| UniProt ID | LIF_HUMAN | |
|---|---|---|
| UniProt AC | P15018 | |
| Protein Name | Leukemia inhibitory factor | |
| Gene Name | LIF | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 202 | |
| Subcellular Localization | Secreted. | |
| Protein Description | LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.. | |
| Protein Sequence | MKVLAAGVVPLLLVLHWKHGAGSPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFHANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF | |
| 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 |
|---|---|---|---|---|---|
| 31 | N-linked_Glycosylation | PLPITPVNATCAIRH CCCCCCCCCEEEECC | 30.64 | 8489250 | |
| 56 | N-linked_Glycosylation | RSQLAQLNGSANALF HHHHHHHCCCHHEEE | 30.23 | 8489250 | |
| 85 | N-linked_Glycosylation | LDKLCGPNVTDFPPF HHHHCCCCCCCCCCC | 34.31 | 8489250 | |
| 95 | N-linked_Glycosylation | DFPPFHANGTEKAKL CCCCCCCCCCHHHHH | 49.72 | 8489250 | |
| 118 | N-linked_Glycosylation | YLGTSLGNITRDQKI HHCCCCCCCCCCCCC | 37.44 | 8489250 | |
| 138 | N-linked_Glycosylation | LSLHSKLNATADILR HHHHHHHHHHHHHHH | 38.69 | 8489250 |
| 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 LIF_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LIF_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 LIF_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of LIF_HUMAN !! | ||||
| 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 |
| "Glycosylation pattern and disulfide assignments of recombinant humandifferentiation-stimulating factor."; Schmelzer C.H., Harris R.J., Butler D., Yedinak C.M., Wagner K.L.,Burton L.E.; Arch. Biochem. Biophys. 302:484-489(1993). Cited for: DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-31; ASN-56; ASN-85; ASN-95;ASN-118 AND ASN-138. | |
