EDIL3_HUMAN - dbPTM
EDIL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDIL3_HUMAN
UniProt AC O43854
Protein Name EGF-like repeat and discoidin I-like domain-containing protein 3
Gene Name EDIL3
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization Secreted.
Protein Description Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development..
Protein Sequence MKRSVAVWLLVGLSLGVPQFGKGDICDPNPCENGGICLPGLADGSFSCECPDGFTDPNCSSVVEVASDEEEPTSAGPCTPNPCHNGGTCEISEAYRGDTFIGYVCKCPRGFNGIHCQHNINECEVEPCKNGGICTDLVANYSCECPGEFMGRNCQYKCSGPLGIEGGIISNQQITASSTHRALFGLQKWYPYYARLNKKGLINAWTAAENDRWPWIQINLQRKMRVTGVITQGAKRIGSPEYIKSYKIAYSNDGKTWAMYKVKGTNEDMVFRGNIDNNTPYANSFTPPIKAQYVRLYPQVCRRHCTLRMELLGCELSGCSEPLGMKSGHIQDYQITASSIFRTLNMDMFTWEPRKARLDKQGKVNAWTSGHNDQSQWLQVDLLVPTKVTGIITQGAKDFGHVQFVGSYKLAYSNDGEHWTVYQDEKQRKDKVFQGNFDNDTHRKNVIDPPIYARHIRILPWSWYGRITLRSELLGCTEEE
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
73O-linked_GlycosylationASDEEEPTSAGPCTP
CCCCCCCCCCCCCCC
34.1922601780
88O-linked_GlycosylationNPCHNGGTCEISEAY
CCCCCCCEEEECCCC
14.3622601780
99PhosphorylationSEAYRGDTFIGYVCK
CCCCCCCCEEEEEEC
21.7024719451
103PhosphorylationRGDTFIGYVCKCPRG
CCCCEEEEEECCCCC
9.6224719451
140N-linked_GlycosylationICTDLVANYSCECPG
CCCHHHCCEECCCCC
23.0522601780
234 (in isoform 2)Ubiquitination-6.5321890473
234UbiquitinationTGVITQGAKRIGSPE
EEEEECCCCCCCCHH
6.5321890473
2352-HydroxyisobutyrylationGVITQGAKRIGSPEY
EEEECCCCCCCCHHH
51.91-
237UbiquitinationITQGAKRIGSPEYIK
EECCCCCCCCHHHHH
6.7123000965
244UbiquitinationIGSPEYIKSYKIAYS
CCCHHHHHEEEEEEC
47.0021890473
244 (in isoform 1)Ubiquitination-47.0021890473
244UbiquitinationIGSPEYIKSYKIAYS
CCCHHHHHEEEEEEC
47.0023000965
245UbiquitinationGSPEYIKSYKIAYSN
CCHHHHHEEEEEECC
23.3123000965
246PhosphorylationSPEYIKSYKIAYSND
CHHHHHEEEEEECCC
11.04-
247UbiquitinationPEYIKSYKIAYSNDG
HHHHHEEEEEECCCC
28.1323000965
250PhosphorylationIKSYKIAYSNDGKTW
HHEEEEEECCCCCEE
16.1022817900
251UbiquitinationKSYKIAYSNDGKTWA
HEEEEEECCCCCEEE
21.3023000965
255UbiquitinationIAYSNDGKTWAMYKV
EEECCCCCEEEEEEE
43.7023000965
260PhosphorylationDGKTWAMYKVKGTNE
CCCEEEEEEEECCCC
12.6022817900
261UbiquitinationGKTWAMYKVKGTNED
CCEEEEEEEECCCCC
25.1223000965
336O-linked_GlycosylationHIQDYQITASSIFRT
CCCCEEEEHHHHHHH
12.6455829663
339PhosphorylationDYQITASSIFRTLNM
CEEEEHHHHHHHHCC
24.2324719451
452PhosphorylationNVIDPPIYARHIRIL
CCCCCCCCCCEEEEE
11.89-

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 EDIL3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EDIL3_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 EDIL3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRFE_HUMANTFphysical
26186194
ITB5_HUMANITGB5physical
26186194
AGRL1_HUMANLPHN1physical
26186194
ITB5_HUMANITGB5physical
28514442
ZN496_HUMANZNF496physical
28514442
TRFE_HUMANTFphysical
28514442
AGRL1_HUMANLPHN1physical
28514442
ITAV_HUMANITGAVphysical
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 EDIL3_HUMAN

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Related Literatures of Post-Translational Modification

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