Basic Information
Gene Structure
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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:0000166 | nucleotide binding | MF |
| GO:0001882 | nucleoside binding | MF |
| GO:0001883 | purine nucleoside binding | MF |
| GO:0003674 | molecular_function | MF |
| GO:0005488 | binding | MF |
| GO:0005525 | GTP binding | MF |
| GO:0005575 | cellular_component | CC |
| GO:0005622 | intracellular anatomical structure | CC |
| GO:0005623 | obsolete cell | CC |
| GO:0005737 | cytoplasm | CC |
| GO:0005794 | Golgi apparatus | CC |
| GO:0006810 | transport | BP |
| GO:0008104 | protein localization | BP |
| GO:0008150 | biological_process | BP |
| GO:0012505 | endomembrane system | CC |
| GO:0015031 | protein transport | BP |
| GO:0015833 | peptide transport | BP |
| GO:0017076 | purine nucleotide binding | MF |
| GO:0019001 | guanyl nucleotide binding | MF |
| GO:0032549 | ribonucleoside binding | MF |
| GO:0032550 | purine ribonucleoside binding | MF |
| GO:0032553 | ribonucleotide binding | MF |
| GO:0032555 | purine ribonucleotide binding | MF |
| GO:0032561 | guanyl ribonucleotide binding | MF |
| GO:0033036 | macromolecule localization | BP |
| GO:0035639 | purine ribonucleoside triphosphate binding | MF |
| GO:0036094 | small molecule binding | MF |
| GO:0042886 | amide transport | BP |
| GO:0043167 | ion binding | MF |
| GO:0043168 | anion binding | MF |
| GO:0043226 | organelle | CC |
| GO:0043227 | membrane-bounded organelle | CC |
| GO:0043229 | intracellular organelle | CC |
| GO:0043231 | intracellular membrane-bounded organelle | CC |
| GO:0044424 | obsolete intracellular part | CC |
| GO:0044444 | obsolete cytoplasmic part | CC |
| GO:0044464 | obsolete cell part | CC |
| GO:0045184 | establishment of protein localization | BP |
| GO:0051179 | localization | BP |
| GO:0051234 | establishment of localization | BP |
| GO:0071702 | organic substance transport | BP |
| GO:0071705 | nitrogen compound transport | BP |
| GO:0097159 | organic cyclic compound binding | MF |
| GO:0097367 | carbohydrate derivative binding | MF |
| GO:1901265 | nucleoside phosphate binding | MF |
| GO:1901363 | heterocyclic compound binding | MF |
| KEGG Term | Name | Description |
|---|---|---|
| map04144 | Endocytosis | Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type. |
| map04144 | Endocytosis | Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type. |

