ANGP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANGP1_HUMAN
• UniProt AC: Q15389
• Protein Name: Angiopoietin-1
• Gene Name: ANGPT1
• Organism: Homo sapiens (Human).
• Sequence Length: 498
• Subcellular Localization: Secreted.
• Protein Description: Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme..
• Protein Sequence: MTVFLSFAFLAAILTHIGCSNQRRSPENSGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTYIIQELEKQLNRATTNNSVLQKQQLELMDTVHNLVNLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF

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
2	Phosphorylation	------MTVFLSFAF ------CCHHHHHHH	21.69	46163197
6	Phosphorylation	--MTVFLSFAFLAAI --CCHHHHHHHHHHH	11.76	46163191
25	Phosphorylation	GCSNQRRSPENSGRR CCCCCCCCCCCCCCC	38.46	24719451
29	Phosphorylation	QRRSPENSGRRYNRI CCCCCCCCCCCCCCC	31.82	23532336
59	O-linked_Glycosylation	GNCRESTTDQYNTNA CCCCCCCCCHHCCCC	30.31	OGP
92	N-linked_Glycosylation	HLEHVMENYTQWLQK HHHHHHHHHHHHHHH	27.36	UniProtKB CARBOHYD
122	N-linked_Glycosylation	IQQNAVQNHTATMLE HHHHHHHHHHHHHHH	28.07	UniProtKB CARBOHYD
146	Phosphorylation	AEQTRKLTDVETQVL HHHHHCCHHHHHHHH	40.82	21964256
154	N-linked_Glycosylation	DVETQVLNQTSRLEI HHHHHHHCCCCHHHH	44.20	UniProtKB CARBOHYD
181	Phosphorylation	EKQLLQQTNEILKIH HHHHHHHHHHHHHHH	23.12	27251275
186	Acetylation	QQTNEILKIHEKNSL HHHHHHHHHHHHCCH	47.91	20167786
216	Ubiquitination	LDTLKEEKENLQGLV HHHHHHHHHHHHHHH	53.66	-
228	Phosphorylation	GLVTRQTYIIQELEK HHHHHHHHHHHHHHH	6.41	27762562
235	Ubiquitination	YIIQELEKQLNRATT HHHHHHHHHHHHCCC	73.11	-
243	N-linked_Glycosylation	QLNRATTNNSVLQKQ HHHHCCCCCHHHHHH	34.13	UniProtKB CARBOHYD
295	N-linked_Glycosylation	DVYQAGFNKSGIYTI HHHHCCCCCCCEEEE	36.34	UniProtKB CARBOHYD
297	Phosphorylation	YQAGFNKSGIYTIYI HHCCCCCCCEEEEEE	31.37	46163185
300	Phosphorylation	GFNKSGIYTIYINNM CCCCCCEEEEEECCC	7.21	46163209
303	Phosphorylation	KSGIYTIYINNMPEP CCCEEEEEECCCCCC	6.98	50565039
325	Phosphorylation	DVNGGGWTVIQHRED ECCCCCEEEEEECCC	15.82	46163203
386	Phosphorylation	DWEGNRAYSQYDRFH CCCCCCCCCCCCCEE	7.96	7458833
389	Phosphorylation	GNRAYSQYDRFHIGN CCCCCCCCCCEECCC	11.80	7458845
401	Phosphorylation	IGNEKQNYRLYLKGH CCCCCCCEEEEEECC	10.25	50565047
404	Phosphorylation	EKQNYRLYLKGHTGT CCCCEEEEEECCCCC	9.43	46163215
406	Ubiquitination	QNYRLYLKGHTGTAG CCEEEEEECCCCCCC	34.78	-
409	Phosphorylation	RLYLKGHTGTAGKQS EEEEECCCCCCCCCE	44.91	50565055
411	Phosphorylation	YLKGHTGTAGKQSSL EEECCCCCCCCCEEE	33.13	50565063
414	Ubiquitination	GHTGTAGKQSSLILH CCCCCCCCCEEEEEE	44.54	-
485	Phosphorylation	YFKGPSYSLRSTTMM EECCCCCCCCCEEEE	22.95	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ANGP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANGP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ANGP1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ANGP1_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.