RNF25

Protein-coding gene in the species Homo sapiens
RNF25
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2DAY, 2DMF, 5D1M, 5D1L, 5D1K

Identifiers
AliasesRNF25, AO7, ring finger protein 25
External IDsOMIM: 616014; MGI: 1890215; HomoloGene: 11193; GeneCards: RNF25; OMA:RNF25 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for RNF25
Genomic location for RNF25
Band2q35Start218,663,892 bp[1]
End218,672,002 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for RNF25
Genomic location for RNF25
Band1|1 C4Start74,632,907 bp[2]
End74,640,556 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • anterior pituitary

  • granulocyte

  • popliteal artery

  • tibial arteries

  • prefrontal cortex

  • Descending thoracic aorta

  • left testis

  • right testis

  • stromal cell of endometrium

  • right frontal lobe
Top expressed in
  • neural layer of retina

  • granulocyte

  • spermatid

  • superior frontal gyrus

  • yolk sac

  • seminiferous tubule

  • cerebellar cortex

  • dentate gyrus of hippocampal formation granule cell

  • ventricular zone

  • primary visual cortex
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • ubiquitin protein ligase activity
  • NF-kappaB binding
  • ubiquitin-protein transferase activity
  • transferase activity
  • protein binding
Cellular component
  • cytosol
  • nucleus
Biological process
  • positive regulation of NF-kappaB transcription factor activity
  • protein ubiquitination
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

64320

57751

Ensembl

ENSG00000163481

ENSMUSG00000026171

UniProt

Q96BH1

Q9QZR0

RefSeq (mRNA)

NM_022453

NM_021313
NM_001305230

RefSeq (protein)

NP_071898

NP_001292159
NP_067288

Location (UCSC)Chr 2: 218.66 – 218.67 MbChr 1: 74.63 – 74.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

E3 ubiquitin-protein ligase RNF25 is an enzyme that in humans is encoded by the RNF25 gene.[5][6]

Function

The protein encoded by this gene contains a RING finger motif. The mouse counterpart of this protein has been shown to interact with Rela, the p65 subunit of NF-kappaB (NF-κB), and modulate NF-κB-mediated transcription activity. The mouse protein also binds ubiquitin-conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination.[6]

Interactions

RNF25 has been shown to interact with RELA.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163481 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026171 – 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. ^ a b Asamitsu K, Tetsuka T, Kanazawa S, Okamoto T (Jul 2003). "RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit". J. Biol. Chem. 278 (29): 26879–87. doi:10.1074/jbc.M211831200. PMID 12748188.
  6. ^ a b "Entrez Gene: RNF25 ring finger protein 25".

Further reading

  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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.
  • Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM (1999). "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11364–9. Bibcode:1999PNAS...9611364L. doi:10.1073/pnas.96.20.11364. PMC 18039. PMID 10500182.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • v
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  • 2day: Solution structure of the RWD domain of human ring finger protein 25
    2day: Solution structure of the RWD domain of human ring finger protein 25
  • 2dmf: An extended conformation of the RWD domain of human Ring finger protein 25
    2dmf: An extended conformation of the RWD domain of human Ring finger protein 25


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