ANGL4_HUMAN - dbPTM
ANGL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANGL4_HUMAN
UniProt AC Q9BY76
Protein Name Angiopoietin-related protein 4
Gene Name ANGPTL4
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Secreted . Secreted, extracellular space, extracellular matrix. The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (By similarity)..
Protein Description Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorigenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation (By similarity)..
Protein Sequence MSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS
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
6Phosphorylation--MSGAPTAGAALML
--CCCCCHHHHHHHH
36.8722468782
17PhosphorylationALMLCAATAVLLSAQ
HHHHHHHHHHHHHCC
9.9722468782
30PhosphorylationAQGGPVQSKSPRFAS
CCCCCCCCCCCCCCC
35.0246163247
87O-linked_GlycosylationCQGTEGSTDLPLAPE
HCCCCCCCCCCCCCH
53.03OGP
164MethylationAKPARRKRLPEMAQP
HHHHHHCCCHHHCCC
54.38-
177N-linked_GlycosylationQPVDPAHNVSRLHRL
CCCCCCCCHHHHHCC
35.25UniProtKB CARBOHYD
180MethylationDPAHNVSRLHRLPRD
CCCCCHHHHHCCCHH
30.17-
219PhosphorylationFLVNCKMTSDGGWTV
EEEEEEEECCCCEEE
14.7922210691
220PhosphorylationLVNCKMTSDGGWTVI
EEEEEEECCCCEEEE
30.6622210691
234PhosphorylationIQRRHDGSVDFNRPW
EEECCCCCCCCCCCH
25.2722210691
244PhosphorylationFNRPWEAYKAGFGDP
CCCCHHHHHCCCCCC
7.0022210691
315O-linked_GlycosylationVAGQLGATTVPPSGL
CCCCCCCEECCCCCC
26.91OGP
316O-linked_GlycosylationAGQLGATTVPPSGLS
CCCCCCEECCCCCCC
30.40OGP
382PhosphorylationKKGIFWKTWRGRYYP
HCCCCCHHCCCCCCC
15.8128857561

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 ANGL4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANGL4_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 ANGL4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTB_HUMANACTBphysical
22573825
WDR47_HUMANWDR47physical
28514442
NMT2_HUMANNMT2physical
28514442
P20D2_HUMANPM20D2physical
28514442
ADPPT_HUMANAASDHPPTphysical
28514442
NMT1_HUMANNMT1physical
28514442
ITIH2_HUMANITIH2physical
28514442
ARMC8_HUMANARMC8physical
28514442
DNJB4_HUMANDNAJB4physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANGL4_HUMAN

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Related Literatures of Post-Translational Modification

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