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  2. Myosin light-chain kinase - Wikipedia

    en.wikipedia.org/wiki/Myosin_light-chain_kinase

    Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. This myosin binding domain is located at the C-Terminus end of the kinase. On the other side of the kinase at the N-Terminus end, sits the actin-binding domain, which allows MYLK to form interactions with actin filaments, keeping it in place. [4] [5]

  3. MYLK - Wikipedia

    en.wikipedia.org/wiki/MYLK

    This gene, a muscle member of the immunoglobulin superfamily, encodes a myosin light-chain kinase, which is a calcium-/calmodulin-dependent enzyme.This kinase phosphorylates myosin regulatory light chains to facilitate myosin interaction with actin filaments to produce contractile activity.

  4. Myosin - Wikipedia

    en.wikipedia.org/wiki/Myosin

    Virtually all eukaryotic cells contain myosin isoforms. Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous. The structure and function of myosin is globally conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba. [6] [7]

  5. Myosin light chain - Wikipedia

    en.wikipedia.org/wiki/Myosin_light_chain

    Myosin light chain kinase (MLCK) inhibitors are one of the few peptides that can cross the plasma membrane relatively quickly. Under stressful conditions, MLCK's in the human body promotes increased permeability of microvessels. It is thought that MLCK phosphorylates endothelial myosin, leading to cell contraction.

  6. Motor protein - Wikipedia

    en.wikipedia.org/wiki/Motor_protein

    Myosin II is an elongated protein that is formed from two heavy chains with motor heads and two light chains. Each myosin head contains actin and ATP binding site. The myosin heads bind and hydrolyze ATP, which provides the energy to walk toward the plus end of an actin filament. Myosin II are also vital in the process of cell division. For ...

  7. Telokin - Wikipedia

    en.wikipedia.org/wiki/Telokin

    n/a n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Telokin Crystallographic structure of muscle myosin light chain kinase from turkey gizzard. Identifiers Symbol MYLK NCBI gene 4638 HGNC 7590 OMIM 600922 RefSeq NM_053025 UniProt Q5MYA0 Other data EC number 2.7.11.18 Locus Chr. 3 q21 ...

  8. Myosin-light-chain phosphatase - Wikipedia

    en.wikipedia.org/wiki/Myosin-light-chain_phosphatase

    Thus, myosin phosphatase undoes the muscle contraction process initiated by myosin light-chain kinase. The enzyme is composed of three subunits: the catalytic region ( protein phosphatase 1 , or PP1), the myosin binding subunit (MYPT1), and a third subunit (M20) of unknown function.

  9. MYO10 - Wikipedia

    en.wikipedia.org/wiki/MYO10

    4651 17909 Ensembl ENSG00000145555 ENSMUSG00000022272 UniProt Q9HD67 F8VQB6 RefSeq (mRNA) NM_012334 NM_019472 NM_001353141 NM_001353142 RefSeq (protein) NP_036466 NP_062345 NP_001340070 NP_001340071 Location (UCSC) Chr 5: 16.66 – 16.94 Mb Chr 15: 25.62 – 25.81 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Myosin X, also known as MYO10, is a protein that in humans is encoded by ...