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Conserved domains on  [gi|379318535]
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Chain C, Von Hippel-lindau Disease Tumor Suppressor

Protein Classification

pVHL domain-containing protein( domain architecture ID 10144318)

pVHL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pVHL cd05468
von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene ...
 14-153 4.42e-52

von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene product of VHL, is a critical regulator of the ubiquitous oxygen-sensing pathway. It is conserved throughout evolution, as its homologs are found in organisms ranging from mammals to the Drosophila melanogaster, Anopheles gambiae insects and the Caenorhabditis elegans nematode. pVHL acts as the substrate recognition component of an E3 ubiquitin ligase complex. Several proteins have been identified as pVHL-binding proteins that are subject to ubiquitin-mediated proteolysis; the best characterized putative substrates are the alpha subunits of the hypoxia-inducible factor (HIF1alpha, HIF2alpha, and HIF3alpha). In addition to HIF degradation, pVHL has been implicated to be involved in HIF independent cellular processes. Germline VHL mutations cause renal cell carcinomas, hemangioblastomas and pheochromocytomas in humans. pVHL can bind to and direct the proper deposition of fibronectin and collagen IV within the extracellular matrix. It works to stabilize microtubules and foster the maintenance of primary cilium. It also has been reported to promote the stabilization and activation of p53 in a HIF-independent manner and, in neuronal cells, promote apoptosis by down-regulation of Jun-B.


:

Pssm-ID: 176472 [Multi-domain]  Cd Length: 141  Bit Score: 162.64  E-value: 4.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379318535  14 RSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVD 93
Cdd:cd05468    1 RSVNSRVPSTVRFVNRTDRPVELYWIDYDGKPVSYGTLQPGETVRQNTYVGHPWLFRDAETGEKLLVNRKEVFVPSPWRV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379318535  94 GQPIFANITLPVYTLKERCLQVVRSLVkPENYRRLDI--VRSLYEDLEDHPNVQKDLERLTQ 153
Cdd:cd05468   81 GRPIDGNGTLPVTSLDERCLQLVRSLV-PEDVRGLEIrvPRSLYEDLDIEPTLPRDLQRLLS 141
 
Name Accession Description Interval E-value
pVHL cd05468
von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene ...
 14-153 4.42e-52

von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene product of VHL, is a critical regulator of the ubiquitous oxygen-sensing pathway. It is conserved throughout evolution, as its homologs are found in organisms ranging from mammals to the Drosophila melanogaster, Anopheles gambiae insects and the Caenorhabditis elegans nematode. pVHL acts as the substrate recognition component of an E3 ubiquitin ligase complex. Several proteins have been identified as pVHL-binding proteins that are subject to ubiquitin-mediated proteolysis; the best characterized putative substrates are the alpha subunits of the hypoxia-inducible factor (HIF1alpha, HIF2alpha, and HIF3alpha). In addition to HIF degradation, pVHL has been implicated to be involved in HIF independent cellular processes. Germline VHL mutations cause renal cell carcinomas, hemangioblastomas and pheochromocytomas in humans. pVHL can bind to and direct the proper deposition of fibronectin and collagen IV within the extracellular matrix. It works to stabilize microtubules and foster the maintenance of primary cilium. It also has been reported to promote the stabilization and activation of p53 in a HIF-independent manner and, in neuronal cells, promote apoptosis by down-regulation of Jun-B.


Pssm-ID: 176472 [Multi-domain]  Cd Length: 141  Bit Score: 162.64  E-value: 4.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379318535  14 RSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVD 93
Cdd:cd05468    1 RSVNSRVPSTVRFVNRTDRPVELYWIDYDGKPVSYGTLQPGETVRQNTYVGHPWLFRDAETGEKLLVNRKEVFVPSPWRV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379318535  94 GQPIFANITLPVYTLKERCLQVVRSLVkPENYRRLDI--VRSLYEDLEDHPNVQKDLERLTQ 153
Cdd:cd05468   81 GRPIDGNGTLPVTSLDERCLQLVRSLV-PEDVRGLEIrvPRSLYEDLDIEPTLPRDLQRLLS 141
VHL pfam01847
VHL beta domain; VHL forms a ternary complex with the elongin B and elongin C proteins. This ...
 13-94 8.87e-52

VHL beta domain; VHL forms a ternary complex with the elongin B and elongin C proteins. This complex binds Cul2, which then is involved in regulation of vascular endothelial growth factor mRNA.


Pssm-ID: 460360  Cd Length: 82  Bit Score: 159.54  E-value: 8.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379318535   13 LRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNV 92
Cdd:pfam01847   1 LRSLNSREPSQVIFCNRSPRVVLPVWINFSGEPQPYPNLQPGTGRRMHTYRGHPWMFRDAGTDDGLLVNQKELFLPSPNE 80


                  ..
gi 379318535   93 DG 94
Cdd:pfam01847  81 NG 82
 
Name Accession Description Interval E-value
pVHL cd05468
von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene ...
 14-153 4.42e-52

von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene product of VHL, is a critical regulator of the ubiquitous oxygen-sensing pathway. It is conserved throughout evolution, as its homologs are found in organisms ranging from mammals to the Drosophila melanogaster, Anopheles gambiae insects and the Caenorhabditis elegans nematode. pVHL acts as the substrate recognition component of an E3 ubiquitin ligase complex. Several proteins have been identified as pVHL-binding proteins that are subject to ubiquitin-mediated proteolysis; the best characterized putative substrates are the alpha subunits of the hypoxia-inducible factor (HIF1alpha, HIF2alpha, and HIF3alpha). In addition to HIF degradation, pVHL has been implicated to be involved in HIF independent cellular processes. Germline VHL mutations cause renal cell carcinomas, hemangioblastomas and pheochromocytomas in humans. pVHL can bind to and direct the proper deposition of fibronectin and collagen IV within the extracellular matrix. It works to stabilize microtubules and foster the maintenance of primary cilium. It also has been reported to promote the stabilization and activation of p53 in a HIF-independent manner and, in neuronal cells, promote apoptosis by down-regulation of Jun-B.


Pssm-ID: 176472 [Multi-domain]  Cd Length: 141  Bit Score: 162.64  E-value: 4.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379318535  14 RSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVD 93
Cdd:cd05468    1 RSVNSRVPSTVRFVNRTDRPVELYWIDYDGKPVSYGTLQPGETVRQNTYVGHPWLFRDAETGEKLLVNRKEVFVPSPWRV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379318535  94 GQPIFANITLPVYTLKERCLQVVRSLVkPENYRRLDI--VRSLYEDLEDHPNVQKDLERLTQ 153
Cdd:cd05468   81 GRPIDGNGTLPVTSLDERCLQLVRSLV-PEDVRGLEIrvPRSLYEDLDIEPTLPRDLQRLLS 141
VHL pfam01847
VHL beta domain; VHL forms a ternary complex with the elongin B and elongin C proteins. This ...
 13-94 8.87e-52

VHL beta domain; VHL forms a ternary complex with the elongin B and elongin C proteins. This complex binds Cul2, which then is involved in regulation of vascular endothelial growth factor mRNA.


Pssm-ID: 460360  Cd Length: 82  Bit Score: 159.54  E-value: 8.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379318535   13 LRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNV 92
Cdd:pfam01847   1 LRSLNSREPSQVIFCNRSPRVVLPVWINFSGEPQPYPNLQPGTGRRMHTYRGHPWMFRDAGTDDGLLVNQKELFLPSPNE 80


                  ..
gi 379318535   93 DG 94
Cdd:pfam01847  81 NG 82
VHL_C pfam17211
VHL box domain; This domain represents the short C-terminal alpha helical domain from the VHL ...
 106-154 2.84e-25

VHL box domain; This domain represents the short C-terminal alpha helical domain from the VHL protein.


Pssm-ID: 407332  Cd Length: 49  Bit Score: 91.39  E-value: 2.84e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 379318535  106 YTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQE 154
Cdd:pfam17211   1 YTLKERCLQVVRSLVRPEDYRRLEIVRSLYEDLEDRPSVQKDLRRISQR 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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