CUL2

Cullin-2 is a protein that in humans is encoded by the CUL2 gene.[5][6]

CUL2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4WQO
Identifiers
Aliases	CUL2, cullin 2
External IDs	OMIM: 603135 MGI: 1918995 HomoloGene: 2662 GeneCards: CUL2
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10p11.21 Start 35,008,551 bp[1] End 35,090,642 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 A1 Start 3,382,988 bp[2] End 3,436,377 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity • ubiquitin protein ligase binding • GO:0032403 macromolecular complex binding Cellular component • cullin-RING ubiquitin ligase complex • cytosol • nucleolus • VCB complex • nucleoplasm • Cul2-RING ubiquitin ligase complex • SCF ubiquitin ligase complex Biological process • intrinsic apoptotic signaling pathway • GO:0022415 viral process • protein catabolic process • cell cycle arrest • regulation of transcription from RNA polymerase II promoter in response to hypoxia • negative regulation of cell proliferation • ubiquitin-dependent protein catabolic process • post-translational modification • G1/S transition of mitotic cell cycle • protein ubiquitination • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process • proteasome-mediated ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8453	71745
Ensembl	ENSG00000108094	ENSMUSG00000024231
UniProt	Q13617	Q9D4H8
RefSeq (mRNA)	NM_001198777 NM_001198778 NM_001198779 NM_003591 NM_001324375 NM_001324376	NM_029402 NM_001360829
RefSeq (protein)	NP_001185706 NP_001185707 NP_001185708 NP_001311304 NP_001311305 NP_003582	NP_083678 NP_001347758
Location (UCSC)	Chr 10: 35.01 – 35.09 Mb	Chr 18: 3.38 – 3.44 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

CUL2 has been shown to interact with:

• CAND1,[7][8]
• DCUN1D1,[9]
• RBX1,[10][11]
• SAP130,[7]
• TCEB2[7][12] and
• Von Hippel-Lindau tumor suppressor.[7][12][13][14][15]

References

1. GRCh38: Ensembl release 89: ENSG00000108094 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024231 - Ensembl, 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. "Entrez Gene: CUL2 cullin 2".
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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.
13. 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.
14. 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.
15. 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. doi:10.1371/journal.pone.0003801. PMC 2583047. PMID 19030229.

External links

• Human CUL2 genome location and CUL2 gene details page in the UCSC Genome Browser.

Further reading

• Kibel A, Iliopoulos O, DeCaprio JA, Kaelin WG (1995). "Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C". Science. 269 (5229): 1444–6. doi:10.1126/science.7660130. PMID 7660130. S2CID 25410108.
• Pause A, Lee S, Worrell RA, Chen DY, Burgess WH, Linehan WM, Klausner RD (1997). "The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins". Proc. Natl. Acad. Sci. U.S.A. 94 (6): 2156–61. doi:10.1073/pnas.94.6.2156. PMC 20057. PMID 9122164.
• Lonergan KM, Iliopoulos O, Ohh M, Kamura T, Conaway RC, Conaway JW, Kaelin WG (1998). "Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2". Mol. Cell. Biol. 18 (2): 732–41. doi:10.1128/mcb.18.2.732. PMC 108784. PMID 9447969.
• Wada H, Yeh ET, Kamitani T (1999). "Identification of NEDD8-conjugation site in human cullin-2". Biochem. Biophys. Res. Commun. 257 (1): 100–5. doi:10.1006/bbrc.1999.0339. PMID 10092517.
• Ohta T, Michel JJ, Schottelius AJ, Xiong Y (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.
• Pause A, Peterson B, Schaffar G, Stearman R, Klausner RD (1999). "Studying interactions of four proteins in the yeast two-hybrid system: structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein". Proc. Natl. Acad. Sci. U.S.A. 96 (17): 9533–8. doi:10.1073/pnas.96.17.9533. PMC 22243. PMID 10449727.
• Iwai K, Yamanaka K, Kamura T, Minato N, Conaway RC, Conaway JW, Klausner RD, Pause A (1999). "Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12436–41. doi:10.1073/pnas.96.22.12436. PMC 22941. PMID 10535940.
• Hori T, Osaka F, Chiba T, Miyamoto C, Okabayashi K, Shimbara N, Kato S, Tanaka K (2000). "Covalent modification of all members of human cullin family proteins by NEDD8". Oncogene. 18 (48): 6829–34. doi:10.1038/sj.onc.1203093. PMID 10597293.
• Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW (2000). "Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex". Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10430–5. doi:10.1073/pnas.190332597. PMC 27041. PMID 10973499.
• Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, Zhou C, Wolf DA, Wei N, Shevchenko A, Deshaies RJ (2001). "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome". Science. 292 (5520): 1382–5. doi:10.1126/science.1059780. PMID 11337588. S2CID 14224920.
• Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E, Branton PE, Shilatifard A, Conaway RC, Conaway JW (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.
• Ohh M, Kim WY, Moslehi JJ, Chen Y, Chau V, Read MA, Kaelin WG (2002). "An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells". EMBO Rep. 3 (2): 177–82. doi:10.1093/embo-reports/kvf028. PMC 1083969. PMID 11818338.
• Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science. 296 (5574): 1886–9. doi:10.1126/science.1073440. PMID 12004076. S2CID 19641938.
• Brower CS, Sato S, Tomomori-Sato C, Kamura T, Pause A, Stearman R, Klausner RD, Malik S, Lane WS, Sorokina I, Roeder RG, Conaway JW, Conaway RC (2002). "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase". Proc. Natl. Acad. Sci. U.S.A. 99 (16): 10353–8. doi:10.1073/pnas.162424199. PMC 124918. PMID 12149480.
• Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". J. Biol. Chem. 278 (18): 15905–10. doi:10.1074/jbc.M213070200. PMID 12609982.
• Yan Q, Kamura T, Cai Y, Jin J, Ivan M, Mushegian A, Conaway RC, Conaway JW (2004). "Identification of Elongin C and Skp1 sequences that determine Cullin selection". J. Biol. Chem. 279 (41): 43019–26. doi:10.1074/jbc.M408018200. PMID 15280393.