Type |
Details |
Score |
GXD Expression |
Probe: |
MGI:6842968 |
Assay Type: |
Immunohistochemistry |
Annotation Date: |
2022-01-05 |
Strength: |
Weak |
Sex: |
Female |
Emaps: |
EMAPS:1796222 |
Pattern: |
Regionally restricted |
Stage: |
TS22 |
Assay Id: |
MGI:6845039 |
Age: |
embryonic day 14.5 |
Image: |
1Ab |
Note: |
Expression is in the somatic cells around the cysts. |
Specimen Label: |
1Ab |
Detected: |
true |
Specimen Num: |
2 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5309467 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Strong |
Sex: |
Not Specified |
Emaps: |
EMAPS:1768022 |
Pattern: |
Regionally restricted |
Stage: |
TS22 |
Assay Id: |
MGI:5422835 |
Age: |
embryonic day 14.5 |
Image: |
MH2907; Specimen C3979 |
Note: |
Expression was strong in the skull (base and vault). |
Specimen Label: |
MH2907; Specimen C3979 |
Detected: |
true |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:4416687 |
Assay Type: |
RNA in situ |
Annotation Date: |
2010-09-14 |
Strength: |
Moderate |
Sex: |
Not Specified |
Emaps: |
EMAPS:1791823 |
Pattern: |
Regionally restricted |
Stage: |
TS23 |
Assay Id: |
MGI:4824180 |
Age: |
embryonic day 14.5 |
Image: |
euxassay_010645_12 |
|
Specimen Label: |
euxassay_010645_12 |
Detected: |
true |
Specimen Num: |
12 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:4416687 |
Assay Type: |
RNA in situ |
Annotation Date: |
2010-09-14 |
Strength: |
Moderate |
Sex: |
Not Specified |
Emaps: |
EMAPS:1791823 |
Pattern: |
Regionally restricted |
Stage: |
TS23 |
Assay Id: |
MGI:4824180 |
Age: |
embryonic day 14.5 |
Image: |
euxassay_010645_13 |
|
Specimen Label: |
euxassay_010645_13 |
Detected: |
true |
Specimen Num: |
13 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:4416687 |
Assay Type: |
RNA in situ |
Annotation Date: |
2010-09-14 |
Strength: |
Moderate |
Sex: |
Not Specified |
Emaps: |
EMAPS:1791823 |
Pattern: |
Regionally restricted |
Stage: |
TS23 |
Assay Id: |
MGI:4824180 |
Age: |
embryonic day 14.5 |
Image: |
euxassay_010645_16 |
|
Specimen Label: |
euxassay_010645_16 |
Detected: |
true |
Specimen Num: |
16 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:5309467 |
Assay Type: |
RNA in situ |
Annotation Date: |
2012-06-12 |
Strength: |
Strong |
Sex: |
Not Specified |
Emaps: |
EMAPS:2672022 |
Pattern: |
Regionally restricted |
Stage: |
TS22 |
Assay Id: |
MGI:5422835 |
Age: |
embryonic day 14.5 |
Image: |
MH2907; Specimen C3979 |
Note: |
Expression was strong in whisker follicle. |
Specimen Label: |
MH2907; Specimen C3979 |
Detected: |
true |
Specimen Num: |
1 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:6842968 |
Assay Type: |
Immunohistochemistry |
Annotation Date: |
2022-01-05 |
Strength: |
Present |
Sex: |
Female |
Emaps: |
EMAPS:3792826 |
Pattern: |
Regionally restricted |
Stage: |
TS26 |
Assay Id: |
MGI:6845039 |
Age: |
embryonic day 19.5 |
Image: |
1Ae |
Note: |
Expression is in the oocyte cytoplasm of the primordial follicles in the medulla. |
Specimen Label: |
1Ae |
Detected: |
true |
Specimen Num: |
5 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:6842968 |
Assay Type: |
Immunohistochemistry |
Annotation Date: |
2022-01-05 |
Strength: |
Present |
Sex: |
Female |
Emaps: |
EMAPS:3792726 |
Pattern: |
Regionally restricted |
Stage: |
TS26 |
Assay Id: |
MGI:6845039 |
Age: |
embryonic day 19.5 |
Image: |
1Ae |
Note: |
Expression is in the nucleus of oocytes within the cysts in the cortex of the ovary. |
Specimen Label: |
1Ae |
Detected: |
true |
Specimen Num: |
5 |
|
•
•
•
•
•
|
GXD Expression |
Probe: |
MGI:6441933 |
Assay Type: |
Immunohistochemistry |
Annotation Date: |
2020-07-20 |
Strength: |
Absent |
Sex: |
Female |
Emaps: |
EMAPS:3803228 |
|
Stage: |
TS28 |
Assay Id: |
MGI:6442555 |
Age: |
postnatal adult |
|
|
Specimen Label: |
2b |
Detected: |
false |
Specimen Num: |
2 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
Year: |
2000 |
Journal: |
Database Release |
Title: |
Entrez Gene Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
The Jackson Laboratory Mouse Radiation Hybrid Database |
Year: |
2004 |
Journal: |
Database Release |
Title: |
Mouse T31 Radiation Hybrid Data 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: |
Lennon G |
Year: |
1999 |
Journal: |
Database Download |
Title: |
WashU-HHMI Mouse EST Project |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2). |
|
|
|
|
•
•
•
•
•
|
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: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Strömstedt M |
Year: |
1996 |
Journal: |
Arch Biochem Biophys |
Title: |
The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. |
Volume: |
329 |
Issue: |
1 |
Pages: |
73-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhu J |
Year: |
2014 |
Journal: |
J Lipid Res |
Title: |
FoxO4 interacts with the sterol regulatory factor SREBP2 and the hypoxia inducible factor HIF2α at the CYP51 promoter. |
Volume: |
55 |
Issue: |
3 |
Pages: |
431-42 |
|
•
•
•
•
•
|
HT Experiment |
Series Id: |
GSE58271 |
Experiment Type: |
transcription profiling by array |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
|
•
•
•
•
•
|
Publication |
First Author: |
Rozman D |
Year: |
1996 |
Journal: |
Arch Biochem Biophys |
Title: |
The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family. |
Volume: |
333 |
Issue: |
2 |
Pages: |
466-74 |
|
•
•
•
•
•
|
Publication |
First Author: |
Debeljak N |
Year: |
2000 |
Journal: |
Pflugers Arch |
Title: |
Molecular cloning and partial characterisation of the mouse Cyp51 cDNA. |
Volume: |
439 |
Issue: |
3 Suppl |
Pages: |
R7-8 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
503
 |
Fragment?: |
false |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Tamboli IY |
Year: |
2008 |
Journal: |
J Neurosci |
Title: |
Loss of gamma-secretase function impairs endocytosis of lipoprotein particles and membrane cholesterol homeostasis. |
Volume: |
28 |
Issue: |
46 |
Pages: |
12097-106 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gatticchi L |
Year: |
2020 |
Journal: |
Front Cell Dev Biol |
Title: |
Tm7sf2 Disruption Alters Radial Gene Positioning in Mouse Liver Leading to Metabolic Defects and Diabetes Characteristics. |
Volume: |
8 |
|
Pages: |
592573 |
|
•
•
•
•
•
|
Publication |
First Author: |
Shu L |
Year: |
2019 |
Journal: |
Endocrinology |
Title: |
Prenatal Bisphenol A Exposure in Mice Induces Multitissue Multiomics Disruptions Linking to Cardiometabolic Disorders. |
Volume: |
160 |
Issue: |
2 |
Pages: |
409-429 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nelson DR |
Year: |
1996 |
Journal: |
Pharmacogenetics |
Title: |
P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. |
Volume: |
6 |
Issue: |
1 |
Pages: |
1-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rozman D |
Year: |
1996 |
Journal: |
Genomics |
Title: |
Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. |
Volume: |
38 |
Issue: |
3 |
Pages: |
371-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Leamy LJ |
Year: |
2013 |
Journal: |
Bone |
Title: |
Quantitative trait loci for bone mineral density and femoral morphology in an advanced intercross population of mice. |
Volume: |
55 |
Issue: |
1 |
Pages: |
222-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hara S |
Year: |
1994 |
Journal: |
J Biol Chem |
Title: |
Isolation and molecular cloning of prostacyclin synthase from bovine endothelial cells. |
Volume: |
269 |
Issue: |
31 |
Pages: |
19897-903 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reaction chemistry. In mammals, these proteins are found primarily in microsomes of hepatocytes and other cell types, where they oxidise steroids, fatty acids and xenobiotics, and are important for the detoxification and clearance of various compounds, as well as for hormone synthesis and breakdown, cholesterol synthesis and vitamin D metabolism. In plants, these proteins are important for the biosynthesis of several compounds such as hormones, defensive compounds and fatty acids. In bacteria, they are important for several metabolic processes, such as the biosynthesis of antibiotic erythromycin in Saccharopolyspora erythraea (Streptomyces erythraeus).Cytochrome P450 enzymes use haem to oxidise their substrates, using protons derived from NADH or NADPH to split the oxygen so a single atom can be added to a substrate. They also require electrons, which they receive from a variety of redox partners. In certain cases, cytochrome P450 can be fused to its redox partner to produce a bi-functional protein, such as with P450BM-3 from Bacillus megaterium [], which has haem and flavin domains.Organisms produce many different cytochrome P450 enzymes (at least 58 in humans), which together with alternative splicing can provide a wide array of enzymes with different substrate and tissue specificities. Individual cytochrome P450 proteins follow the nomenclature: CYP, followed by a number (family), then a letter (subfamily), and another number (protein); e.g. CYP3A4 is the fourth protein in family 3, subfamily A. In general, family members should share >40% identity, while subfamily members should share >55% identity.Cytochrome P450 proteins can also be grouped by two different schemes. One scheme was based on a taxonomic split: class I (prokaryotic/mitochondrial) and class II (eukaryotic microsomes). The other scheme was based on the number of components in the system: class B (3-components) and class E (2-components). These classes merge to a certain degree. Most prokaryotes and mitochondria (and fungal CYP55) have 3-component systems (class I/class B) - a FAD-containing flavoprotein (NAD(P)H-dependent reductase), an iron-sulphur protein and P450. Most eukaryotic microsomes have 2-component systems (class II/class E) - NADPH:P450 reductase (FAD and FMN-containing flavoprotein) and P450. There are exceptions to this scheme, such as 1-component systems that resemble class E enzymes [, , ]. The class E enzymes can be further subdivided into five sequence clusters, groups I-V, each of which may contain more than one cytochrome P450 family (eg, CYP1 and CYP2 are both found in group I). The divergence of the cytochrome P450 superfamily into B- and E-classes, and further divergence into stable clusters within the E-class, appears to be very ancient, occurring before the appearance of eukaryotes.This entry represents class E cytochrome P450 proteins that fall into sequence cluster group IV. Group IV comprises the CYP7 (cholesterol 7-alpha-hydroxylase) and CYP51 (lanosterol 14-alpha-demethylase) families, which show significant sequence similarity even though there is no apparent functional resemblance. The CYP8 (prostacyclin synthase) family also falls into this group, and shows high sequence similarity to CYP7 members []. Proteins required in the biosynthesis of fungal mycotoxins are also included: cytochrome P450 monooxygenases gloO and gloP from Glarea lozoyensis are required for synthesis of lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Hüttel W |
Year: |
2017 |
Journal: |
Z Naturforsch C |
Title: |
Structural diversity in echinocandin biosynthesis: the impact of oxidation steps and approaches toward an evolutionary explanation. |
Volume: |
72 |
Issue: |
1-2 |
Pages: |
1-20 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
470
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
500
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
507
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
501
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
509
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
470
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
507
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
421
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
168
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
404
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
507
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
500
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
404
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
503
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
512
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
497
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
524
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
497
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
437
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
290
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
175
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
321
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
86
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
503
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
McLean KJ |
Year: |
2005 |
Journal: |
Biochem Soc Trans |
Title: |
Biodiversity of cytochrome P450 redox systems. |
Volume: |
33 |
Issue: |
Pt 4 |
Pages: |
796-801 |
|
•
•
•
•
•
|
Publication |
First Author: |
Munro AW |
Year: |
2007 |
Journal: |
Biochim Biophys Acta |
Title: |
Cytochrome P450--redox partner fusion enzymes. |
Volume: |
1770 |
Issue: |
3 |
Pages: |
345-59 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nelson DR |
Year: |
2004 |
Journal: |
Pharmacogenetics |
Title: |
Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. |
Volume: |
14 |
Issue: |
1 |
Pages: |
1-18 |
|
•
•
•
•
•
|
Publication |
First Author: |
Degtyarenko KN |
Year: |
1995 |
Journal: |
Protein Eng |
Title: |
Structural domains of P450-containing monooxygenase systems. |
Volume: |
8 |
Issue: |
8 |
Pages: |
737-47 |
|
•
•
•
•
•
|