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Q9WTI7

- MYO1C_MOUSE

UniProt

Q9WTI7 - MYO1C_MOUSE

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Protein

Unconventional myosin-Ic

Gene

Myo1c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.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.

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 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
Complete GO annotation...

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 vesicle Source: UniProtKB-KW
  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. mitochondrion Source: Ensembl
  11. myosin I complex Source: MGI
  12. nuclear pore Source: UniProtKB-KW
  13. stereocilium Source: MGI
Complete GO annotation...

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

BgeeiQ9WTI7.
CleanExiMM_MYO1C.
ExpressionAtlasiQ9WTI7. baseline and differential.
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 44-781.
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
Domaini873 – 1058186Myosin tailSequence AnalysisAdd
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 the myosin tail domain (PH-like) present in its tail domain.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118956.
HOVERGENiHBG062373.
InParanoidiQ9WTI7.
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

        10         20         30         40         50
MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD
60 70 80 90 100
FVLLENFTSE AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH
110 120 130 140 150
MERYRGVSFY EVPPHLFAVA DTVYRALRTE RRDQAVMISG ESGAGKTEAT
160 170 180 190 200
KRLLQFYAET CPAPERGGAV RDRLLQSNPV LEAFGNAKTL RNDNSSRFGK
210 220 230 240 250
YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF YQLLEGGEEE
260 270 280 290 300
TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE
310 320 330 340 350
VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR
360 370 380 390 400
EALTHRKIIA KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS
410 420 430 440 450
LASKDAESPS WRSTTVLGLL DIYGFEVFQH NSFEQFCINY CNEKLQQLFI
460 470 480 490 500
ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC DLVEEKFKGI ISILDEECLR
510 520 530 540 550
PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG EFRLLHYAGE
560 570 580 590 600
VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV
610 620 630 640 650
ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG
660 670 680 690 700
LMENLRVRRA GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH
710 720 730 740 750
LGYKPEEYKM GRTKIFIRFP KTLFATEDSL EVRRQSLATK IQAAWRGFHW
760 770 780 790 800
RQKFLRVKRS AICIQSWWRG TLGRRKAAKR KWAAQTIRRL IRGFILRHSP
810 820 830 840 850
RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL REASELLREL
860 870 880 890 900
CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR
910 920 930 940 950
LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KGYKPRPRQL LLTPSAVVIV
960 970 980 990 1000
EDAKVKQRID YANLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI
1010 1020 1030 1040 1050
ETLTKTALSA DRVNNININQ GSITFAGGPG RDGIIDFTSG SELLITKAKN
1060
GHLAVVAPRL NSR

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 44-781.
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 ENSGT00760000118956.
HOVERGENi HBG062373.
InParanoidi Q9WTI7.
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

Bgeei Q9WTI7.
CleanExi MM_MYO1C.
ExpressionAtlasi Q9WTI7. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 133 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