RNF111

RNF111
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2KIZ
Identifiers
Aliases	RNF111 , ARK, ring finger protein 111, hRNF111
External IDs	OMIM: 605840 MGI: 1934919 HomoloGene: 9741 GeneCards: RNF111
Gene location (Human)
Chr.	Chromosome 15 (human)
End	59,097,419 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	70,411,007 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; endothelial cell; ; monocyte; ; ganglionic eminence; ; stromal cell of endometrium; ; thymus; ; sural nerve; ; Achilles tendon; ; blood; ; corpus epididymis;
	Top expressed in
	cumulus cell; ; secondary oocyte; ; primitive streak; ; blood; ; parotid gland; ; pineal gland; ; lymph node; ; aortic valve; ; renal corpuscle; ; skin of back;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	SUMO polymer binding ; protein binding ; metal ion binding ; ubiquitin protein ligase activity ; transferase activity ; SMAD binding ;
Cellular component	nucleoplasm ; nucleus ; cytoplasm ; cytosol ; PML body ; protein-containing complex ;
Biological process	positive regulation of transcription, DNA-templated ; ubiquitin-dependent SMAD protein catabolic process ; protein polyubiquitination ; multicellular organism development ; positive regulation of transforming growth factor beta receptor signaling pathway ; positive regulation of protein ubiquitination ; pattern specification process ; proteasome-mediated ubiquitin-dependent protein catabolic process ; protein ubiquitination ; global genome nucleotide-excision repair ; positive regulation of transcription by RNA polymerase II ; DNA repair ; cellular response to DNA damage stimulus ; ubiquitin-dependent protein catabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	54778
	93836
	ENSG00000157450
	ENSMUSG00000032217
	Q6ZNA4
	Q99ML9
	NM_001270528 ; NM_001270529 ; NM_001270530 ; NM_017610 ; NM_001330331 Contents Function ; Interactions ; References ; Further reading ;
	NM_033604 ; NM_001357494 ; NM_001374753
	NP_001257457 ; NP_001257458 ; NP_001257459 ; NP_001317260 ; NP_060080
	NP_291082 ; NP_001344423 ; NP_001361682
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 12, 2024

E3 ubiquitin-protein ligase Arkadia is an enzyme that in humans is encoded by the RNF111 gene.^[5]^[6]

Function

The protein encoded by this gene contains a RING finger domain, a motif known to be involved in protein-protein and protein-DNA interactions. The mouse counterpart of this gene (Rnf111/arkadia) has been shown to genetically interact with the transforming growth factor (TGF) beta-like factor Nodal, and act as a modulator of the nodal signaling cascade, which is essential for the induction of mesoderm during embryonic development.^[6]

Interactions

RNF111 has been shown to interact with Mothers against decapentaplegic homolog 7 ^[7] and Mothers against decapentaplegic homolog 3.^[7]^[8]

Related Research Articles

Mothers against decapentaplegic homolog 2, also known as SMAD family member 2 or SMAD2, is a protein that in humans is encoded by the SMAD2 gene. MAD homolog 2 belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways.

SMAD4, also called SMAD family member 4, Mothers against decapentaplegic homolog 4, or DPC4 is a highly conserved protein present in all metazoans. It belongs to the SMAD family of transcription factor proteins, which act as mediators of TGF-β signal transduction. The TGFβ family of cytokines regulates critical processes during the lifecycle of metazoans, with important roles during embryo development, tissue homeostasis, regeneration, and immune regulation.

SMAD family member 6, also known as SMAD6, is a protein that in humans is encoded by the SMAD6 gene.

Mothers against decapentaplegic homolog 7 or SMAD7 is a protein that in humans is encoded by the SMAD7 gene.

R-SMADs are receptor-regulated SMADs. SMADs are transcription factors that transduce extracellular TGF-β superfamily ligand signaling from cell membrane bound TGF-β receptors into the nucleus where they activate transcription TGF-β target genes. R-SMADS are directly phosphorylated on their c-terminus by type 1 TGF-β receptors through their intracellular kinase domain, leading to R-SMAD activation.

Smads comprise a family of structurally similar proteins that are the main signal transducers for receptors of the transforming growth factor beta (TGF-B) superfamily, which are critically important for regulating cell development and growth. The abbreviation refers to the homologies to the Caenorhabditis elegans SMA and MAD family of genes in Drosophila.

The transforming growth factor beta (TGFB) signaling pathway is involved in many cellular processes in both the adult organism and the developing embryo including cell growth, cell differentiation, cell migration, apoptosis, cellular homeostasis and other cellular functions. The TGFB signaling pathways are conserved. In spite of the wide range of cellular processes that the TGFβ signaling pathway regulates, the process is relatively simple. TGFβ superfamily ligands bind to a type II receptor, which recruits and phosphorylates a type I receptor. The type I receptor then phosphorylates receptor-regulated SMADs (R-SMADs) which can now bind the coSMAD SMAD4. R-SMAD/coSMAD complexes accumulate in the nucleus where they act as transcription factors and participate in the regulation of target gene expression.

Lefty are a class of proteins that are closely related members of the TGF-beta superfamily of growth factors. These proteins are secreted and play a role in left-right asymmetry determination of organ systems during development. Mutations of the genes encoding these proteins have been associated with left-right axis malformations, particularly in the heart and lungs.

The bone morphogenetic protein receptor, type IA also known as BMPR1A is a protein which in humans is encoded by the BMPR1A gene. BMPR1A has also been designated as CD292.

Activin receptor type-1B is a protein that in humans is encoded by the ACVR1B gene.

Betaglycan also known as Transforming growth factor beta receptor III (TGFBR3), is a cell-surface chondroitin sulfate / heparan sulfate proteoglycan >300 kDa in molecular weight. Betaglycan binds to various members of the TGF-beta superfamily of ligands via its core protein, and bFGF via its heparan sulfate chains. TGFBR3 is the most widely expressed type of TGF-beta receptor. Its affinity towards all individual isoforms of TGF-beta is similarly high and therefore it plays an important role as a coreceptor mediating the binding of TGF-beta to its other receptors - specifically TGFBR2. The intrinsic kinase activity of this receptor has not yet been described. In regard of TGF-beta signalling it is generally considered a non-signaling receptor or a coreceptor. By binding to various member of the TGF-beta superfamily at the cell surface it acts as a reservoir of TGF-beta.

Transforming growth factor beta receptor I is a membrane-bound TGF beta receptor protein of the TGF-beta receptor family for the TGF beta superfamily of signaling ligands. TGFBR1 is its human gene.

Transforming growth factor, beta receptor II (70/80kDa) is a TGF beta receptor. TGFBR2 is its human gene.

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA gene.

Mitogen-activated protein kinase kinase kinase 7-interacting protein 1 is an enzyme that in humans is encoded by the TAB1 gene.

E3 ubiquitin-protein ligase SMURF1 is an enzyme that in humans is encoded by the SMURF1 gene. The SMURF1 Gene encodes a protein with a size of 757 amino acids and the molecular mass of this protein is 86114 Da.

Ski-like protein is a protein that in humans is encoded by the SKIL gene.

Axin-2, also known as axin-like protein (Axil), axis inhibition protein 2 (AXIN2), or conductin, is a protein that in humans is encoded by the AXIN2 gene.

NEDD4-like E3 ubiquitin-protein ligase WWP1 is an enzyme that in humans is encoded by the WWP1 gene.

E3 ubiquitin-protein ligase SMURF2 is an enzyme that in humans is encoded by the SMURF2 gene which is located at chromosome 17q23.3-q24.1.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000157450 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032217 - 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.
↑ Episkopou V, Arkell R, Timmons PM, Walsh JJ, Andrew RL, Swan D (Apr 2001). "Induction of the mammalian node requires Arkadia function in the extraembryonic lineages". Nature. 410 (6830): 825–30. Bibcode:2001Natur.410..825E. doi:10.1038/35071095. PMID 11298452. S2CID 38456861.
1 2 "Entrez Gene: RNF111 ring finger protein 111".
1 2 Koinuma D, Shinozaki M, Komuro A, Goto K, Saitoh M, Hanyu A, Ebina M, Nukiwa T, Miyazawa K, Imamura T, Miyazono K (Dec 2003). "Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7". The EMBO Journal. 22 (24): 6458–70. doi:10.1093/emboj/cdg632. PMC 291827 . PMID 14657019.
↑ Yuzawa H, Koinuma D, Maeda S, Yamamoto K, Miyazawa K, Imamura T (Jan 2009). "Arkadia represses the expression of myoblast differentiation markers through degradation of Ski and the Ski-bound Smad complex in C2C12 myoblasts". Bone. 44 (1): 53–60. doi:10.1016/j.bone.2008.09.013. PMID 18950738.

Patten I, Placzek M (Aug 2001). "Vertebrate development: Et in Arkadia". Current Biology. 11 (15): R616-9. Bibcode:2001CBio...11.R616P. doi: 10.1016/S0960-9822(01)00367-0 . PMID 11516970.
Niederländer C, Walsh JJ, Episkopou V, Jones CM (Apr 2001). "Arkadia enhances nodal-related signalling to induce mesendoderm". Nature. 410 (6830): 830–4. Bibcode:2001Natur.410..830N. doi:10.1038/35071103. PMID 11298453. S2CID 4322926.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (Dec 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Koinuma D, Shinozaki M, Komuro A, Goto K, Saitoh M, Hanyu A, Ebina M, Nukiwa T, Miyazawa K, Imamura T, Miyazono K (Dec 2003). "Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7". The EMBO Journal. 22 (24): 6458–70. doi:10.1093/emboj/cdg632. PMC 291827 . PMID 14657019.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148 . PMID 15231748.
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 (Oct 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.
Liu W, Rui H, Wang J, Lin S, He Y, Chen M, Li Q, Ye Z, Zhang S, Chan SC, Chen YG, Han J, Lin SC (Apr 2006). "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia". The EMBO Journal. 25 (8): 1646–58. doi:10.1038/sj.emboj.7601057. PMC 1440825 . PMID 16601693.
Nagano Y, Mavrakis KJ, Lee KL, Fujii T, Koinuma D, Sase H, Yuki K, Isogaya K, Saitoh M, Imamura T, Episkopou V, Miyazono K, Miyazawa K (Jul 2007). "Arkadia induces degradation of SnoN and c-Ski to enhance transforming growth factor-beta signaling". The Journal of Biological Chemistry. 282 (28): 20492–501. doi: 10.1074/jbc.M701294200 . PMID 17510063.
Levy L, Howell M, Das D, Harkin S, Episkopou V, Hill CS (Sep 2007). "Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation". Molecular and Cellular Biology. 27 (17): 6068–83. doi:10.1128/MCB.00664-07. PMC 1952153 . PMID 17591695.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000157450 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032217 - 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.

[pmid11298452-5] Episkopou V, Arkell R, Timmons PM, Walsh JJ, Andrew RL, Swan D (Apr 2001). "Induction of the mammalian node requires Arkadia function in the extraembryonic lineages". Nature. 410 (6830): 825–30. Bibcode:2001Natur.410..825E. doi:10.1038/35071095. PMID 11298452. S2CID 38456861.

[entrez-6] 1 2 "Entrez Gene: RNF111 ring finger protein 111".

[pmid14657019-7] 1 2 Koinuma D, Shinozaki M, Komuro A, Goto K, Saitoh M, Hanyu A, Ebina M, Nukiwa T, Miyazawa K, Imamura T, Miyazono K (Dec 2003). "Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7". The EMBO Journal. 22 (24): 6458–70. doi:10.1093/emboj/cdg632. PMC 291827 . PMID 14657019.

[pmid18950738-8] Yuzawa H, Koinuma D, Maeda S, Yamamoto K, Miyazawa K, Imamura T (Jan 2009). "Arkadia represses the expression of myoblast differentiation markers through degradation of Ski and the Ski-bound Smad complex in C2C12 myoblasts". Bone. 44 (1): 53–60. doi:10.1016/j.bone.2008.09.013. PMID 18950738.

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RNF111

Contents

Function

Interactions

Related Research Articles

References

Further reading