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SYNE2

Enables actin binding activity. Involved in several processes, including centrosome localization; nuclear migration; and regulation of cilium assembly. Acts upstream of or within several processes, including fibroblast migration; nuclear envelope organization; and protein localization to nucleus. Located in Z disc and nuclear outer membrane. Is expressed in several structures, including alimentary system; brain; genitourinary system; integumental system; and sensory organ. Human ortholog(s) of this gene implicated in autosomal dominant Emery-Dreifuss muscular dystrophy 5.
Protein class

Disease related genes, Human disease related genes, Plasma proteins

Predicted location

Intracellular, Membrane (different isoforms)

Single cell type specificity

Cell type enhanced (Rod photoreceptor cells, Granulosa cells)

Immune cell specificity

Immune cell enhanced (eosinophil)

Cell line specificity

Cell line enhanced (Daudi, SiHa, U-698)

Interaction

Core component of LINC complexes which are composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, some LINC complex constituents are tissue- or cell type-specific. At least SUN1/2-containing core LINC complexes are proposed to be hexameric composed of three protomers of each KASH and SUN domain-containing protein. The SUN2:SYNE2/KASH2 complex is a heterohexamer; the homotrimeric cloverleave-like conformation of the SUN domain is a prerequisite for LINC complex formation in which three separate SYNE2/KASH2 peptides bind at the interface of adjacent SUN domains. Interacts with EMD, LMNA, MKS3 and F-actin via its N-terminal domain. Interacts with DCTN1 and DYNC1I1/2; suggesting the association with the dynein-dynactin motor complex. Associates with kinesin motor complexes. Interacts with TMEM67. Interacts (via KASH domain) with TMEM258 (PubMed:28716842).

Molecular function

Actin-binding

More Types Infomation

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