PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19151537-3 2009 The expression of HIF alpha-chains is post-translationally regulated and hydroxylation at one or two of the conserved proline residues by prolyl-hydroxylase domains (PHDs) is a critical step for the oxygen-dependent recruitment of the von Hippel-Lindau gene product (pVHL), a recognition component of the E3 ubiquitin ligase complex, and degradation of HIF-alpha. Proline 118-125 von Hippel-Lindau tumor suppressor Homo sapiens 267-271 17942596-6 2008 We show that hydroxylation on proline 402 is altered by Ang II, decreasing pVHL binding to HIF-1alpha and allowing HIF-1alpha protein to escape subsequent ubiquitination and degradation mechanisms. Proline 30-37 von Hippel-Lindau tumor suppressor Homo sapiens 75-79 18694926-3 2008 At normoxia two specific proline residues (Pro(402) and Pro(563)) of mHIF-1alpha are hydroxylated and recognized by the von Hippel-Lindau E3 ubiquitin ligase (pVHL) complex, which upon binding mediates degradation of the protein. Proline 25-32 von Hippel-Lindau tumor suppressor Homo sapiens 159-163 18694926-3 2008 At normoxia two specific proline residues (Pro(402) and Pro(563)) of mHIF-1alpha are hydroxylated and recognized by the von Hippel-Lindau E3 ubiquitin ligase (pVHL) complex, which upon binding mediates degradation of the protein. Proline 43-46 von Hippel-Lindau tumor suppressor Homo sapiens 159-163 18694926-3 2008 At normoxia two specific proline residues (Pro(402) and Pro(563)) of mHIF-1alpha are hydroxylated and recognized by the von Hippel-Lindau E3 ubiquitin ligase (pVHL) complex, which upon binding mediates degradation of the protein. Proline 56-59 von Hippel-Lindau tumor suppressor Homo sapiens 159-163 18694926-4 2008 Previous studies have demonstrated that these two proline residues are critical for high affinity binding to pVHL. Proline 50-57 von Hippel-Lindau tumor suppressor Homo sapiens 109-113 18285459-3 2008 A hydroxylated proline 1465 within an LXXLAP motif located N-terminal to the CTD allows the interaction of Rpb1 with pVHL. Proline 15-22 von Hippel-Lindau tumor suppressor Homo sapiens 117-121 17579185-4 2007 HIF in turn is regulated through its alpha subunit, which under normoxic conditions is hydroxylated on specific prolines and targeted for degradation by the von Hippel Lindau (VHL) protein. Proline 112-120 von Hippel-Lindau tumor suppressor Homo sapiens 157-174 17579185-4 2007 HIF in turn is regulated through its alpha subunit, which under normoxic conditions is hydroxylated on specific prolines and targeted for degradation by the von Hippel Lindau (VHL) protein. Proline 112-120 von Hippel-Lindau tumor suppressor Homo sapiens 176-179 17189520-4 2007 Interaction with VHL requires hydroxylation of HIF-1alpha proline residues by prolyl hydroxylases (PHDs). Proline 58-65 von Hippel-Lindau tumor suppressor Homo sapiens 17-20 17551816-2 2007 O(2)-dependent hydroxylation of two proline residues in the HIF-1alpha subunit is necessary for the binding of the von Hippel-Lindau (VHL) protein, which is a component of a ubiquitin protein ligase that ubiquitinates HIF-1alpha, leading to its degradation by the proteasome. Proline 36-43 von Hippel-Lindau tumor suppressor Homo sapiens 115-132 17551816-2 2007 O(2)-dependent hydroxylation of two proline residues in the HIF-1alpha subunit is necessary for the binding of the von Hippel-Lindau (VHL) protein, which is a component of a ubiquitin protein ligase that ubiquitinates HIF-1alpha, leading to its degradation by the proteasome. Proline 36-43 von Hippel-Lindau tumor suppressor Homo sapiens 134-137 11292861-4 2001 Here we show that the interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by an enzyme we have termed HIF-alpha prolyl-hydroxylase (HIF-PH). Proline 141-148 von Hippel-Lindau tumor suppressor Homo sapiens 48-52 15084514-5 2004 Recently, we demonstrated that Leu-574 of human HIF-1alpha--10 residues downstream of Pro-564--is essential for VHL recognition. Proline 86-89 von Hippel-Lindau tumor suppressor Homo sapiens 112-115 12393546-2 2003 The tumor suppressor von Hippel-Lindau (VHL) participates in the hypoxia-sensing pathway, as it binds to the proline-hydroxylated form of the hypoxia-inducible factor 1alpha (HIF-1alpha) and mediates its ubiquitination and proteosomal degradation. Proline 109-116 von Hippel-Lindau tumor suppressor Homo sapiens 40-43 11504942-0 2001 HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proline 61-68 von Hippel-Lindau tumor suppressor Homo sapiens 22-25 11504942-7 2001 The data furthermore show that this proline hydroxylation is the primary regulator of VHL binding. Proline 36-43 von Hippel-Lindau tumor suppressor Homo sapiens 86-89 16509823-3 2006 In the presence of oxygen, they hydroxylate specific proline residues in HIF-alpha, allowing recognition by pVHL (von Hippel-Lindau protein) and subsequent ubiquitylation and proteasomal destruction. Proline 53-60 von Hippel-Lindau tumor suppressor Homo sapiens 108-112 12604794-5 2003 In agreement with the computational model, we show biochemical evidence that pVHL specifically binds the hyperphosphorylated Rpb1 in a proline-hydroxylation-dependent manner, targeting it for ubiquitination. Proline 135-142 von Hippel-Lindau tumor suppressor Homo sapiens 77-81 12205091-4 2002 In particular, the von Hippel-Lindau (VHL) protein complex, an E3 ubiquitin ligase, binds to the ODD upon hydroxylation of HIF-1alpha Pro-564. Proline 134-137 von Hippel-Lindau tumor suppressor Homo sapiens 19-36 12205091-4 2002 In particular, the von Hippel-Lindau (VHL) protein complex, an E3 ubiquitin ligase, binds to the ODD upon hydroxylation of HIF-1alpha Pro-564. Proline 134-137 von Hippel-Lindau tumor suppressor Homo sapiens 38-41 12004076-2 2002 pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. Proline 40-47 von Hippel-Lindau tumor suppressor Homo sapiens 0-4 11292862-0 2001 HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Proline 50-57 von Hippel-Lindau tumor suppressor Homo sapiens 22-25 11292862-3 2001 We found that human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. Proline 79-86 von Hippel-Lindau tumor suppressor Homo sapiens 20-24 34860252-4 2022 We show that pVHL directly interacts with conserved lysine and proline residues in the MH2 domain of SMAD3, triggering degradation. Proline 63-70 von Hippel-Lindau tumor suppressor Homo sapiens 13-17 32640193-5 2020 Mutation of the hydroxylation acceptor proline precludes tyrosine autophosphorylation and folding of DYRK1, resulting in a kinase unable to preserve VHL function and lacking glioma suppression activity. Proline 39-46 von Hippel-Lindau tumor suppressor Homo sapiens 149-152 34537235-2 2021 The principal step in this critical cellular process is the hydroxylation of either or both of the two conserved proline residues P402 and P564 within the oxygen-dependent degradation domain (ODD) of HIF-1alpha subunit via prolyl hydroxylases, which is necessary for binding VHL. Proline 113-120 von Hippel-Lindau tumor suppressor Homo sapiens 275-278 35505422-4 2022 These mutations are predicted to cause Serine (c.193T > C) to Proline and Tryptophan (c.194C > G) substitution at residue 65 of VHL protein (p.Ser65Pro and Ser65Trp). Proline 62-69 von Hippel-Lindau tumor suppressor Homo sapiens 128-131 31035491-3 2019 At physiological oxygen levels (normoxia), HIF-prolyl hydroxylases (PHDs) hydroxylate proline residues on HIF-alpha subunits leading to their destabilization by promoting ubiquitination by the von-Hippel Lindau (VHL) ubiquitin ligase and subsequent proteasomal degradation. Proline 86-93 von Hippel-Lindau tumor suppressor Homo sapiens 193-210 32023483-6 2020 SFMBT1 hydroxylation on Proline residue 651 by EglN1 mediated its ubiquitination and degradation governed by pVHL. Proline 24-31 von Hippel-Lindau tumor suppressor Homo sapiens 109-113 31035491-3 2019 At physiological oxygen levels (normoxia), HIF-prolyl hydroxylases (PHDs) hydroxylate proline residues on HIF-alpha subunits leading to their destabilization by promoting ubiquitination by the von-Hippel Lindau (VHL) ubiquitin ligase and subsequent proteasomal degradation. Proline 86-93 von Hippel-Lindau tumor suppressor Homo sapiens 212-215 27902963-2 2017 Under normoxic conditions, a conserved proline in HIF2alpha is hydroxylated by PHD2 in an oxygen-dependent manner, and then pVHL binds and promotes the degradation of HIF2alpha. Proline 39-46 von Hippel-Lindau tumor suppressor Homo sapiens 124-128 26972007-4 2016 In normoxia, PHD2 hydroxylates the proline residues P2309 and P2316 in FLNA, leading to von Hippel-Lindau (VHL)-mediated ubiquitination and proteasomal degradation. Proline 35-42 von Hippel-Lindau tumor suppressor Homo sapiens 88-105 24563687-2 2014 HIF-alpha is degraded under normoxic conditions by proline hydroxylation, which allows for recognition and ubiquitination by the von-Hippel-Lindau (VHL) E3 ligase complex. Proline 51-58 von Hippel-Lindau tumor suppressor Homo sapiens 129-146 24563687-2 2014 HIF-alpha is degraded under normoxic conditions by proline hydroxylation, which allows for recognition and ubiquitination by the von-Hippel-Lindau (VHL) E3 ligase complex. Proline 51-58 von Hippel-Lindau tumor suppressor Homo sapiens 148-151 24563687-5 2014 We found that HIF-1alpha proline-hydroxylated at both VHL binding sites (Pro402 and Pro564), was present in hypoxic regions of a wide range of tumours, tumour xenografts and in moderately hypoxic cells in vitro. Proline 25-32 von Hippel-Lindau tumor suppressor Homo sapiens 54-57 22649785-4 2012 Proline hydroxylation on key sites of HIFalpha provides the binding signal for pVHL E3 ligase complex. Proline 0-7 von Hippel-Lindau tumor suppressor Homo sapiens 79-83 19584355-4 2009 We further show that the interaction of pVHL with beta(2)AR is dependent on proline hydroxylation (proline-382 and -395) and that the dioxygenase EGLN3 interacts directly with the beta(2)AR to serve as an endogenous beta(2)AR prolyl hydroxylase. Proline 76-83 von Hippel-Lindau tumor suppressor Homo sapiens 40-44 19584355-4 2009 We further show that the interaction of pVHL with beta(2)AR is dependent on proline hydroxylation (proline-382 and -395) and that the dioxygenase EGLN3 interacts directly with the beta(2)AR to serve as an endogenous beta(2)AR prolyl hydroxylase. Proline 99-106 von Hippel-Lindau tumor suppressor Homo sapiens 40-44 27563096-0 2016 pVHL suppresses kinase activity of Akt in a proline-hydroxylation-dependent manner. Proline 44-51 von Hippel-Lindau tumor suppressor Homo sapiens 0-4 20978146-1 2010 PURPOSE: We have previously shown that von Hippel-Lindau (VHL) regulates ubiquitylation and proline 1465 hydroxylation of the large subunit of RNA polymerase II, Rpb1, in human renal clear cell carcinoma (RCC) cell lines. Proline 92-99 von Hippel-Lindau tumor suppressor Homo sapiens 39-56