Browse our VHL Proteins (VHL)

Full name:
Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase Proteins (VHL)
On are 7 Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) Proteins from 5 different suppliers available. Additionally we are shipping VHL Antibodies (132) and VHL Kits (15) and many more products for this protein. A total of 163 VHL products are currently listed.
BcDNA:RH61560, CG13221, d-vhl, Dmel\\CG13221, dmVHL, dVHL, hrca1, pVHL, rca1, vhl, vhl1, Vhlh, zgc:158722
list all proteins Gene Name GeneID UniProt
VHL 7428 P40337
Mouse VHL VHL 22346 P40338
VHL 24874 Q64259

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VHL Proteins (VHL) by Origin

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Top referenced VHL Proteins

  1. Human VHL Protein expressed in Wheat germ - ABIN1325000 : Kim, Lee, Jang, Yi, Kim, Han, Lee, Tong, Vincelette, Gao, Yin, Evans, Choi, Qin, Liu, Zhang, Deng, Jen, Zhang, Wang, Lou: WSB1 promotes tumor metastasis by inducing pVHL degradation. in Genes & development 2015 (PubMed)

More Proteins for VHL Interaction Partners

Human Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) interaction partners

  1. Loss of VHL gene is associated with paragangliomas.

  2. It has been proposed that the archetypal linker protein Rootletin maintains centrosome cohesion in part through inhibition of VHL-mediated Cep68 degradation.

  3. Results show that VHL missense mutations may exert mild, moderate or strong impact on protein stability. Besides the HIF binding domain, other pVHL binding sites seem to be non-randomly altered by missense mutations in sporadic clear cell renal cell carcinoma (show MOK Proteins).

  4. Data identify VHL as an E3 ligase with important cellular functions under both normoxic and hypoxic conditions.

  5. Moderate/strong NEMO (show IKBKG Proteins) protein expression is more frequent in VHL wild-type ccRCCs.

  6. The Absence of MCM7 (show MCM7 Proteins) weakened the interaction between Cep68 and VHL, whereas MCM7 (show MCM7 Proteins) overexpression facilitated the Cep68-VHL association.

  7. this meta-analysis indicates that VHL gene alteration has no prognostic or predictive value in patients with clear cell renal cell carcinoma (show MOK Proteins)

  8. Low VHL expression is associated with Clear cell renal cell carcinoma (show MOK Proteins).

  9. The negative feedback modulation between LncRNA-SARCC/AR complex and HIF-2alpha (show EPAS1 Proteins) signaling may then lead to differentially modulated RCC (show XRCC1 Proteins) progression in a VHL-dependent manner. Together, these results may provide us a new therapeutic approach via targeting this newly identified signal from LncRNA-SARCC to AR-mediated HIF-2alpha (show EPAS1 Proteins)/C-MYC (show MYC Proteins) signals against RCC (show XRCC1 Proteins) progression.

  10. Our study reveals a novel mechanism regulating VHL proteostasis and function, which is significant for identifying new drug targets and developing new therapeutic approaches targeting VHL deficiency in VHL diseases.

Fruit Fly (Drosophila melanogaster) Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) interaction partners

  1. Interaction between Nm23 (show NME1 Proteins) and the tumor suppressor VHL

  2. Transgenic pVHL can fully maintain normal dVHL-HIF1-alpha (show HIF1A Proteins) downstream pathways in flies.

  3. Codepletion of Vhl with Mgr (show GRHL1 Proteins) gives partial rescue of tubulin (show TUBB Proteins) instability, monopolar spindle formation, and loss of centrosomes.

  4. The results establish a developmental function of the VHL gene that is relevant to its tumor-suppressor activity.

  5. findings reveal a second type of tracheal hypoxic response in which Sima activation conflicts with developmental tracheogenesis, and identify the dVHL and ago ubiquitin ligases as key determinants of hypoxia sensitivity in tracheal cells

Zebrafish Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) interaction partners

  1. In this review, we have tried to bring together knowledge on the HIF/hypoxic signaling pathway in zebrafish, including what is known on VHL functions.

  2. by modulating hypoxia-inducible factor activity via up-regulation of VHL, FOXO3a (show FOXO3 Proteins) (foxo3b) plays an important role in survival in response to hypoxic stress.

  3. Zebrafish embryos lacking endogenous vhl lead to defective phenotypes in the renal system that were characterized by the curved and cystic pronephric tubule or/and a cystic and malformed glomerulus.

  4. Inhibiting PHD (show PDC Proteins) or knocking down VHL rescues Methyl tert (show TERT Proteins)-butyl ether induced vascular lesions.

  5. Zebrafish vhl mutants display a marked increase in blood vessel formation throughout the embryo, and the most severe neovascularization is observed in distinct areas that overlap with high vegfa (show VEGFA Proteins) mRNA expression, including the vhl mutant brain and eye.

  6. Vhl mutants develop polycythemia with increased epo (show EPO Proteins)/epor (show EPOR Proteins) mRNA & erythropoietin (show EPO Proteins) signaling. VHL regulates hematopoiesis & erythroid differentiation. Zebrafish vhl mutants are the 1st congenital embryonic viable systemic vertebrate animal model for VHL.

Mouse (Murine) Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) interaction partners

  1. Codeletion of VHL together with HIF2A (show EPAS1 Proteins) but not with HIF1A (show HIF1A Proteins) led to apparently normal kidneys, and the animals reached normal age but were anemic because of low erythropoietin (show EPO Proteins) levels. Stromal deletion of HIF2A (show EPAS1 Proteins) or HIF1A (show HIF1A Proteins) alone did not affect kidney development.

  2. High VHL expression is associated with liver fibrosis.

  3. Study demonstrated that mice with a loss of one allele of the VHL gene exhibited normal phenotypes without evidence of predisposition to the development of CNS-hemangioblastomas. Heterozygous VHL +/- mice exhibited the neuroprotective response to acute cerebral ischemia/reperfusion injury due to enhanced angiogenesis by HIF-dependent regulation and HIF-independent Twist 1 (show TWIST1 Proteins) signaling.

  4. These results support the idea that the development of a full-blown VHL disease phenotype requires inactivation of the VHL gene not only in the tumor proper, but also in the stromal compartment.

  5. Combined deletion of Vhl, Trp53 (show TP53 Proteins) and Rb1 (show RB1 Proteins) specifically in renal epithelial cells in mice caused clear cell renal cell carcinoma (show MOK Proteins).

  6. pVHL has a pivotal role in bleomycin-induced pulmonary fibrosis.

  7. These findings reveal VHL-HIF-mediated metabolic compartmentalization in the developing heart and the connection between metabolism and myocardial differentiation.

  8. Longitudinal microcomputed tomography (muCT) imaging and histopathological analyses revealed an increased rate of cyst formation, increased proportion of cysts with proliferating cells, higher frequency of atypical cysts as well as the development of neoplasms in Vhl/Kif3a (show KIF3A Proteins)/Trp53 (show TP53 Proteins) mutant kidneys compared to Kif3a (show KIF3A Proteins)/Trp53 (show TP53 Proteins) or Vhl/Kif3a (show KIF3A Proteins) mutant kidneys.

  9. Loss of Vhl in mesenchymal progenitors of the limb bud caused severe fibrosis of the synovial joints and formation of aggressive masses with histologic features of mesenchymal tumors.

  10. These data suggested that intestinal epithelial cells were injured after IM treatment through the pVHL overexpression-induced degradation of collagen I or HIF-1alpha (show HIF1A Proteins).

VHL Protein Profile

Protein Summary

Von Hippel-Lindau syndrome (VHL) is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign tumors. A germline mutation of this gene is the basis of familial inheritance of VHL syndrome. The protein encoded by this gene is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible-factor (HIF), which is a transcription factor that plays a central role in the regulation of gene expression by oxygen. RNA polymerase II subunit POLR2G/RPB7 is also reported to be a target of this protein. Alternatively spliced transcript variants encoding distinct isoforms have been observed.

Alternative names and synonyms associated with VHL

  • von Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase (VHL)
  • von Hippel-Lindau (Vhl)
  • von Hippel-Lindau tumor suppressor (VHL)
  • von Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase (vhl)
  • von Hippel-Lindau tumor suppressor (vhl)
  • von Hippel-Lindau disease tumor suppressor (CpipJ_CPIJ009992)
  • von Hippel-Lindau tumor suppressor (Vhl)
  • von Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase (Vhl)
  • BcDNA:RH61560 protein
  • CG13221 protein
  • d-vhl protein
  • Dmel\\CG13221 protein
  • dmVHL protein
  • dVHL protein
  • hrca1 protein
  • pVHL protein
  • rca1 protein
  • vhl protein
  • vhl1 protein
  • Vhlh protein
  • zgc:158722 protein

Protein level used designations for VHL

elongin binding protein , protein G7 , von Hippel-Lindau disease tumor suppressor , CG13221-PA , CG13221-PB , Vhl-PA , Vhl-PB , von hippel lindau , von hippel lindau protein , pVHL , von Hippel-Lindau tumor suppressor , von Hippel-Lindau syndrome homolog , von Hippel-Lindau syndrome protein homolog , Von Hippel-Lindau disease tumor suppressor

7428 Homo sapiens
53433 Drosophila melanogaster
100173372 Pongo abelii
494000 Canis lupus familiaris
416117 Gallus gallus
549121 Xenopus (Silurana) tropicalis
791202 Danio rerio
540957 Bos taurus
6042662 Culex quinquefasciatus
22346 Mus musculus
24874 Rattus norvegicus
100380306 Salmo salar
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