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Conserved domains on  [gi|51972218|ref|NP_001004319|]
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von Hippel-Lindau-like protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pVHL super family cl03381
von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene ...
 45-126 1.41e-36

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.


The actual alignment was detected with superfamily member pfam01847:

Pssm-ID: 470794  Cd Length: 82  Bit Score: 120.25  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51972218    45 LRSVNSRELSRIIICNHSPRIVLPVWLNYYGKLLPYLTLLPGRDFRIHNFRSHPWLFRDARTHDKLLVNQTELFVPSSNV 124
Cdd:pfam01847   1 LRSLNSREPSQVIFCNRSPRVVLPVWINFSGEPQPYPNLQPGTGRRMHTYRGHPWMFRDAGTDDGLLVNQKELFLPSPNE 80


                  ..
gi 51972218   125 NG 126
Cdd:pfam01847  81 NG 82
 
Name Accession Description Interval E-value
VHL pfam01847
VHL beta domain; VHL forms a ternary complex with the elongin B and elongin C proteins. This ...
 45-126 1.41e-36

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: 120.25  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51972218    45 LRSVNSRELSRIIICNHSPRIVLPVWLNYYGKLLPYLTLLPGRDFRIHNFRSHPWLFRDARTHDKLLVNQTELFVPSSNV 124
Cdd:pfam01847   1 LRSLNSREPSQVIFCNRSPRVVLPVWINFSGEPQPYPNLQPGTGRRMHTYRGHPWMFRDAGTDDGLLVNQKELFLPSPNE 80


                  ..
gi 51972218   125 NG 126
Cdd:pfam01847  81 NG 82
pVHL cd05468
von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene ...
 46-135 3.57e-31

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: 108.33  E-value: 3.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51972218  46 RSVNSRELSRIIICNHSPRIVLPVWLNYYGKLLPYLTLLPGRDFRIHNFRSHPWLFRDARTHDKLLVNQTELFVPSSNVN 125
Cdd:cd05468   1 RSVNSRVPSTVRFVNRTDRPVELYWIDYDGKPVSYGTLQPGETVRQNTYVGHPWLFRDAETGEKLLVNRKEVFVPSPWRV 80

                        90
                ....*....|
gi 51972218 126 GQPVFANITL 135
Cdd:cd05468  81 GRPIDGNGTL 90
 
Name Accession Description Interval E-value
VHL pfam01847
VHL beta domain; VHL forms a ternary complex with the elongin B and elongin C proteins. This ...
 45-126 1.41e-36

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: 120.25  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51972218    45 LRSVNSRELSRIIICNHSPRIVLPVWLNYYGKLLPYLTLLPGRDFRIHNFRSHPWLFRDARTHDKLLVNQTELFVPSSNV 124
Cdd:pfam01847   1 LRSLNSREPSQVIFCNRSPRVVLPVWINFSGEPQPYPNLQPGTGRRMHTYRGHPWMFRDAGTDDGLLVNQKELFLPSPNE 80


                  ..
gi 51972218   125 NG 126
Cdd:pfam01847  81 NG 82
pVHL cd05468
von Hippel-Landau (pVHL) tumor suppressor protein; von Hippel-Landau (pVHL) protein, the gene ...
 46-135 3.57e-31

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: 108.33  E-value: 3.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51972218  46 RSVNSRELSRIIICNHSPRIVLPVWLNYYGKLLPYLTLLPGRDFRIHNFRSHPWLFRDARTHDKLLVNQTELFVPSSNVN 125
Cdd:cd05468   1 RSVNSRVPSTVRFVNRTDRPVELYWIDYDGKPVSYGTLQPGETVRQNTYVGHPWLFRDAETGEKLLVNRKEVFVPSPWRV 80

                        90
                ....*....|
gi 51972218 126 GQPVFANITL 135
Cdd:cd05468  81 GRPIDGNGTL 90
 
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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