RNF12
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Official Full Name
RLIM ring finger protein, LIM domain interacting -
Overview
The protein encoded by this gene is a RING-H2 zinc finger protein. It has been shown to be an E3 ubiquitin protein ligase that targets LIM domain binding 1 (LDB1/CLIM), and causes proteasome-dependent degradation of LDB1. This protein and LDB1 are co-repressors of LHX1/LIM-1, a homeodomain transcription factor. Multiple alternatively spliced variants, encoding the same protein, have been identified. -
Synonyms
RNF12;FLJ25923;FLJ41093;FLJ42887;FLJ45986;MGC15161;NY-REN-43;DKFZp686N06224;E3 ubiquitin-protein ligase RLIM;R-LIM;OTTHUMP00000023574;OTTHUMP00000023575;ring finger protein 12;E3 ubiquitin-protein ligase RNF12;renal carcinoma antigen NY-REN-43;RING finger LIM domain-binding protein;ring zinc finger protein NY-REN-43antigen;LIM domain-interacting RING finger protein;ring zinc finger LIM domain binding protein
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Involved Pathway
RNF12 involved in several pathways and played different roles in them. We selected most pathways RNF12 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with RNF12 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
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Protein Function
RNF12 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by RNF12 itself. We selected most functions RNF12 had, and list some proteins which have the same functions with RNF12. You can find most of the proteins on our site.
| Function | Related Protein |
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Interacting Protein
RNF12 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 RNF12 here. Most of them are supplied by our site. Hope this information will be useful for your research of RNF12.
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References
- Fukuda, A; Tomikawa, J; et al. The role of maternal-specific H3K9me3 modification in establishing imprinted X-chromosome inactivation and embryogenesis in mice. NATURE COMMUNICATIONS 5:-(2014).
- Shin, J; Wallingford, MC; et al. RLIM is dispensable for X-chromosome inactivation in the mouse embryonic epiblast. NATURE 511:86-U443(2014).
