RNF7

Protein-coding gene in the species Homo sapiens

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]
Band	3q23	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]
Band	9\|9 E3.3	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 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.