| Type |
Details |
Score |
| Genotype |
| Symbol: |
Slc17a1/Slc17a1 |
| Background: |
C57BL/6NJ-Slc17a1/Mmjax |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Slc25a42/Slc25a42<+> |
| Background: |
C57BL/6NJ-Slc25a42/Mmjax |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Socs2/Socs2 |
| Background: |
C57BL/6NTac-Socs2/H |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Stimate/Stimate |
| Background: |
C57BL/6N-Stimate/Wtsi |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Taf5/Taf5<+> |
| Background: |
C57BL/6NJ-Taf5/Mmjax |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tent5c/Tent5c<+> |
| Background: |
C57BL/6N-Tent5c/Wtsi |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tecrl/Tecrl |
| Background: |
C57BL/6NJ-Tecrl/Mmjax |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tfpi2/Tfpi2 |
| Background: |
C57BL/6NTac-Tfpi2/Kmpc |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tm2d3/Tm2d3<+> |
| Background: |
C57BL/6NJ-Tm2d3/Mmjax |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tubb2a/Tubb2a |
| Background: |
C57BL/6NJ-Tubb2a/J |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Vps51/Vps51<+> |
| Background: |
C57BL/6N-Vps51/Wtsi |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Wdr24/Wdr24<+> |
| Background: |
C57BL/6N-Wdr24/J |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Zfp146/Zfp146 |
| Background: |
C57BL/6NJ-Zfp146/Mmjax |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Zfp711/Zfp711 |
| Background: |
C57BL/6NJ-Zfp711/J |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Zftraf1/Zftraf1 |
| Background: |
C57BL/6NTac-Zftraf1/H |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Znfx1/Znfx1 |
| Background: |
C57BL/6NJ-Znfx1/Mmjax |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Allele |
| Name: |
DnaJ heat shock protein family (Hsp40) member A1; targeted mutation 1.1, Velocigene |
| Allele Type: |
Targeted |
| Attribute String: |
Null/knockout, Reporter |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Limd1/Limd1 |
| Background: |
C57BL/6NTac-Limd1/H |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tm4sf5/Tm4sf5 |
| Background: |
C57BL/6NTac-Tm4sf5/Kmpc |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fan C |
| Year: |
1995 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. |
| Volume: |
92 |
| Issue: |
4 |
| Pages: |
1172-6 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
T6SS bacteria employ toxic effectors to inhibit rival cells and concurrently use effector cognate immunity proteins to protect their sibling cells. The effector and immunity pairs (E-I pairs) endow the bacteria with a great advantage in niche competition. This is the C-terminal domain of Tli4. The Tle cognate immunity proteins (Tlis) can directly disable the transported Tle protein and thereby mediate the self-protection process. The Tle-Tli effector-immunity (E-I) pairs confer substantial advantage to the donor cell during interbacterial competition. Tli4 displays a two-domain structure, in which a large lobe and a small lobe form a crab claw-like conformation. Tli4 uses this crab claw to grasp the cap domain of Tle4, especially the lid2 region, which prevents the interfacial activation of Tle4 and thus causes enzymatic dysfunction of Tle4. Structural comparison indicates similarity between this C-terminal domain of Tli4 and Tsi3, which is the cognate immunity protein of the effector protein Tse3 in P. aeruginosa PDB:4n7s []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The ATP-grasp superfamily currently includes 17 groups of enzymes, catalyzing ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule []. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate. For example, DD-ligase transfers phosphate from ATP to D-alanine on the first step of catalysis. On the second step the resulting acylphosphate is attacked by a second D-alanine to produce a DD dipeptide following phosphate elimination [].The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site []. The fold is characterised by two α-β subdomains that grasp the ATP molecule between them. Each subdomain provides a variable loop that formspart of the active site, with regions from other domains also contributing to the active site, even though these other domains are not conserved between the various ATP-grasp enzymes []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The ATP-grasp superfamily currently includes 17 groups of enzymes, catalysing ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule []. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate. For example, DD-ligase transfers phosphate from ATP to D-alanine on the first step of catalysis. On the second step the resulting acylphosphate is attacked by a second D-alanine to produce a DD dipeptide following phosphate elimination [].The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site []. The fold is characterised by two α-β subdomains that grasp the ATP molecule between them. Each subdomain provides a variable loop that forms a part of the active site, completed by region of other domains not conserved between the various ATP-grasp enzymes [].The ATP-grasp domain represented by this entry is found primarily in succinyl-CoA synthetases (). |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fan C |
| Year: |
1994 |
| Journal: |
Science |
| Title: |
Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. |
| Volume: |
266 |
| Issue: |
5184 |
| Pages: |
439-43 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This family represents PurK, N5-carboxyaminoimidazole ribonucleotide (N5_CAIR) synthetase, which catalyzes the conversion of 5-aminoimidazole ribonucleotide (AIR), ATP, and bicarbonate to N5-CAIR, ADP, and Pi. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. PurK belongs to the ATP grasp superfamily of C-N ligase enzymes. Each subunit of PurK is composed of three domains (A, B, and C). The B domain contains a flexible, glycine-rich loop (B loop, T123-G130) that is disordered in the sulphate-PurK structure and becomes ordered in the MgADP-PurK structure. MgADP is wedged between the B and C domains, as with all members of the ATP grasp superfamily. Other enzymes in this superfamily contain a conserved Omega loop proposed to interact with the B loop, define the specificity of their nonnucleotide substrate, and protect the acyl phosphate intermediate formed from this substrate. PurK contains a minimal Omega loopwithout conserved residues. In the reaction catalyzed by PurK, carboxyphosphate is the putative acyl phosphate intermediate. The sulphate of the sulphate ion-liganded PurK interacts electrostatically with Arg 242 and the backbone amide group of Asn 245, components of the J loop of the C domain. This sulphate may reveal the location of the carboxyphosphate binding site. Conserved residues within the C terminus of the C domain define a pocket that is proposed to bind AIR in collaboration with an N-terminal strand loop helix motif in the A domain (P loop, G8-L1). The P loop is proposed to bind the phosphate of AIR on the basis of similar binding sites observed in PurN and PurE and proposed in PurD and PurT, four other enzymes in the purine pathway []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Takeda Y |
| Year: |
2003 |
| Journal: |
J Neurobiol |
| Title: |
Impaired motor coordination in mice lacking neural recognition molecule NB-3 of the contactin/F3 subgroup. |
| Volume: |
56 |
| Issue: |
3 |
| Pages: |
252-65 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Goldshmit Y |
| Year: |
2004 |
| Journal: |
J Neurosci |
| Title: |
Axonal regeneration and lack of astrocytic gliosis in EphA4-deficient mice. |
| Volume: |
24 |
| Issue: |
45 |
| Pages: |
10064-73 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nevrivy DJ |
| Year: |
2000 |
| Journal: |
J Biol Chem |
| Title: |
Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. |
| Volume: |
275 |
| Issue: |
22 |
| Pages: |
16827-36 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kleven GA |
| Year: |
2013 |
| Journal: |
Eur J Neurosci |
| Title: |
Prenatal ontogeny of the dopamine-dependent neurobehavioral phenotype in Pitx3-deficient mice. |
| Volume: |
37 |
| Issue: |
10 |
| Pages: |
1564-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chevalier NR |
| Year: |
2021 |
| Journal: |
Commun Biol |
| Title: |
A neural crest cell isotropic-to-nematic phase transition in the developing mammalian gut. |
| Volume: |
4 |
| Issue: |
1 |
| Pages: |
770 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Blaney CE |
| Year: |
2013 |
| Journal: |
Behav Brain Res |
| Title: |
Maternal genotype influences behavioral development of 3×Tg-AD mouse pups. |
| Volume: |
252 |
|
| Pages: |
40-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Traboulsi H |
| Year: |
2014 |
| Journal: |
PLoS Genet |
| Title: |
Dynamic partnership between TFIIH, PGC-1α and SIRT1 is impaired in trichothiodystrophy. |
| Volume: |
10 |
| Issue: |
10 |
| Pages: |
e1004732 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Stamenkovic V |
| Year: |
2017 |
| Journal: |
Behav Brain Res |
| Title: |
Enriched environment alters the behavioral profile of tenascin-C deficient mice. |
| Volume: |
331 |
|
| Pages: |
241-253 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cordell PA |
| Year: |
2010 |
| Journal: |
Blood |
| Title: |
Association of coagulation factor XIII-A with Golgi proteins within monocyte-macrophages: implications for subcellular trafficking and secretion. |
| Volume: |
115 |
| Issue: |
13 |
| Pages: |
2674-81 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fleming SM |
| Year: |
2004 |
| Journal: |
J Neurosci |
| Title: |
Early and progressive sensorimotor anomalies in mice overexpressing wild-type human alpha-synuclein. |
| Volume: |
24 |
| Issue: |
42 |
| Pages: |
9434-40 |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Allele |
| Name: |
large tumor suppressor; endonuclease-mediated mutation 1, Harwell |
| Allele Type: |
Endonuclease-mediated |
| Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
| Allele |
| Name: |
solute carrier family 30 (zinc transporter), member 4; endonuclease-mediated mutation 1, The Centre for Phenogenomics |
| Allele Type: |
Endonuclease-mediated |
| Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Acox1/Acox1 |
| Background: |
C57BL/6N-Acox1/Bay |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Dnaja1/Dnaja1<+> |
| Background: |
C57BL/6N-Dnaja1/J |
| Zygosity: |
ht |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
451
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
446
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
451
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
317
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
451
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
351
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
431
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
431
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
283
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
446
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Murzin AG |
| Year: |
1996 |
| Journal: |
Curr Opin Struct Biol |
| Title: |
Structural classification of proteins: new superfamilies. |
| Volume: |
6 |
| Issue: |
3 |
| Pages: |
386-94 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Alonso C |
| Year: |
2023 |
| Journal: |
Neuropharmacology |
| Title: |
Disease-modifying effects of cannabidiol, β-caryophyllene and their combination in Syn1-Cre/Scn1a(WT/A1783V) mice, a preclinical model of Dravet syndrome. |
| Volume: |
237 |
|
| Pages: |
109602 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Becker MI |
| Year: |
2020 |
| Journal: |
J Neurophysiol |
| Title: |
Online control of reach accuracy in mice. |
| Volume: |
124 |
| Issue: |
6 |
| Pages: |
1637-1655 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fenrich KK |
| Year: |
2015 |
| Journal: |
Behav Brain Res |
| Title: |
Improved single pellet grasping using automated ad libitum full-time training robot. |
| Volume: |
281 |
|
| Pages: |
137-48 |
|
•
•
•
•
•
|
| 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: |
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 |
|
•
•
•
•
•
|