CUL2

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Template:Short description An Error has occurred retrieving Wikidata item for infobox Cullin-2 is a protein that in humans is encoded by the CUL2 gene.[1][2]

Interactions

CUL2 has been shown to interact with:

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References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.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.
  2. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: CUL2 cullin 2".
  3. ^ a b c d Page Module:Citation/CS1/styles.css has no content.Menon S, Tsuge T, Dohmae N, Takio K, Wei N (2008). "Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome". BMC Biochem. 9: 1. doi:10.1186/1471-2091-9-1. PMC 2265268. PMID 18173839.
  4. ^ Page Module:Citation/CS1/styles.css has no content.Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". J. Biol. Chem. 278 (18): 15905–10. doi:10.1074/jbc.M213070200. PMID 12609982.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". J. Biol. Chem. 283 (48): 33211–20. doi:10.1074/jbc.M804440200. PMC 2586271. PMID 18826954.
  6. ^ Page Module:Citation/CS1/styles.css has no content.Dias DC, Dolios G, Wang R, Pan ZQ (Dec 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16601–6. doi:10.1073/pnas.252646399. PMC 139190. PMID 12481031.
  7. ^ Page Module:Citation/CS1/styles.css has no content.Ohta T, Michel JJ, Schottelius AJ, 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): 535–41. doi:10.1016/s1097-2765(00)80482-7. PMID 10230407. S2CID 19371828.
  8. ^ a b Page Module:Citation/CS1/styles.css has no content.Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E, Branton PE, Shilatifard A, Conaway RC, Conaway JW (Aug 2001). "Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase". J. Biol. Chem. 276 (32): 29748–53. doi:10.1074/jbc.M103093200. PMID 11384984.
  9. ^ Page Module:Citation/CS1/styles.css has no content.Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  10. ^ Page Module:Citation/CS1/styles.css has no content.Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B, Conaway RC, Conaway JW, Kaelin WG (Dec 1999). "Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein". J. Clin. Invest. 104 (11): 1583–91. doi:10.1172/JCI8161. PMC 481054. PMID 10587522.
  11. ^ Page Module:Citation/CS1/styles.css has no content.Hacker KE, Lee CM, Rathmell WK (2008). Zhang B (ed.). "VHL type 2B mutations retain VBC complex form and function". PLOS ONE. 3 (11) e3801. Bibcode:2008PLoSO...3.3801H. doi:10.1371/journal.pone.0003801. PMC 2583047. PMID 19030229.

Further reading

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