Gene description for Myh9l1
Gene name myosin, heavy chain 9, non-muscle-like 1
Gene symbol Myh9l1
Other names/aliases -
Species Rattus norvegicus
 Database cross references - Myh9l1
ExoCarta ExoCarta_25745
Vesiclepedia VP_25745
Entrez Gene 25745
UniProt Q62812  
 Myh9l1 identified in sEVs derived from the following tissue/cell type
Hepatocytes 19367702    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
Reticulocytes 21828046    
 Gene ontology annotations for Myh9l1
Molecular Function
    microfilament motor activity GO:0000146 IBA
    microfilament motor activity GO:0000146 ISO
    microfilament motor activity GO:0000146 ISO
    microfilament motor activity GO:0000146 ISS
    virus receptor activity GO:0001618 ISO
    G-protein alpha-subunit binding GO:0001965 IDA
    cytoskeletal motor activity GO:0003774 IEA
    actin binding GO:0003779 IEA
    actin binding GO:0003779 ISO
    integrin binding GO:0005178 ISO
    integrin binding GO:0005178 ISS
    P-type sodium:potassium-exchanging transporter activity GO:0005391 ISS
    protein binding GO:0005515 IPI
    calmodulin binding GO:0005516 IEA
    ATP binding GO:0005524 IEA
    ATP binding GO:0005524 ISO
    protein kinase binding GO:0019901 IPI
    protein domain specific binding GO:0019904 IEA
    protein domain specific binding GO:0019904 ISO
    follicle-stimulating hormone receptor binding GO:0031762 IDA
    identical protein binding GO:0042802 IDA
    identical protein binding GO:0042802 ISO
    protein homodimerization activity GO:0042803 ISO
    protein homodimerization activity GO:0042803 ISS
    protein-membrane adaptor activity GO:0043495 ISO
    protein-membrane adaptor activity GO:0043495 ISS
    ADP binding GO:0043531 ISO
    actin filament binding GO:0051015 IBA
    actin filament binding GO:0051015 IEA
    actin filament binding GO:0051015 ISO
    actin filament binding GO:0051015 ISO
    actin filament binding GO:0051015 ISS
    scaffold protein binding GO:0097110 IDA
Biological Process
    meiotic spindle organization GO:0000212 IEA
    meiotic spindle organization GO:0000212 ISO
    cell morphogenesis GO:0000902 IEA
    cell morphogenesis GO:0000902 ISO
    angiogenesis GO:0001525 ISO
    angiogenesis GO:0001525 ISS
    in utero embryonic development GO:0001701 IEA
    in utero embryonic development GO:0001701 ISO
    establishment of T cell polarity GO:0001768 IEA
    establishment of T cell polarity GO:0001768 ISO
    plasma membrane repair GO:0001778 ISO
    membrane protein ectodomain proteolysis GO:0006509 ISO
    membrane protein ectodomain proteolysis GO:0006509 ISS
    vesicle targeting GO:0006903 ISO
    phagocytosis, engulfment GO:0006911 IEA
    phagocytosis, engulfment GO:0006911 ISO
    cell adhesion GO:0007155 ISO
    phospholipase C-activating G protein-coupled receptor signaling pathway GO:0007200 IMP
    myoblast fusion GO:0007520 IEA
    myoblast fusion GO:0007520 ISO
    regulation of cell shape GO:0008360 IEA
    regulation of cell shape GO:0008360 ISO
    regulation of cell shape GO:0008360 ISO
    regulation of cell shape GO:0008360 ISS
    establishment or maintenance of transmembrane electrochemical gradient GO:0010248 IEA
    protein transport GO:0015031 ISO
    protein transport GO:0015031 ISS
    actin cytoskeleton organization GO:0030036 ISO
    actin cytoskeleton organization GO:0030036 ISS
    actin filament polymerization GO:0030041 ISO
    actin filament-based movement GO:0030048 ISO
    actin filament-based movement GO:0030048 ISO
    actin filament-based movement GO:0030048 ISS
    platelet formation GO:0030220 ISO
    platelet formation GO:0030220 ISS
    monocyte differentiation GO:0030224 ISO
    monocyte differentiation GO:0030224 ISS
    actomyosin structure organization GO:0031032 ISO
    lysosome localization GO:0032418 ISO
    cytokinetic process GO:0032506 ISO
    cytokinetic process GO:0032506 ISS
    uropod organization GO:0032796 IEA
    uropod organization GO:0032796 ISO
    positive regulation of inositol trisphosphate biosynthetic process GO:0032962 IMP
    positive regulation of insulin secretion involved in cellular response to glucose stimulus GO:0035774 IMP
    endodermal cell differentiation GO:0035987 IEA
    endodermal cell differentiation GO:0035987 ISO
    cellular response to platelet-derived growth factor stimulus GO:0036120 IEP
    follicle-stimulating hormone signaling pathway GO:0042699 IMP
    blood vessel endothelial cell migration GO:0043534 ISO
    blood vessel endothelial cell migration GO:0043534 ISS
    regulated exocytosis GO:0045055 ISO
    positive regulation of G protein-coupled receptor signaling pathway GO:0045745 IMP
    positive regulation of endocytosis GO:0045807 IMP
    symbiont entry into host cell GO:0046718 ISO
    cell motility GO:0048870 IEA
    cell motility GO:0048870 ISO
    positive regulation of phagocytosis GO:0050766 IMP
    actin filament bundle assembly GO:0051017 IMP
    establishment of meiotic spindle localization GO:0051295 IEA
    establishment of meiotic spindle localization GO:0051295 ISO
    actin filament capping GO:0051693 ISO
    positive regulation of focal adhesion assembly GO:0051894 IMP
    cortical granule exocytosis GO:0060471 IEA
    cortical granule exocytosis GO:0060471 ISO
    cortical granule exocytosis GO:0060471 ISS
    positive regulation of ERK1 and ERK2 cascade GO:0070374 IMP
    platelet aggregation GO:0070527 ISO
    actin filament bundle distribution GO:0070650 IMP
    cellular response to mechanical stimulus GO:0071260 IEP
    cell-cell adhesion GO:0098609 IEA
    cell-cell adhesion GO:0098609 IMP
    cell-cell adhesion GO:0098609 ISO
    regulation of actin filament organization GO:0110053 IMP
    negative regulation of actin filament severing GO:1903919 IEA
    negative regulation of actin filament severing GO:1903919 ISO
    positive regulation of protein processing in phagocytic vesicle GO:1903923 IEA
    positive regulation of protein processing in phagocytic vesicle GO:1903923 ISO
    negative regulation of vascular associated smooth muscle cell migration GO:1904753 IMP
    regulation of plasma membrane repair GO:1905684 ISO
Subcellular Localization
    stress fiber GO:0001725 IEA
    stress fiber GO:0001725 ISO
    stress fiber GO:0001725 ISS
    ruffle GO:0001726 ISO
    ruffle GO:0001726 ISS
    immunological synapse GO:0001772 IEA
    immunological synapse GO:0001772 ISO
    uropod GO:0001931 IEA
    uropod GO:0001931 ISO
    nucleus GO:0005634 ISO
    nucleus GO:0005634 ISS
    cytoplasm GO:0005737 IBA
    cytoplasm GO:0005737 IEA
    cytoplasm GO:0005737 ISO
    cytoplasm GO:0005737 ISS
    endosome GO:0005768 IDA
    spindle GO:0005819 IEA
    spindle GO:0005819 ISO
    actomyosin contractile ring GO:0005826 ISO
    actomyosin contractile ring GO:0005826 ISS
    cytosol GO:0005829 ISO
    cytosol GO:0005829 ISS
    actin filament GO:0005884 IDA
    plasma membrane GO:0005886 ISO
    plasma membrane GO:0005886 ISS
    brush border GO:0005903 IDA
    brush border GO:0005903 IEA
    brush border GO:0005903 ISO
    adherens junction GO:0005912 IEA
    adherens junction GO:0005912 ISO
    focal adhesion GO:0005925 IEA
    focal adhesion GO:0005925 ISO
    cell cortex GO:0005938 IEA
    cell cortex GO:0005938 ISO
    cell cortex GO:0005938 ISS
    COP9 signalosome GO:0008180 ISO
    cytoplasmic side of plasma membrane GO:0009898 IEA
    cytoplasmic side of plasma membrane GO:0009898 ISO
    cell surface GO:0009986 ISO
    actin cytoskeleton GO:0015629 ISO
    actin cytoskeleton GO:0015629 ISS
    apical plasma membrane GO:0016324 IDA
    lateral plasma membrane GO:0016328 IDA
    myosin complex GO:0016459 IEA
    myosin complex GO:0016459 ISO
    myosin II complex GO:0016460 IBA
    myosin II complex GO:0016460 IEA
    myosin II complex GO:0016460 ISO
    nuclear body GO:0016604 ISO
    lamellipodium GO:0030027 IDA
    cortical cytoskeleton GO:0030863 IEA
    cortical cytoskeleton GO:0030863 ISO
    cell leading edge GO:0031252 ISO
    cell leading edge GO:0031252 ISS
    neuromuscular junction GO:0031594 IEA
    neuromuscular junction GO:0031594 ISO
    cleavage furrow GO:0032154 ISO
    cleavage furrow GO:0032154 ISS
    myosin filament GO:0032982 IBA
    protein-containing complex GO:0032991 IDA
    protein-containing complex GO:0032991 ISO
    protein-containing complex GO:0032991 ISS
    actomyosin GO:0042641 ISO
    phagocytic vesicle GO:0045335 IDA
    cortical granule GO:0060473 IEA
    cortical granule GO:0060473 ISO
    cortical granule GO:0060473 ISS
    exocytic vesicle GO:0070382 ISO
    myosin II filament GO:0097513 ISO
 Experiment description of studies that identified Myh9l1 in sEVs
1
Experiment ID 35
MISEV standards
CEM
Biophysical techniques
TSG101|Alix|CD81|CD63
Enriched markers
HSPA5
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry
PubMed ID 19367702    
Organism Rattus norvegicus
Experiment description Characterization and Comprehensive Proteome Profiling of Exosomes Secreted by Hepatocytes.
Authors "Conde-Vancells J, Rodriguez-Suarez E, Embade N, Gil D, Matthiesen R, Valle M, Elortza F, Lu SC, Mato JM, Falcon-Perez JM"
Journal name JPR
Publication year 2008
Sample Hepatocytes
Sample name Hepatocytes
Isolation/purification methods Differential centrifugation
Filtration
Sucrose density gradient
Flotation density -
Molecules identified in the study Protein
Methods used in the study Mass spectrometry [QTOF]
Western blotting
2
Experiment ID 90
MISEV standards
EM
Biophysical techniques
HSC70|HSP90|TSG101|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E"
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D2 Rep 1
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
3
Experiment ID 94
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D4 Rep 1
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
4
Experiment ID 95
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D7 Rep 1
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.13-1.25 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
5
Experiment ID 96
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D2 Rep 2
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
6
Experiment ID 97
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D4 Rep 2
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
7
Experiment ID 98
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [Orbitrap]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D7 Rep 2
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.13-1.25 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
8
Experiment ID 99
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [QSTAR]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D2 Rep 3
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
9
Experiment ID 100
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [QSTAR]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D4 Rep 3
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.16-1.21 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
10
Experiment ID 101
MISEV standards
EM
Biophysical techniques
TSG101|HSP90|HSC70|MHCI
Enriched markers
Negative markers
Particle analysis
Identified molecule protein
Identification method Mass spectrometry [QSTAR]
PubMed ID 21828046    
Organism Rattus norvegicus
Experiment description The proteo-lipidic composition of exosomes changes during reticulocyte maturation.
Authors "Carayon K, Chaoui K, Ronzier E, Lazar I, Bertrand-Michel J, Roques V, Balor S, Terce F, Lopez A, Salome L, Joly E."
Journal name JBC
Publication year 2011
Sample Reticulocytes
Sample name Reticulocytes - D7 Rep 3
Isolation/purification methods Differential centrifugation
Ultracentrifugation
Sucrose density gradient
Flotation density 1.13-1.25 g/mL
Molecules identified in the study Protein
Lipids
Methods used in the study Mass spectrometry [QSTAR]
Mass spectrometry [Orbitrap]
Western blotting
 Protein-protein interactions for Myh9l1
  Protein Interactor ExoCarta ID Identification method PubMed Species
1 Dao  
Affinity Capture-MS Rattus norvegicus
2 Sumo3  
Affinity Capture-MS Rattus norvegicus
3 Pdlim2  
Reconstituted Complex Rattus norvegicus
View the network image/svg+xml
 Pathways in which Myh9l1 is involved
No pathways found





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