From Wikipedia, the free encyclopedia
(Redirected from CUL5 (gene))
CUL5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases CUL5, VACM-1, VACM1, cullin 5, CUL-5
External IDs OMIM: 601741; MGI: 1922967; HomoloGene: 2597; GeneCards: CUL5; OMA: CUL5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003478

NM_001161618
NM_027807

RefSeq (protein)

NP_003469

NP_001155090
NP_082083

Location (UCSC) Chr 11: 108.01 – 108.11 Mb Chr 9: 53.53 – 53.58 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cullin-5 is a protein that in humans is encoded by the CUL5 gene. [5] [6] [7]

Discovery

The mammalian gene product was originally discovered by expression cloning, due to the protein's ability to mobilize intracellular calcium in response to the peptide hormone arginine vasopressin. It was first titled VACM-1, for vasopressin-activated, calcium-mobilizing receptor. [8] Since then, VACM-1 has been shown to be homologous to the Cullin family of proteins, and was subsequently dubbed cul5.

Tissue distribution

Studies have shown that the cul5 protein is expressed at its highest levels in heart and skeletal tissue, and is specifically expressed in vascular endothelium and renal collecting tubules. [9]

Function

Cul5 inhibits cellular proliferation, potentially through its involvement in the SOCS/ BC-box/ eloBC/ cul5/ RING E3 ligase complex, which functions as part of the ubiquitin system for protein degradation. [10]

One study have shown that Cul5 plays a role in Reelin signaling cascade, participating in the DAB1 degradation and thus ensuring the negative feedback mechanism of Reelin signaling during corticogenesis. [11]

Interactions

CUL5 has been shown to interact with RBX1. [12] [13]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166266Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032030Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kipreos ET, Lander LE, Wing JP, He WW, Hedgecock EM (Aug 1996). "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family". Cell. 85 (6): 829–39. doi: 10.1016/S0092-8674(00)81267-2. PMID  8681378. S2CID  15805562.
  6. ^ Byrd PJ, Stankovic T, McConville CM, Smith AD, Cooper PR, Taylor AM (May 1997). "Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23". Genome Res. 7 (1): 71–5. doi: 10.1101/gr.7.1.71. PMID  9037604.
  7. ^ "Entrez Gene: CUL5 cullin 5".
  8. ^ Burnatowska-Hledin MA, Spielman WS, Smith WL, et al. (1995). "Expression cloning of an AVP-activated, calcium-mobilizing receptor from rabbit kidney medulla". Am J Physiol. 268 (6): F1198–210. doi: 10.1152/ajprenal.1995.268.6.F1198. PMID  7611460.
  9. ^ Burnatowska-Hledin M, Lazdins IB, Listenberger L, et al. (1999). "VACM-1 receptor is specifically expressed in rabbit vascular endothelium and renal collecting tubule". Am J Physiol. 276 (2 Pt 2): F199–209. doi: 10.1152/ajprenal.1999.276.2.F199. PMID  9950950.
  10. ^ Petroski MD, Deshaies RJ (2005). "Function and regulation of cullin-RING E3 ligases" (PDF). Nature Reviews Molecular Cell Biology. 6 (1): 9–21. doi: 10.1038/nrm1547. PMID  15688063. S2CID  24159190.
  11. ^ Feng L, Allen NS, Simo S, Cooper JA (November 2007). "Cullin 5 regulates Dab1 protein levels and neuron positioning during cortical development". Genes Dev. 21 (21): 2717–30. doi: 10.1101/gad.1604207. PMC  2045127. PMID  17974915.
  12. ^ Duda DM, Borg Laura A, Scott Daniel C, Hunt Harold W, Hammel Michal, Schulman Brenda A (Sep 2008). "Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation". Cell. 134 (6). United States: 995–1006. doi: 10.1016/j.cell.2008.07.022. PMC  2628631. PMID  18805092.
  13. ^ Ohta T, Michel J J, Schottelius A J, Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Mol. Cell. 3 (4). UNITED STATES: 535–41. doi: 10.1016/S1097-2765(00)80482-7. ISSN  1097-2765. PMID  10230407. S2CID  19371828.

External links

Further reading


From Wikipedia, the free encyclopedia
(Redirected from CUL5 (gene))
CUL5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases CUL5, VACM-1, VACM1, cullin 5, CUL-5
External IDs OMIM: 601741; MGI: 1922967; HomoloGene: 2597; GeneCards: CUL5; OMA: CUL5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003478

NM_001161618
NM_027807

RefSeq (protein)

NP_003469

NP_001155090
NP_082083

Location (UCSC) Chr 11: 108.01 – 108.11 Mb Chr 9: 53.53 – 53.58 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cullin-5 is a protein that in humans is encoded by the CUL5 gene. [5] [6] [7]

Discovery

The mammalian gene product was originally discovered by expression cloning, due to the protein's ability to mobilize intracellular calcium in response to the peptide hormone arginine vasopressin. It was first titled VACM-1, for vasopressin-activated, calcium-mobilizing receptor. [8] Since then, VACM-1 has been shown to be homologous to the Cullin family of proteins, and was subsequently dubbed cul5.

Tissue distribution

Studies have shown that the cul5 protein is expressed at its highest levels in heart and skeletal tissue, and is specifically expressed in vascular endothelium and renal collecting tubules. [9]

Function

Cul5 inhibits cellular proliferation, potentially through its involvement in the SOCS/ BC-box/ eloBC/ cul5/ RING E3 ligase complex, which functions as part of the ubiquitin system for protein degradation. [10]

One study have shown that Cul5 plays a role in Reelin signaling cascade, participating in the DAB1 degradation and thus ensuring the negative feedback mechanism of Reelin signaling during corticogenesis. [11]

Interactions

CUL5 has been shown to interact with RBX1. [12] [13]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166266Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032030Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kipreos ET, Lander LE, Wing JP, He WW, Hedgecock EM (Aug 1996). "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family". Cell. 85 (6): 829–39. doi: 10.1016/S0092-8674(00)81267-2. PMID  8681378. S2CID  15805562.
  6. ^ Byrd PJ, Stankovic T, McConville CM, Smith AD, Cooper PR, Taylor AM (May 1997). "Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23". Genome Res. 7 (1): 71–5. doi: 10.1101/gr.7.1.71. PMID  9037604.
  7. ^ "Entrez Gene: CUL5 cullin 5".
  8. ^ Burnatowska-Hledin MA, Spielman WS, Smith WL, et al. (1995). "Expression cloning of an AVP-activated, calcium-mobilizing receptor from rabbit kidney medulla". Am J Physiol. 268 (6): F1198–210. doi: 10.1152/ajprenal.1995.268.6.F1198. PMID  7611460.
  9. ^ Burnatowska-Hledin M, Lazdins IB, Listenberger L, et al. (1999). "VACM-1 receptor is specifically expressed in rabbit vascular endothelium and renal collecting tubule". Am J Physiol. 276 (2 Pt 2): F199–209. doi: 10.1152/ajprenal.1999.276.2.F199. PMID  9950950.
  10. ^ Petroski MD, Deshaies RJ (2005). "Function and regulation of cullin-RING E3 ligases" (PDF). Nature Reviews Molecular Cell Biology. 6 (1): 9–21. doi: 10.1038/nrm1547. PMID  15688063. S2CID  24159190.
  11. ^ Feng L, Allen NS, Simo S, Cooper JA (November 2007). "Cullin 5 regulates Dab1 protein levels and neuron positioning during cortical development". Genes Dev. 21 (21): 2717–30. doi: 10.1101/gad.1604207. PMC  2045127. PMID  17974915.
  12. ^ Duda DM, Borg Laura A, Scott Daniel C, Hunt Harold W, Hammel Michal, Schulman Brenda A (Sep 2008). "Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation". Cell. 134 (6). United States: 995–1006. doi: 10.1016/j.cell.2008.07.022. PMC  2628631. PMID  18805092.
  13. ^ Ohta T, Michel J J, Schottelius A J, Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Mol. Cell. 3 (4). UNITED STATES: 535–41. doi: 10.1016/S1097-2765(00)80482-7. ISSN  1097-2765. PMID  10230407. S2CID  19371828.

External links

Further reading



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