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''TMEM261'' is located at 9p24.1,its length is 91,891 [[base pairs]] (bp) on the reverse strand.<ref name = "GeneCards">{{cite web|title=GeneCards:TMEM261 Gene|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=TMEM261&search=b6dd0fe61f84418762b84e0f9a3a0892}}</ref>Its neighbouring gene is ''[[PTPRD]]'' located at 9p23-p24.3 also on the reverse strand and encodes [[protein tyrosine phosphatase]] receptor type delta.<ref name = "entrez">{{cite web|title=Entrez Protein: TMEM261|url=http://www.ncbi.nlm.nih.gov/gene/90871}}</ref><ref name = GeneCards>{{cite web|title=GeneCards: PTPRD|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=PTPRD&search=ec5eebdfa3e88e99844e476b922bd273}}</ref>
''TMEM261'' is located at 9p24.1,its length is 91,891 [[base pairs]] (bp) on the reverse strand.<ref name = "GeneCards">{{cite web|title=GeneCards:TMEM261 Gene|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=TMEM261&search=b6dd0fe61f84418762b84e0f9a3a0892}}</ref>Its neighbouring gene is ''[[PTPRD]]'' located at 9p23-p24.3 also on the reverse strand and encodes [[protein tyrosine phosphatase]] receptor type delta.<ref name = "entrez">{{cite web|title=Entrez Protein: TMEM261|url=http://www.ncbi.nlm.nih.gov/gene/90871}}</ref><ref name = GeneCards>{{cite web|title=GeneCards: PTPRD|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=PTPRD&search=ec5eebdfa3e88e99844e476b922bd273}}</ref>
''TMEM261'' has 2 [[exons]] and 1 [[intron]], and 6 [[primary transcript|transcript]] variants; the largest mRNA transcript variant consisting of 742bp with a protein 129 [[amino acids]] (aa) in length and 13,500 [[Daltons]] (Da) in size, and the smallest coding transcript variant being 381bp with a protein 69aa long and 6,100 Da in size.<ref>{{cite journal|last=Thierry-Mieg|first=D|author2=Thierry-Mieg, J.|title=AceView: a comprehensive cDNA-supported gene and transcripts annotation|journal=Genome Biology|year=2006|volume=7|issue=Suppl 1|pages=S12|doi=10.1186/gb-2006-7-s1-s12|pmid=16925834|pmc=1810549}}</ref><ref name = "AceView">{{cite web|title=AceView:Homo sapiens gene C9orf123|url=http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=c9orf123&submit=Go}}</ref>
''TMEM261'' has 2 [[exons]] and 1 [[intron]], and 6 [[primary transcript|transcript]] variants; the largest mRNA transcript variant consisting of 742bp with a protein 129 [[amino acids]] (aa) in length and 13,500 [[Daltons]] (Da) in size, and the smallest coding transcript variant being 381bp with a protein 69aa long and 6,100 Da in size.<ref>{{cite journal|last=Thierry-Mieg|first=D|author2=Thierry-Mieg, J.|title=AceView: a comprehensive cDNA-supported gene and transcripts annotation|journal=Genome Biology|year=2006|volume=7|issue=Suppl 1|pages=S12.1–14|doi=10.1186/gb-2006-7-s1-s12|pmid=16925834|pmc=1810549}}</ref><ref name = "AceView">{{cite web|title=AceView:Homo sapiens gene C9orf123|url=http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=c9orf123&submit=Go}}</ref>
[[File:TMEM261 features.jpg|thumb|Annotated features of TMEM261 protein including topology and important sites for phosphorylation and Myristoylation as well DUF4536 and transmembrane helical domains.]]
[[File:TMEM261 features.jpg|thumb|Annotated features of TMEM261 protein including topology and important sites for phosphorylation and Myristoylation as well DUF4536 and transmembrane helical domains.]]


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==== Structure ====
==== Structure ====
[[File:TMEM261interactions.jpg|thumb|Some proteins found to interact with TMEM261]]
[[File:TMEM261interactions.jpg|thumb|Some proteins found to interact with TMEM261]]
TMEM261 contains a [[domain of unknown function]], DUF4536 (pfam15055), predicted as a helical membrane spanning domain about 45aa ([[Cys]] 47- [[Ser]] 92) in length with no known domain relationships.<ref name="conserved domains">{{cite web | title = NCBI Conserved Domains: DUF4536| url =http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=259192}}</ref><ref name="EMBL-EBI>{{cite web | title = EMBL-EBI Interpro: Transmembrane protein 261 (Q96GE9)| url =http://www.ebi.ac.uk/s4/summary/molecular?term=TMEM261&classification=9606&tid=nameOrgENSG00000137038}}</ref> Two further transmembrane helical domains are predicted of lengths 18aa ([[Val]] 52-[[Ala]] 69) and 23aa ([[Pro]] 81-[[Ala]] 102]).<ref name=Bioinformatics Centre Stockholm>{{cite web | title = Phobius: A combined transmembrane topology and signal peptide predictor| url =http://phobius.sbc.su.se/}}</ref><ref>{{cite web|title=Q96GE9 - TM261_HUMAN|url=http://www.uniprot.org/uniprot/Q96GE9|website=UniProt|publisher=UniProt Consortium}}</ref>There is also a low complexity region spanning 25aa ([[Thr]] 14-[[Ala]] 39).<ref name="Vega Genome Browser 58>{{cite web | title = Vega: Transcript: C9orf123-003| url =http://vega.sanger.ac.uk/Homo_sapiens/Transcript/ProteinSummary?db=core;g=OTTHUMG00000019539;r=9:7796490-7888380;t=OTTHUMT00000051705}}</ref> The [[protein tertiary structure|tertiary structure]] for TMEM261 has not yet been determined. However, its [[Protein secondary structure|secondary structure]] is mostly composed of [[Coiled-coil|coiled-coil]] regions with [[Beta strand|beta strands]] and [[Alpha helices|alpha helices]] found within the [[transmembrane]] and [[domain of unknown function]] reigons. The N-terminal region of TMEM261 is composed of a disordered region<ref>{{cite web|title=PHYRE: Protein Homology/analogY Recognition Engine|url=http://www.sbg.bio.ic.ac.uk/phyre2/html/page.cgi?id=index|website=PHYRE}}</ref> <ref>{{cite journal|last1=Kelley|first1=LA|last2=Sternberg|first2= MJE|title=Protein structure prediction on the Web: a case study using the Phyre server|journal=MJE|date=2009|volume=4|pages=363 - 371|doi=10.1038/nprot.2009.2|pmid=19247286|url=http://www.nature.com/nprot/journal/v4/n3/full/nprot.2009.2.html}}</ref> which contains the low complexity region<ref name="Vega Genome Browser 58>{{cite web | title = Vega: Transcript: C9orf123-003| url =http://vega.sanger.ac.uk/Homo_sapiens/Transcript/ProteinSummary?db=core;g=OTTHUMG00000019539;r=9:7796490-7888380;t=OTTHUMT00000051705}}</ref> that is not highly conserved amongst orthologues<ref name = "SDSC Biology ">{{cite web|title= ClustalW|url=http://workbench.sdsc.edu/}}</ref><ref name= Thompson>{{cite journal|last1=Thompson|first1=Julie D|last2=Higgins|first2=Desmond G|last3=Gibson|first3=Toby J|title=CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.|journal=Nucleic Acids Res|date=1994|volume=22|issue=22|pages=4673–4680.|pmid=308517|url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC308517/}}</ref>.
TMEM261 contains a [[domain of unknown function]], DUF4536 (pfam15055), predicted as a helical membrane spanning domain about 45aa ([[Cys]] 47- [[Ser]] 92) in length with no known domain relationships.<ref name="conserved domains">{{cite web | title = NCBI Conserved Domains: DUF4536| url =http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=259192}}</ref><ref name="EMBL-EBI>{{cite web | title = EMBL-EBI Interpro: Transmembrane protein 261 (Q96GE9)| url =http://www.ebi.ac.uk/s4/summary/molecular?term=TMEM261&classification=9606&tid=nameOrgENSG00000137038}}</ref> Two further transmembrane helical domains are predicted of lengths 18aa ([[Val]] 52-[[Ala]] 69) and 23aa ([[Pro]] 81-[[Ala]] 102]).<ref name=Bioinformatics Centre Stockholm>{{cite web | title = Phobius: A combined transmembrane topology and signal peptide predictor| url =http://phobius.sbc.su.se/}}</ref><ref>{{cite web|title=Q96GE9 - TM261_HUMAN|url=http://www.uniprot.org/uniprot/Q96GE9|website=UniProt|publisher=UniProt Consortium}}</ref>There is also a low complexity region spanning 25aa ([[Thr]] 14-[[Ala]] 39).<ref name="Vega Genome Browser 58>{{cite web | title = Vega: Transcript: C9orf123-003| url =http://vega.sanger.ac.uk/Homo_sapiens/Transcript/ProteinSummary?db=core;g=OTTHUMG00000019539;r=9:7796490-7888380;t=OTTHUMT00000051705}}</ref> The [[protein tertiary structure|tertiary structure]] for TMEM261 has not yet been determined. However, its [[Protein secondary structure|secondary structure]] is mostly composed of [[Coiled-coil|coiled-coil]] regions with [[Beta strand|beta strands]] and [[Alpha helices|alpha helices]] found within the [[transmembrane]] and [[domain of unknown function]] reigons. The N-terminal region of TMEM261 is composed of a disordered region<ref>{{cite web|title=PHYRE: Protein Homology/analogY Recognition Engine|url=http://www.sbg.bio.ic.ac.uk/phyre2/html/page.cgi?id=index|website=PHYRE}}</ref> <ref>{{cite journal|last1=Kelley|first1=LA|last2=Sternberg|first2= MJE|title=Protein structure prediction on the Web: a case study using the Phyre server|journal=MJE|date=2009|volume=4|issue=3|pages=363–371|doi=10.1038/nprot.2009.2|pmid=19247286|hdl=10044/1/18157|s2cid=12497300|url=http://www.nature.com/nprot/journal/v4/n3/full/nprot.2009.2.html}}</ref> which contains the low complexity region<ref name="Vega Genome Browser 58>{{cite web | title = Vega: Transcript: C9orf123-003| url =http://vega.sanger.ac.uk/Homo_sapiens/Transcript/ProteinSummary?db=core;g=OTTHUMG00000019539;r=9:7796490-7888380;t=OTTHUMT00000051705}}</ref> that is not highly conserved amongst orthologues<ref name = "SDSC Biology ">{{cite web|title= ClustalW|url=http://workbench.sdsc.edu/}}</ref><ref name= Thompson>{{cite journal|last1=Thompson|first1=Julie D|last2=Higgins|first2=Desmond G|last3=Gibson|first3=Toby J|title=CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.|journal=Nucleic Acids Res|date=1994|volume=22|issue=22|pages=4673–4680|doi=10.1093/nar/22.22.4673|pmid=308517|pmc=308517}}</ref>.


==== Modifications ====
==== Modifications ====
A N-myristoylation domain is shown to be present in most TMEM261 protein variants.<ref name = "AceView">{{cite web|title=AceView:Homo sapiens gene C9orf123|url=http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=c9orf123&submit=Go}}</ref> Post-translational modifications include [[myristoylation]] of the [[N-terminal]] [[Glycine]] residue ([[Gly]]2)<ref name = "AceView">{{cite web|title=AceView:Homo sapiens gene C9orf123|url=http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=c9orf123&submit=Go}}</ref><ref>{{cite web|last1=Gallo|first1=Vincenzo|title=Myristoylation : Proteins Post-translational Modifications|url=http://flipper.diff.org/app/pathways/info/4026|website=http://flipper.diff.org/|publisher=University of Turin}}</ref> of the TMEM261 protein as well as [[phosphorylation]] of [[Threonine]] 31.<ref name = "Nextprot">{{cite web|title=Nextprot:TMEM261 » Transmembrane protein 261|url=http://www.nextprot.org/db/entry/NX_Q96GE9/sequence}}</ref> <br />
A N-myristoylation domain is shown to be present in most TMEM261 protein variants.<ref name = "AceView">{{cite web|title=AceView:Homo sapiens gene C9orf123|url=http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=c9orf123&submit=Go}}</ref> Post-translational modifications include [[myristoylation]] of the [[N-terminal]] [[Glycine]] residue ([[Gly]]2)<ref name = "AceView">{{cite web|title=AceView:Homo sapiens gene C9orf123|url=http://www.ncbi.nlm.nih.gov/IEB/Research/Acembly/av.cgi?db=human&term=c9orf123&submit=Go}}</ref><ref>{{cite web|last1=Gallo|first1=Vincenzo|title=Myristoylation : Proteins Post-translational Modifications|url=http://flipper.diff.org/app/pathways/info/4026|website=http://flipper.diff.org/|publisher=University of Turin}}</ref> of the TMEM261 protein as well as [[phosphorylation]] of [[Threonine]] 31.<ref name = "Nextprot">{{cite web|title=Nextprot:TMEM261 » Transmembrane protein 261|url=http://www.nextprot.org/db/entry/NX_Q96GE9/sequence}}</ref> <br />


==== Interactions ====
==== Interactions ====
Proteins shown to interact with TMEM261 include [http://www.genecards.org/cgi-bin/carddisp.pl?gene=NAAA NAAA] ([[protein-protein interaction]]), [http://www.genecards.org/cgi-bin/carddisp.pl?gene=QTRT1&search=d6edd4112f517825968a5a6978882712 QTRT1] ([https://www.lifetechnologies.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/methods-detecting-protein-rna-interactions.html RNA-protein interaction]),[http://www.genecards.org/cgi-bin/carddisp.pl?gene=ZC4H2&search=79ba8f7afa868106306bf83d200ba523 ZC4H2]([[DNA-protein interaction]])<ref>{{cite journal|last1=Dash|first1=A et al.|title=Changes in differential gene expression because of warm ischemia time of radical prostatectomy specimens.|journal=Am J Pathol.|date=2002|volume=161|issue=5|pages=1743-1748|doi=10.1016/S0002-9440(10)64451-3|url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1850797/}}</ref> and [http://www.genecards.org/cgi-bin/carddisp.pl?gene=ZNF454&search=68835d4da3192d71bcf7818742536191 ZNF454](DNA-protein interaction)<ref>{{cite journal|last1=Rovillain|first1=E et al.|title=An RNA interference screen for identifying downstream effectors of the p53 and pRB tumour suppressor pathways involved in senescence.|journal=BMC Genomics.|date=2011|volume=12|issue=355|doi=10.1186/1471-2164-12-355|pmid=21740549|url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3161017/}}</ref><ref>{{cite web|title=c9orf123 protein (Homo Sapiens)- STRING Network View|url=http://string-db.org/newstring_cgi/show_input_page.pl?UserId=65EMVhw9LAhY&sessionId=N5_gHtjz1Wbz|website=STRING - Known and Predicted Protein-Protein Interactions}}</ref>. It has also shown to interact with [http://www.genecards.org/cgi-bin/carddisp.pl?gene=APP APP](protein-protein interaction)<ref>{{cite journal|last1=Oláh|first1=J et al.|title=Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein.|journal=J Biol Chem.|date=2011|volume=286|issue=39|pages=34088-34100|doi=10.1074/jbc.M111.243907|url=http://www.jbc.org/content/286/39/34088.long}}</ref>,[http://www.genecards.org/cgi-bin/carddisp.pl?gene=ARHGEF38&search=1bcacaca34542f4b438e308c6b02cfd2 ARHGEF38](protein-protein interaction)<ref>{{cite journal|last1=Huttlin|first1=E L et al.|title=High-Throughput Proteomic Mapping of Human Interaction Networks via Affinity-Purification Mass Spectrometry (Pre-Publication)|journal=Pre-Publication|date=2014|url=http://thebiogrid.org/166968/publication/high-throughput-proteomic-mapping-of-human-interaction-networks-via-affinity-purification-mass-spectrometry.html}}</ref> and [http://www.genecards.org/cgi-bin/carddisp.pl?gene=HNRNPD&search=c4b9dd1c49f01a5dfb3c401f24182f32 HNRNPD]([https://www.lifetechnologies.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/methods-detecting-protein-rna-interactions.html RNA-protein interaction])<ref>{{cite journal|last1=Lehner|first1=B|last2=Sanderson|first2=C M|title=A protein interaction framework for human mRNA degradation.|journal=Genome Res.|date=2004|volume=14|issue=7|pages=1315-1323|doi=10.1101/gr.2122004|pmid=15231747|url=http://genome.cshlp.org/content/14/7/1315.long}}</ref>.<ref>{{cite web|title=9ORF123 chromosome 9 open reading frame 123|url=http://thebiogrid.org/124777/summary/homo-sapiens/c9orf123.html|website=BioGRID: Database of Protein and Genetic Interactions|publisher=TyersLab}}</ref>
Proteins shown to interact with TMEM261 include [http://www.genecards.org/cgi-bin/carddisp.pl?gene=NAAA NAAA] ([[protein-protein interaction]]), [http://www.genecards.org/cgi-bin/carddisp.pl?gene=QTRT1&search=d6edd4112f517825968a5a6978882712 QTRT1] ([https://www.lifetechnologies.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/methods-detecting-protein-rna-interactions.html RNA-protein interaction]),[http://www.genecards.org/cgi-bin/carddisp.pl?gene=ZC4H2&search=79ba8f7afa868106306bf83d200ba523 ZC4H2]([[DNA-protein interaction]])<ref>{{cite journal|last1=Dash|first1=A et al.|title=Changes in differential gene expression because of warm ischemia time of radical prostatectomy specimens.|journal=Am J Pathol.|date=2002|volume=161|issue=5|pages=1743–1748|doi=10.1016/S0002-9440(10)64451-3|pmid=12414521|pmc=1850797}}</ref> and [http://www.genecards.org/cgi-bin/carddisp.pl?gene=ZNF454&search=68835d4da3192d71bcf7818742536191 ZNF454](DNA-protein interaction)<ref>{{cite journal|last1=Rovillain|first1=E et al.|title=An RNA interference screen for identifying downstream effectors of the p53 and pRB tumour suppressor pathways involved in senescence.|journal=BMC Genomics.|date=2011|volume=12|issue=355|page=355|doi=10.1186/1471-2164-12-355|pmid=21740549|pmc=3161017}}</ref><ref>{{cite web|title=c9orf123 protein (Homo Sapiens)- STRING Network View|url=http://string-db.org/newstring_cgi/show_input_page.pl?UserId=65EMVhw9LAhY&sessionId=N5_gHtjz1Wbz|website=STRING - Known and Predicted Protein-Protein Interactions}}</ref>. It has also shown to interact with [http://www.genecards.org/cgi-bin/carddisp.pl?gene=APP APP](protein-protein interaction)<ref>{{cite journal|last1=Oláh|first1=J et al.|title=Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein.|journal=J Biol Chem.|date=2011|volume=286|issue=39|pages=34088–34100|doi=10.1074/jbc.M111.243907|pmid=21832049|pmc=3190826|url=http://www.jbc.org/content/286/39/34088.long}}</ref>,[http://www.genecards.org/cgi-bin/carddisp.pl?gene=ARHGEF38&search=1bcacaca34542f4b438e308c6b02cfd2 ARHGEF38](protein-protein interaction)<ref>{{cite journal|last1=Huttlin|first1=E L et al.|title=High-Throughput Proteomic Mapping of Human Interaction Networks via Affinity-Purification Mass Spectrometry (Pre-Publication)|journal=Pre-Publication|date=2014|url=http://thebiogrid.org/166968/publication/high-throughput-proteomic-mapping-of-human-interaction-networks-via-affinity-purification-mass-spectrometry.html}}</ref> and [http://www.genecards.org/cgi-bin/carddisp.pl?gene=HNRNPD&search=c4b9dd1c49f01a5dfb3c401f24182f32 HNRNPD]([https://www.lifetechnologies.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/methods-detecting-protein-rna-interactions.html RNA-protein interaction])<ref>{{cite journal|last1=Lehner|first1=B|last2=Sanderson|first2=C M|title=A protein interaction framework for human mRNA degradation.|journal=Genome Res.|date=2004|volume=14|issue=7|pages=1315–1323|doi=10.1101/gr.2122004|pmid=15231747|pmc=442147|url=http://genome.cshlp.org/content/14/7/1315.long}}</ref>.<ref>{{cite web|title=9ORF123 chromosome 9 open reading frame 123|url=http://thebiogrid.org/124777/summary/homo-sapiens/c9orf123.html|website=BioGRID: Database of Protein and Genetic Interactions|publisher=TyersLab}}</ref>
[[File:Tissueexpression.jpg|thumb|Tissue expression of TMEM261 showing tissue enriched gene (TEG) expression <ref name="She X et al.">{{vcite2 journal |vauthors=She X, Rohl CA, Castle JC, Kulkarni AV, Johnson JM, Chen R |title=Definition, conservation and epigenetics of housekeeping and tissue-enriched genes |journal=BMC Genomics |volume=10 |issue= |pages=269 |year=2009 |pmid=19534766 |pmc=2706266 |doi=10.1186/1471-2164-10-269 |url=}}</ref>]]Additional [[transcription factor]] binding sites (DNA-protein interaction) predicted include one binding site for [http://www.genecards.org/cgi-bin/carddisp.pl?gene=MEF2C&search=b74dc542dd9d720d31835d8b921cab5f MEF2C] a [[monocyte]]-specific [[Transcription factor|enhancement factor]] that is involved in [[Muscle cell|muscle-cell]] regulation particularly in the [[cardiovascular system]] <ref name = "GeneCards">{{cite web|title=GeneCards:TMEM261 Gene|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=TMEM261&search=b6dd0fe61f84418762b84e0f9a3a0892}}</ref><ref>{{cite web|title=GeneCards:MEF2C Gene|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=MEF2C&search=b74dc542dd9d720d31835d8b921cab5f}}</ref> and two binding sites for [http://www.genecards.org/cgi-bin/carddisp.pl?gene=GATA1&search=a9de4a756db711a75e3c928b363bde71 GATA1] which is a globin transcription factor 1 involved in [[erythroblast]] development regulation<ref>{{cite journal|last1=Welch|first1=J J et al.|title=Global regulation of erythroid gene expression by transcription factor GATA-1.|journal=Blood|date=2004|volume=104|issue=10|pages=3136-3147|pmid=15297311|url=http://www.bloodjournal.org/content/104/10/3136?sso-checked=true}}</ref><ref>{{cite journal|last1=Merryweather-Clarke|first1=A T et al.|title=Global gene expression analysis of human erythroid progenitors|journal=Blood|date=2011|volume=117|issue=13|pages=e96-108|doi=10.1182/blood-2010-07-290825|pmid=21270440|url=http://www.bloodjournal.org/content/117/13/e96.long}}</ref>. <ref>{{cite web|title=Genomatics- NGS Data Analysis and Personalised Medicine|url=https://www.genomatix.de/|website=Genomatix|publisher=Genomatix Software GmbH}}</ref>
[[File:Tissueexpression.jpg|thumb|Tissue expression of TMEM261 showing tissue enriched gene (TEG) expression <ref name="She X et al.">{{cite journal |vauthors=She X, Rohl CA, Castle JC, Kulkarni AV, Johnson JM, Chen R |title=Definition, conservation and epigenetics of housekeeping and tissue-enriched genes |journal=BMC Genomics |volume=10 |issue= |pages=269 |year=2009 |pmid=19534766 |pmc=2706266 |doi=10.1186/1471-2164-10-269 |url=}}</ref>]]Additional [[transcription factor]] binding sites (DNA-protein interaction) predicted include one binding site for [http://www.genecards.org/cgi-bin/carddisp.pl?gene=MEF2C&search=b74dc542dd9d720d31835d8b921cab5f MEF2C] a [[monocyte]]-specific [[Transcription factor|enhancement factor]] that is involved in [[Muscle cell|muscle-cell]] regulation particularly in the [[cardiovascular system]] <ref name = "GeneCards">{{cite web|title=GeneCards:TMEM261 Gene|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=TMEM261&search=b6dd0fe61f84418762b84e0f9a3a0892}}</ref><ref>{{cite web|title=GeneCards:MEF2C Gene|url=http://www.genecards.org/cgi-bin/carddisp.pl?gene=MEF2C&search=b74dc542dd9d720d31835d8b921cab5f}}</ref> and two binding sites for [http://www.genecards.org/cgi-bin/carddisp.pl?gene=GATA1&search=a9de4a756db711a75e3c928b363bde71 GATA1] which is a globin transcription factor 1 involved in [[erythroblast]] development regulation<ref>{{cite journal|last1=Welch|first1=J J et al.|title=Global regulation of erythroid gene expression by transcription factor GATA-1.|journal=Blood|date=2004|volume=104|issue=10|pages=3136–3147|doi=10.1182/blood-2004-04-1603|pmid=15297311|url=http://www.bloodjournal.org/content/104/10/3136?sso-checked=true}}</ref><ref>{{cite journal|last1=Merryweather-Clarke|first1=A T et al.|title=Global gene expression analysis of human erythroid progenitors|journal=Blood|date=2011|volume=117|issue=13|pages=e96-108|doi=10.1182/blood-2010-07-290825|pmid=21270440|url=http://www.bloodjournal.org/content/117/13/e96.long}}</ref>. <ref>{{cite web|title=Genomatics- NGS Data Analysis and Personalised Medicine|url=https://www.genomatix.de/|website=Genomatix|publisher=Genomatix Software GmbH}}</ref>


==Expression==
==Expression==
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==Function==
==Function==


Currently the function for TMEM261 is unknown. However, [[Gene duplication|gene amplification]] and rearrangements of its locus have been associated with various cancers including [[colorectal cancer]]<ref>{{cite journal|last1=Gaspar|first1=C|title=Cross-Species Comparison of Human and Mouse Intestinal Polyps Reveals Conserved Mechanisms in Adenomatous Polyposis Coli (APC)-Driven Tumorigenesis|journal=Am J Pathol|date=2008|volume=172|issue=5|pages=1363–1380|doi=10.2353/ajpath.2008.070851|pmid=18403596 |url=http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2329845/}}</ref>,
Currently the function for TMEM261 is unknown. However, [[Gene duplication|gene amplification]] and rearrangements of its locus have been associated with various cancers including [[colorectal cancer]]<ref>{{cite journal|last1=Gaspar|first1=C|title=Cross-Species Comparison of Human and Mouse Intestinal Polyps Reveals Conserved Mechanisms in Adenomatous Polyposis Coli (APC)-Driven Tumorigenesis|journal=Am J Pathol|date=2008|volume=172|issue=5|pages=1363–1380|doi=10.2353/ajpath.2008.070851|pmid=18403596 |pmc=2329845}}</ref>,
[[breast cancer]]<ref>{{cite journal|last1=Wu|first1=J|title=Identification and functional analysis of 9p24 amplified genes in human breast cancer|journal=Oncogene|date=2012|volume=31|issue=3|pages=333-341|doi=10.1038/onc.2011.227|pmid=21666724|url=http://www.nature.com/onc/journal/v31/n3/full/onc2011227a.html}}</ref> and [[lymphomas]]<ref>{{cite journal|last1=Twa|first1=D D W et al.|title=Genomic Rearrangements Involving Programmed Death Ligands Are Recurrent in Primary Mediastinal Large B-Cell Lymphoma|journal=Blood|date=2014|volume=123|issue=13|pages=2062-2065|doi=10.1182/blood-2013-10-535443|pmid=24497532|url=http://www.bloodjournal.org/content/123/13/2062.long?sso-checked=true}}</ref><ref>{{cite journal|last1=Green|first1=M R et al.|title=Integrative Analysis Reveals Selective 9p24.1 Amplification, Increased PD-1 Ligand Expression, and Further Induction via JAK2 in Nodular Sclerosing Hodgkin Lymphoma and Primary Mediastinal Large B-Cell Lymphoma|journal=Blood|date=2010|volume=116|issue=17|pages=3268-3277|doi=10.1182/blood-2010-05-282780|pmid=20628145|url=http://www.bloodjournal.org/content/116/17/3268.long}}</ref>.
[[breast cancer]]<ref>{{cite journal|last1=Wu|first1=J|title=Identification and functional analysis of 9p24 amplified genes in human breast cancer|journal=Oncogene|date=2012|volume=31|issue=3|pages=333–341|doi=10.1038/onc.2011.227|pmid=21666724|pmc=3886828|url=http://www.nature.com/onc/journal/v31/n3/full/onc2011227a.html}}</ref> and [[lymphomas]]<ref>{{cite journal|last1=Twa|first1=D D W et al.|title=Genomic Rearrangements Involving Programmed Death Ligands Are Recurrent in Primary Mediastinal Large B-Cell Lymphoma|journal=Blood|date=2014|volume=123|issue=13|pages=2062–2065|doi=10.1182/blood-2013-10-535443|pmid=24497532|url=http://www.bloodjournal.org/content/123/13/2062.long?sso-checked=true}}</ref><ref>{{cite journal|last1=Green|first1=M R et al.|title=Integrative Analysis Reveals Selective 9p24.1 Amplification, Increased PD-1 Ligand Expression, and Further Induction via JAK2 in Nodular Sclerosing Hodgkin Lymphoma and Primary Mediastinal Large B-Cell Lymphoma|journal=Blood|date=2010|volume=116|issue=17|pages=3268–3277|doi=10.1182/blood-2010-05-282780|pmid=20628145|pmc=2995356|url=http://www.bloodjournal.org/content/116/17/3268.long}}</ref>.


==Evolution==
==Evolution==
==== Orthologues ====
==== Orthologues ====
The [[orthologues]] and [[homologues]] of TMEM261 are limited to [[vertebrates]], its oldest homologue dates to that of the [[cartilaginous fishes]]<ref name = "NCBI BLAST">{{cite web|title= NCBI BLAST:Basic Local Alignment Search Tool|url=http://blast.ncbi.nlm.nih.gov/Blast.cgi}}</ref> which diverged from [[Homo sapiens]] 462.5 million years ago <ref>{{cite journal|last1=Hedges|first1=S. Blaire|last2=Dudley|first2=Joel|last3=Kumar|first3=Sudhir|title=TimeTree: a public knowledge-base of divergence times among organisms|date=22 September 2006|volume=22|issue=23|pages=2971–2972|doi=10.1093/bioinformatics/btl505|url=http://kumarlab.net/pdf_new/HedgesKumar06.pdf|}}</ref>. The [[Protein primary structure|primary structure]] of TMEM261 shows higher overall conservation in [[mammals]], however high conservation of the [[domain of unknown function]] (DUF4536) to the [[C-terminus]] region is seen in all orthologues, including distant homologues. The [[Protein secondary structure|secondary structure]] of TMEM261 shows conservation across most orthologues.<ref name = "SDSC Biology ">{{cite web|title= ClustalW|url=http://workbench.sdsc.edu/}}</ref><ref name= Thompson/>
The [[orthologues]] and [[homologues]] of TMEM261 are limited to [[vertebrates]], its oldest homologue dates to that of the [[cartilaginous fishes]]<ref name = "NCBI BLAST">{{cite web|title= NCBI BLAST:Basic Local Alignment Search Tool|url=http://blast.ncbi.nlm.nih.gov/Blast.cgi}}</ref> which diverged from [[Homo sapiens]] 462.5 million years ago <ref>{{cite journal|last1=Hedges|first1=S. Blaire|last2=Dudley|first2=Joel|last3=Kumar|first3=Sudhir|title=TimeTree: a public knowledge-base of divergence times among organisms|journal=Bioinformatics|date=22 September 2006|volume=22|issue=23|pages=2971–2972|doi=10.1093/bioinformatics/btl505|pmid=17021158|url=http://kumarlab.net/pdf_new/HedgesKumar06.pdf}}</ref>. The [[Protein primary structure|primary structure]] of TMEM261 shows higher overall conservation in [[mammals]], however high conservation of the [[domain of unknown function]] (DUF4536) to the [[C-terminus]] region is seen in all orthologues, including distant homologues. The [[Protein secondary structure|secondary structure]] of TMEM261 shows conservation across most orthologues.<ref name = "SDSC Biology ">{{cite web|title= ClustalW|url=http://workbench.sdsc.edu/}}</ref><ref name= Thompson/>
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==Further Reading==
==Further Reading==


*{{cite journal | author=Nicholas K. Tonks|title=Protein tyrosine phosphatases: from genes, to function, to disease|journal=Cancer Cell |volume=7 |pages= 833-846 |year= 2006 |doi=10.1038/nrm2039| author-separator=,}}
*{{cite journal | author=Nicholas K. Tonks|title=Protein tyrosine phosphatases: from genes, to function, to disease|journal=Cancer Cell |volume=7 |pages= 833–846 |year= 2006 |issue=11|doi=10.1038/nrm2039|pmid=17057753|s2cid=1302726| author-separator=,}}
*{{cite journal | author=Merryweather-Clarke AT et al.|title=Global gene expression analysis of human erythroid progenitors. |journal=Blood |volume=117 |issue= 13 |pages= e96-108 |year= 2011 |pmid= 21270440 |doi= 10.1182/blood-2010-07-290825 | author-separator=,}}
*{{cite journal | author=Merryweather-Clarke AT et al.|title=Global gene expression analysis of human erythroid progenitors. |journal=Blood |volume=117 |issue= 13 |pages= e96-108 |year= 2011 |pmid= 21270440 |doi= 10.1182/blood-2010-07-290825 | author-separator=,}}
*{{cite journal | author=Welch JJ, Watts JA, Vakoc CR, et al.|title=Global regulation of erythroid gene expression by transcription factor GATA-1 |journal=Blood |volume=104 |issue= 10 |pages= 3136-3147 |year= 2004 |pmid= 15297311 |doi=10.1182/blood-2004-04-1603| author-separator=,}}
*{{cite journal | author=Welch JJ, Watts JA, Vakoc CR, et al.|title=Global regulation of erythroid gene expression by transcription factor GATA-1 |journal=Blood |volume=104 |issue= 10 |pages= 3136–3147 |year= 2004 |pmid= 15297311 |doi=10.1182/blood-2004-04-1603| author-separator=,}}
*{{cite journal | author=Nickeleit I et al.|title=Argyrin a reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition.|journal=Cancer Cell |volume=14 |issue= 1 |pages= 23-35 |year= 2008 |pmid= 18598941|doi=10.1016/j.ccr.2008.05.016| author-separator=,}}
*{{cite journal | author=Nickeleit I et al.|title=Argyrin a reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition.|journal=Cancer Cell |volume=14 |issue= 1 |pages= 23–35 |year= 2008 |pmid= 18598941|doi=10.1016/j.ccr.2008.05.016|hdl=11858/00-001M-0000-0012-DB84-4| author-separator=,}}

Latest revision as of 01:49, 10 May 2021

TMEM261
Transmembrane protein 261 is a protein that in humans is encoded by the TMEM261 gene located on chromosome 9.[1]TMEM261 is also known as C9ORF123, Chromosome 9 Open Reading Frame 123 and Transmembrane Protein C9orf123.[2]

Gene Features

[edit]


TMEM261 is located at 9p24.1,its length is 91,891 base pairs (bp) on the reverse strand.[2]Its neighbouring gene is PTPRD located at 9p23-p24.3 also on the reverse strand and encodes protein tyrosine phosphatase receptor type delta.[1][2] TMEM261 has 2 exons and 1 intron, and 6 transcript variants; the largest mRNA transcript variant consisting of 742bp with a protein 129 amino acids (aa) in length and 13,500 Daltons (Da) in size, and the smallest coding transcript variant being 381bp with a protein 69aa long and 6,100 Da in size.[3][4]

Annotated features of TMEM261 protein including topology and important sites for phosphorylation and Myristoylation as well DUF4536 and transmembrane helical domains.

Protein Features

[edit]

TMEM261 is a protein of 112aa with a molecular weight of 11,800 Da.[5] The isoelectric is predicted to be 10.2Cite error: The <ref> tag has too many names (see the help page)., whilst its posttranslational modification value is 9.9[4].

Structure

[edit]
Some proteins found to interact with TMEM261

TMEM261 contains a domain of unknown function, DUF4536 (pfam15055), predicted as a helical membrane spanning domain about 45aa (Cys 47- Ser 92) in length with no known domain relationships.[6][7] Two further transmembrane helical domains are predicted of lengths 18aa (Val 52-Ala 69) and 23aa (Pro 81-Ala 102]).Cite error: The <ref> tag has too many names (see the help page).[8]There is also a low complexity region spanning 25aa (Thr 14-Ala 39).[9] The tertiary structure for TMEM261 has not yet been determined. However, its secondary structure is mostly composed of coiled-coil regions with beta strands and alpha helices found within the transmembrane and domain of unknown function reigons. The N-terminal region of TMEM261 is composed of a disordered region[10] [11] which contains the low complexity region[9] that is not highly conserved amongst orthologues[12][13].

Modifications

[edit]

A N-myristoylation domain is shown to be present in most TMEM261 protein variants.[4] Post-translational modifications include myristoylation of the N-terminal Glycine residue (Gly2)[4][14] of the TMEM261 protein as well as phosphorylation of Threonine 31.[15]

Interactions

[edit]

Proteins shown to interact with TMEM261 include NAAA (protein-protein interaction), QTRT1 (RNA-protein interaction),ZC4H2(DNA-protein interaction)[16] and ZNF454(DNA-protein interaction)[17][18]. It has also shown to interact with APP(protein-protein interaction)[19],ARHGEF38(protein-protein interaction)[20] and HNRNPD(RNA-protein interaction)[21].[22]

Tissue expression of TMEM261 showing tissue enriched gene (TEG) expression [23]

Additional transcription factor binding sites (DNA-protein interaction) predicted include one binding site for MEF2C a monocyte-specific enhancement factor that is involved in muscle-cell regulation particularly in the cardiovascular system [2][24] and two binding sites for GATA1 which is a globin transcription factor 1 involved in erythroblast development regulation[25][26]. [27]

Expression

[edit]

TMEM261 shows ubiquitous expression in humans detected in almost all tissue types[28][29] and shows tissue-enriched gene (TEG) expression when compared to housekeeping gene (HKG) expression[23]. Its highest expression is seen in the heart (overall relative expression 94%) particularly in heart fibroblast cells, thymus (overall relative expression 90%), and thyroid (overall relative expression 93%) particularly in thyroid glandular cells.[23][28]Staining intensity of cancer cells showed intermediate to high expression in breast, colorectal, ovarian, skin, urothelial, head and neck cells. [28].


Function

[edit]

Currently the function for TMEM261 is unknown. However, gene amplification and rearrangements of its locus have been associated with various cancers including colorectal cancer[30], breast cancer[31] and lymphomas[32][33].

Evolution

[edit]

Orthologues

[edit]

The orthologues and homologues of TMEM261 are limited to vertebrates, its oldest homologue dates to that of the cartilaginous fishes[34] which diverged from Homo sapiens 462.5 million years ago [35]. The primary structure of TMEM261 shows higher overall conservation in mammals, however high conservation of the domain of unknown function (DUF4536) to the C-terminus region is seen in all orthologues, including distant homologues. The secondary structure of TMEM261 shows conservation across most orthologues.[12][13]

Organism Scientific Name Accession Number Date of Divergence from Humans (million years) Amino acids (aa) Identity (%) Class
Humans Homo sapiens NP_219500.1 0 112 100 Mammalia
Gorilla Gorilla gorilla XP_004047847.1 8.8 112 99 Mammalia
Olive Baboon Papio anubis XP_003911767.1 29 112 84 Mammalia
Sunda Flying Lemur Galeopterus variegatus XP_008587957.1 81.5 112 68 Mammalia
Lesser Egyptian Jerboa Jaculus Jaculus XP_004653029.1 92.3 109 56 Mammalia
Naked Mole Rat Heterocephalus glaber XP_004898193.1 92.3 114 45 Mammalia
White Rhinoceros Ceratotherium simum simum XP_004436891.1 94.2 112 66 Mammalia
Nine-banded armadillo Dasypus novemcinctus XP_004459147.1 104.4 112 59 Mammalia
Green Sea Turtle Chelonia mydas XP_007056940.1 296 85 49 Reptilia
Zebra Finch Taeniopygia Guttata XP_002187613.2 296 72 47 Aves
Western Clawed Frog Xenopus tropicalis XP_002943025.1 371.2 85 45 Amphibia
Haplochromis burtoni Haplochromis burtoni XP_005928614.1 400.1 91 51 Actinopterygii
Australian Ghost Shark Callorhinchus milii XP_007884223.1 426.5 86 43 Chondrichthyes

Paralogues

[edit]

TMEM261 has no known paralogs[34].

References

[edit]
  1. ^ a b "Entrez Protein: TMEM261".
  2. ^ a b c d "GeneCards:TMEM261 Gene". Cite error: The named reference "GeneCards" was defined multiple times with different content (see the help page).
  3. ^ Thierry-Mieg, D; Thierry-Mieg, J. (2006). "AceView: a comprehensive cDNA-supported gene and transcripts annotation". Genome Biology. 7 (Suppl 1): S12.1–14. doi:10.1186/gb-2006-7-s1-s12. PMC 1810549. PMID 16925834.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  4. ^ a b c d "AceView:Homo sapiens gene C9orf123".
  5. ^ "Ensemble:Transcript TMEM261-003".
  6. ^ "NCBI Conserved Domains: DUF4536".
  7. ^ "EMBL-EBI Interpro: Transmembrane protein 261 (Q96GE9)".
  8. ^ "Q96GE9 - TM261_HUMAN". UniProt. UniProt Consortium.
  9. ^ a b "Vega: Transcript: C9orf123-003".
  10. ^ "PHYRE: Protein Homology/analogY Recognition Engine". PHYRE.
  11. ^ Kelley, LA; Sternberg, MJE (2009). "Protein structure prediction on the Web: a case study using the Phyre server". MJE. 4 (3): 363–371. doi:10.1038/nprot.2009.2. hdl:10044/1/18157. PMID 19247286. S2CID 12497300.
  12. ^ a b "ClustalW".
  13. ^ a b Thompson, Julie D; Higgins, Desmond G; Gibson, Toby J (1994). "CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice". Nucleic Acids Res. 22 (22): 4673–4680. doi:10.1093/nar/22.22.4673. PMC 308517. PMID 308517.
  14. ^ Gallo, Vincenzo. "Myristoylation : Proteins Post-translational Modifications". http://flipper.diff.org/. University of Turin. {{cite web}}: External link in |website= (help)
  15. ^ "Nextprot:TMEM261 » Transmembrane protein 261".
  16. ^ Dash, A; et al. (2002). "Changes in differential gene expression because of warm ischemia time of radical prostatectomy specimens". Am J Pathol. 161 (5): 1743–1748. doi:10.1016/S0002-9440(10)64451-3. PMC 1850797. PMID 12414521. {{cite journal}}: Explicit use of et al. in: |first1= (help)
  17. ^ Rovillain, E; et al. (2011). "An RNA interference screen for identifying downstream effectors of the p53 and pRB tumour suppressor pathways involved in senescence". BMC Genomics. 12 (355): 355. doi:10.1186/1471-2164-12-355. PMC 3161017. PMID 21740549. {{cite journal}}: Explicit use of et al. in: |first1= (help)CS1 maint: unflagged free DOI (link)
  18. ^ "c9orf123 protein (Homo Sapiens)- STRING Network View". STRING - Known and Predicted Protein-Protein Interactions.
  19. ^ Oláh, J; et al. (2011). "Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein". J Biol Chem. 286 (39): 34088–34100. doi:10.1074/jbc.M111.243907. PMC 3190826. PMID 21832049. {{cite journal}}: Explicit use of et al. in: |first1= (help)CS1 maint: unflagged free DOI (link)
  20. ^ Huttlin, E L; et al. (2014). "High-Throughput Proteomic Mapping of Human Interaction Networks via Affinity-Purification Mass Spectrometry (Pre-Publication)". Pre-Publication. {{cite journal}}: Explicit use of et al. in: |first1= (help)
  21. ^ Lehner, B; Sanderson, C M (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–1323. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
  22. ^ "9ORF123 chromosome 9 open reading frame 123". BioGRID: Database of Protein and Genetic Interactions. TyersLab.
  23. ^ a b c She X, Rohl CA, Castle JC, Kulkarni AV, Johnson JM, Chen R (2009). "Definition, conservation and epigenetics of housekeeping and tissue-enriched genes". BMC Genomics. 10: 269. doi:10.1186/1471-2164-10-269. PMC 2706266. PMID 19534766.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  24. ^ "GeneCards:MEF2C Gene".
  25. ^ Welch, J J; et al. (2004). "Global regulation of erythroid gene expression by transcription factor GATA-1". Blood. 104 (10): 3136–3147. doi:10.1182/blood-2004-04-1603. PMID 15297311. {{cite journal}}: Explicit use of et al. in: |first1= (help)
  26. ^ Merryweather-Clarke, A T; et al. (2011). "Global gene expression analysis of human erythroid progenitors". Blood. 117 (13): e96-108. doi:10.1182/blood-2010-07-290825. PMID 21270440. {{cite journal}}: Explicit use of et al. in: |first1= (help)
  27. ^ "Genomatics- NGS Data Analysis and Personalised Medicine". Genomatix. Genomatix Software GmbH.
  28. ^ a b c "The Human Protein Atlas:TMEM261".
  29. ^ "EST profile: TMEM261". UniGene. National Library of Medicine.
  30. ^ Gaspar, C (2008). "Cross-Species Comparison of Human and Mouse Intestinal Polyps Reveals Conserved Mechanisms in Adenomatous Polyposis Coli (APC)-Driven Tumorigenesis". Am J Pathol. 172 (5): 1363–1380. doi:10.2353/ajpath.2008.070851. PMC 2329845. PMID 18403596.
  31. ^ Wu, J (2012). "Identification and functional analysis of 9p24 amplified genes in human breast cancer". Oncogene. 31 (3): 333–341. doi:10.1038/onc.2011.227. PMC 3886828. PMID 21666724.
  32. ^ Twa, D D W; et al. (2014). "Genomic Rearrangements Involving Programmed Death Ligands Are Recurrent in Primary Mediastinal Large B-Cell Lymphoma". Blood. 123 (13): 2062–2065. doi:10.1182/blood-2013-10-535443. PMID 24497532. {{cite journal}}: Explicit use of et al. in: |first1= (help)
  33. ^ Green, M R; et al. (2010). "Integrative Analysis Reveals Selective 9p24.1 Amplification, Increased PD-1 Ligand Expression, and Further Induction via JAK2 in Nodular Sclerosing Hodgkin Lymphoma and Primary Mediastinal Large B-Cell Lymphoma". Blood. 116 (17): 3268–3277. doi:10.1182/blood-2010-05-282780. PMC 2995356. PMID 20628145. {{cite journal}}: Explicit use of et al. in: |first1= (help)
  34. ^ a b "NCBI BLAST:Basic Local Alignment Search Tool".
  35. ^ Hedges, S. Blaire; Dudley, Joel; Kumar, Sudhir (22 September 2006). "TimeTree: a public knowledge-base of divergence times among organisms" (PDF). Bioinformatics. 22 (23): 2971–2972. doi:10.1093/bioinformatics/btl505. PMID 17021158.


[edit]

Further Reading

[edit]
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