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Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
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EGLN2 / PHD1
egl-9 family hypoxia-inducible factor 2
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferencially recognized via a LXXLAP motif.
Gene Name:
egl-9 family hypoxia-inducible factor 2
Synonyms:
EGLN2, EIT6, EGL nine (C.elegans) homolog 2, Egl nine homolog 2, HPH-1, HPH-3, Estrogen-induced tag 6, PHD1, HIF-PH1, HIF-prolyl hydroxylase 1, HIFPH1
OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. Baek JH, Mahon PC, Oh J, Kelly B, Krishnamachary B, Pearson M, Chan DA, Giaccia AJ, Semenza GL. Molecular cell. 2005 17:503-12. (IP; Human)
[PubMed:15721254]
2
Activation of hypoxia-inducible factors in hyperoxia through prolyl 4-hydroxylase blockade in cells and explants of primate lung. Asikainen TM, Schneider BK, Waleh NS, Clyman RI, Ho WB, Flippin LA, Gnzler V, White CW. Proceedings of the National Academy of Sciences of the United States of America. 2005 102:10212-7. (WB; Human)
[PubMed:16009933]
[PMC:PMC1177409]
3
Dynamic HIF1A regulation during human placental development. Ietta F, Wu Y, Winter J, Xu J, Wang J, Post M, Caniggia I. Biology of reproduction. 2006 75:112-21. (WB; Human)
[PubMed:16611863]
4
Transforming growth factor beta1 induces hypoxia-inducible factor-1 stabilization through selective inhibition of PHD2 expression. McMahon S, Charbonneau M, Grandmont S, Richard DE, Dubois CM. The Journal of biological chemistry. 2006 281:24171-81. (WB; Human)
[PubMed:16815840]
5
Expression and actions of HIF prolyl-4-hydroxylase in the rat kidneys. Li N, Yi F, Sundy CM, Chen L, Hilliker ML, Donley DK, Muldoon DB, Li PL. American journal of physiology. Renal physiology. 2007 292:F207-16. (WB, IHC-P; Rat)
[PubMed:16885149]
6
Hypoxia-inducible factors in the first trimester human lung. Groenman F, Rutter M, Caniggia I, Tibboel D, Post M. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 2007 55:355-63.
[PubMed:17189520]
7
Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins. Takeda K, Aguila HL, Parikh NS, Li X, Lamothe K, Duan LJ, Takeda H, Lee FS, Fong GH. Blood. 2008 111:3229-35.
[PubMed:18056838]
[PMC:PMC2265459]
8
The von Hippel-Lindau tumor suppressor protein and Egl-9-Type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress. Mikhaylova O, Ignacak ML, Barankiewicz TJ, Harbaugh SV, Yi Y, Maxwell PH, Schneider M, Van Geyte K, Carmeliet P, Revelo MP, Wyder M, Greis KD, Meller J, Czyzyk-Krzeska MF. Molecular and cellular biology. 2008 28:2701-17.
[PubMed:18285459]
[PMC:PMC2293119]
9
The biphasic role of the hypoxia-inducible factor prolyl-4-hydroxylase, PHD2, in modulating tumor-forming potential. Lee, Lynd JD, O'Reilly S, Kiupel M, McCormick JJ, LaPres JJ. Molecular cancer research : MCR. 2008 6:829-42.
[PubMed:18505927]
10
Prolyl hydroxylase 2 deficiency limits proliferation of vascular smooth muscle cells by hypoxia-inducible factor-1{alpha}-dependent mechanisms. Schultz K, Murthy V, Tatro JB, Beasley D. American journal of physiology. Lung cellular and molecular physiology. 2009 296:L921-7. (WB; Human)
[PubMed:19304911]
[PMC:PMC2692800]
11
HIF-prolyl hydroxylases in the rat kidney: physiologic expression patterns and regulation in acute kidney injury. Schdel J, Klanke B, Weidemann A, Buchholz B, Bernhardt W, Bertog M, Amann K, Korbmacher C, Wiesener M, Warnecke C, Kurtz A, Eckardt KU, Willam C. The American journal of pathology. 2009 174:1663-74. (WB; Mouse)
[PubMed:19349364]
[PMC:PMC2671255]
12
Prolyl hydroxylases 2 and 3 act in gliomas as protective negative feedback regulators of hypoxia-inducible factors. Henze AT, Riedel J, Diem T, Wenner J, Flamme I, Pouyseggur J, Plate KH, Acker T. Cancer research. 2010 70:357-66.
[PubMed:20028863]
13
Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Pyott SM, Schwarze U, Christiansen HE, Pepin MG, Leistritz DF, Dineen R, Harris C, Burton BK, Angle B, Kim K, Sussman MD, Weis M, Eyre DR, Russell DW, McCarthy KJ, Steiner RD, Byers PH. Human molecular genetics. 2011 20:1595-609.
[PubMed:21282188]
[PMC:PMC3063987]
14
Prolyl hydroxylase domain protein 3 targets Pax2 for destruction. Yan B, Jiao S, Zhang HS, Lv DD, Xue J, Fan L, Wu GH, Fang J. Biochemical and biophysical research communications. 2011 409:315-20.
[PubMed:21575608]
15
Expressions of individual PHDs associate with good prognostic factors and increased proliferation in breast cancer patients. Peurala E, Koivunen P, Bloigu R, Haapasaari KM, Jukkola-Vuorinen A. Breast cancer research and treatment. 2012 133:179-88. (IHC; Human)
[PubMed:21877141]
16
Low expression of prolyl hydroxylase 2 is associated with tumor grade and poor prognosis in patients with colorectal cancer. Xie G, Zheng L, Ou J, Huang H, He J, Li J, Pan F, Liang H. Experimental biology and medicine (Maywood, N.J.). 2012 237:860-6. (IHC; Human)
[PubMed:22802519]
17
HIF-independent role of prolyl hydroxylases in the cellular response to amino acids. Ramachandran S, Chahwan R, Nepal RM, Frieder D, Panier S, Roa S, Zaheen A, Durocher D, Scharff MD, Martin A. Oncogene. 2012 (WB; Human)
[PubMed:23085753]
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For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.
The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).
