HGFL_HUMAN - dbPTM
HGFL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HGFL_HUMAN
UniProt AC P26927
Protein Name Hepatocyte growth factor-like protein
Gene Name MST1
Organism Homo sapiens (Human).
Sequence Length 711
Subcellular Localization Secreted.
Protein Description
Protein Sequence MGWLPLLLLLTQCLGVPGQRSPLNDFQVLRGTELQHLLHAVVPGPWQEDVADAEECAGRCGPLMDCRAFHYNVSSHGCQLLPWTQHSPHTRLRRSGRCDLFQKKDYVRTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLRNGLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKSCREAACVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGKFLDQGLDDNYCRNPDGSERPWCYTTDPQIEREFCDLPRCGSEAQPRQEATTVSCFRGKGEGYRGTANTTTAGVPCQRWDAQIPHQHRFTPEKYACKDLRENFCRNPDGSEAPWCFTLRPGMRAAFCYQIRRCTDDVRPQDCYHGAGEQYRGTVSKTRKGVQCQRWSAETPHKPQFTFTSEPHAQLEENFCRNPDGDSHGPWCYTMDPRTPFDYCALRRCADDQPPSILDPPDQVQFEKCGKRVDRLDQRRSKLRVVGGHPGNSPWTVSLRNRQGQHFCGGSLVKEQWILTARQCFSSCHMPLTGYEVWLGTLFQNPQHGEPSLQRVPVAKMVCGPSGSQLVLLKLERSVTLNQRVALICLPPEWYVVPPGTKCEIAGWGETKGTGNDTVLNVALLNVISNQECNIKHRGRVRESEMCTEGLLAPVGACEGDYGGPLACFTHNCWVLEGIIIPNRVCARSRWPAVFTRVSVFVDWIHKVMRLG
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
11PhosphorylationLPLLLLLTQCLGVPG
HHHHHHHHHHHCCCC
19.7324043423
72N-linked_GlycosylationDCRAFHYNVSSHGCQ
CHHHCCEECCCCCEE
20.72UniProtKB CARBOHYD
86N-linked_GlycosylationQLLPWTQHSPHTRLR
EECCCCCCCCCCCCC
35.6010068459
185PhosphorylationFQSCGIKSCREAACV
CCCCCCCHHHHEEEE
19.2421214269
199PhosphorylationVWCNGEEYRGAVDRT
EEECCCEECCCCCCC
15.2821214269
213PhosphorylationTESGRECQRWDLQHP
CCCCCCCCCCCCCCC
44.75-
296N-linked_GlycosylationEGYRGTANTTTAGVP
CCCCCCCCCCCCCCC
37.4816335952
310N-linked_GlycosylationPCQRWDAQIPHQHRF
CCCCCCCCCCCCCCC
47.4716335952
310N-linked_GlycosylationPCQRWDAQIPHQHRF
CCCCCCCCCCCCCCC
47.4716335952
345PhosphorylationSEAPWCFTLRPGMRA
CCCCCEEEECCCCHH
20.7924719451
407O-linked_GlycosylationHKPQFTFTSEPHAQL
CCCCCEECCCCCCHH
29.17OGP
480PhosphorylationDRLDQRRSKLRVVGG
HHHHHHHHCEEEECC
37.93-
551PhosphorylationNPQHGEPSLQRVPVA
CCCCCCCCHHHCCEE
32.6026091039
587UbiquitinationLNQRVALICLPPEWY
CCCEEEEEEECCCEE
1.31-
615N-linked_GlycosylationGETKGTGNDTVLNVA
CCCCCCCCCCHHHHH
41.4319159218
629N-linked_GlycosylationALLNVISNQECNIKH
HHHHHHCCCCCCCCC
30.4619159218
629N-linked_GlycosylationALLNVISNQECNIKH
HHHHHHCCCCCCCCC
30.4619159218

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 HGFL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HGFL_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 HGFL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXO1_HUMANFOXO1physical
18786403
TNNI3_HUMANTNNI3physical
18986304
TNNC1_HUMANTNNC1physical
18986304
TNNT2_HUMANTNNT2physical
18986304

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 HGFL_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-615, AND MASSSPECTROMETRY.
"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-296, AND MASSSPECTROMETRY.

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