ANGP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANGP2_HUMAN
• UniProt AC: O15123
• Protein Name: Angiopoietin-2
• Gene Name: ANGPT2
• Organism: Homo sapiens (Human).
• Sequence Length: 496
• Subcellular Localization: Secreted.
• Protein Description: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal..
• Protein Sequence: MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF

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
25	Phosphorylation	AYNNFRKSMDSIGKK HHHHHHHHHHHHCCC	24.46	23403867
28	Phosphorylation	NFRKSMDSIGKKQYQ HHHHHHHHHCCCEEE	25.30	23403867
89	N-linked_Glycosylation	VLENIMENNTQWLMK HHHHHHHCCHHHHHH	39.20	UniProtKB CARBOHYD
119	N-linked_Glycosylation	IQQNAVQNQTAVMIE HHHHHHHCCCEEEEE	34.27	UniProtKB CARBOHYD
133	N-linked_Glycosylation	EIGTNLLNQTAEQTR EEHHHHHHHHHHHHH	40.08	UniProtKB CARBOHYD
151	N-linked_Glycosylation	DVEAQVLNQTTRLEL HHHHHHHCCCCHHHH	37.99	UniProtKB CARBOHYD
208	Phosphorylation	KHIIQLQSIKEEKDQ HHEEEEHHHHHHHHH	44.19	166220839
236	Phosphorylation	ELEKKIVTATVNNSV HHHHHHHHHHCCHHH	21.78	23532336
240	N-linked_Glycosylation	KIVTATVNNSVLQKQ HHHHHHCCHHHHHHH	30.61	UniProtKB CARBOHYD
242	Phosphorylation	VTATVNNSVLQKQQH HHHHCCHHHHHHHHH	20.99	69101583
294	Phosphorylation	VFKSGHTTNGIYTLT HHHCCCCCCEEEEEE	26.27	25003641
299	Phosphorylation	HTTNGIYTLTFPNST CCCCEEEEEECCCCH	19.87	25003641
304	N-linked_Glycosylation	IYTLTFPNSTEEIKA EEEEECCCCHHHHHH	58.32	UniProtKB CARBOHYD
359	Ubiquitination	EYWLGNEFVSQLTNQ CEEECHHHHHHHHHC	8.11	21963094
360	Ubiquitination	YWLGNEFVSQLTNQQ EEECHHHHHHHHHCC	2.65	21963094
411	Ubiquitination	KGLTGTAGKISSISQ ECCCCCCCCCCCCCC	27.89	21963094
412	Ubiquitination	GLTGTAGKISSISQP CCCCCCCCCCCCCCC	36.63	21963094
482	Phosphorylation	YYWKGSGYSLKATTM EEECCCCCCCEEEEE	16.72	2033135
483	Phosphorylation	YWKGSGYSLKATTMM EECCCCCCCEEEEEE	27.24	24719451

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

Oops, there are no upstream regulatory protein records of ANGP2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANGP2_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 ANGP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIE2_HUMAN	TEK	physical	25237190
ITB1_HUMAN	ITGB1	physical	25237190
ITA5_HUMAN	ITGA5	physical	25237190
ITB1_HUMAN	ITGB1	physical	16424009
ITA5_HUMAN	ITGA5	physical	16424009
ITAV_HUMAN	ITGAV	physical	16424009
ZZEF1_HUMAN	ZZEF1	physical	28514442
FBX28_HUMAN	FBXO28	physical	28514442
HECD3_HUMAN	HECTD3	physical	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.