MFGM_HUMAN - dbPTM
MFGM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MFGM_HUMAN
UniProt AC Q08431
Protein Name Lactadherin
Gene Name MFGE8
Organism Homo sapiens (Human).
Sequence Length 387
Subcellular Localization Membrane
Peripheral membrane protein . Secreted .
Protein Description Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.; Medin is the main constituent of aortic medial amyloid..
Protein Sequence MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGMENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
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
42PhosphorylationGGLCEEISQEVRGDV
CCHHHHHHHHHCCCC
24.4624670416
59UbiquitinationSYTCTCLKGYAGNHC
CCCEEEEECCCCCCC
52.61-
69UbiquitinationAGNHCETKCVEPLGM
CCCCCCCEEEEECCC
17.62-
84PhosphorylationENGNIANSQIAASSV
CCCCCCCHHHHHHHE
17.5928450419
89PhosphorylationANSQIAASSVRVTFL
CCHHHHHHHEEEEEE
21.9722468782
90PhosphorylationNSQIAASSVRVTFLG
CHHHHHHHEEEEEEC
14.8228450419
94PhosphorylationAASSVRVTFLGLQHW
HHHHEEEEEECCHHH
11.5422468782
112UbiquitinationLARLNRAGMVNAWTP
HHHCCCCCCEEEECC
19.82-
133UbiquitinationPWIQVNLLRRMWVTG
CCHHHHHHHHHHHHH
2.48-
156UbiquitinationLASHEYLKAFKVAYS
HHCHHHHHHHEEEHH
51.3721890473
156UbiquitinationLASHEYLKAFKVAYS
HHCHHHHHHHEEEHH
51.3721890473
156UbiquitinationLASHEYLKAFKVAYS
HHCHHHHHHHEEEHH
51.3721890473
177UbiquitinationDFIHDVNKKHKEFVG
EEEEECCHHHHHHHC
56.98-
228N-linked_GlycosylationELLGCELNGCANPLG
HHHCCEECCCCCCCC
22.6218780401
238N-linked_GlycosylationANPLGLKNNSIPDKQ
CCCCCCCCCCCCCCE
53.1518780401
247PhosphorylationSIPDKQITASSSYKT
CCCCCEEECCCCCCE
20.2820166139
249PhosphorylationPDKQITASSSYKTWG
CCCEEECCCCCCEEE
15.9220166139
250PhosphorylationDKQITASSSYKTWGL
CCEEECCCCCCEEEE
34.9120166139
252PhosphorylationQITASSSYKTWGLHL
EEECCCCCCEEEEEE
17.8720166139
261PhosphorylationTWGLHLFSWNPSYAR
EEEEEEEEECHHHEE
32.1026091039
265PhosphorylationHLFSWNPSYARLDKQ
EEEEECHHHEEECCC
28.3626091039
266PhosphorylationLFSWNPSYARLDKQG
EEEECHHHEEECCCC
9.3026091039
325N-linked_GlycosylationSYKVAYSNDSANWTE
EEEEEECCCCCCCCE
34.2818780401
329N-linked_GlycosylationAYSNDSANWTEYQDP
EECCCCCCCCEECCC
50.5918780401
350N-linked_GlycosylationIFPGNWDNHSHKKNL
CCCCCCCCCCCCCCC
30.1218780401

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
42SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MFGM_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 MFGM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YTHD1_HUMANYTHDF1physical
26186194
ITB5_HUMANITGB5physical
26186194
ITB5_HUMANITGB5physical
28514442
YTHD1_HUMANYTHDF1physical
28514442

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 MFGM_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228; ASN-238; ASN-325;ASN-329 AND ASN-350, AND MASS SPECTROMETRY.

TOP