UniProt ID | HGF_HUMAN | |
---|---|---|
UniProt AC | P14210 | |
Protein Name | Hepatocyte growth factor | |
Gene Name | HGF | |
Organism | Homo sapiens (Human). | |
Sequence Length | 728 | |
Subcellular Localization | ||
Protein Description | Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.. | |
Protein Sequence | MWVTKLLPALLLQHVLLHLLLLPIAIPYAEGQRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEGSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
32 | Pyrrolidone_carboxylic_acid | AIPYAEGQRKRRNTI HCCCCCCHHHHHCCH | 38.95 | - | |
32 | Pyrrolidone_carboxylic_acid | AIPYAEGQRKRRNTI HCCCCCCHHHHHCCH | 38.95 | 1826837 | |
32 | Pyrrolidone_carboxylic_acid | AIPYAEGQRKRRNTI HCCCCCCHHHHHCCH | 38.95 | 1826837 | |
45 | Phosphorylation | TIHEFKKSAKTTLIK CHHHHHHHCCCEEEE | 35.27 | 18785766 | |
48 | Phosphorylation | EFKKSAKTTLIKIDP HHHHHCCCEEEEECC | 26.93 | - | |
294 | N-linked_Glycosylation | TCADNTMNDTDVPLE ECCCCCCCCCCCCCC | 47.17 | UniProtKB CARBOHYD | |
402 | N-linked_Glycosylation | NGKNYMGNLSQTRSG CCCCCCCCCHHCCCC | 21.71 | UniProtKB CARBOHYD | |
476 | O-linked_Glycosylation | CEGDTTPTIVNLDHP CCCCCCCCEEECCCC | 35.15 | 1482348 | |
522 | Phosphorylation | NKHICGGSLIKESWV CCCCCCCCCHHHHHE | 16.53 | 24719451 | |
531 | Phosphorylation | IKESWVLTARQCFPS HHHHHEEEEHHHCCC | 15.35 | 24719451 | |
566 | N-linked_Glycosylation | EKCKQVLNVSQLVYG HHHHHHEEHHHHHCC | 32.32 | UniProtKB CARBOHYD | |
653 | N-linked_Glycosylation | HRGKVTLNESEICAG CCCCCCCCHHHCCCC | 41.19 | UniProtKB CARBOHYD |
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 HGF_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HGF_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 HGF_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SDC2_HUMAN | SDC2 | physical | 8157651 | |
HGF_HUMAN | HGF | physical | 11597998 | |
MET_HUMAN | MET | physical | 1655405 | |
MEOX2_HUMAN | MEOX2 | physical | 25416956 | |
ATL4_HUMAN | ADAMTSL4 | physical | 25416956 | |
BRCA1_HUMAN | BRCA1 | physical | 25184681 | |
FKBP7_HUMAN | FKBP7 | physical | 26186194 | |
FINC_HUMAN | FN1 | physical | 25241761 | |
FKBP7_HUMAN | FKBP7 | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
608265 | Deafness, autosomal recessive, 39 (DFNB39) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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O-linked Glycosylation | |
Reference | PubMed |
"Hepatocyte growth factor is linked by O-glycosylated oligosaccharideon the alpha chain."; Shimizu N., Hara H., Sogabe T., Sakai H., Ihara I., Inoue H.,Nakamura T., Shimizu S.; Biochem. Biophys. Res. Commun. 189:1329-1335(1992). Cited for: GLYCOSYLATION AT THR-476. |