Entry - *607119 - RING FINGER PROTEIN 19A, RBR E3 UBIQUITIN PROTEIN LIGASE; RNF19A - OMIM
 
* 607119

RING FINGER PROTEIN 19A, RBR E3 UBIQUITIN PROTEIN LIGASE; RNF19A


Alternative titles; symbols

DOUBLE RING FINGER PROTEIN
DORFIN


HGNC Approved Gene Symbol: RNF19A

Cytogenetic location: 8q22.2   Genomic coordinates (GRCh38) : 8:100,257,067-100,336,204 (from NCBI)


TEXT

Cloning and Expression

Niwa et al. (2001) identified DORFIN by random sequencing of clones amplified from spinal cord total RNA. They obtained the full-length cDNA by PCR of a fetal brain library. The deduced 838-amino acid protein has a calculated molecular mass of 90.7 kD. It is predicted to contain 2 N-terminal cys/his-rich RING finger motifs separated by an 'in between RING fingers' (IBR) motif, 2 hydrophobic regions in the C terminus, a monopartite nuclear localization sequence (NLS), and 2 bipartite basic NLSs. DORFIN shares 94% sequence identity with mouse Xybp protein, and its C terminus is identical to an SP1 (189906)-binding protein isolated by Gunther et al. (2000). Northern blot analysis detected expression of a 4.4-kb transcript at high levels in heart and at low levels in all other tissues tested. GFP-DORFIN fusion studies localized the protein in the centrosome.


Gene Function

Niwa et al. (2001) found that DORFIN interacts with components of the ubiquitin-proteasome system. Cotransfection and coimmunoprecipitation studies revealed that DORFIN interacts directly with UBCH7 (UBE2L3; 603721) and UBCH8 (UBE2L6; 603890), but not with other ubiquitin-conjugating enzymes. With use of deletion mutants, Niwa et al. (2001) found that the interaction between DORFIN and UBCH7 is mediated by the RING finger/IBR domain. They also found that the C-terminal region is necessary for binding with ubiquitinated proteins, suggesting that DORFIN functions as a ubiquitin protein ligase.


Mapping

Gross (2021) mapped the RNF19A gene to chromosome 8q22.2 based on an alignment of the RNF19A sequence (GenBank BC062676) with the genomic sequence (GRCh38).


REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 8/16/2021.

  2. Gunther, M., Laithier, M., Brison, O. A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening. Molec. Cell. Biochem. 210: 131-142, 2000. [PubMed: 10976766, related citations] [Full Text]

  3. Niwa, J., Ishigaki, S., Doyu, M., Suzuki, T., Tanaka, K., Sobue, G. A novel centrosomal RING-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem. Biophys. Res. Commun. 281: 706-713, 2001. [PubMed: 11237715, related citations] [Full Text]


Contributors:
Matthew B. Gross - updated : 08/16/2021
Creation Date:
Patricia A. Hartz : 7/29/2002
mgross : 08/16/2021
carol : 07/29/2002

* 607119

RING FINGER PROTEIN 19A, RBR E3 UBIQUITIN PROTEIN LIGASE; RNF19A


Alternative titles; symbols

DOUBLE RING FINGER PROTEIN
DORFIN


HGNC Approved Gene Symbol: RNF19A

Cytogenetic location: 8q22.2   Genomic coordinates (GRCh38) : 8:100,257,067-100,336,204 (from NCBI)


TEXT

Cloning and Expression

Niwa et al. (2001) identified DORFIN by random sequencing of clones amplified from spinal cord total RNA. They obtained the full-length cDNA by PCR of a fetal brain library. The deduced 838-amino acid protein has a calculated molecular mass of 90.7 kD. It is predicted to contain 2 N-terminal cys/his-rich RING finger motifs separated by an 'in between RING fingers' (IBR) motif, 2 hydrophobic regions in the C terminus, a monopartite nuclear localization sequence (NLS), and 2 bipartite basic NLSs. DORFIN shares 94% sequence identity with mouse Xybp protein, and its C terminus is identical to an SP1 (189906)-binding protein isolated by Gunther et al. (2000). Northern blot analysis detected expression of a 4.4-kb transcript at high levels in heart and at low levels in all other tissues tested. GFP-DORFIN fusion studies localized the protein in the centrosome.


Gene Function

Niwa et al. (2001) found that DORFIN interacts with components of the ubiquitin-proteasome system. Cotransfection and coimmunoprecipitation studies revealed that DORFIN interacts directly with UBCH7 (UBE2L3; 603721) and UBCH8 (UBE2L6; 603890), but not with other ubiquitin-conjugating enzymes. With use of deletion mutants, Niwa et al. (2001) found that the interaction between DORFIN and UBCH7 is mediated by the RING finger/IBR domain. They also found that the C-terminal region is necessary for binding with ubiquitinated proteins, suggesting that DORFIN functions as a ubiquitin protein ligase.


Mapping

Gross (2021) mapped the RNF19A gene to chromosome 8q22.2 based on an alignment of the RNF19A sequence (GenBank BC062676) with the genomic sequence (GRCh38).


REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 8/16/2021.

  2. Gunther, M., Laithier, M., Brison, O. A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening. Molec. Cell. Biochem. 210: 131-142, 2000. [PubMed: 10976766] [Full Text: https://doi.org/10.1023/a:1007177623283]

  3. Niwa, J., Ishigaki, S., Doyu, M., Suzuki, T., Tanaka, K., Sobue, G. A novel centrosomal RING-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem. Biophys. Res. Commun. 281: 706-713, 2001. [PubMed: 11237715] [Full Text: https://doi.org/10.1006/bbrc.2001.4414]


Contributors:
Matthew B. Gross - updated : 08/16/2021

Creation Date:
Patricia A. Hartz : 7/29/2002

Edit History:
mgross : 08/16/2021
carol : 07/29/2002