Basic Information
Gene Structure
upstream:
Get Sequence
Domain
| Database | EntryID | E-Value | Start | end | InterPro ID | Description |
|---|
Regulation&Interaction
Annotation
Orthologous Group
| Orthologous ID | Species Number | All hits in PereRegDB | Hits of this species | Orthologous Detail |
|---|
Expression Profile
| DataSet | Number of Samples expressed(TPM>1) | Mean | Min | Max | Standard deviation(SD) | Coeffcient variation(CV) |
|---|
Pathway
| GO Term | Description | GO Category |
|---|---|---|
| GO:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005634 | nucleus | CC |
| GO:0005652 | nuclear lamina | CC |
| GO:0005694 | chromosome | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0006996 | organelle organization | BP |
| GO:0006997 | nucleus organization | BP |
| GO:0008150 | biological_process | BP |
| GO:0009507 | chloroplast | CC |
| GO:0009536 | plastid | CC |
| GO:0009987 | cellular process | BP |
| GO:0010369 | chromocenter | CC |
| GO:0016043 | cellular component organization | BP |
| GO:0031974 | membrane-enclosed lumen | CC |
| GO:0031981 | nuclear lumen | CC |
| GO:0032535 | regulation of cellular component size | BP |
| GO:0034399 | nuclear periphery | CC |
| GO:0043226 | organelle | CC |
| GO:0043227 | membrane-bounded organelle | CC |
| GO:0043228 | non-membrane-bounded organelle | CC |
| GO:0043229 | intracellular organelle | CC |
| GO:0043231 | intracellular membrane-bounded organelle | CC |
| GO:0043232 | intracellular non-membrane-bounded organelle | CC |
| GO:0043233 | organelle lumen | CC |
| GO:0044422 | obsolete organelle part | CC |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044427 | obsolete chromosomal part | CC |
| GO:0044428 | obsolete nuclear part | CC |
| GO:0044444 | obsolete cytoplasmic part | CC |
| GO:0044446 | obsolete intracellular organelle part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0065007 | biological regulation | BP |
| GO:0065008 | regulation of biological quality | BP |
| GO:0070013 | intracellular organelle lumen | CC |
| GO:0071840 | cellular component organization or biogenesis | BP |
| GO:0090066 | regulation of anatomical structure size | BP |
| GO:0097298 | regulation of nucleus size | BP |
| GO:0098687 | chromosomal region | CC |
| KEGG Term | Name | Description |
|---|---|---|
| map01110 | Biosynthesis of secondary metabolites | - |
| map01100 | Metabolic pathways | - |
| map00966 | Glucosinolate biosynthesis | Glucosinolates are biologically active secondary metabolites found in Brassicaceae (mustard family) and related families.These compounds are genetically variable within plant species and used as natural pesticides, such as against insect herbivores. All glucosinolates share a common structure consisting of a beta-thioglucose moiety, a sulfonated oxime moiety, and a variable aglycone side chain derived from an alpha-amino acid. Genes encoding glucosinolate biosynthetic enzymes have been identified in Arabidopsis thaliana by genetic polymorphisms and loss-of-function mutations. This map shows examples of side chain elongation in methionine-derived glucosinolates and the core pathway for biosynthesis of glucosinolates from amino acids. |
| map00770 | Pantothenate and CoA biosynthesis | - |
| map00290 | Valine, leucine and isoleucine biosynthesis | - |
| map00280 | Valine, leucine and isoleucine degradation | - |
| map00270 | Cysteine and methionine metabolism | Cysteine and methionine are sulfur-containing amino acids. Cysteine is synthesized from serine through different pathways in different organism groups. In bacteria and plants, cysteine is converted from serine (via acetylserine) by transfer of hydrogen sulfide [MD:M00021]. In animals, methionine-derived homocysteine is used as sulfur source and its condensation product with serine (cystathionine) is converted to cysteine [MD:M00338]. Cysteine is metabolized to pyruvate in multiple routes. Methionine is an essential amino acid, which animals cannot synthesize. In bacteria and plants, methionine is synthesized from aspartate [MD:M00017]. S-Adenosylmethionine (SAM), synthesized from methionine and ATP, is a methyl group donor in many important transfer reactions including DNA methylation for regulation of gene expression. SAM may also be used to regenerate methionine in the methionine salvage pathway [MD:M00034]. |

