ANGPT2

Angiopoietin 2

PDB rendering based on 1z3s.

Available structures
PDB	1Z3S, 1Z3U, 2GY7

Identifiers

Symbols

ANGPT2; AGPT2; ANG2

External IDs

OMIM: 601922 MGI: 1202890 HomoloGene: 22401 GeneCards: ANGPT2 Gene

Gene Ontology
Molecular function	• receptor binding • protein binding • receptor tyrosine kinase binding • metal ion binding
Cellular component	• extracellular region • extracellular space • nucleus • plasma membrane • cell projection
Biological process	• response to hypoxia • signal transduction • multicellular organismal development • germ cell development • blood coagulation • response to radiation • response to mechanical stimulus • response to glucose stimulus • negative regulation of cell-substrate adhesion • response to organic cyclic compound • response to activity • negative regulation of angiogenesis • cell differentiation • organ regeneration • negative regulation of blood vessel endothelial cell migration • positive regulation of angiogenesis • Tie receptor signaling pathway • leukocyte migration • negative regulation of positive chemotaxis • response to protein stimulus • maternal process involved in female pregnancy
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
6.36 – 6.42 Mb

Chr 8:
18.69 – 18.74 Mb

PubMed search

[1]

[2]

Angiopoietin-2 is a protein that in humans is encoded by the ANGPT2 gene.^[1]

Naturally occurring antagonist for both ANGPT1 and TIE2; expressed only at the sites of vascular remodeling; similar to angiopoietin-1^[2]

1 Interactions
2 See also
3 References
4 Further reading

Interactions

ANGPT2 has been shown to interact with TEK tyrosine kinase.^[3]^[4]^[5]

References

^ Cheung AH, Stewart RJ, Marsden PA (Jun 1998). "Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and angiopoietin-2 (ANGPT2): regional localization of the human genes to 8q22.3-q23 and 8p23". Genomics 48 (3): 389–91. doi:10.1006/geno.1997.5207. PMID 9545648.
^ "Entrez Gene: ANGPT2 angiopoietin 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=285.
^ Fiedler, Ulrike; Krissl Tanja, Koidl Stefanie, Weiss Cornelia, Koblizek Thomas, Deutsch Urban, Martiny-Baron Georg, Marmé Dieter, Augustin Hellmut G (Jan. 2003). "Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig-like loop and the epidermal growth factor-like repeats". J. Biol. Chem. (United States) 278 (3): 1721–7. doi:10.1074/jbc.M208550200. ISSN 0021-9258. PMID 12427764.
^ Sato, A; Iwama A, Takakura N, Nishio H, Yancopoulos G D, Suda T (Aug. 1998). "Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells". Int. Immunol. (ENGLAND) 10 (8): 1217–27. doi:10.1093/intimm/10.8.1217. ISSN 0953-8178. PMID 9723709.
^ Maisonpierre, P C; Suri C, Jones P F, Bartunkova S, Wiegand S J, Radziejewski C, Compton D, McClain J, Aldrich T H, Papadopoulos N, Daly T J, Davis S, Sato T N, Yancopoulos G D (Jul. 1997). "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis". Science (UNITED STATES) 277 (5322): 55–60. doi:10.1126/science.277.5322.55. ISSN 0036-8075. PMID 9204896.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Maisonpierre PC, Suri C, Jones PF, et al. (1997). "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis". Science 277 (5322): 55–60. doi:10.1126/science.277.5322.55. PMID 9204896.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Sato A, Iwama A, Takakura N, et al. (1998). "Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells". Int. Immunol. 10 (8): 1217–27. doi:10.1093/intimm/10.8.1217. PMID 9723709.
Tanaka S, Mori M, Sakamoto Y, et al. (1999). "Biologic significance of angiopoietin-2 expression in human hepatocellular carcinoma". J. Clin. Invest. 103 (3): 341–5. doi:10.1172/JCI4891. PMC 407900. PMID 9927494. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=407900.
Valenzuela DM, Griffiths JA, Rojas J, et al. (1999). "Angiopoietins 3 and 4: Diverging gene counterparts in mice and humans". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 1904–9. doi:10.1073/pnas.96.5.1904. PMC 26709. PMID 10051567. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=26709.
Grosios K, Leek JP, Markham AF, et al. (1999). "Assignment of ANGPT4, ANGPT1, and ANGPT2 encoding angiopoietins 4, 1 and 2 to human chromosome bands 20p13, 8q22.3→q23 and 8p23.1, respectively, by in situ hybridization and radiation hybrid mapping". Cytogenet. Cell Genet. 84 (1–2): 118–20. doi:10.1159/000015235. PMID 10343124.
Procopio WN, Pelavin PI, Lee WM, Yeilding NM (1999). "Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity". J. Biol. Chem. 274 (42): 30196–201. doi:10.1074/jbc.274.42.30196. PMID 10514510.
Kim I, Kim JH, Ryu YS, et al. (2000). "Characterization and expression of a novel alternatively spliced human angiopoietin-2". J. Biol. Chem. 275 (24): 18550–6. doi:10.1074/jbc.M910084199. PMID 10766762.
Mezquita J, Mezquita P, Montserrat P, et al. (2000). "Genomic structure and alternative splicing of chicken angiopoietin-2". Biochem. Biophys. Res. Commun. 275 (2): 643–51. doi:10.1006/bbrc.2000.3345. PMID 10964717.
Xu Y, Yu Q (2001). "Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its linker peptide region". J. Biol. Chem. 276 (37): 34990–8. doi:10.1074/jbc.M103661200. PMID 11447223.
Acker T, Beck H, Plate KH (2002). "Cell type specific expression of vascular endothelial growth factor and angiopoietin-1 and -2 suggests an important role of astrocytes in cerebellar vascularization". Mech. Dev. 108 (1–2): 45–57. doi:10.1016/S0925-4773(01)00471-3. PMID 11578860.
Ward EG, Grosios K, Markham AF, Jones PF (2002). "Genomic structures of the human angiopoietins show polymorphism in angiopoietin-2". Cytogenet. Cell Genet. 94 (3–4): 147–54. doi:10.1159/000048807. PMID 11856872.
Huang YQ, Li JJ, Hu L, et al. (2002). "Thrombin induces increased expression and secretion of angiopoietin-2 from human umbilical vein endothelial cells". Blood 99 (5): 1646–50. doi:10.1182/blood.V99.5.1646. PMID 11861279.
Hata K, Udagawa J, Fujiwaki R, et al. (2002). "Expression of angiopoietin-1, angiopoietin-2, and Tie2 genes in normal ovary with corpus luteum and in ovarian cancer". Oncology 62 (4): 340–8. doi:10.1159/000065066. PMID 12138242.
Lin S, Shyu KG, Lee CC, et al. (2002). "Hyperbaric oxygen selectively induces angiopoietin-2 in human umbilical vein endothelial cells". Biochem. Biophys. Res. Commun. 296 (3): 710–5. doi:10.1016/S0006-291X(02)00924-5. PMID 12176040.
Geva E, Ginzinger DG, Zaloudek CJ, et al. (2002). "Human placental vascular development: vasculogenic and angiogenic (branching and nonbranching) transformation is regulated by vascular endothelial growth factor-A, angiopoietin-1, and angiopoietin-2". J. Clin. Endocrinol. Metab. 87 (9): 4213–24. doi:10.1210/jc.2002-020195. PMID 12213874.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Paradis V, Bièche I, Dargère D, et al. (2003). "A quantitative gene expression study suggests a role for angiopoietins in focal nodular hyperplasia". Gastroenterology 124 (3): 651–9. doi:10.1053/gast.2003.50104. PMID 12612904.