RNF12

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

RLIM
Identifiers
Aliases	RLIM, NY-REN-43, RNF12, ring finger protein, LIM domain interacting, MRX61, TOKAS
External IDs	OMIM: 300379 MGI: 1342291 HomoloGene: 7920 GeneCards: RLIM
Gene location (Human) Chr. X chromosome (human)[1] Band Xq13.2 Start 74,582,976 bp[1] End 74,614,624 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X 46.42 cM|X D Start 103,957,163 bp[2] End 103,981,284 bp[2]
Gene ontology Molecular function • GO:0001106 transcription corepressor activity • metal ion binding • transferase activity • ubiquitin-protein transferase activity • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity • GO:0001948 protein binding Cellular component • transcriptional repressor complex • cell nucleus • cytosol • nucleoplasm Biological process • negative regulation of transcription, DNA-templated • transcription, DNA-templated • protein ubiquitination • proteasome-mediated ubiquitin-dependent protein catabolic process • protein polyubiquitination • regulation of transcription, DNA-templated • negative regulation of transcription from RNA polymerase II promoter • ubiquitin-dependent protein catabolic process • negative regulation of sequence-specific DNA binding transcription factor activity • random inactivation of X chromosome • regulation of dosage compensation by inactivation of X chromosome Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51132	19820
Ensembl	ENSG00000131263	ENSMUSG00000056537
UniProt	Q9NVW2	Q9WTV7
RefSeq (mRNA)	NM_183353 NM_016120	NM_011276 NM_001358205
RefSeq (protein)	NP_057204 NP_899196	NP_035406 NP_001345134
Location (UCSC)	Chr X: 74.58 – 74.61 Mb	Chr X: 103.96 – 103.98 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is a RING-H2 zinc finger protein. It has been shown to be a ubiquitin protein ligase that targets LIM domain binding 1 (LDB1/CLIM), and causes proteasome-dependent degradation of LDB1. This protein and LDB1 are co-repressors of LHX1/LIM-1, a homeodomain transcription factor. Alternatively spliced transcript variants encoding the same protein have been reported.[6] Functions in female mice as a regulator of X chromosome inactivation .

Interactions

RNF12 has been shown to interact with Estrogen receptor alpha.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000131263 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000056537 - 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. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jäger D, Jäger E, Knuth A, Chen YT, Old LJ (Nov 1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479.
6. "Entrez Gene: RNF12 ring finger protein 12".
7. Johnsen SA, Güngör C, Prenzel T, Riethdorf S, Riethdorf L, Taniguchi-Ishigaki N, Rau T, Tursun B, Furlow JD, Sauter G, Scheffner M, Pantel K, Gannon F, Bach I (Jan 2009). "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer". Cancer Res. 69 (1): 128–36. doi:10.1158/0008-5472.CAN-08-1630. PMC 2713826. PMID 19117995.

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. doi:10.1038/nature04209. PMID 16189514.
• Hiratani I, Yamamoto N, Mochizuki T, Ohmori SY, Taira M (2003). "Selective degradation of excess Ldb1 by Rnf12/RLIM confers proper Ldb1 expression levels and Xlim-1/Ldb1 stoichiometry in Xenopus organizer functions". Development. 130 (17): 4161–75. doi:10.1242/dev.00621. PMID 12874135.
• Ostendorff HP, Peirano RI, Peters MA, Schlüter A, Bossenz M, Scheffner M, Bach I (2002). "Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors". Nature. 416 (6876): 99–103. doi:10.1038/416099a. PMID 11882901.
• Ostendorff HP, Bossenz M, Mincheva A, Copeland NG, Gilbert DJ, Jenkins NA, Lichter P, Bach I (2000). "Functional characterization of the gene encoding RLIM, the corepressor of LIM homeodomain factors". Genomics. 69 (1): 120–30. doi:10.1006/geno.2000.6311. PMID 11013082.
• Bach I, Rodriguez-Esteban C, Carrière C, Bhushan A, Krones A, Rose DW, Glass CK, Andersen B, Izpisúa Belmonte JC, Rosenfeld MG (1999). "RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex". Nat. Genet. 22 (4): 394–9. doi:10.1038/11970. PMID 10431247.
• Shin J, Bossenz M, Chung Y, Ma H, Byron M, Taniguchi-Ishigaki N, Zhu X, Jiao B, Hall LL, Green MR, Jones SN, Hermans-Borgmeyer I, Lawrence JB, Bach I (2010). "Maternal Rnf12/RLIM is required for imprinted X-chromosome inactivation in mice". Nature. 467 (7318): 977–81. doi:10.1038/nature09457. PMC 2967734. PMID 20962847.
• Jiao B, Taniguchi-Ishigaki N, Güngör C, Peters MA, Chen YW, Riethdorf S, Drung A, Ahronian LG, Shin J, Pagnis R, Pantel K, Tachibana T, Lewis BC, Johnsen SA, Bach I (2013). "Functional activity of RLIM/Rnf12 is regulated by phosphorylation-dependent nucleocytoplasmic shuttling". Mol Biol Cell. 24 (19): 3085–96. doi:10.1091/mbc.E13-05-0239. PMC 3784382. PMID 23904271.