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)
End	141,747,560 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	96,360,728 bp
RNA expression pattern
	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
	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
	9616
	19823
	ENSG00000114125
	ENSMUSG00000051234
	Q9UBF6
	Q9WTZ1
	NM_001201370; NM_014245; NM_183063; NM_183237
	NM_011279; NM_001311135
	NP_001188299; NP_055060; NP_899060
	NP_001298064; NP_035409
	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 p27Kip1(CDKN1B). Alternatively spliced transcript variants encoding distinct isoforms have been reported.^[7]

Interactions

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

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000114125 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000051234 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: RNF7 ring finger protein 7".
^ 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.

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)

This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000114125 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid10082581-5] 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.

[pmid10230407-6] 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.

[entrez-7] "Entrez Gene: RNF7 ring finger protein 7".

[pmid11710515-8] 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.

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[7]

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[2]

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[4]

[8]

RNF7

Contents

Interactions

See also

References

Further reading

External links