HGF_HUMAN - dbPTM
HGF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
32Pyrrolidone_carboxylic_acidAIPYAEGQRKRRNTI
HCCCCCCHHHHHCCH
38.95-
32Pyrrolidone_carboxylic_acidAIPYAEGQRKRRNTI
HCCCCCCHHHHHCCH
38.951826837
32Pyrrolidone_carboxylic_acidAIPYAEGQRKRRNTI
HCCCCCCHHHHHCCH
38.951826837
45PhosphorylationTIHEFKKSAKTTLIK
CHHHHHHHCCCEEEE
35.2718785766
48PhosphorylationEFKKSAKTTLIKIDP
HHHHHCCCEEEEECC
26.93-
294N-linked_GlycosylationTCADNTMNDTDVPLE
ECCCCCCCCCCCCCC
47.17UniProtKB CARBOHYD
402N-linked_GlycosylationNGKNYMGNLSQTRSG
CCCCCCCCCHHCCCC
21.71UniProtKB CARBOHYD
476O-linked_GlycosylationCEGDTTPTIVNLDHP
CCCCCCCCEEECCCC
35.151482348
522PhosphorylationNKHICGGSLIKESWV
CCCCCCCCCHHHHHE
16.5324719451
531PhosphorylationIKESWVLTARQCFPS
HHHHHEEEEHHHCCC
15.3524719451
566N-linked_GlycosylationEKCKQVLNVSQLVYG
HHHHHHEEHHHHHCC
32.32UniProtKB CARBOHYD
653N-linked_GlycosylationHRGKVTLNESEICAG
CCCCCCCCHHHCCCC
41.19UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HGF_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDC2_HUMANSDC2physical
8157651
HGF_HUMANHGFphysical
11597998
MET_HUMANMETphysical
1655405
MEOX2_HUMANMEOX2physical
25416956
ATL4_HUMANADAMTSL4physical
25416956
BRCA1_HUMANBRCA1physical
25184681
FKBP7_HUMANFKBP7physical
26186194
FINC_HUMANFN1physical
25241761
FKBP7_HUMANFKBP7physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608265Deafness, autosomal recessive, 39 (DFNB39)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HGF_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"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.

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