dbPTM

HGFA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HGFA_HUMAN
UniProt AC	Q04756
Protein Name	Hepatocyte growth factor activator
Gene Name	HGFAC
Organism	Homo sapiens (Human).
Sequence Length	655
Subcellular Localization	Secreted. Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.
Protein Description	Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form..
Protein Sequence	MGRWAWVPSPWPPPGLGPFLLLLLLLLLLPRGFQPQPGGNRTESPEPNATATPAIPTILVTSVTSETPATSAPEAEGPQSGGLPPPPRAVPSSSSPQAQALTEDGRPCRFPFRYGGRMLHACTSEGSAHRKWCATTHNYDRDRAWGYCVEATPPPGGPAALDPCASGPCLNGGSCSNTQDPQSYHCSCPRAFTGKDCGTEKCFDETRYEYLEGGDRWARVRQGHVEQCECFGGRTWCEGTRHTACLSSPCLNGGTCHLIVATGTTVCACPPGFAGRLCNIEPDERCFLGNGTGYRGVASTSASGLSCLAWNSDLLYQELHVDSVGAAALLGLGPHAYCRNPDNDERPWCYVVKDSALSWEYCRLEACESLTRVQLSPDLLATLPEPASPGRQACGRRHKKRTFLRPRIIGGSSSLPGSHPWLAAIYIGDSFCAGSLVHTCWVVSAAHCFSHSPPRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPYTLYSVFNPSDHDLVLIRLKKKGDRCATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVADHKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWINDRIRPPRRLVAPS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	N-linked_Glycosylation	RTESPEPNATATPAI CCCCCCCCCCCCCCC	48.54	UniProtKB CARBOHYD
70	O-linked_Glycosylation	VTSETPATSAPEAEG ECCCCCCCCCCCCCC	26.99	OGP
92	O-linked_Glycosylation	PPPRAVPSSSSPQAQ CCCCCCCCCCCHHHH	35.93	OGP
94	O-linked_Glycosylation	PRAVPSSSSPQAQAL CCCCCCCCCHHHHHC	50.83	OGP
95	O-linked_Glycosylation	RAVPSSSSPQAQALT CCCCCCCCHHHHHCC	23.99	OGP
113	Methylation	RPCRFPFRYGGRMLH CCCCCCCEECCEEEE	29.44	30759923
130	Methylation	TSEGSAHRKWCATTH CCCCCHHCEECCCCC	33.61	30759929
290	N-linked_Glycosylation	DERCFLGNGTGYRGV CCCEECCCCCCCCCC	47.18	18638581
382	O-linked_Glycosylation	LSPDLLATLPEPASP CCHHHHHCCCCCCCC	42.70	OGP
468	N-linked_Glycosylation	VLGQHFFNRTTDVTQ EEEEHHHCCCCCHHH	39.17	18077410
475	N-linked_Glycosylation	NRTTDVTQTFGIEKY CCCCCHHHHCCCCCC	34.38	16335952
482	Phosphorylation	QTFGIEKYIPYTLYS HHCCCCCCCCEEEEE	8.37	22817900
485	Phosphorylation	GIEKYIPYTLYSVFN CCCCCCCEEEEECCC	10.38	22817900
492	N-linked_Glycosylation	YTLYSVFNPSDHDLV EEEEECCCCCCCCEE	32.77	UniProtKB CARBOHYD
546	N-linked_Glycosylation	GWGHLDENVSGYSSS CCCCCCCCCCCCCHH	32.68	UniProtKB CARBOHYD
569	Phosphorylation	VADHKCSSPEVYGAD HHCCCCCCCHHCCCC	34.25	24505115

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 HGFA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HGFA_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 HGFA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HGFA_HUMAN !!

Drug and Disease Associations

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.

Regulatory Network of HGFA_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural insight into distinct mechanisms of protease inhibition byantibodies."; Wu Y., Eigenbrot C., Liang W.C., Stawicki S., Shia S., Fan B.,Ganesan R., Lipari M.T., Kirchhofer D.; Proc. Natl. Acad. Sci. U.S.A. 104:19784-19789(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 373-655 IN COMPLEX WITHANTIBODY, GLYCOSYLATION AT ASN-468, AND DISULFIDE BONDS.	18077410 [Abstract]
"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-468, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-468, AND MASSSPECTROMETRY.	16335952 [Abstract]