myom1

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myom1

Official Full Name myomesin 1, 185kDa
Background The giant protein titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to M-band constituents of apparent molecular masses of 190 kD (myomesin 1) and 165 kD (myomesin 2). This protein, myomesin 1, like myomesin 2, titin, and other myofibrillar proteins contains structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. Myomesin 1 and myomesin 2 each have a unique N-terminal region followed by 12 modules of motif I or motif II, in the arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteins share 50% sequence identity in this repeat-containing region. The head structure formed by these 2 proteins on one end of the titin string extends into the center of the M band. The integrating structure of the sarcomere arises from muscle-specific members of the superfamily of immunoglobulin-like proteins. Alternatively spliced transcript variants encoding different isoforms have been identified.
Synonyms MYOM1; myomesin 1, 185kDa; myomesin 1 (skelemin) (185kD) , myomesin 1 (skelemin) 185kDa; myomesin-1; skelemin; EH-myomesin; myomesin family member 1; myomesin 1 (skelemin) 185kDa; myomesin (M-protein) 1 (190kD); 190 kDa titin-associated protein; 190 kDa
    • Species :
    • Chicken
    • Human
    • Mouse
    • Source :
    • E.coli
    • Mammalian Cell
    • Wheat Germ
    • Tag :
    • GST
    • His
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human MYOM1-1148H Recombinant Human MYOM1, GST-tagged E.coli GST
    Human MYOM1-5854H Recombinant Human MYOM1 Protein, GST-tagged Wheat Germ GST
    Mouse MYOM1-10352M Recombinant Mouse MYOM1 Protein Mammalian Cell His
    Chicken MYOM1-6518C Recombinant Chicken MYOM1 Mammalian Cell His

    myom1 involved in several pathways and played different roles in them. We selected most pathways myom1 participated on our site, such as Striated Muscle Contraction, which may be useful for your reference. Also, other proteins which involved in the same pathway with myom1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Striated Muscle Contraction CMLC1; TNNI2A.1; TNNI2A.4; MYOM1; TNNI2B.1; SMYHC2; TNNI2A.3; TMOD2; TNNT3; MYBPC2A

    myom1 has several biochemical functions, for example, identical protein binding, protein binding, protein homodimerization activity. Some of the functions are cooperated with other proteins, some of the functions could acted by myom1 itself. We selected most functions myom1 had, and list some proteins which have the same functions with myom1. You can find most of the proteins on our site.

    Function Related Protein
    identical protein binding CLDN4; NUP153; BNIP2; TRIM8; C1QL4; COL1A1; BAK1; PYCARD; ITGB3; CLDN3
    protein binding TP53RK; CIRBP; SCHIP1; HIST1H4L; FAM153C; CCDC108; ABHD14B; SLC39A13; EGR1; ARFGAP1
    protein homodimerization activity CAMK2B; VPS24; DMRTA2; ROPN1B; MTERFD3; MCL1B; ZFP365; SHMT1; DMRT3A; HRSP12
    structural constituent of muscle OBSCN; MYL6; PDLIM3; TPM2; MYBPC1; MYH11; SMTN; MYBPH; NEXN; CSRP3

    myom1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with myom1 here. Most of them are supplied by our site. Hope this information will be useful for your research of myom1.

    DYSF; ANKRD28; DNAJB6; C1QTNF9; SYNE1; TTN

    O'Brien, AMP; Utsunomiya, YT; et al. Assessing signatures of selection through variation in linkage disequilibrium between taurine and indicine cattle. GENETICS SELECTION EVOLUTION 46:-(2014).
    Occella, C; Bleidl, D; et al. Identification of an Interstitial 18p11.32-p11.31 Duplication Including the EMILIN2 Gene in a Family with Porokeratosis of Mibelli. PLOS ONE 8:-(2013).

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