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Official Full Name RAN binding protein 17
Background The transport of protein and large RNAs through the nuclear pore complexes (NPC) is an energy-dependent and regulated process. The import of proteins with a nuclear localization signal (NLS) is accomplished by recognition of one or more clusters of basic amino acids by the importin-alpha/beta complex; see MIM 600685 and MIM 602738. The small GTPase RAN (MIM 601179) plays a key role in NLS-dependent protein import. RAN-binding protein-17 is a member of the importin-beta superfamily of nuclear transport receptors.
Synonyms RANBP17; RAN binding protein 17; ran-binding protein 17; FLJ32916
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RANBP17 involved in several pathways and played different roles in them. We selected most pathways RANBP17 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with RANBP17 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein

RANBP17 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by RANBP17 itself. We selected most functions RANBP17 had, and list some proteins which have the same functions with RANBP17. You can find most of the proteins on our site.

Function Related Protein

RANBP17 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 RANBP17 here. Most of them are supplied by our site. Hope this information will be useful for your research of RANBP17.

Broker, P; Lucke, K; et al. A nanostructured SAW chip-based biosensor detecting cancer cells. SENSORS AND ACTUATORS B-CHEMICAL 165:1-6(2012).
Chen, ZH; et al. A phospholamban-tethered cardiac Ca2+ pump reveals stoichiometry and dynamic interactions between the two proteins. BIOCHEMICAL JOURNAL 439:313-319(2011).

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