TRIM3 Protein, tripartite motif containing 3


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Official Full Name tripartite motif containing 3
Background The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also called the RING-B-box-coiled-coil (RBCC) subgroup of RING finger proteins. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to cytoplasmic filaments. It is similar to a rat protein which is a specific partner for the tail domain of myosin V, a class of myosins which are involved in the targeted transport of organelles. The rat protein can also interact with alpha-actinin-4. Thus it is suggested that this human protein may play a role in myosin V-mediated cargo transport. Alternatively spliced transcript variants encoding the same isoform have been identified.
Synonyms TRIM3; tripartite motif containing 3; RNF22, tripartite motif containing 3; tripartite motif-containing protein 3; BERP; brain expressed ring finger; HAC1; ring finger protein 22; RNF97; tripartite motif protein TRIM3; Brain-expressed RING finger protein; FLJ16135; RING finger protein 97; RNF22; TRIM3_HUMAN; tripartite motif-containing 3
    • Species :
    • Human
    • Mouse
    • Rat
    • Rhesus Macaque
    • Source :
    • E.coli
    • HEK293
    • Mammalian Cell
    • Tag :
    • His
    • N/A
    Species Cat.# Product name Source (Host) Tag Protein Length Price
    Human TRIM3-423H Recombinant Human TRIM3 Protein, His-tagged E.coli His
    Human TRIM3-784HCL Recombinant Human TRIM3 293 Cell Lysate HEK293 N/A
    Human TRIM3-785HCL Recombinant Human TRIM3 293 Cell Lysate HEK293 N/A
    Mouse TRIM3-17355M Recombinant Mouse TRIM3 Protein Mammalian Cell His
    Rat TRIM3-6276R Recombinant Rat TRIM3 Protein Mammalian Cell His
    Rhesus Macaque TRIM3-4961R Recombinant Rhesus monkey TRIM3 Protein, His-tagged Mammalian Cell His

    TRIM3 involved in several pathways and played different roles in them. We selected most pathways TRIM3 participated on our site, such as Cytokine Signaling in Immune system, Immune System, Interferon Signaling, which may be useful for your reference. Also, other proteins which involved in the same pathway with TRIM3 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Cytokine Signaling in Immune system RASGEF1A; HLA-DQB2; TRIM46; FRS2; FGF18B; JAK3; CSF2RA; CRKL; CNKSR1; IL17RD
    Immune System SIGLEC15; SH2D1B; PJA2; CFHL1; DUSP3B; TRIM2; IRF2; TLR10; TRIM62; DEFB116
    Interferon Signaling EIF4E3; TRIM38; HERC5; GBP5; FCGR1B; IFIT3; TRIM62; IRF4; TRIM6; GBP1
    Interferon gamma signaling TRIM68; GBP2; TRIM8; IFI30; TRIM48; TRIM26; TRIM3; HLA-DQB2; TRIM31; IRF6

    TRIM3 has several biochemical functions, for example, protein C-terminus binding, protein binding, ubiquitin protein ligase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by TRIM3 itself. We selected most functions TRIM3 had, and list some proteins which have the same functions with TRIM3. You can find most of the proteins on our site.

    Function Related Protein
    protein C-terminus binding PLEKHB1; PEX12; ERCC2; VPS4A; PIAS4; ABL1; PIAS3; PEX26; ERCC3; NEIL1
    protein binding WBP1; IL10RA; HTATIP2; ABCG8; GTF2H2; ITSN1; MTMR7; NPL; KLHL22; KIAA1524
    ubiquitin protein ligase activity PRPF19; TRIM63; RNF4; ITCHA; UBE2T; AKTIP; UBE2G2; RNF121; RNF144B; XIAP
    zinc ion binding ASTL; KLF4; ATRX; MT1; NR1D2B; LANCL1; EDEM3; CRIP1; RBM14B; ZNF385C

    TRIM3 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 TRIM3 here. Most of them are supplied by our site. Hope this information will be useful for your research of TRIM3.

    UBE2G2; UBE2U; cutF

    Sun, Y; Ho, GH; et al. Down-regulation of Tripartite-motif containing 22 expression in breast cancer is associated with a lack of p53-mediated induction. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 441:600-606(2013).
    Alloush, J; Roof, SR; et al. Expression levels-of sarcolemmal membrane repair proteins following prolonged exercise training in mice. INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS 50:428-435(2013).

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