Type |
Details |
Score |
Publication |
First Author: |
Knejzlík Z |
Year: |
2022 |
Journal: |
FEBS J |
Title: |
The mycobacterial guaB1 gene encodes a guanosine 5'-monophosphate reductase with a cystathionine-β-synthase domain. |
|
|
|
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
In Methanosarcina acetivorans, MA1821 is a L-aspartate semialdehyde sulfurtransferase required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis [, ]. It contains two C-terminal cystathionine beta-synthase (CBS) domains. The CBS domains bind S-adenosyl-l-methionine (SAM) and 5'-methylthioadenosine (MTA), which induce a conformational change consistent with regulatory function. Another protein in the same pathway, MA1822, is involved in the reduction of the disulfide formed in MA1821 during the conversion of Asa (aspartate semialdehyde) to Hcy [, ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This family of proteins restricted to the high GC Gram-positive bacteria includes GMP reductase from Mycobacterium smegmatis (GUAB1), which is involved in the purine-salvage pathway. This protein is composed of two domains: a catalytic domain with a TIM barrel structure and another that folds as a typical Bateman domain composed of two CBS domains (cystathionine-beta-synthase domain, CBS, ), which are essential for the NADPH-dependent conversion of GMP to IMP []. |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
GSE54286 |
Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
GSE54287 |
Experiment Type: |
RNA-Seq |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus pahari |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus pahari |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus spretus |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus spretus |
|
•
•
•
•
•
|
Publication |
First Author: |
Guo D |
Year: |
2005 |
Journal: |
Mol Pain |
Title: |
Physical interaction and functional coupling between ACDP4 and the intracellular ion chaperone COX11, an implication of the role of ACDP4 in essential metal ion transport and homeostasis. |
Volume: |
1 |
|
Pages: |
15 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chandran U |
Year: |
2016 |
Journal: |
Biol Reprod |
Title: |
Expression of Cnnm1 and Its Association with Stemness, Cell Cycle, and Differentiation in Spermatogenic Cells in Mouse Testis. |
Volume: |
95 |
Issue: |
1 |
Pages: |
7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang C |
Year: |
2000 |
Journal: |
GenBank Submission |
Title: |
Mus musculus ancient conserved domain protein 3 (Adcp3) mRNA, compkete cds |
|
|
Pages: |
AF216964 |
|
•
•
•
•
•
|
Publication |
First Author: |
Meredith TC |
Year: |
2006 |
Journal: |
Biochem J |
Title: |
Characterization of Escherichia coli D-arabinose 5-phosphate isomerase encoded by kpsF: implications for group 2 capsule biosynthesis. |
Volume: |
395 |
Issue: |
2 |
Pages: |
427-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bohmann K |
Year: |
1995 |
Journal: |
J Cell Biol |
Title: |
Mutational analysis of p80 coilin indicates a functional interaction between coiled bodies and the nucleolus. |
Volume: |
131 |
Issue: |
4 |
Pages: |
817-31 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hebert MD |
Year: |
2000 |
Journal: |
Mol Biol Cell |
Title: |
Self-association of coilin reveals a common theme in nuclear body localization. |
Volume: |
11 |
Issue: |
12 |
Pages: |
4159-71 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Coilin is a nuclear phosphoprotein that concentrates within Cajal bodies (CBs) and has a role in small nuclear ribonucleoprotein (snRNP) biogenesis []. Coilin also acts to repress polymerase I activity in response to cisplatin-induced DNA damage, which could indicate a link between the DNA damage response and the inhibition of rRNA synthesis [].Conservation at the amino acid level is highest within coilin's N- and C-termini. The first N-terminal 92-amino acid domain have been shown to self-interact and to be essential for proper targeting of coilin to CBs [, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Maclean KN |
Year: |
2019 |
Journal: |
FASEB J |
Title: |
Taurine alleviates repression of betaine-homocysteine S-methyltransferase and significantly improves the efficacy of long-term betaine treatment in a mouse model of cystathionine β-synthase-deficient homocystinuria. |
Volume: |
33 |
Issue: |
5 |
Pages: |
6339-6353 |
|
•
•
•
•
•
|
Publication |
First Author: |
Marechal D |
Year: |
2015 |
Journal: |
PLoS One |
Title: |
Dosage of the Abcg1-U2af1 region modifies locomotor and cognitive deficits observed in the Tc1 mouse model of Down syndrome. |
Volume: |
10 |
Issue: |
2 |
Pages: |
e0115302 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rauch BJ |
Year: |
2014 |
Journal: |
Mol Microbiol |
Title: |
Novel proteins for homocysteine biosynthesis in anaerobic microorganisms. |
Volume: |
94 |
Issue: |
6 |
Pages: |
1330-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Allen KD |
Year: |
2015 |
Journal: |
Biochemistry |
Title: |
Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea. |
Volume: |
54 |
Issue: |
20 |
Pages: |
3129-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Resch CT |
Year: |
2010 |
Journal: |
Biochemistry |
Title: |
The putative Na+/H+ antiporter of Vibrio cholerae, Vc-NhaP2, mediates the specific K+/H+ exchange in vivo. |
Volume: |
49 |
Issue: |
11 |
Pages: |
2520-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang CY |
Year: |
2004 |
Journal: |
BMC Genomics |
Title: |
Molecular cloning and characterization of the mouse Acdp gene family. |
Volume: |
5 |
Issue: |
1 |
Pages: |
7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Fanourgakis G |
Year: |
2016 |
Journal: |
PLoS Genet |
Title: |
Chromatoid Body Protein TDRD6 Supports Long 3' UTR Triggered Nonsense Mediated mRNA Decay. |
Volume: |
12 |
Issue: |
5 |
Pages: |
e1005857 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yabuta Y |
Year: |
2011 |
Journal: |
J Cell Biol |
Title: |
TDRD5 is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis in mice. |
Volume: |
192 |
Issue: |
5 |
Pages: |
781-95 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kabil O |
Year: |
2016 |
Journal: |
J Biol Chem |
Title: |
Heme-dependent Metabolite Switching Regulates H2S Synthesis in Response to Endoplasmic Reticulum (ER) Stress. |
Volume: |
291 |
Issue: |
32 |
Pages: |
16418-16423 |
|
•
•
•
•
•
|
Publication |
First Author: |
Anania C |
Year: |
2022 |
Journal: |
Nat Genet |
Title: |
In vivo dissection of a clustered-CTCF domain boundary reveals developmental principles of regulatory insulation. |
Volume: |
54 |
Issue: |
7 |
Pages: |
1026-1036 |
|
•
•
•
•
•
|
Pseudogene |
Type: |
pseudogene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
570
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
573
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
572
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Gilder AS |
Year: |
2011 |
Journal: |
Mol Biol Cell |
Title: |
Coilin participates in the suppression of RNA polymerase I in response to cisplatin-induced DNA damage. |
Volume: |
22 |
Issue: |
7 |
Pages: |
1070-9 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Synonym(s): Inosine-5'-monophosphate dehydrogenase, Inosinic acid dehydrogenase; Synonym(s): Guanosine 5'-monophosphate oxidoreductase This entry contains two related enzymes: IMP dehydrogenase and GMP reductase. These enzymes adopt a TIM barrel structure.IMP dehydrogenase () (IMPDH) catalyses the rate-limiting reaction of de novoGTP biosynthesis, the NAD-dependent reduction of IMP into XMP [].Inosine 5-phosphate + NAD++ H2O = xanthosine 5-phosphate + NADHIMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans []. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.GMP reductase () catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [].NADPH + guanosine 5-phosphate = NADP++ inosine 5-phosphate + NH3It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotides. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Conserved_site |
Description: |
Synonym(s): Inosine-5'-monophosphate dehydrogenase, Inosinic acid dehydrogenase; Synonym(s): Guanosine 5'-monophosphate oxidoreductase This entry contains two related enzymes: IMP dehydrogenase and GMP reductase. These enzymes adopt a TIM barrel structure.IMP dehydrogenase () (IMPDH) catalyses the rate-limiting reaction of de novoGTP biosynthesis, the NAD-dependent reduction of IMP into XMP [].Inosine 5-phosphate + NAD++ H2O = xanthosine 5-phosphate + NADHIMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans []. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.GMP reductase () catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [].NADPH + guanosine 5-phosphate = NADP++ inosine 5-phosphate + NH3It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotides. |
|
•
•
•
•
•
|
Publication |
First Author: |
Andrews SC |
Year: |
1988 |
Journal: |
Biochem J |
Title: |
Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12. |
Volume: |
255 |
Issue: |
1 |
Pages: |
35-43 |
|
•
•
•
•
•
|
Publication |
First Author: |
Collart FR |
Year: |
1988 |
Journal: |
J Biol Chem |
Title: |
Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs. |
Volume: |
263 |
Issue: |
30 |
Pages: |
15769-72 |
|
•
•
•
•
•
|
Publication |
First Author: |
Natsumeda Y |
Year: |
1990 |
Journal: |
J Biol Chem |
Title: |
Two distinct cDNAs for human IMP dehydrogenase. |
Volume: |
265 |
Issue: |
9 |
Pages: |
5292-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gibson MM |
Year: |
1991 |
Journal: |
Mol Microbiol |
Title: |
Magnesium transport in Salmonella typhimurium: the influence of new mutations conferring Co2+ resistance on the CorA Mg2+ transport system. |
Volume: |
5 |
Issue: |
11 |
Pages: |
2753-62 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|