| UniProt ID | INHBE_HUMAN | |
|---|---|---|
| UniProt AC | P58166 | |
| Protein Name | Inhibin beta E chain | |
| Gene Name | INHBE | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 350 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.. | |
| Protein Sequence | MRLPDVQLWLVLLWALVRAQGTGSVCPSCGGSKLAPQAERALVLELAKQQILDGLHLTSRPRITHPPPQAALTRALRRLQPGSVAPGNGEEVISFATVTDSTSAYSSLLTFHLSTPRSHHLYHARLWLHVLPTLPGTLCLRIFRWGPRRRRQGSRTLLAEHHITNLGWHTLTLPSSGLRGEKSGVLKLQLDCRPLEGNSTVTGQPRRLLDTAGHQQPFLELKIRANEPGAGRARRRTPTCEPATPLCCRRDHYVDFQELGWRDWILQPEGYQLNYCSGQCPPHLAGSPGIAASFHSAVFSLLKANNPWPASTSCCVPTARRPLSLLYLDHNGNVVKTDVPDMVVEACGCS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 28 | Phosphorylation | GTGSVCPSCGGSKLA CCCCCCCCCCCCCCC | 21.92 | - | |
| 32 | Phosphorylation | VCPSCGGSKLAPQAE CCCCCCCCCCCHHHH | 15.13 | - | |
| 198 | N-linked_Glycosylation | DCRPLEGNSTVTGQP EEEECCCCCCCCCCC | 25.73 | 19159218 | |
| 237 | O-linked_Glycosylation | AGRARRRTPTCEPAT CCCCCCCCCCCCCCC | 22.57 | OGP | |
| 239 | O-linked_Glycosylation | RARRRTPTCEPATPL CCCCCCCCCCCCCCC | 28.96 | OGP | |
| 300 | Phosphorylation | SFHSAVFSLLKANNP HHHHHHHHHHHHCCC | 26.62 | 24719451 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of INHBE_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of INHBE_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of INHBE_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| FST_HUMAN | FST | physical | 12242034 | |
| VHL_HUMAN | VHL | physical | 28514442 | |
| F169A_HUMAN | FAM169A | physical | 28514442 | |
| GRP78_HUMAN | HSPA5 | physical | 28514442 | |
| MYO1F_HUMAN | MYO1F | physical | 28514442 | |
| ANM7_HUMAN | PRMT7 | physical | 28514442 | |
| ANR46_HUMAN | ANKRD46 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198, AND MASSSPECTROMETRY. | |
