CUL4B

Cullin 4B

PDB rendering based on 2do7.
Identifiers
Symbols CUL4B; DKFZp686F1470; KIAA0695; MRXHF2; MRXS15; MRXSC; SFM2
External IDs OMIM300304 MGI1919834 HomoloGene2660 GeneCards: CUL4B Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 8450 72584
Ensembl ENSG00000158290 ENSMUSG00000031095
UniProt Q13620 n/a
RefSeq (mRNA) NM_001079872.1 NM_028288
RefSeq (protein) NP_001073341.1 NP_082564
Location (UCSC) Chr X:
119.66 – 119.71 Mb
Chr X:
35.88 – 35.93 Mb
PubMed search [1] [2]

Cullin-4B is a protein that in humans is encoded by the CUL4B gene.[1][2]

This gene is a member of the cullin family. The encoded protein forms a complex that functions as an E3 ubiquitin ligase and catalyzes the polyubiquitination of specific protein substrates in the cell. The protein interacts with a ring finger protein, and is required for the proteolysis of several regulators of DNA replication including chromatin licensing and DNA replication factor 1 and cyclin E. Multiple transcript variants encoding different isoforms have been found for this gene.[2]

Interactions

CUL4B has been shown to interact with DDB2,[3] CAND1[4] and DDB1.[3]

References

  1. ^ 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. 
  2. ^ a b "Entrez Gene: CUL4B cullin 4B". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8450. 
  3. ^ a b Guerrero-Santoro, Jennifer; Kapetanaki Maria G, Hsieh Ching L, Gorbachinsky Ilya, Levine Arthur S, Rapić-Otrin Vesna (Jul. 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Res. (United States) 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899. 
  4. ^ Min, Kyoeng-Woo; Hwang Ji-Won, Lee Jong-Sik, Park Yoon, Tamura Taka-aki, Yoon Jong-Bok (May. 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". J. Biol. Chem. (United States) 278 (18): 15905–10. doi:10.1074/jbc.M213070200. ISSN 0021-9258. PMID 12609982. 

Further reading