GoPubMed Proteins lists recent and important papers and reviews for
proteins. Page last changed on 19 Dec 2016.
Praja1, RING-H2 motif containing
Praja1, PJA1
This gene encodes an enzyme that has E2-dependent E3 ubiquitin-protein ligase activity. This enzyme belongs to a class of ubiquitin ligases that include a RING finger motif, and it can interact with the E2 ubiquitin-conjugating enzyme UbcH5B. This gene is located in an area of chromosome X where several X-linked mental retardation disorders have been associated, and it has also been found as part of a contiguous gene deletion associated with craniofrontonasal syndrome, though a direct link to any disorder has yet to be demonstrated. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2010] (from
NCBI)
Sponsored links
Top mentioned proteins:
Ephrin-B1, OPHN1, Ubiquitin, ACID, lacZ
Papers on
Praja1
The roles of MAGE-D1 in the neuronal functions and pathology of the central nervous system.
Review
Nagoya, Japan. In Rev Neurosci, 2012
MAGE-D1 regulates Dlx-dependent migration-related transcription by binding to necdin or praja-1.
Xq12q13.1 microduplication encompassing the EFNB1 gene in a boy with congenital diaphragmatic hernia.
Lille, France. In Eur J Med Genet, 2011
We report on a microduplication identified by array-CGH (comparative genomic hybridization) including five contiguous genes (OPHN1, YIPF6, STARD8, EFNB1 and PJA1) and arising de novo in a male presenting a congenital diaphragmatic hernia (CDH).
Duplication of the EFNB1 gene in familial hypertelorism: imbalance in ephrin-B1 expression and abnormal phenotypes in humans and mice.
Oxford, United Kingdom. In Hum Mutat, 2011
DNA sequencing of EFNB1 was normal, but further analysis revealed a duplication of 937 kb including EFNB1 and two flanking genes: PJA1 and STARD8.
Protein microarrays for the identification of praja1 e3 ubiquitin ligase substrates.
GeneRIF
United States. In Cell Biochem Biophys, 2011
Data provide clues into novel aspects of Praja1 function.
PRAJA1 is a ubiquitin ligase for the polycomb repressive complex 2 proteins.
GeneRIF
Haifa, Israel. In Biochem Biophys Res Commun, 2011
these results suggest a role for PRAJA1 in regulating the level of PRC2 by targeting its free subunits for Ub-mediated proteasomal degradation.
Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome.
Magdeburg, Germany. In Clin Genet, 2007
In one patient the deletion interval includes the genes for oligophrenin-1 (OPHN1 [MIM 300127]) and praja 1 (PJA1 [MIM 300420]).
Susceptibility of ammonia-oxidizing bacteria to nitrification inhibitors.
Machida, Japan. In Z Naturforsch C, 2003
PJA1 and Nitrosolobus multiformis ATCC25196, were 77.85, 91.53 and 90.29, respectively.
A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1.
GeneRIF
Ōbu, Japan. In J Biol Chem, 2002
A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1.
PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain.
GeneRIF
Frederick, United States. In Genomics, 2002
Involved in protein ubiquitination in the brain. Candidate gene for X-linked mental retardation.
Expansion of hepatic and hematopoietic stem cells utilizing mouse embryonic liver explants.
Washington, D.C., United States. In Cell Transplant, 2001
Under these conditions, we also demonstrate the role of a novel marker PRAJA-1 to identify hepatic stem cells and transitional hepatocytes.
Praja1, a novel gene encoding a RING-H2 motif in mouse development.
Washington, D.C., United States. In Oncogene, 1997
As part of a cloning strategy to identify genes involved in early mouse liver development we have isolated Praja1, a gene with similar sequences to the Drosophila melanogaster gene goliath (gl) which is involved in the fate of mesodermal cells ultimately forming gut musculatures, fat body, and the heart.
Effect of the transcription start region of the herpes simplex virus type 1 latency-associated transcript promoter on expression of productively infected neurons in vivo.
In J Virol, 1994
We have confirmed these data by showing that an ICP4-expressing plasmid will downregulate lacZ expression from a plasmid containing the LAT promoter and transcription start site (pJA1) and does not downregulate lacZ expression from a plasmid in which the start site has been mutagenized (pWAG15).
