633
    Turni265 – 2673
    Beta strandi269 – 2713
    Helixi280 – 29314
    Helixi298 – 31619
    Helixi333 – 34210
    Helixi346 – 3549
    Beta strandi355 – 3573
    Beta strandi366 – 3683
    Helixi371 – 40131
    Beta strandi408 – 4136
    Beta strandi415 – 4217
    Beta strandi429 – 4313
    Helixi433 – 45321
    Helixi455 – 46410
    Helixi477 – 4848
    Turni486 – 4883
    Helixi490 – 4967
    Beta strandi499 – 5035
    Helixi506 – 51611
    Beta strandi528 – 5303
    Beta strandi535 – 5373
    Beta strandi539 – 5468
    Beta strandi549 – 5546
    Helixi558 – 5625
    Helixi568 – 5758
    Helixi580 – 5856
    Helixi600 – 61617
    Beta strandi618 – 6269
    Helixi639 – 64911
    Helixi651 – 66010
    Beta strandi663 – 6675
    Helixi668 – 6758
    Helixi676 – 6783
    Beta strandi682 – 6843
    Helixi690 – 70112
    Beta strandi707 – 7104
    Beta strandi712 – 7187
    Helixi720 – 75334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BYFX-ray2.74A/C36-760[»]
    ProteinModelPortaliO00159.
    SMRiO00159. Positions 44-755, 771-801.
    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 motifBy similarityAdd
    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 By similarity.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5022.
    HOGENOMiHOG000260264.
    InParanoidiO00159.
    KOiK10356.
    OMAiYAETCPA.
    OrthoDBiEOG7V49XQ.
    PhylomeDBiO00159.
    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. 3 hits.
    SM00242. MYSc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS50096. IQ. 2 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00159-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MALQVELVPT 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 NHGERNFHIF YQLLEGGEEE 250
    TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVVRKA LTVIDFTEDE 300
    VEDLLSIVAS VLHLGNIHFA ANEESNAQVT TENQLKYLTR LLSVEGSTLR 350
    EALTHRKIIA KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVGKINRS 400
    LASKDVESPS WRSTTVLGLL DIYGFEVFQH NSFEQFCINY CNEKLQQLFI 450
    ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC DLVEEKFKGI ISILDEECLR 500
    PGEATDLTFL EKLEDTVKHH PHFLTHKLAD QRTRKSLGRG EFRLLHYAGE 550
    VTYSVTGFLD KNNDLLFRNL KETMCSSKNP IMSQCFDRSE LSDKKRPETV 600
    ATQFKMSLLQ LVEILQSKEP AYVRCIKPND AKQPGRFDEV LIRHQVKYLG 650
    LLENLRVRRA GFAYRRKYEA FLQRYKSLCP ETWPTWAGRP QDGVAVLVRH 700
    LGYKPEEYKM GRTKIFIRFP KTLFATEDAL EVRRQSLATK IQAAWRGFHW 750
    RQKFLRVKRS AICIQSWWRG TLGRRKAAKR KWAAQTIRRL IRGFVLRHAP 800
    RCPENAFFLD HVRTSFLLNL RRQLPQNVLD TSWPTPPPAL REASELLREL 850
    CIKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 900
    LGTDEISPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV 950
    EDAKVKQRID YANLTGISVS SLSDSLFVLH VQRADNKQKG DVVLQSDHVI 1000
    ETLTKTALSA NRVNSININQ GSITFAGGPG RDGTIDFTPG SELLITKAKN 1050
    GHLAVVAPRL NSR 1063
    Length:1,063
    Mass (Da):121,682
    Last modified:January 11, 2011 - v4
    Checksum:iB105197BA07317B8
    GO
    Isoform 2 (identifier: O00159-2) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: Missing.

    Note: Contains a N-acetylmethionine at position 1.

    Show »
    Length:1,028
    Mass (Da):117,907
    Checksum:i06D3340F7D2A199F
    GO
    Isoform 3 (identifier: O00159-3) [UniParc]FASTAAdd to Basket

    Also known as: B, Nuclear myosin 1, NM1, NMI

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

    Show »
    Length:1,044
    Mass (Da):119,628
    Checksum:iE78D68A46592DC89
    GO

    Sequence cautioni

    The sequence AAH68013.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE06097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAF85599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371E → D in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti152 – 1521R → K in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti165 – 1651E → Q in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti200 – 2001K → E in BU855623. 1 PublicationCurated
    Sequence conflicti324 – 3241E → D in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti379 – 3791D → N in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti453 – 4531T → P in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti832 – 8321S → Y in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti986 – 9861N → I in CAA67131. (PubMed:9119401)Curated
    Sequence conflicti1062 – 10621S → Y in CAA67131. (PubMed:9119401)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti795 – 7951V → I.4 Publications
    Corresponds to variant rs8081370 [ dbSNP | Ensembl ].
    VAR_054855
    Natural varianti826 – 8261Q → R.4 Publications
    Corresponds to variant rs9905106 [ dbSNP | Ensembl ].
    VAR_054856

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535Missing in isoform 2. 2 PublicationsVSP_036861Add
    BLAST
    Alternative sequencei1 – 2525MALQV…RPCKL → MRYRAS in isoform 3. 1 PublicationVSP_036862Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98507 mRNA. Translation: CAA67131.1.
    AK292910 mRNA. Translation: BAF85599.1. Different initiation.
    AB210015 mRNA. Translation: BAE06097.1. Different initiation.
    AC100748 Genomic DNA. No translation available.
    BC044891 mRNA. Translation: AAH44891.2.
    BC068013 mRNA. Translation: AAH68013.1. Different initiation.
    BU855623 mRNA. No translation available.
    CCDSiCCDS11003.1. [O00159-2]
    CCDS42226.1. [O00159-1]
    CCDS45562.1. [O00159-3]
    PIRiA59253.
    RefSeqiNP_001074248.1. NM_001080779.1. [O00159-1]
    NP_001074419.1. NM_001080950.1. [O00159-3]
    NP_203693.3. NM_033375.4. [O00159-2]
    UniGeneiHs.286226.

    Genome annotation databases

    EnsembliENST00000359786; ENSP00000352834; ENSG00000197879. [O00159-1]
    ENST00000361007; ENSP00000354283; ENSG00000197879. [O00159-2]
    ENST00000438665; ENSP00000412197; ENSG00000197879. [O00159-3]
    ENST00000575158; ENSP00000459174; ENSG00000197879. [O00159-2]
    GeneIDi4641.
    KEGGihsa:4641.
    UCSCiuc002fsn.3. human. [O00159-3]
    uc002fso.3. human. [O00159-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98507 mRNA. Translation: CAA67131.1 .
    AK292910 mRNA. Translation: BAF85599.1 . Different initiation.
    AB210015 mRNA. Translation: BAE06097.1 . Different initiation.
    AC100748 Genomic DNA. No translation available.
    BC044891 mRNA. Translation: AAH44891.2 .
    BC068013 mRNA. Translation: AAH68013.1 . Different initiation.
    BU855623 mRNA. No translation available.
    CCDSi CCDS11003.1. [O00159-2 ]
    CCDS42226.1. [O00159-1 ]
    CCDS45562.1. [O00159-3 ]
    PIRi A59253.
    RefSeqi NP_001074248.1. NM_001080779.1. [O00159-1 ]
    NP_001074419.1. NM_001080950.1. [O00159-3 ]
    NP_203693.3. NM_033375.4. [O00159-2 ]
    UniGenei Hs.286226.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BYF X-ray 2.74 A/C 36-760 [» ]
    ProteinModelPortali O00159.
    SMRi O00159. Positions 44-755, 771-801.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110725. 38 interactions.
    DIPi DIP-33109N.
    IntActi O00159. 16 interactions.
    MINTi MINT-1149702.
    STRINGi 9606.ENSP00000352834.

    PTM databases

    PhosphoSitei O00159.

    Proteomic databases

    MaxQBi O00159.
    PaxDbi O00159.
    PeptideAtlasi O00159.
    PRIDEi O00159.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359786 ; ENSP00000352834 ; ENSG00000197879 . [O00159-1 ]
    ENST00000361007 ; ENSP00000354283 ; ENSG00000197879 . [O00159-2 ]
    ENST00000438665 ; ENSP00000412197 ; ENSG00000197879 . [O00159-3 ]
    ENST00000575158 ; ENSP00000459174 ; ENSG00000197879 . [O00159-2 ]
    GeneIDi 4641.
    KEGGi hsa:4641.
    UCSCi uc002fsn.3. human. [O00159-3 ]
    uc002fso.3. human. [O00159-1 ]

    Organism-specific databases

    CTDi 4641.
    GeneCardsi GC17M001367.
    H-InvDB HIX0202539.
    HGNCi HGNC:7597. MYO1C.
    HPAi CAB037023.
    HPA001768.
    MIMi 606538. gene.
    neXtProti NX_O00159.
    PharmGKBi PA31399.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5022.
    HOGENOMi HOG000260264.
    InParanoidi O00159.
    KOi K10356.
    OMAi YAETCPA.
    OrthoDBi EOG7V49XQ.
    PhylomeDBi O00159.
    TreeFami TF312960.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi MYO1C. human.
    GeneWikii MYO1C.
    GenomeRNAii 4641.
    NextBioi 17880.
    PROi O00159.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00159.
    Bgeei O00159.
    CleanExi HS_MYO1C.
    Genevestigatori O00159.

    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. 3 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. "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] (ISOFORM 2), VARIANTS ILE-795 AND ARG-826.
      Tissue: Kidney.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-795 AND ARG-826.
      Tissue: Trachea.
    3. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-795 AND ARG-826.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2), VARIANTS ILE-795 AND ARG-826.
      Tissue: Eye and Liver.
    6. Strausberg R.L.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206 (ISOFORM 3).
      Tissue: Teratocarcinoma.
    7. Bienvenut W.V., Calvo F.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 36-43; 92-98; 104-125; 133-146; 172-188; 198-209; 255-269; 341-350; 357-396; 400-412; 562-568; 606-624; 633-643; 648-656; 666-674; 715-734; 814-822; 827-841; 875-884; 886-894; 901-930; 937-956 AND 988-1047, ACETYLATION AT MET-1 (ISOFORM 2), METHYLATION AT LYS-383, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "Nuclear distribution of actin and myosin I depends on transcriptional activity of the cell."
      Kysela K., Philimonenko A.A., Philimonenko V.V., Janacek J., Kahle M., Hozak P.
      Histochem. Cell Biol. 124:347-358(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Small ribosomal subunits associate with nuclear myosin and actin in transit to the nuclear pores."
      Cisterna B., Necchi D., Prosperi E., Biggiogera M.
      FASEB J. 20:1901-1903(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPS6 AND ACTIN, SUBCELLULAR LOCATION.
    10. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
      Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
      J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Identification and characterization of a novel myosin Ic isoform that localizes to the nucleus."
      Ihnatovych I., Migocka-Patrzalek M., Dukh M., Hofmann W.A.
      Cytoskeleton 69:555-565(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1).
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: implications for Ca(2+)-regulation and 14-3-3 binding."
      Stefan Munnich M.H., Manstein D.J.
      J. Mol. Biol. 426:2070-2081(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 36-760 (ISOFORM 2) IN COMPLEX WITH ADP ORTHOVANADATE AND CALM, INTERACTION WITH CALM AND YWHAB, FUNCTION, ACTIN-BINDING, FUNCTION IN ACTIN-DEPENDENT ATP HYDROLYSIS, MUTAGENESIS OF SER-736.

    Entry informationi

    Entry nameiMYO1C_HUMAN
    AccessioniPrimary (citable) accession number: O00159
    Secondary accession number(s): Q4LE56, Q6NVJ7, Q86Y95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 145 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3