View source for RNF113A

'''Ring Finger Protein 113A''' is a protein that in humans is encoded by the RNF113A gene. It is found in humans on the [[X Chromosome]]. RNF113A contains two highly conserved domains, the [[RING finger domain|RING (Really Interesting New Gene) finger domain]] and [[Zinc finger]] domain.<ref name=NM_006978.2>{{cite web|title=Homo sapiens ring finger protein 113A (RNF113A), mRNA|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_006978.2|website=NCBI Nucleotide|accessdate=30 April 2015}}</ref> [[RING finger domain]]s have been associated with some [[Tumor suppressor gene|tumor suppressors]] and cytokine receptor-associated molecules. These domains also act in [[DNA repair]] and mediating protein-protein interactions.<ref name=NM_006978.2 /><ref name="Gene ID: 7737">{{cite web|title=RNF113A ring finger protein 113A [ Homo sapiens (human) ]|url=https://www.ncbi.nlm.nih.gov/gene/7737|website=NCBI Gene|accessdate=30 April 2015}}</ref> Aliases of RNF113A across taxa include RNF113, CWC24, and ZNF183.
==Gene==
The gene is found on the human [[X Chromosome]] and reverse strand. The specific locus in humans is Xq24.<ref name=NM_006978.2 /> RNF113A contains 1312 [[nucleotides]].
[[File:RNF113A Human Xq24 Locus.JPG|thumb|center|upright=5.0|The red bar in white band q24 represents the location of the gene RFN113A on the human X chromosome.]]
===Gene Structure===
An upstream in-frame stop codon is found within the [[5' UTR]]. RNF113A is an [[intron]]less gene with one [[Gene isoform|isoform]] in humans.<ref name=NM_006978.2 />
==Protein==
RNF113A [[Translation|translates]] a human protein 343 [[amino acid]]s long and molecular weight of 38.8 [[Dalton (unit)|kilodaltons]].<ref name=NP_008909.1>{{cite web|title=RING finger protein 113A [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/5902158|website=NCBI Protein|accessdate=2 May 2015}}</ref> The protein is found ubiquitously in the human body.<ref>Identification of a new member (ZNF183) of the Ring finger gene family in Xq24-25</ref><ref name=Frattini>{{cite journal|last1=Frattini|first1=Annalisa|last2=Faranda|first2=Sara|last3=Bagnasco|first3=Luca|last4=Patrosso|first4=Cristina|last5=Nulli|first5=Paola|last6=Zucchi|first6=Ileana|last7=Vezzoni|first7=Paolo|title=Identification of a new member (ZNF183) of the Ring finger gene family in Xq24-25|journal=Gene|date=June 1997|volume=192|issue=2|pages=291–298|doi=10.1016/S0378-1119(97)00108-X|pmid=9224902}}</ref>
[[Two-hybrid screening|Yeast Two Hybrid Screens]] link RNF113A with other proteins. Most of these proteins are currently known to function in the human [[Spliceosome]].<ref name=Hegele>{{cite journal|last1=Hegele|first1=Anna|last2=Kamburov|first2=Atanas|last3=Grossmann|first3=Arndt|last4=Sourlis|first4=Chrysovalantis|last5=Wowro|first5=Sylvia|last6=Weimann|first6=Mareike|last7=Will|first7=Cindy L.|last8=Pena|first8=Vlad|last9=Lührmann|first9=Reinhard|last10=Stelzl|first10=Ulrich|title=Dynamic Protein-Protein Interaction Wiring of the Human Spliceosome|journal=Molecular Cell|date=February 2012|volume=45|issue=4|pages=567–580|doi=10.1016/j.molcel.2011.12.034|pmid=22365833|doi-access=free}}</ref> Some of these associations are within the U4, U5, and U6 [[snRNP]]s much the same as within yeast models.<ref name=Coltri>{{cite journal|last1=Coltri|first1=Patricia P.|last2=Oliveira|first2=Carla C.|last3=Maas|first3=Stefan|title=Cwc24p Is a General Saccharomyces cerevisiae Splicing Factor Required for the Stable U2 snRNP Binding to Primary Transcripts|journal=PLOS ONE|date=24 September 2012|volume=7|issue=9|pages=e45678|doi=10.1371/journal.pone.0045678|pmid=23029180|pmc=3454408|bibcode=2012PLoSO...745678C|doi-access=free}}</ref>
===Protein Structure===
RNF113A also contains one acetylation and four phosphorylation sites.<ref name=NM_006978.2 /> The protein has both an [[acetylation]] and four [[phosphorylation]] sites which have been confirmed experimentally.<ref name=Mayya>{{cite journal|last1=Mayya|first1=V.|last2=Lundgren|first2=D. H.|last3=Hwang|first3=S.-I.|last4=Rezaul|first4=K.|last5=Wu|first5=L.|last6=Eng|first6=J. K.|last7=Rodionov|first7=V.|last8=Han|first8=D. K.|title=Quantitative Phosphoproteomic Analysis of T Cell Receptor Signaling Reveals System-Wide Modulation of Protein-Protein Interactions|journal=Science Signaling|date=18 August 2009|volume=2|issue=84|pages=ra46|doi=10.1126/scisignal.2000007|pmid=19690332|s2cid=206670149}}</ref><ref name=Dephoure>{{cite journal|last1=Dephoure|first1=N.|last2=Zhou|first2=C.|last3=Villen|first3=J.|last4=Beausoleil|first4=S. A.|last5=Bakalarski|first5=C. E.|last6=Elledge|first6=S. J.|last7=Gygi|first7=S. P.|title=A quantitative atlas of mitotic phosphorylation|journal=Proceedings of the National Academy of Sciences|date=31 July 2008|volume=105|issue=31|pages=10762–10767|doi=10.1073/pnas.0805139105|pmid=18669648|pmc=2504835|bibcode=2008PNAS..10510762D|doi-access=free}}</ref><ref name=Rigbolt>{{cite journal|last1=Rigbolt|first1=K. T. G.|last2=Prokhorova|first2=T. A.|last3=Akimov|first3=V.|last4=Henningsen|first4=J.|last5=Johansen|first5=P. T.|last6=Kratchmarova|first6=I.|last7=Kassem|first7=M.|last8=Mann|first8=M.|last9=Olsen|first9=J. V.|last10=Blagoev|first10=B.|title=System-Wide Temporal Characterization of the Proteome and Phosphoproteome of Human Embryonic Stem Cell Differentiation|journal=Science Signaling|date=15 March 2011|volume=4|issue=164|pages=rs3|doi=10.1126/scisignal.2001570|pmid=21406692|s2cid=206670774}}</ref><ref name=Olsen>{{cite journal|last1=Olsen|first1=J. V.|last2=Vermeulen|first2=M.|last3=Santamaria|first3=A.|last4=Kumar|first4=C.|last5=Miller|first5=M. L.|last6=Jensen|first6=L. J.|last7=Gnad|first7=F.|last8=Cox|first8=J.|last9=Jensen|first9=T. S.|last10=Nigg|first10=E. A.|last11=Brunak|first11=S.|last12=Mann|first12=M.|title=Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis|journal=Science Signaling|date=12 January 2010|volume=3|issue=104|pages=ra3|doi=10.1126/scisignal.2000475|pmid=20068231|s2cid=24775963}}</ref><ref name=Gauci>{{cite journal|last1=Gauci|first1=Sharon|last2=Helbig|first2=Andreas O.|last3=Slijper|first3=Monique|last4=Krijgsveld|first4=Jeroen|last5=Heck|first5=Albert J. R.|last6=Mohammed|first6=Shabaz|title=Lys-N and Trypsin Cover Complementary Parts of the Phosphoproteome in a Refined SCX-Based Approach|journal=Analytical Chemistry|date=June 2009|volume=81|issue=11|pages=4493–4501|doi=10.1021/ac9004309|pmid=19413330}}</ref> Additional phosphorylation sites and one glycosylation site are also predicted.<ref name=NetPhos>{{cite web|title=NetPhos 2.0|url=http://www.cbs.dtu.dk/cgi-bin/webface2.fcgi?jobid=554428310000471A9D6069C2&wait=20|website=ExPasy|accessdate=2 May 2015}}</ref> The [[N terminus]] or [[3']] end of the gene contains the conserved [[RING finger domain|RING]] and [[Zinc finger]] domains. The [[RING finger domain]] contains a cross-brace motif consisting of 6 [[Cystine]]s and 1 [[Histidine]].The [[Zinc finger]] is formed by 3 [[Cystine]]s and 1 [[Histidine]]<ref>NCBI Protein NP_008909.1 https://www.ncbi.nlm.nih.gov/protein/NP_008909.1</ref><ref name="GenBank: AAP35839.1">{{cite web|title=zinc finger protein 183 (RING finger, C3HC4 type) [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/AAP35839.1|website=NCBI Protein|accessdate=30 April 2015}}</ref><ref name=EAW89841.1>{{cite web|title=ring finger protein 113A [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/EAW89841.1|website=NCBI Protein|accessdate=30 April 2015}}</ref><ref name="GenBank: CAA66907.1">{{cite web|title=ZNF183 [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/CAA66907.1|website=NCBI Protein|accessdate=30 April 2015}}</ref><ref name="GenBank: AAH20556.1">{{cite web|title=Ring finger protein 113A [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/AAH20556.1|website=NCBI Protein|accessdate=30 April 2015}}</ref><ref name="GenBank: AAH00832.1">{{cite web|title=Ring finger protein 113A [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/AAH00832.1|website=NCBI Protein|accessdate=30 April 2015}}</ref> Typically, [[RING finger domain]]s are located near the [[C terminus]] or [[5']] end of the protein rather than the [[N terminus]] making RNF113A unique. RING finger proteins also usually have multiple types of domains outside of the [[Zinc finger]] family.<ref name="Frattini"/>
[[File:Solution Structure of the Ring Domain of the Zinc Finger Protein 183-like 1.JPG|thumb|upright=1.5|The C-terminus end of the early isolated paralog RNF113B, formerly known as Zing Finger Protein 183-like 1, contains the RING domain in yellow to the C-terminus. The known alpha-helices and beta-sheets are visible. The two grey spheres represent zinc atoms.]]
[[Secondary structure]] of the RING domain has been confirmed for the paralog, RNF113B. Two [[Beta sheet]]s and one [[Alpha helix]] are present within the domain.<ref name="Protein Structure">{{cite web|title=MMDB Protein Structure Summary|url=https://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=36404|website=NCBI Structure|accessdate=2 May 2015}}</ref> A second [[Alpha helix]] is present on the 5' side of the RING domain.
==Function==
===Human===
The RNF113A protein was identified as a [[phosphoprotein]] in a human prostate cancer cell line but the function was not tested.<ref name=Giorgianni>{{cite journal|last1=Giorgianni|first1=Francesco|last2=Zhao|first2=Yingxin|last3=Desiderio|first3=Dominic M.|last4=Beranova-Giorgianni|first4=Sarka|title=Toward a global characterization of the phosphoproteome in prostate cancer cells: Identification of phosphoproteins in the LNCaP cell line|journal=Electrophoresis|date=June 2007|volume=28|issue=12|pages=2027–2034|doi=10.1002/elps.200600782|pmid=17487921|s2cid=27568834}}</ref> [[OMIM|Online Mendelian Inheritance in Man (OMIM)]] links mutation of RNF113A with [[trichothiodystrophy]] 5, nonphotosensitive.<ref name=OMIM300953>{{cite web | title=OMIM Entry - #300953 - TRICHOTHIODYSTROPHY 5, NONPHOTOSENSITIVE; TTD5 | url=http://omim.org/entry/300953 | website=OMIM | accessdate=1 October 2015}}</ref> One case study reported a [[nonsense mutation]] resulting from changing a [[cytosine]] to a [[thymidine]] in RNF113A that causes [[X-linked]] [[recessive]] [[trichothiodystrophy]].  Mothers are the carriers for the disease and display only slightly altered [[phenotype]]s that were linked to the [[mutation]] compared to their more severely affected sons.<ref name=Corbett>{{cite journal|last1=Corbett|first1=M. A.|last2=Dudding-Byth|first2=T.|last3=Crock|first3=P. A.|last4=Botta|first4=E.|last5=Christie|first5=L. M.|last6=Nardo|first6=T.|last7=Caligiuri|first7=G.|last8=Hobson|first8=L.|last9=Boyle|first9=J.|last10=Mansour|first10=A.|last11=Friend|first11=K. L.|last12=Crawford|first12=J.|last13=Jackson|first13=G.|last14=Vandeleur|first14=L.|last15=Hackett|first15=A.|last16=Tarpey|first16=P.|last17=Stratton|first17=M. R.|last18=Turner|first18=G.|last19=Gecz|first19=J.|last20=Field|first20=M.|title=A novel X-linked trichothiodystrophy associated with a nonsense mutation in RNF113A|journal=Journal of Medical Genetics|date=22 January 2015|volume=52|issue=4|pages=269–274|doi=10.1136/jmedgenet-2014-102418|pmid=25612912|s2cid=33872845}}</ref> [[Myelodysplastic syndrome]] and [[Chromosome 5q deletion syndrome|5q-syndrome]] have also been linked to an upregulation of ZNF183, an alias of RNF113A.<ref name=Pellagatti>{{cite journal|last1=Pellagatti|first1=Andrea|last2=Esoof|first2=Noor|last3=Watkins|first3=Fiona|last4=Langford|first4=Cordelia F.|last5=Vetrie|first5=David|last6=Campbell|first6=Lisa J.|last7=Fidler|first7=Carrie|last8=Cavenagh|first8=James D.|last9=Eagleton|first9=Helen|last10=Gordon|first10=Peter|last11=Woodcock|first11=Barrie|last12=Pushkaran|first12=Beena|last13=Kwan|first13=Mark|last14=Wainscoat|first14=James S.|last15=Boultwood|first15=Jacqueline|title=Gene expression profiling in the myelodysplastic syndromes using cDNA microarray technology|journal=British Journal of Haematology|date=June 2004|volume=125|issue=5|pages=576–583|doi=10.1111/j.1365-2141.2004.04958.x|pmid=15147372|doi-access=free}}</ref> It appears RNF113A may allow for a more stable activated [[spliceosome]] and post-catalytic [[spliceosome]].<ref name=Ilagan>{{cite journal|last1=Ilagan|first1=J. O.|last2=Chalkley|first2=R. J.|last3=Burlingame|first3=A. L.|last4=Jurica|first4=M. S.|title=Rearrangements within human spliceosomes captured after exon ligation|journal=RNA|date=23 January 2013|volume=19|issue=3|pages=400–412|doi=10.1261/rna.034223.112|pmid=23345524|pmc=3677250}}</ref><ref name=Bessonov>{{cite journal|last1=Bessonov|first1=S.|last2=Anokhina|first2=M.|last3=Krasauskas|first3=A.|last4=Golas|first4=M. M.|last5=Sander|first5=B.|last6=Will|first6=C. L.|last7=Urlaub|first7=H.|last8=Stark|first8=H.|last9=Luhrmann|first9=R.|title=Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis|journal=RNA|date=27 October 2010|volume=16|issue=12|pages=2384–2403|doi=10.1261/rna.2456210|pmid=20980672|pmc=2995400}}</ref>
===Yeast===
The yeast [[Homology (biology)|ortholog]] Cwc24p is predicted to have a [[spliceosome]] function.<ref name=Fabrizio>{{cite journal|last1=Fabrizio|first1=Patrizia|last2=Dannenberg|first2=Julia|last3=Dube|first3=Prakash|last4=Kastner|first4=Berthold|last5=Stark|first5=Holger|last6=Urlaub|first6=Henning|last7=Lührmann|first7=Reinhard|title=The Evolutionarily Conserved Core Design of the Catalytic Activation Step of the Yeast Spliceosome|journal=Molecular Cell|date=November 2009|volume=36|issue=4|pages=593–608|doi=10.1016/j.molcel.2009.09.040|pmid=19941820|doi-access=free|hdl=11858/00-001M-0000-0010-9378-C|hdl-access=free}}</ref> The protein acts in a complex with Cef1p to process pre-rRNA. The splicing is dependent on the [[Zinc finger]] and [[RING finger domain]]s.<ref name=Goldfeder>{{cite journal|last1=Goldfeder|first1=M. B.|last2=Oliveira|first2=C. C.|title=Cwc24p, a Novel Saccharomyces cerevisiae Nuclear Ring Finger Protein, Affects Pre-snoRNA U3 Splicing|journal=Journal of Biological Chemistry|date=1 November 2007|volume=283|issue=5|pages=2644–2653|doi=10.1074/jbc.M707885200|pmid=17974558|doi-access=free}}</ref>
===Drosophila===
The [[Homology (biology)|ortholog]] in [[Drosophila|fruit flies]] has been suggested to act as a [[spliceosome]]. Based on the observed phenotype of incomplete [[neuroblast]] differentiation, the [[Homology (biology)|ortholog]] is hypothesized to be involved in [[RNA splicing|splicing]] namely within the central nervous system.<ref name=Carney>{{cite journal|last1=Carney|first1=T. D.|last2=Struck|first2=A. J.|last3=Doe|first3=C. Q.|title=midlife crisis encodes a conserved zinc-finger protein required to maintain neuronal differentiation in Drosophila|journal=Development|date=11 September 2013|volume=140|issue=20|pages=4155–4164|doi=10.1242/dev.093781|pmid=24026126|pmc=3787755}}</ref> Additional research conclude a [[cytosine]] to [[thymidine]] [[nonsense mutation]] such as that of [[trichothiodystrophy]] discussed above has resulted in abnormal development in which tissues of the [[ectoderm]] [[germ layer]] are affected.<ref name="Corbett"/>
===Nematodes===
The ''[[Caenorhabditis elegans]]'' Tag-331 [[Homology (biology)|ortholog]] has been linked to larval arrest and legality when a knock-out is created<ref name=Haerty>{{cite journal|last1=Haerty|first1=Wilfried|last2=Artieri|first2=Carlo|last3=Khezri|first3=Navid|last4=Singh|first4=Rama S|last5=Gupta|first5=Bhagwati P|title=Comparative analysis of function and interaction of transcription factors in nematodes: Extensive conservation of orthology coupled to rapid sequence evolution|journal=BMC Genomics|date=2008|volume=9|issue=1|pages=399|doi=10.1186/1471-2164-9-399|pmid=18752680|pmc=2533025 |doi-access=free }}</ref> The RNF-113 ortholog has been predicted to function as an [[ubiquitin ligase]] that is involved in DNA repair of inter-strand crosslinks<ref name=Lee>{{cite journal|last1=Lee|first1=Hyojin|last2=Alpi|first2=Arno F.|last3=Park|first3=Mi So|last4=Rose|first4=Ann|last5=Koo|first5=Hyeon-Sook|last6=Leng|first6=Fenfei|title=C. elegans Ring Finger Protein RNF-113 Is Involved in Interstrand DNA Crosslink Repair and Interacts with a RAD51C Homolog|journal=PLOS ONE|date=28 March 2013|volume=8|issue=3|pages=e60071|doi=10.1371/journal.pone.0060071|pmid=23555887|pmc=3610817|bibcode=2013PLoSO...860071L|doi-access=free}}</ref>
==Paralog==
'''RNF113B''' is the primate-specific [[Retroposon|retrogene]] of RNF113A.<ref name=Szczesniak>{{cite journal|last1=Szczesniak|first1=M. W.|last2=Ciomborowska|first2=J.|last3=Nowak|first3=W.|last4=Rogozin|first4=I. B.|last5=Makalowska|first5=I.|title=Primate and Rodent Specific Intron Gains and the Origin of Retrogenes with Splice Variants|journal=Molecular Biology and Evolution|date=1 October 2010|volume=28|issue=1|pages=33–37|doi=10.1093/molbev/msq260|pmid=20889727|pmc=3002245}}</ref> The gene is a rare example of [[intron]] gain into a gene. In humans, RNF113B is found on Chromosome 13.<ref name=NM_178861.4>{{cite web|title=Homo sapiens ring finger protein 113B (RNF113B), mRNA|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_178861.4|website=NCBI Nucleotide|accessdate=2 May 2015}}</ref>  RNF113B [[mRNA]] transcript contains an upstream in-frame [[stop codon]]. The protein has both a [[RING finger domain]] (really interesting new gene) and a [[zinc finger]] motif.<ref name=NP_849192.1>{{cite web|title=RING finger protein 113B [Homo sapiens]|url=https://www.ncbi.nlm.nih.gov/protein/30578416|website=NCBI Protein|accessdate=2 May 2015}}</ref>
RNF113B currently is not associated with any human diseases according to the [[Online Mendelian Inheritance in Man]] (OMIM) database. Preliminary research has suggested the gene to be linked to development and [[Cellular differentiation|differentiation]].<ref name=Czugala>{{cite journal|last1=Czugala|first1=Marta|last2=Karolak|first2=Justyna A|last3=Nowak|first3=Dorota M|last4=Polakowski|first4=Piotr|last5=Pitarque|first5=Jose|last6=Molinari|first6=Andrea|last7=Rydzanicz|first7=Malgorzata|last8=Bejjani|first8=Bassem A|last9=Yue|first9=Beatrice Y J T|last10=Szaflik|first10=Jacek P|last11=Gajecka|first11=Marzena|title=Novel mutation and three other sequence variants segregating with phenotype at keratoconus 13q32 susceptibility locus|journal=European Journal of Human Genetics|date=2 November 2011|volume=20|issue=4|pages=389–397|doi=10.1038/ejhg.2011.203|pmid=22045297|pmc=3306853}}</ref> RNF113B has also been predicted to be a part of the [[ubiquitin ligase]] family and involved with DNA repair mechanisms after treatment with [[cisplatin]], a chemotherapy drug that induces [[Crosslinking of DNA|DNA inter-strand crosslinks]].<ref name=Szczesniak /><ref name="Carroll Thesis">{{cite web|last1=Carroll|first1=Eilis|title=Investigation into ubiquitin signalling in response to cisplatin|url=http://discovery.dundee.ac.uk/portal/en/theses/investigation-into-ubiquitin-signalling-in-response-to-cisplatin(bb2af7ef-0130-4eb7-8758-937e1a8e1824).html|website=Discovery Research Portal|publisher=University of Dundee|accessdate=2 May 2015}}</ref> Further research indicates RNF113B is [[Transcription (genetics)|transcribed]] in a wide assortment of tissues. The transcripts can be [[RNA splicing|spliced or unspliced]] and this action is specific to the tissue of expression. However, the mechanisms and functions of this gene specially in these tissues are still unknown.
==Homology==
[[Homology (biology)|Orthologs]] have been found in [[mammal]]s, [[bird]]s, [[reptile]]s, [[amphibian]]s, [[fish]], and [[invertebrate]]s. Distant orthologs have been recognized in [[fungi]], [[yeast]], and plants. The [[zinc finger]] domain and [[RING finger domain]] are the regions of highest [[conservation (ethic)|conservation]]. The upstream region displays the most conservation in mammals.
{| class="wikitable sortable"
|-
! [[Nomenclature|Scientific name]] !! Common name !! E value !! Query cover !! Identity !! Accession !! Protein length !! [[Taxon|Taxa]] !! [[Divergent evolution|Divergence]] ([[myr]])
|-
|[[Rhesus macaque|Macaca mulatta]] || [[Rhesus macaque|Rhesus monkey]] || 0 || 1.00 || 0.98 || [https://www.ncbi.nlm.nih.gov/gene/?term=NP_001185630.1%20 NP_001185630.1] || 344 || Mammal || 26.8
|-
| [[Horse|Equus caballus]] || [[Horse]] || 0 || 1.00 || 0.93 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_001491864.1 XP_001491864.1] || 344 || Mammal || 96.2
|-
| [[Painted turtle|Chrymsemys picta bellii]] || [[Painted turtle|Western painted turtle]] || 0 || 0.94 || 0.80 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 XP_005309675.1] || 323 || Reptile || 322.4
|-
| [[Red junglefowl|Gallus gallus]] || [[Red junglefowl|Chicken]] || 9E-177 || 0.93 || 0.77 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 NP_001004396.1] || 328 || Bird || 322.4
|-
| [[African clawed frog|Xenopus laevis]] || [[African clawed frog]] || 5E-157 || 0.90 || 0.71 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 AAR97523.1] || 319 || Amphibian || 359.1
|-
| [[Zebrafish|Danio rerio]] || [[Zebrafish]] || 5E-160 || 0.98 || 0.71 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 NP_001004536.1] || 321 || Fish || 436.8
|-
| [[Echinococcus multilocularis]] || [[Flatworm]] || 2E-100 || 0.90 || 0.5 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 CDI98689.1] || 389 || Flatworm || 625
|-
| [[Apis florea]] || [[Apis florea|Little honeybee]] || 2E-130 || 0.88 || 0.62 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 XP_003695009.1] || 325 || Insect || 725.5
|-
| [[Ciona intestinalis]] || [[Ciona intestinalis|Vase Tunicate]] || 2E-127 || 0.92 || 0.61 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 NP_001027830.1] || 325 || Tunicate || 763.5
|-
| [[Saccharomyces cerevisiae]] || [[Fungus]] || 4E-40 || 0.59 || 0.44 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 NP_013427.1] || 259 || Yeast || 1211
|-
| [[Amborella|Amorella trichopoda]] || [[Shrub]] || 4E-62 || 0.92 || 0.40 || [https://www.ncbi.nlm.nih.gov/gene/?term=XP_005309675.1 XP_006842511.1] || 322 || Plant || 1375
|}
The table above displays the results of an NCBI [[BLAST (biotechnology)|Blast]] from 2015 with selected taxa from main branches of vertebrates and invertebrates. This is not a complete list.
==References==
{{reflist}}
[[Category:Spliceosome]]
[[Category:RING finger proteins]]
[[Category:Zinc finger proteins]]