RNF7

From Wikipedia, the free encyclopedia

Ring finger protein 7

Identifiers

RNF7; ROC2; SAG; CKBBP1

External IDs

OMIM: 603863 MGI: 1337096 HomoloGene: 84476

Gene ontology
Molecular Function:	• copper ion binding • protein binding • zinc ion binding • metal ion binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• ubiquitin cycle • anti-apoptosis • redox signal response • induction of apoptosis by oxidative stress

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_014245 (mRNA)
NP_055060 (protein)

XM_905787 (mRNA)
XP_910880 (protein)

Location

Chr 3: 142.94 - 142.95 Mb

n/a

Pubmed search

[1]

[2]

Ring finger protein 7, also known as RNF7, is a human gene.^[1]

The protein encoded by this gene is a highly conserved ring finger protein. It is an essential subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases, which are a part of the protein degradation machinery important for cell cycle progression and signal transduction. This protein interacts with, and is a substrate of, casein kinase II (CSNK2A1/CKII). The phosphorylation of this protein by CSNK2A1 has been shown to promote the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B). Alternatively spliced transcript variants encoding distinct isoforms have been reported.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

RING finger domain

[edit] References

^ ^a ^b Entrez Gene: RNF7 ring finger protein 7.

[edit] Further reading

Duan H, Wang Y, Aviram M, et al. (1999). "SAG, a novel zinc RING finger protein that protects cells from apoptosis induced by redox agents.". Mol. Cell. Biol. 19 (4): 3145–55. PMID 10082581.
Tan P, Fuchs SY, Chen A, et al. (1999). "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha.". Mol. Cell 3 (4): 527–33. PMID 10230406.
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. PMID 10230407.
Swaroop M, Bian J, Aviram M, et al. (1999). "Expression, purification, and biochemical characterization of SAG, a ring finger redox-sensitive protein.". Free Radic. Biol. Med. 27 (1-2): 193–202. PMID 10443936.
Sun Y (1999). "Alterations of SAG mRNA in human cancer cell lines: requirement for the RING finger domain for apoptosis protection.". Carcinogenesis 20 (10): 1899–903. PMID 10506102.
Son MY, Park JW, Kim YS, et al. (1999). "Protein kinase CKII interacts with and phosphorylates the SAG protein containing ring-H2 finger motif.". Biochem. Biophys. Res. Commun. 263 (3): 743–8. doi:10.1006/bbrc.1999.1460. PMID 10512750.
Chen A, Wu K, Fuchs SY, et al. (2000). "The conserved RING-H2 finger of ROC1 is required for ubiquitin ligation.". J. Biol. Chem. 275 (20): 15432–9. doi:10.1074/jbc.M907300199. PMID 10748083.
Swaroop M, Wang Y, Miller P, et al. (2000). "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: chip profiling implicates its role in cell cycle regulation.". Oncogene 19 (24): 2855–66. doi:10.1038/sj.onc.1203635. PMID 10851089.
Furukawa M, Zhang Y, McCarville J, et al. (2000). "The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1.". Mol. Cell. Biol. 20 (21): 8185–97. PMID 11027288.
Duan H, Tsvetkov LM, Liu Y, et al. (2001). "Promotion of S-phase entry and cell growth under serum starvation by SAG/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: association with inhibition of p27 accumulation.". Mol. Carcinog. 30 (1): 37–46. PMID 11255262.
Swaroop M, Gosink M, Sun Y (2001). "SAG/ROC2/Rbx2/Hrt2, a component of SCF E3 ubiquitin ligase: genomic structure, a splicing variant, and two family pseudogenes.". DNA Cell Biol. 20 (7): 425–34. doi:10.1089/104454901750361488. PMID 11506706.
Ahn BH, Kim TH, Bae YS (2002). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins.". Mol. Cells 12 (2): 158–63. PMID 11710515.
Furukawa M, Ohta T, Xiong Y (2002). "Activation of UBC5 ubiquitin-conjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins.". J. Biol. Chem. 277 (18): 15758–65. doi:10.1074/jbc.M108565200. PMID 11861641.
Kim SY, Bae YS, Park JW (2002). "Thiol-linked peroxidase activity of human sensitive to apoptosis gene (SAG) protein.". Free Radic. Res. 36 (1): 73–8. PMID 11999705.
Kim YS, Ha KS, Kim YH, Bae YS (2003). "The Ring-H2 finger motif of CKBBP1/SAG is necessary for interaction with protein kinase CKII and optimal cell proliferation.". J. Biochem. Mol. Biol. 35 (6): 629–36. PMID 12470599.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Kim SY, Lee JH, Yang ES, et al. (2003). "Human sensitive to apoptosis gene protein inhibits peroxynitrite-induced DNA damage.". Biochem. Biophys. Res. Commun. 301 (3): 671–4. PMID 12565832.
Kim YS, Lee JY, Son MY, et al. (2003). "Phosphorylation of threonine 10 on CKBBP1/SAG/ROC2/Rbx2 by protein kinase CKII promotes the degradation of IkappaBalpha and p27Kip1.". J. Biol. Chem. 278 (31): 28462–9. doi:10.1074/jbc.M302584200. PMID 12748192.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.