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CUL2

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(Redirected from Cullin-2) Protein-coding gene in humans
CUL2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4WQO

Identifiers
AliasesCUL2, cullin 2
External IDsOMIM: 603135; MGI: 1918995; HomoloGene: 2662; GeneCards: CUL2; OMA:CUL2 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)
Chromosome 10 (human)Genomic location for CUL2Genomic location for CUL2
Band10p11.21Start35,008,504 bp
End35,127,006 bp
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)
Chromosome 18 (mouse)Genomic location for CUL2Genomic location for CUL2
Band18|18 A1Start3,382,988 bp
End3,436,377 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • sperm

  • muscle of thigh

  • gastrocnemius muscle

  • gonad

  • Achilles tendon

  • ventricular zone

  • stromal cell of endometrium

  • islet of Langerhans

  • ganglionic eminence

  • biceps brachii
Top expressed in
  • superior cervical ganglion

  • epiblast

  • abdominal wall

  • facial motor nucleus

  • arcuate nucleus

  • ventromedial nucleus

  • paraventricular nucleus of hypothalamus

  • lateral hypothalamus

  • sternocleidomastoid muscle

  • neural tube
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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 – 35.13 MbChr 18: 3.38 – 3.44 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Cullin-2 is a protein that in humans is encoded by the CUL2 gene.

Interactions

CUL2 has been shown to interact with:

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000108094Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000024231Ensembl, 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. S2CID 19371828.
  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. Bibcode:2008PLoSO...3.3801H. doi:10.1371/journal.pone.0003801. PMC 2583047. PMID 19030229.

External links

Further reading


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