RNF7

RNF7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ECL
Identifiers
Aliases	RNF7 , CKBBP1, ROC2, SAG, ring finger protein 7, rbx2
External IDs	OMIM: 603863; MGI: 1337096; HomoloGene: 84476; GeneCards: RNF7; OMA:RNF7 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3q23 Start 141,738,249 bp [1] End 141,747,560 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 E3.3 Start 96,352,990 bp [2] End 96,360,728 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left adrenal gland left adrenal cortex right adrenal gland right adrenal cortex right testis muscle layer of sigmoid colon left testis anterior pituitary body of pancreas muscle of thigh Top expressed in Epithelium of choroid plexus ureter morula morula iris median eminence gastrula supraoptic nucleus epithelium of lens vestibular membrane of cochlear duct More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding zinc ion binding copper ion binding cullin family protein binding metal ion binding NEDD8 transferase activity ubiquitin protein ligase activity Cellular component nucleoplasm nucleus Cul5-RING ubiquitin ligase complex cytoplasm cytosol Cul2-RING ubiquitin ligase complex Cul3-RING ubiquitin ligase complex Cul7-RING ubiquitin ligase complex nuclear SCF ubiquitin ligase complex Cul4-RING E3 ubiquitin ligase complex cullin-RING ubiquitin ligase complex Biological process response to redox state protein ubiquitination protein neddylation post-translational protein modification SCF-dependent proteasomal ubiquitin-dependent protein catabolic process ubiquitin-dependent protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9616 19823 Ensembl ENSG00000114125 ENSMUSG00000051234 UniProt Q9UBF6 Q9WTZ1 RefSeq (mRNA) NM_001201370 NM_014245 NM_183063 NM_183237 NM_011279 NM_001311135 RefSeq (protein) NP_001188299 NP_055060 NP_899060 NP_001298064 NP_035409 Location (UCSC) Chr 3: 141.74 – 141.75 Mb Chr 9: 96.35 – 96.36 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

RING-box protein 2 is a protein that in humans is encoded by the RNF7 gene. ^{[5] [6] [7]}

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 p27^Kip1(CDKN1B). Alternatively spliced transcript variants encoding distinct isoforms have been reported. ^[7]

Interactions

RNF7 has been shown to interact with CSNK2B. ^[8]

See also

• RING finger domain

References

1. GRCh38: Ensembl release 89: ENSG00000114125 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000051234 – 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. Duan H, Wang Y, Aviram M, Swaroop M, Loo JA, Bian J, Tian Y, Mueller T, Bisgaier CL, Sun Y (April 1999). "SAG, a novel zinc RING finger protein that protects cells from apoptosis induced by redox agents". Mol Cell Biol. 19 (4): 3145–55. doi:10.1128/MCB.19.4.3145. PMC   84108 . PMID   10082581.
6. Ohta T, Michel JJ, Schottelius AJ, Xiong Y (May 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.
7. "Entrez Gene: RNF7 ring finger protein 7".
8. Ahn BH, Kim T H, Bae Y S (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells. 12 (2). Korea (South): 158–63. doi: 10.1016/S1016-8478(23)17077-4 . ISSN   1016-8478. PMID   11710515.

Further reading

• 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. doi: 10.1016/S1097-2765(00)80481-5 . PMID   10230406.
• 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. doi:10.1016/S0891-5849(99)00078-7. 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. doi: 10.1093/carcin/20.10.1899 . 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. doi:10.1128/MCB.20.21.8185-8197.2000. PMC   86428 . 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. doi:10.1002/1098-2744(200101)30:1<37::AID-MC1011>3.0.CO;2-7. PMID   11255262. S2CID   12999764.
• 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" (PDF). DNA Cell Biol. 20 (7): 425–34. doi:10.1089/104454901750361488. hdl: 2027.42/63441 . 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. doi: 10.1016/S1016-8478(23)17077-4 . 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. doi:10.1080/10715760210164. PMID   11999705. S2CID   39810540.
• 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. doi: 10.5483/bmbrep.2002.35.6.629 . 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . 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. doi:10.1016/S0006-291X(03)00018-4. 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. PMC   528928 . 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.

External links

• RNF7+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)