Entry - *613142 - DELTEX E3 UBIQUITIN LIGASE 3; DTX3 - OMIM

 
 
* 613142

DELTEX E3 UBIQUITIN LIGASE 3; DTX3


Alternative titles; symbols

DELTEX, DROSOPHILA, HOMOLOG OF, 3


HGNC Approved Gene Symbol: DTX3

Cytogenetic location: 12q13.3     Genomic coordinates (GRCh38): 12:57,604,824-57,609,802 (from NCBI)


TEXT

▼ Description

DTX3 functions as an E3 ubiquitin ligase (Takeyama et al., 2003).


▼ Cloning and Expression

Using primers based on mouse Dtx3 for RT-PCR, Takeyama et al. (2003) cloned human DTX3. The deduced 347-amino acid protein has a truncated N-terminal domain compared with other DTX proteins, but it contains the proline-rich region and C-terminal RING-HC domain.


▼ Gene Function

Using an in vitro ubiquitination assay, Takeyama et al. (2003) showed that recombinant DTX3 functioned as a ubiquitin E3 ligase. It showed highest ubiquitination activity in conjunction with the E2 enzyme UBCH5A (UBE2D1; 602961).


▼ Mapping

Hartz (2009) mapped the DTX3 gene to chromosome 12q13.3 based on an alignment of the DTX3 sequence (GenBank AK092085) with the genomic sequence (GRCh37).

▼ REFERENCES

  1. Hartz, P. A. Personal Communication. Baltimore, Md. 11/23/2009.

  2. Takeyama, K., Aguiar, R. C. T., Gu, L., He, C., Freeman, G. J., Kutok, J. L., Aster, J. C., Shipp, M. A. The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity. J. Biol. Chem. 278: 21930-21937, 2003. [PubMed: 12670957, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 11/23/2009
Edit History:
carol : 01/03/2020
mgross : 11/23/2009

* 613142

DELTEX E3 UBIQUITIN LIGASE 3; DTX3


Alternative titles; symbols

DELTEX, DROSOPHILA, HOMOLOG OF, 3


HGNC Approved Gene Symbol: DTX3

Cytogenetic location: 12q13.3     Genomic coordinates (GRCh38): 12:57,604,824-57,609,802 (from NCBI)


TEXT

Description

DTX3 functions as an E3 ubiquitin ligase (Takeyama et al., 2003).


Cloning and Expression

Using primers based on mouse Dtx3 for RT-PCR, Takeyama et al. (2003) cloned human DTX3. The deduced 347-amino acid protein has a truncated N-terminal domain compared with other DTX proteins, but it contains the proline-rich region and C-terminal RING-HC domain.


Gene Function

Using an in vitro ubiquitination assay, Takeyama et al. (2003) showed that recombinant DTX3 functioned as a ubiquitin E3 ligase. It showed highest ubiquitination activity in conjunction with the E2 enzyme UBCH5A (UBE2D1; 602961).


Mapping

Hartz (2009) mapped the DTX3 gene to chromosome 12q13.3 based on an alignment of the DTX3 sequence (GenBank AK092085) with the genomic sequence (GRCh37).

REFERENCES

  1. Hartz, P. A. Personal Communication. Baltimore, Md. 11/23/2009.

  2. Takeyama, K., Aguiar, R. C. T., Gu, L., He, C., Freeman, G. J., Kutok, J. L., Aster, J. C., Shipp, M. A. The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity. J. Biol. Chem. 278: 21930-21937, 2003. [PubMed: 12670957] [Full Text: https://doi.org/10.1074/jbc.M301157200]


Creation Date:
Patricia A. Hartz : 11/23/2009

Edit History:
carol : 01/03/2020
mgross : 11/23/2009



NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: May 29, 2024