Version 5.4
Homo sapiens Protein: RNF212
Summary
InnateDB Protein IDBP-6408.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol RNF212
Protein Name ring finger protein 212
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000372428
InnateDB Gene IDBG-6406 (RNF212)
Protein Structure
UniProt Annotation
Function SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associates to the synaptonemal complex. Localizes to a minority of double-strand breaks (DSBs) sites. Marks crossover sites during midpachynema (By similarity). {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
Biological Process
GO:0006311 meiotic gene conversion
GO:0007131 reciprocal meiotic recombination
GO:0016925 protein sumoylation
GO:0051026 chiasma assembly
Cellular Component
GO:0000795 synaptonemal complex
Protein Structure and Domains
PDB ID
InterPro IPR001841 Zinc finger, RING-type
PFAM PF13639
PF14634
PRINTS
PIRSF
SMART SM00184
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q495C1
PhosphoSite PhosphoSite-Q495C1
TrEMBL
UniProt Splice Variant
Entrez Gene 285498
UniGene
RefSeq NP_919420
HUGO HGNC:27729
OMIM 612041
CCDS CCDS3345
HPRD 14158
IMGT
EMBL AC019103 AC092535 AK096160 BC036250 BC050356 BC101258 BC101259 BC101260 BC101261
GenPept AAH36250 AAH50356 AAI01259 AAI01260 AAI01261 AAI01262 BAC04714

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca