Type |
Details |
Score |
Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
Year: |
2000 |
Journal: |
Database Release |
Title: |
Entrez Gene Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Allen Institute for Brain Science |
Year: |
2004 |
Journal: |
Allen Institute |
Title: |
Allen Brain Atlas: mouse riboprobes |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Consensus CDS project |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Lee JC |
Year: |
2002 |
Journal: |
J Cell Biol |
Title: |
DEDD regulates degradation of intermediate filaments during apoptosis. |
Volume: |
158 |
Issue: |
6 |
Pages: |
1051-66 |
|
•
•
•
•
•
|
Allele |
Name: |
death effector domain-containing; endonuclease-mediated mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhan Y |
Year: |
2002 |
Journal: |
Cell Death Differ |
Title: |
Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC. |
Volume: |
9 |
Issue: |
4 |
Pages: |
439-47 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
168
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Roth W |
Year: |
2002 |
Journal: |
J Biol Chem |
Title: |
Identification and characterization of DEDD2, a death effector domain-containing protein. |
Volume: |
277 |
Issue: |
9 |
Pages: |
7501-8 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes death effector domain-containing proteins, DEDD and DEDD2. DEDD is a scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis []. DEDD2 is involved in the regulation of nuclear events mediated by the extrinsic apoptosis pathway []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
210
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
142
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Couté Y |
Year: |
2008 |
Journal: |
Mol Cell Proteomics |
Title: |
ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesis. |
Volume: |
7 |
Issue: |
3 |
Pages: |
546-59 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Interferon-stimulated 20kDa exonuclease-like 2 (ISG20L2) is a 3' to 5' exoribonuclease involved in the processing of the 12 S precursor rRNA during ribosome biogenesis. Its N-terminal half promotes nucleolar localization and its C-terminal half contains an exonuclease domain responsible for the exoribonuclease activity. The exonuclease domain belongs to the DEDDh group of the DEDD superfamily []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Schäfer IB |
Year: |
2014 |
Journal: |
Nat Struct Mol Biol |
Title: |
The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase. |
Volume: |
21 |
Issue: |
7 |
Pages: |
591-8 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The poly(A)-specific nuclease (PAN) is a deadenylating enzyme involved in cytoplasmic mRNA turnover and consists of two subunits, PAN2 and PAN3, which form a conserved complex acting in the initial trimming of poly(A) tails, a process followed by the processive action of CCR4-NOT complex. PAN2 is the catalytic subunit and has two independent structural units, the N-terminal assembly unit which engages in a bipartite interaction with PAN3 dimers and the C-terminal catalytic unit [, , ]. The C-terminal unit contains the ubiquitin C-terminal hydrolase (UCH) domain, represented in this entry, and a RNase domain of the DEDD superfamily () [, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Sur R |
Year: |
2005 |
Journal: |
Biochem J |
Title: |
Vanishin is a novel ubiquitinylated death-effector domain protein that blocks ERK activation. |
Volume: |
387 |
Issue: |
Pt 2 |
Pages: |
315-24 |
|
•
•
•
•
•
|
Publication |
First Author: |
Viswanathan P |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
Mouse CAF1 can function as a processive deadenylase/3'-5'-exonuclease in vitro but in yeast the deadenylase function of CAF1 is not required for mRNA poly(A) removal. |
Volume: |
279 |
Issue: |
23 |
Pages: |
23988-95 |
|
•
•
•
•
•
|
Publication |
First Author: |
Temme C |
Year: |
2004 |
Journal: |
EMBO J |
Title: |
A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila. |
Volume: |
23 |
Issue: |
14 |
Pages: |
2862-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bianchin C |
Year: |
2005 |
Journal: |
RNA |
Title: |
Conservation of the deadenylase activity of proteins of the Caf1 family in human. |
Volume: |
11 |
Issue: |
4 |
Pages: |
487-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
He GJ |
Year: |
2013 |
Journal: |
Biochim Biophys Acta |
Title: |
Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis. |
Volume: |
1834 |
Issue: |
6 |
Pages: |
1089-98 |
|
•
•
•
•
•
|
Publication |
First Author: |
Reverdatto SV |
Year: |
2004 |
Journal: |
RNA |
Title: |
mRNA deadenylation by PARN is essential for embryogenesis in higher plants. |
Volume: |
10 |
Issue: |
8 |
Pages: |
1200-14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cevher MA |
Year: |
2010 |
Journal: |
EMBO J |
Title: |
Nuclear deadenylation/polyadenylation factors regulate 3' processing in response to DNA damage. |
Volume: |
29 |
Issue: |
10 |
Pages: |
1674-87 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The major pathways of mRNA turnover in eukaryotes initiate with shortening of the poly(A) tail. CAF1 (also known as CCR4-associated factor 1) is an RNase of the DEDD superfamily, and a subunit of the CCR4-NOT complex that mediates 3' to 5' mRNA deadenylation [, ]. In yeast, CAF1 () is also known as POP2, and encodes a critical component of the major cytoplasmic deadenylase [, ]. It is required for normal mRNA deadenylation in vivoand localises to the cytoplasm. CAF1 copurifies with a CCR4-dependent poly(A)-specific exonuclease activity. The crystal structure of Saccharomyces cerevisiae POP2 has been resolved [].Some members of this family contain a single-stranded nucleic acid binding domain, R3H, such aspoly(A)-specific ribonuclease (PARN), which also contains an RRM domain []. PARN is only conserved in vertebrates and may be important in regulated deadenylation such as early developmentand DNA damage response [, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Thore S |
Year: |
2003 |
Journal: |
EMBO Rep |
Title: |
X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex. |
Volume: |
4 |
Issue: |
12 |
Pages: |
1150-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Daugeron MC |
Year: |
2001 |
Journal: |
Nucleic Acids Res |
Title: |
The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation. |
Volume: |
29 |
Issue: |
12 |
Pages: |
2448-55 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
318
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
330
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
234
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
318
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
155
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
318
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
178
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Boeck R |
Year: |
1996 |
Journal: |
J Biol Chem |
Title: |
The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity. |
Volume: |
271 |
Issue: |
1 |
Pages: |
432-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jonas S |
Year: |
2014 |
Journal: |
Nat Struct Mol Biol |
Title: |
An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay. |
Volume: |
21 |
Issue: |
7 |
Pages: |
599-608 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
285
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
292
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
531
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
188
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
248
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
104
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
82
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
285
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
206
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
315
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
261
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
189
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
285
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Tucker M |
Year: |
2001 |
Journal: |
Cell |
Title: |
The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. |
Volume: |
104 |
Issue: |
3 |
Pages: |
377-86 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
368
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
368
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
209
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
511
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
424
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1200
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
624
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
624
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
624
 |
Fragment?: |
false |
|
•
•
•
•
•
|