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{{Infobox gene}}
{{Infobox gene}}


[[File:Homo sapiens THAP3 Tertiary Structure.png|thumb|303x303px|Predicted Tertiary Structure of ''Homo sapiens'' THAP3 protein.<ref name=":9">{{Cite journal |last=Jumper |first=John |last2=Evans |first2=Richard |last3=Pritzel |first3=Alexander |last4=Green |first4=Tim |last5=Figurnov |first5=Michael |last6=Ronneberger |first6=Olaf |last7=Tunyasuvunakool |first7=Kathryn |last8=Bates |first8=Russ |last9=Žídek |first9=Augustin |last10=Potapenko |first10=Anna |last11=Bridgland |first11=Alex |last12=Meyer |first12=Clemens |last13=Kohl |first13=Simon A. A. |last14=Ballard |first14=Andrew J. |last15=Cowie |first15=Andrew |date=August 2021f |title=Highly accurate protein structure prediction with AlphaFold |url=https://www.nature.com/articles/s41586-021-03819-2 |journal=Nature |language=en |volume=596 |issue=7873 |pages=583–589 |doi=10.1038/s41586-021-03819-2 |issn=1476-4687 |pmc=8371605 |pmid=34265844}}</ref><ref name=":10">{{Cite journal |last=Varadi |first=Mihaly |last2=Anyango |first2=Stephen |last3=Deshpande |first3=Mandar |last4=Nair |first4=Sreenath |last5=Natassia |first5=Cindy |last6=Yordanova |first6=Galabina |last7=Yuan |first7=David |last8=Stroe |first8=Oana |last9=Wood |first9=Gemma |last10=Laydon |first10=Agata |last11=Žídek |first11=Augustin |last12=Green |first12=Tim |last13=Tunyasuvunakool |first13=Kathryn |last14=Petersen |first14=Stig |last15=Jumper |first15=John |date=2021-11-17 |title=AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models |url=https://doi.org/10.1093/nar/gkab1061 |journal=Nucleic Acids Research |volume=50 |issue=D1 |pages=D439–D444 |doi=10.1093/nar/gkab1061 |issn=0305-1048 |pmc=8728224 |pmid=34791371}}</ref>]]
[[File:Homo sapiens THAP3 Tertiary Structure.png|thumb|303x303px|Predicted Tertiary Structure of ''Homo sapiens'' THAP3 protein.<ref name=":9">{{Cite journal |last1=Jumper |first1=John |last2=Evans |first2=Richard |last3=Pritzel |first3=Alexander |last4=Green |first4=Tim |last5=Figurnov |first5=Michael |last6=Ronneberger |first6=Olaf |last7=Tunyasuvunakool |first7=Kathryn |last8=Bates |first8=Russ |last9=Žídek |first9=Augustin |last10=Potapenko |first10=Anna |last11=Bridgland |first11=Alex |last12=Meyer |first12=Clemens |last13=Kohl |first13=Simon A. A. |last14=Ballard |first14=Andrew J. |last15=Cowie |first15=Andrew |date=August 2021f |title=Highly accurate protein structure prediction with AlphaFold |journal=Nature |language=en |volume=596 |issue=7873 |pages=583–589 |doi=10.1038/s41586-021-03819-2 |issn=1476-4687 |pmc=8371605 |pmid=34265844|bibcode=2021Natur.596..583J }}</ref><ref name=":10">{{Cite journal |last1=Varadi |first1=Mihaly |last2=Anyango |first2=Stephen |last3=Deshpande |first3=Mandar |last4=Nair |first4=Sreenath |last5=Natassia |first5=Cindy |last6=Yordanova |first6=Galabina |last7=Yuan |first7=David |last8=Stroe |first8=Oana |last9=Wood |first9=Gemma |last10=Laydon |first10=Agata |last11=Žídek |first11=Augustin |last12=Green |first12=Tim |last13=Tunyasuvunakool |first13=Kathryn |last14=Petersen |first14=Stig |last15=Jumper |first15=John |date=2021-11-17 |title=AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models |url=https://doi.org/10.1093/nar/gkab1061 |journal=Nucleic Acids Research |volume=50 |issue=D1 |pages=D439–D444 |doi=10.1093/nar/gkab1061 |issn=0305-1048 |pmc=8728224 |pmid=34791371}}</ref>]]
'''THAP domain-containing protein 3''' ('''THAP3''') is a [[protein]] that, in ''[[Human|Homo sapiens]]'' (humans), is encoded by the THAP3 [[gene]].<ref name=":2">{{Cite web |title=THAP3 THAP domain containing 3 [Homo sapiens (human)] - Gene - NCBI |url=https://www.ncbi.nlm.nih.gov/gene/90326#gene-expression |access-date=2022-12-08 |website=www.ncbi.nlm.nih.gov}}</ref> The THAP3 [[protein]] is as known as MGC33488, LOC90326, and THAP domain-containing, [[apoptosis]] associated [[protein]] 3. This [[protein]] contains the [[Thanatos]]-associated protein (THAP) [[Protein domain|domain]]<ref>{{Cite journal |last=Roussigne |first=Myriam |last2=Kossida |first2=Sophia |last3=Lavigne |first3=Anne-Claire |last4=Clouaire |first4=Thomas |last5=Ecochard |first5=Vincent |last6=Glories |first6=Alexandra |last7=Amalric |first7=François |last8=Girard |first8=Jean-Philippe |date=2003-02-01 |title=The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase |url=https://www.cell.com/trends/biochemical-sciences/abstract/S0968-0004(02)00013-0 |journal=Trends in Biochemical Sciences |language=English |volume=28 |issue=2 |pages=66–69 |doi=10.1016/S0968-0004(02)00013-0 |issn=0968-0004 |pmid=12575992}}</ref> and a [[Host cell factor C1|host-cell factor 1C]] binding motif.<ref>{{Cite journal |date=2022-04-22 |title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 1, mRNA |url=http://www.ncbi.nlm.nih.gov/nuccore/NM_001195752.2 |language=en-US}}</ref> These [[Protein domain|domains]] allow THAP3 to influence a variety of processes, including [[Transcription (biology)|transcription]] and [[Development of the nervous system|neuronal development]].<ref name=":11">{{Cite journal |last=Sabogal |first=Alex |last2=Lyubimov |first2=Artem Y. |last3=Corn |first3=Jacob E. |last4=Berger |first4=James M. |last5=Rio |first5=Donald C. |date=January 2010 |title=THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves |url=https://www.nature.com/articles/nsmb.1742 |journal=Nature Structural & Molecular Biology |language=en |volume=17 |issue=1 |pages=117–123 |doi=10.1038/nsmb.1742 |issn=1545-9985 |pmc=2933787 |pmid=20010837}}</ref> THAP3 is ubiquitously [[Gene expression|expressed]] in ''[[Human|H. sapiens]],'' though expression is highest in the [[Kidney|kidneys]].<ref name=":2" />
'''THAP domain-containing protein 3''' ('''THAP3''') is a [[protein]] that, in ''[[Human|Homo sapiens]]'' (humans), is encoded by the THAP3 [[gene]].<ref name=":2">{{Cite web |title=THAP3 THAP domain containing 3 [Homo sapiens (human)] - Gene - NCBI |url=https://www.ncbi.nlm.nih.gov/gene/90326#gene-expression |access-date=2022-12-08 |website=www.ncbi.nlm.nih.gov}}</ref> The THAP3 [[protein]] is as known as MGC33488, LOC90326, and THAP domain-containing, [[apoptosis]] associated [[protein]] 3. This [[protein]] contains the [[Thanatos]]-associated protein (THAP) [[Protein domain|domain]]<ref>{{Cite journal |last1=Roussigne |first1=Myriam |last2=Kossida |first2=Sophia |last3=Lavigne |first3=Anne-Claire |last4=Clouaire |first4=Thomas |last5=Ecochard |first5=Vincent |last6=Glories |first6=Alexandra |last7=Amalric |first7=François |last8=Girard |first8=Jean-Philippe |date=2003-02-01 |title=The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase |url=https://www.cell.com/trends/biochemical-sciences/abstract/S0968-0004(02)00013-0 |journal=Trends in Biochemical Sciences |language=English |volume=28 |issue=2 |pages=66–69 |doi=10.1016/S0968-0004(02)00013-0 |issn=0968-0004 |pmid=12575992}}</ref> and a [[Host cell factor C1|host-cell factor 1C]] binding motif.<ref>{{Cite journal |date=2022-04-22 |title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 1, mRNA |url=http://www.ncbi.nlm.nih.gov/nuccore/NM_001195752.2 |language=en-US}}</ref> These [[Protein domain|domains]] allow THAP3 to influence a variety of processes, including [[Transcription (biology)|transcription]] and [[Development of the nervous system|neuronal development]].<ref name=":11">{{Cite journal |last1=Sabogal |first1=Alex |last2=Lyubimov |first2=Artem Y. |last3=Corn |first3=Jacob E. |last4=Berger |first4=James M. |last5=Rio |first5=Donald C. |date=January 2010 |title=THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves |journal=Nature Structural & Molecular Biology |language=en |volume=17 |issue=1 |pages=117–123 |doi=10.1038/nsmb.1742 |issn=1545-9985 |pmc=2933787 |pmid=20010837}}</ref> THAP3 is ubiquitously [[Gene expression|expressed]] in ''[[Human|H. sapiens]],'' though expression is highest in the [[Kidney|kidneys]].<ref name=":2" />


== Gene ==
== Gene ==
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=== Expression ===
=== Expression ===
In ''[[Human|H. sapiens]]'', THAP3 [[gene]] is expressed ubiquitously throughout different [[Tissue (biology)|tissues]], and [[Gene expression|expression]] is greatest in the [[Kidney|kidneys]].<ref name=":7">{{Cite journal |last=Fagerberg |first=Linn |last2=Hallström |first2=Björn M. |last3=Oksvold |first3=Per |last4=Kampf |first4=Caroline |last5=Djureinovic |first5=Dijana |last6=Odeberg |first6=Jacob |last7=Habuka |first7=Masato |last8=Tahmasebpoor |first8=Simin |last9=Danielsson |first9=Angelika |last10=Edlund |first10=Karolina |last11=Asplund |first11=Anna |last12=Sjöstedt |first12=Evelina |last13=Lundberg |first13=Emma |last14=Szigyarto |first14=Cristina Al-Khalili |last15=Skogs |first15=Marie |date=February 2014 |title=Analysis of the Human Tissue-specific Expression by Genome-wide Integration of Transcriptomics and Antibody-based Proteomics |url=https://linkinghub.elsevier.com/retrieve/pii/S1535947620346338 |journal=Molecular & Cellular Proteomics |language=en |volume=13 |issue=2 |pages=397–406 |doi=10.1074/mcp.M113.035600}}</ref> It has also been determined that [[Gene expression|expression]] of THAP3 tends to be slightly higher in [[Organ (biology)|organs]] located in the [[abdomen]] and male and female sexual organs, such as the [[Ovary|ovaries]], [[Testicle|testes]], [[prostate]], [[adrenal gland]], [[spleen]], [[liver]], and [[Large intestine|colon]], though [[Gene expression|expression]] in the [[Kidney|kidneys]] is 1.4-1.5x higher than those [[Organ (biology)|organs]].<ref name=":7" /> THAP3 [[Messenger RNA|mRNA]] is 1.3x. more abundant in ''[[Human|H. sapiens]]'' fetal [[brain]] [[Tissue (biology)|tissue]] than in ''[[Human|H. sapiens]]'' adult [[kidney]] [[Tissue (biology)|tissue]].<ref>{{Cite journal |last=Duff |first=Michael O. |last2=Olson |first2=Sara |last3=Wei |first3=Xintao |last4=Garrett |first4=Sandra C. |last5=Osman |first5=Ahmad |last6=Bolisetty |first6=Mohan |last7=Plocik |first7=Alex |last8=Celniker |first8=Susan E. |last9=Graveley |first9=Brenton R. |date=2015-05-21 |title=Genome-wide identification of zero nucleotide recursive splicing in Drosophila |url=https://pubmed.ncbi.nlm.nih.gov/25970244/ |journal=Nature |volume=521 |issue=7552 |pages=376–379 |doi=10.1038/nature14475 |issn=1476-4687 |pmc=4529404 |pmid=25970244}}</ref>
In ''[[Human|H. sapiens]]'', THAP3 [[gene]] is expressed ubiquitously throughout different [[Tissue (biology)|tissues]], and [[Gene expression|expression]] is greatest in the [[Kidney|kidneys]].<ref name=":7">{{Cite journal |last1=Fagerberg |first1=Linn |last2=Hallström |first2=Björn M. |last3=Oksvold |first3=Per |last4=Kampf |first4=Caroline |last5=Djureinovic |first5=Dijana |last6=Odeberg |first6=Jacob |last7=Habuka |first7=Masato |last8=Tahmasebpoor |first8=Simin |last9=Danielsson |first9=Angelika |last10=Edlund |first10=Karolina |last11=Asplund |first11=Anna |last12=Sjöstedt |first12=Evelina |last13=Lundberg |first13=Emma |last14=Szigyarto |first14=Cristina Al-Khalili |last15=Skogs |first15=Marie |date=February 2014 |title=Analysis of the Human Tissue-specific Expression by Genome-wide Integration of Transcriptomics and Antibody-based Proteomics |journal=Molecular & Cellular Proteomics |language=en |volume=13 |issue=2 |pages=397–406 |doi=10.1074/mcp.M113.035600|pmid=24309898 |pmc=3916642 }}</ref> It has also been determined that [[Gene expression|expression]] of THAP3 tends to be slightly higher in [[Organ (biology)|organs]] located in the [[abdomen]] and male and female sexual organs, such as the [[Ovary|ovaries]], [[Testicle|testes]], [[prostate]], [[adrenal gland]], [[spleen]], [[liver]], and [[Large intestine|colon]], though [[Gene expression|expression]] in the [[Kidney|kidneys]] is 1.4-1.5x higher than those [[Organ (biology)|organs]].<ref name=":7" /> THAP3 [[Messenger RNA|mRNA]] is 1.3x. more abundant in ''[[Human|H. sapiens]]'' fetal [[brain]] [[Tissue (biology)|tissue]] than in ''[[Human|H. sapiens]]'' adult [[kidney]] [[Tissue (biology)|tissue]].<ref>{{Cite journal |last1=Duff |first1=Michael O. |last2=Olson |first2=Sara |last3=Wei |first3=Xintao |last4=Garrett |first4=Sandra C. |last5=Osman |first5=Ahmad |last6=Bolisetty |first6=Mohan |last7=Plocik |first7=Alex |last8=Celniker |first8=Susan E. |last9=Graveley |first9=Brenton R. |date=2015-05-21 |title=Genome-wide identification of zero nucleotide recursive splicing in Drosophila |journal=Nature |volume=521 |issue=7552 |pages=376–379 |doi=10.1038/nature14475 |issn=1476-4687 |pmc=4529404 |pmid=25970244|bibcode=2015Natur.521..376D }}</ref>


== mRNA ==
== mRNA ==
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|2071
|2071
|NM_138350.4<ref>{{Cite web|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_138350.4|title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 2, m - Nucleotide - NCBI|website=www.ncbi.nlm.nih.gov}}</ref>
|NM_138350.4<ref>{{Cite journal|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_138350.4|title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 2, m - Nucleotide - NCBI|website=www.ncbi.nlm.nih.gov|date=22 April 2022 }}</ref>
|-
|-
|3
|3
|1361
|1361
|NM_001195753.2<ref>{{Cite web|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_001195753.2|title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 3, m - Nucleotide - NCBI|website=www.ncbi.nlm.nih.gov}}</ref>
|NM_001195753.2<ref>{{Cite journal|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_001195753.2|title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 3, m - Nucleotide - NCBI|website=www.ncbi.nlm.nih.gov|date=10 June 2022 }}</ref>
|-
|-
|4
|4
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|7
|1123
|1123
|NM_001394499.1<ref>{{Cite web|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_001394499.1|title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 7, m - Nucleotide - NCBI|website=www.ncbi.nlm.nih.gov}}</ref>
|NM_001394499.1<ref>{{Cite journal|url=https://www.ncbi.nlm.nih.gov/nuccore/NM_001394499.1|title=Homo sapiens THAP domain containing 3 (THAP3), transcript variant 7, m - Nucleotide - NCBI|website=www.ncbi.nlm.nih.gov|date=22 April 2022 }}</ref>
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== Protein ==
== Protein ==
[[File:Conceptual Translation of Homo sapiens THAP3.png|thumb|371x371px|Conceptual translation of ''Homo sapiens'' THAP3 aligned mRNA and amino acid sequences. Annotated with start and stop sites of translations, protein domains, and predicted post-translational modification sites. ]]
[[File:Conceptual Translation of Homo sapiens THAP3.png|thumb|371x371px|Conceptual translation of ''Homo sapiens'' THAP3 aligned mRNA and amino acid sequences. Annotated with start and stop sites of translations, protein domains, and predicted post-translational modification sites. ]]
The ''[[Human|H. sapiens]]'' THAP3 [[protein]] is predicted to have a [[Molecular mass|molecular weight]] of 26.9 [[Dalton (unit)|kiloDaltons]]<ref name=":8">{{Cite journal |last=Brendel |first=V |last2=Bucher |first2=P |last3=Nourbakhsh |first3=I R |last4=Blaisdell |first4=B E |last5=Karlin |first5=S |date=1992-03-15 |title=Methods and algorithms for statistical analysis of protein sequences. |url=https://pnas.org/doi/full/10.1073/pnas.89.6.2002 |journal=Proceedings of the National Academy of Sciences |language=en |volume=89 |issue=6 |pages=2002–2006 |doi=10.1073/pnas.89.6.2002 |issn=0027-8424 |pmc=48584 |pmid=1549558}}</ref> and a [[Isoelectric point|pI]] of 10.26.<ref>Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A.; ''Protein Identification and Analysis Tools on the Expasy Server;'' (In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press (2005).</ref> The [[amino acid]] sequence is [[isoleucine]] and [[tyrosine]] rich and [[arginine]] poor.<ref name=":8" /> Characteristics [[Protein domain|domains]] of ''[[Human|H. sapiens]]'' are the THAP [[Protein domain|domain]] (THAP) and the hell-cell factor 1C binding motif (HCM).<ref name=":2" />
The ''[[Human|H. sapiens]]'' THAP3 [[protein]] is predicted to have a [[Molecular mass|molecular weight]] of 26.9 [[Dalton (unit)|kiloDaltons]]<ref name=":8">{{Cite journal |last1=Brendel |first1=V |last2=Bucher |first2=P |last3=Nourbakhsh |first3=I R |last4=Blaisdell |first4=B E |last5=Karlin |first5=S |date=1992-03-15 |title=Methods and algorithms for statistical analysis of protein sequences. |journal=Proceedings of the National Academy of Sciences |language=en |volume=89 |issue=6 |pages=2002–2006 |doi=10.1073/pnas.89.6.2002 |issn=0027-8424 |pmc=48584 |pmid=1549558|bibcode=1992PNAS...89.2002B |doi-access=free }}</ref> and a [[Isoelectric point|pI]] of 10.26.<ref>Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A.; ''Protein Identification and Analysis Tools on the Expasy Server;'' (In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press (2005).</ref> The [[amino acid]] sequence is [[isoleucine]] and [[tyrosine]] rich and [[arginine]] poor.<ref name=":8" /> Characteristics [[Protein domain|domains]] of ''[[Human|H. sapiens]]'' are the THAP [[Protein domain|domain]] (THAP) and the hell-cell factor 1C binding motif (HCM).<ref name=":2" />


=== Isoforms ===
=== Isoforms ===
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=== Structure ===
=== Structure ===
[[File:Cartoon Schematic of Homo sapiens THAP3.png|thumb|372x372px|Schematic of ''Homo sapiens'' THAP3 protein sequence with annotated domains, predicted phosphorylation, glycosylation, and Yin-Yang sites.<ref>{{Cite journal |last=Liu |first=Wenzhong |last2=Xie |first2=Yubin |last3=Ma |first3=Jiyong |last4=Luo |first4=Xiaotong |last5=Nie |first5=Peng |last6=Zuo |first6=Zhixiang |last7=Lahrmann |first7=Urs |last8=Zhao |first8=Qi |last9=Zheng |first9=Yueyuan |last10=Zhao |first10=Yong |last11=Xue |first11=Yu |last12=Ren |first12=Jian |date=2015-06-10 |title=IBS: an illustrator for the presentation and visualization of biological sequences: Fig. 1. |url=https://doi.org/10.1093/bioinformatics/btv362 |journal=Bioinformatics |volume=31 |issue=20 |pages=3359–3361 |doi=10.1093/bioinformatics/btv362 |issn=1367-4803 |pmc=4595897 |pmid=26069263}}</ref> THAP represents the location of the THAP domain, and HBM represents the HCF1C binding motif. Yellow represents glycosylation sites (with scores over 0.5),<ref name=":5">Gupta, R. (2001). ''Prediction of glycosylation sites in proteomes: from post-translational modifications to protein function''. Technical University of Denmark.</ref> green represents phosphorylation sites (with scores over 0.75),<ref name=":12">{{Cite journal |last=Blom |first=Nikolaj |last2=Gammeltoft |first2=Steen |last3=Brunak |first3=Søren |date=December 1999 |title=Sequence and structure-based prediction of eukaryotic protein phosphorylation sites |url=https://linkinghub.elsevier.com/retrieve/pii/S0022283699933107 |journal=Journal of Molecular Biology |language=en |volume=294 |issue=5 |pages=1351–1362 |doi=10.1006/jmbi.1999.3310}}</ref> and diamond shapes represent Yin-Yang sites.<ref name=":5" />]]The predicted ''[[Human|H. sapiens]]'' THAP3 [[Protein tertiary structure|tertiary structure]] contains a [[Globular protein|globular]] region and an [[alpha helix]].<ref name=":9" /><ref name=":10" /> The [[Globular protein|globular]] region is located near the [[N-terminus]] of the sequence and is the structure of the THAP [[Protein domain|domain]]. It spans [[Amino acid|amino acids]] 4-82.<ref name=":13">{{Cite journal |last=Wang |first=Jiyao |last2=Youkharibache |first2=Philippe |last3=Marchler-Bauer |first3=Aron |last4=Lanczycki |first4=Christopher |last5=Zhang |first5=Dachuan |last6=Lu |first6=Shennan |last7=Madej |first7=Thomas |last8=Marchler |first8=Gabriele H. |last9=Cheng |first9=Tiejun |last10=Chong |first10=Li Chuin |last11=Zhao |first11=Sarah |last12=Yang |first12=Kevin |last13=Lin |first13=Jack |last14=Cheng |first14=Zhiyu |last15=Dunn |first15=Rachel |date=2022 |title=iCn3D: From Web-Based 3D Viewer to Structural Analysis Tool in Batch Mode |url=https://pubmed.ncbi.nlm.nih.gov/35252351/ |journal=Frontiers in Molecular Biosciences |volume=9 |pages=831740 |doi=10.3389/fmolb.2022.831740 |issn=2296-889X |pmc=8892267 |pmid=35252351}}</ref> The [[alpha helix]] is located from [[Amino acid|amino acids]] 186-230 and contains the host-cell factor 1C binding motif.<ref name=":13" />
[[File:Cartoon Schematic of Homo sapiens THAP3.png|thumb|372x372px|Schematic of ''Homo sapiens'' THAP3 protein sequence with annotated domains, predicted phosphorylation, glycosylation, and Yin-Yang sites.<ref>{{Cite journal |last1=Liu |first1=Wenzhong |last2=Xie |first2=Yubin |last3=Ma |first3=Jiyong |last4=Luo |first4=Xiaotong |last5=Nie |first5=Peng |last6=Zuo |first6=Zhixiang |last7=Lahrmann |first7=Urs |last8=Zhao |first8=Qi |last9=Zheng |first9=Yueyuan |last10=Zhao |first10=Yong |last11=Xue |first11=Yu |last12=Ren |first12=Jian |date=2015-06-10 |title=IBS: an illustrator for the presentation and visualization of biological sequences: Fig. 1. |url=https://doi.org/10.1093/bioinformatics/btv362 |journal=Bioinformatics |volume=31 |issue=20 |pages=3359–3361 |doi=10.1093/bioinformatics/btv362 |issn=1367-4803 |pmc=4595897 |pmid=26069263}}</ref> THAP represents the location of the THAP domain, and HBM represents the HCF1C binding motif. Yellow represents glycosylation sites (with scores over 0.5),<ref name=":5">Gupta, R. (2001). ''Prediction of glycosylation sites in proteomes: from post-translational modifications to protein function''. Technical University of Denmark.</ref> green represents phosphorylation sites (with scores over 0.75),<ref name=":12">{{Cite journal |last1=Blom |first1=Nikolaj |last2=Gammeltoft |first2=Steen |last3=Brunak |first3=Søren |date=December 1999 |title=Sequence and structure-based prediction of eukaryotic protein phosphorylation sites |url=https://linkinghub.elsevier.com/retrieve/pii/S0022283699933107 |journal=Journal of Molecular Biology |language=en |volume=294 |issue=5 |pages=1351–1362 |doi=10.1006/jmbi.1999.3310|pmid=10600390 }}</ref> and diamond shapes represent Yin-Yang sites.<ref name=":5" />]]The predicted ''[[Human|H. sapiens]]'' THAP3 [[Protein tertiary structure|tertiary structure]] contains a [[Globular protein|globular]] region and an [[alpha helix]].<ref name=":9" /><ref name=":10" /> The [[Globular protein|globular]] region is located near the [[N-terminus]] of the sequence and is the structure of the THAP [[Protein domain|domain]]. It spans [[Amino acid|amino acids]] 4-82.<ref name=":13">{{Cite journal |last1=Wang |first1=Jiyao |last2=Youkharibache |first2=Philippe |last3=Marchler-Bauer |first3=Aron |last4=Lanczycki |first4=Christopher |last5=Zhang |first5=Dachuan |last6=Lu |first6=Shennan |last7=Madej |first7=Thomas |last8=Marchler |first8=Gabriele H. |last9=Cheng |first9=Tiejun |last10=Chong |first10=Li Chuin |last11=Zhao |first11=Sarah |last12=Yang |first12=Kevin |last13=Lin |first13=Jack |last14=Cheng |first14=Zhiyu |last15=Dunn |first15=Rachel |date=2022 |title=iCn3D: From Web-Based 3D Viewer to Structural Analysis Tool in Batch Mode |journal=Frontiers in Molecular Biosciences |volume=9 |pages=831740 |doi=10.3389/fmolb.2022.831740 |issn=2296-889X |pmc=8892267 |pmid=35252351|doi-access=free }}</ref> The [[alpha helix]] is located from [[Amino acid|amino acids]] 186-230 and contains the host-cell factor 1C binding motif.<ref name=":13" />


=== Regulation ===
=== Regulation ===
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==== Post-translation modifications ====
==== Post-translation modifications ====
The ''[[Human|H. sapiens]]'' the THAP3 [[protein]] has 30 predicted [[phosphorylation]] sites, 28 predicted [[O-linked glycosylation|O-β-glycosylation]] sites, and 11 predicted Yin-Yang sites.<ref name=":5" /><ref name=":12" /> Many [[Protein|proteins]] involved in [[Transcriptional regulation|transcription regulation]] are influenced by [[phosphorylation]] and [[glycosylation]] sites, which corroborates THAP3's function.<ref>{{Cite journal |last=Filtz |first=Theresa M. |last2=Vogel |first2=Walter K. |last3=Leid |first3=Mark |date=February 2014 |title=Regulation of transcription factor activity by interconnected, post-translational modifications |url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3954851/ |journal=Trends in pharmacological sciences |volume=35 |issue=2 |pages=76–85 |doi=10.1016/j.tips.2013.11.005 |issn=0165-6147 |pmc=3954851 |pmid=24388790}}</ref>
The ''[[Human|H. sapiens]]'' the THAP3 [[protein]] has 30 predicted [[phosphorylation]] sites, 28 predicted [[O-linked glycosylation|O-β-glycosylation]] sites, and 11 predicted Yin-Yang sites.<ref name=":5" /><ref name=":12" /> Many [[Protein|proteins]] involved in [[Transcriptional regulation|transcription regulation]] are influenced by [[phosphorylation]] and [[glycosylation]] sites, which corroborates THAP3's function.<ref>{{Cite journal |last1=Filtz |first1=Theresa M. |last2=Vogel |first2=Walter K. |last3=Leid |first3=Mark |date=February 2014 |title=Regulation of transcription factor activity by interconnected, post-translational modifications |journal=Trends in Pharmacological Sciences |volume=35 |issue=2 |pages=76–85 |doi=10.1016/j.tips.2013.11.005 |issn=0165-6147 |pmc=3954851 |pmid=24388790}}</ref>


== Homology and evolution ==
== Homology and evolution ==


=== Paralogs ===
=== Paralogs ===
The ''[[Human|H. sapiens]]'' THAP3 [[protein]], along with several other [[Protein|proteins]], is part of the THAP [[Protein family|family of proteins]].<ref>{{Cite journal |last=Sanghavi |first=Hiral M. |last2=Mallajosyula |first2=Sairam S. |last3=Majumdar |first3=Sharmistha |date=2019-03-05 |title=Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region |url=https://doi.org/10.1186/s12900-019-0102-2 |journal=BMC Structural Biology |volume=19 |issue=1 |pages=4 |doi=10.1186/s12900-019-0102-2 |issn=1472-6807 |pmc=6402169 |pmid=30836974}}</ref> All of these [[Protein|proteins]] contain the THAP [[Protein domain|domain]] and are, thus, [[Sequence homology|paralogs]] of ''[[Human|H. sapiens]]'' THAP3.<ref name=":0" />
The ''[[Human|H. sapiens]]'' THAP3 [[protein]], along with several other [[Protein|proteins]], is part of the THAP [[Protein family|family of proteins]].<ref>{{Cite journal |last1=Sanghavi |first1=Hiral M. |last2=Mallajosyula |first2=Sairam S. |last3=Majumdar |first3=Sharmistha |date=2019-03-05 |title=Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region |url=https://doi.org/10.1186/s12900-019-0102-2 |journal=BMC Structural Biology |volume=19 |issue=1 |pages=4 |doi=10.1186/s12900-019-0102-2 |issn=1472-6807 |pmc=6402169 |pmid=30836974}}</ref> All of these [[Protein|proteins]] contain the THAP [[Protein domain|domain]] and are, thus, [[Sequence homology|paralogs]] of ''[[Human|H. sapiens]]'' THAP3.<ref name=":0" />
{| class="wikitable"
{| class="wikitable"
|+Paralogs of ''Homo sapiens'' THAP3 protein!<ref name=":2" />Protein Name
|+Paralogs of ''Homo sapiens'' THAP3 protein!<ref name=":2" />Protein Name
Line 154: Line 154:


=== Orthologs ===
=== Orthologs ===
[[File:MSA of THAP3.png|thumb|734x734px|Multiple sequence alignment of THAP domain in ''Homo'' ''sapiens'' THAP3 (HSa THAP3; accession number NP 001182681.1<ref name=":6">{{Cite web |title=THAP domain-containing protein 3 isoform 1 [Homo sapiens] - Protein - NCBI |url=https://www.ncbi.nlm.nih.gov/protein/NP 001182681.1 |access-date=2022-12-16 |website=www.ncbi.nlm.nih.gov}}</ref>) with distant orthologs.<ref>{{Cite journal |last=Sievers |first=Fabian |last2=Wilm |first2=Andreas |last3=Dineen |first3=David |last4=Gibson |first4=Toby J |last5=Karplus |first5=Kevin |last6=Li |first6=Weizhong |last7=Lopez |first7=Rodrigo |last8=McWilliam |first8=Hamish |last9=Remmert |first9=Michael |last10=Söding |first10=Johannes |last11=Thompson |first11=Julie D |last12=Higgins |first12=Desmond G |date=January 2011 |title=Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega |url=https://onlinelibrary.wiley.com/doi/10.1038/msb.2011.75 |journal=Molecular Systems Biology |language=en |volume=7 |issue=1 |pages=539 |doi=10.1038/msb.2011.75 |issn=1744-4292 |pmc=3261699 |pmid=21988835}}</ref> Boxing represents the location of the THAP domain in ''H. sapiens''. Bolding and asterisks below groups of sequence indicate that an amino acid is highly conserved at that position. Full sequences include that of Sumatra barb (PTe THAP3), Electric eel (EEl THAP3), Lake whitefish (CCL THAP3), Baby whale (BBr THAP3), Whale shark (ARa THAP3), White-spotted bamboo shark (RTy THAP3), and Thorny skate (CPl THAP3). Accession numbers as in ortholog table.]]
[[File:MSA of THAP3.png|thumb|734x734px|Multiple sequence alignment of THAP domain in ''Homo'' ''sapiens'' THAP3 (HSa THAP3; accession number NP 001182681.1<ref name=":6">{{Cite web |title=THAP domain-containing protein 3 isoform 1 [Homo sapiens] - Protein - NCBI |url=https://www.ncbi.nlm.nih.gov/protein/NP 001182681.1 |access-date=2022-12-16 |website=www.ncbi.nlm.nih.gov}}</ref>) with distant orthologs.<ref>{{Cite journal |last1=Sievers |first1=Fabian |last2=Wilm |first2=Andreas |last3=Dineen |first3=David |last4=Gibson |first4=Toby J |last5=Karplus |first5=Kevin |last6=Li |first6=Weizhong |last7=Lopez |first7=Rodrigo |last8=McWilliam |first8=Hamish |last9=Remmert |first9=Michael |last10=Söding |first10=Johannes |last11=Thompson |first11=Julie D |last12=Higgins |first12=Desmond G |date=January 2011 |title=Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega |journal=Molecular Systems Biology |language=en |volume=7 |issue=1 |pages=539 |doi=10.1038/msb.2011.75 |issn=1744-4292 |pmc=3261699 |pmid=21988835}}</ref> Boxing represents the location of the THAP domain in ''H. sapiens''. Bolding and asterisks below groups of sequence indicate that an amino acid is highly conserved at that position. Full sequences include that of Sumatra barb (PTe THAP3), Electric eel (EEl THAP3), Lake whitefish (CCL THAP3), Baby whale (BBr THAP3), Whale shark (ARa THAP3), White-spotted bamboo shark (RTy THAP3), and Thorny skate (CPl THAP3). Accession numbers as in ortholog table.]]
There are approximately 206 [[Sequence homology|orthlologs]] of ''[[Human|H. sapiens]]'' THAP3.<ref name=":2" /> Orthologs can be found in a variety of taxomonic [[Class (biology)|classes]], including [[Mammal|mammals]], [[Reptile|reptiles]], [[Amphibian|amphibians]], [[Osteichthyes|bony fishes]], and [[Chondrichthyes|cartilaginous fishes]].<ref name=":0" /> However, there are no [[Sequence homology|orthologs]] in [[bacteria]], [[Fungus|fungi]], [[Protist|protists]], [[archaea]], [[Plant|plants]], [[Invertebrate|invertebrates]], or [[Bird|birds]].<ref name=":0" /> Additionally, not all [[Order (biology)|orders]] are represented with in a [[Class (biology)|class]]. For example, in [[Reptile|reptiles]], [[Sequence homology|orthologs]] to ''[[Human|H. sapiens]]'' THAP3 are found in [[Turtle|testudines]] (turtles or tortoises) and not found in [[crocodilia]] (crocodiles and alligators) or [[squamata]] (lizards and snakes).<ref name=":0" /> Similarly, there are only [[Sequence homology|orthologs]] in [[Caecilian|apoda]] within [[Amphibian|amphibians]].<ref name=":0" /> There are no [[Sequence homology|orthologs]] in [[Frog|anura]] (frogs) or [[Salamander|urodela]] (salamanders).<ref name=":0" />
There are approximately 206 [[Sequence homology|orthlologs]] of ''[[Human|H. sapiens]]'' THAP3.<ref name=":2" /> Orthologs can be found in a variety of taxomonic [[Class (biology)|classes]], including [[Mammal|mammals]], [[Reptile|reptiles]], [[Amphibian|amphibians]], [[Osteichthyes|bony fishes]], and [[Chondrichthyes|cartilaginous fishes]].<ref name=":0" /> However, there are no [[Sequence homology|orthologs]] in [[bacteria]], [[Fungus|fungi]], [[Protist|protists]], [[archaea]], [[Plant|plants]], [[Invertebrate|invertebrates]], or [[Bird|birds]].<ref name=":0" /> Additionally, not all [[Order (biology)|orders]] are represented with in a [[Class (biology)|class]]. For example, in [[Reptile|reptiles]], [[Sequence homology|orthologs]] to ''[[Human|H. sapiens]]'' THAP3 are found in [[Turtle|testudines]] (turtles or tortoises) and not found in [[crocodilia]] (crocodiles and alligators) or [[squamata]] (lizards and snakes).<ref name=":0" /> Similarly, there are only [[Sequence homology|orthologs]] in [[Caecilian|apoda]] within [[Amphibian|amphibians]].<ref name=":0" /> There are no [[Sequence homology|orthologs]] in [[Frog|anura]] (frogs) or [[Salamander|urodela]] (salamanders).<ref name=":0" />


Line 164: Line 164:
![[Common name|Common Name]]
![[Common name|Common Name]]
!Taxonomic [[Order (biology)|Order]]
!Taxonomic [[Order (biology)|Order]]
!Date of [[Divergent evolution|Divergence]]!<ref>{{Cite journal |last=Kumar |first=Sudhir |last2=Suleski |first2=Michael |last3=Craig |first3=Jack M |last4=Kasprowicz |first4=Adrienne E |last5=Sanderford |first5=Maxwell |last6=Li |first6=Michael |last7=Stecher |first7=Glen |last8=Hedges |first8=S Blair |date=2022-08-03 |title=TimeTree 5: An Expanded Resource for Species Divergence Times |url=https://academic.oup.com/mbe/article/doi/10.1093/molbev/msac174/6657692 |journal=Molecular Biology and Evolution |language=en |volume=39 |issue=8 |pages=msac174 |doi=10.1093/molbev/msac174 |issn=0737-4038}}</ref>Accession Number!<ref name=":0">{{Cite web |title=Protein BLAST: search protein databases using a protein query |url=https://blast.ncbi.nlm.nih.gov/Blast.cgi?PROGRAM=blastp&PAGE_TYPE=BlastSearch&LINK_LOC=blasthome |access-date=2022-12-08 |website=blast.ncbi.nlm.nih.gov |language=en}}</ref>Percent Identity to THAP3!<ref name=":0" />Percent Similarity to THAP3<ref>{{Cite web |title=EMBOSS Needle < Pairwise Sequence Alignment < EMBL-EBI |url=https://www.ebi.ac.uk/Tools/psa/emboss_needle/ |access-date=2022-12-08 |website=www.ebi.ac.uk}}</ref>
!Date of [[Divergent evolution|Divergence]]!<ref>{{Cite journal |last1=Kumar |first1=Sudhir |last2=Suleski |first2=Michael |last3=Craig |first3=Jack M |last4=Kasprowicz |first4=Adrienne E |last5=Sanderford |first5=Maxwell |last6=Li |first6=Michael |last7=Stecher |first7=Glen |last8=Hedges |first8=S Blair |date=2022-08-03 |title=TimeTree 5: An Expanded Resource for Species Divergence Times |url=https://academic.oup.com/mbe/article/doi/10.1093/molbev/msac174/6657692 |journal=Molecular Biology and Evolution |language=en |volume=39 |issue=8 |pages=msac174 |doi=10.1093/molbev/msac174 |pmid=35932227 |pmc=9400175 |issn=0737-4038}}</ref>Accession Number!<ref name=":0">{{Cite web |title=Protein BLAST: search protein databases using a protein query |url=https://blast.ncbi.nlm.nih.gov/Blast.cgi?PROGRAM=blastp&PAGE_TYPE=BlastSearch&LINK_LOC=blasthome |access-date=2022-12-08 |website=blast.ncbi.nlm.nih.gov |language=en}}</ref>Percent Identity to THAP3!<ref name=":0" />Percent Similarity to THAP3<ref>{{Cite web |title=EMBOSS Needle < Pairwise Sequence Alignment < EMBL-EBI |url=https://www.ebi.ac.uk/Tools/psa/emboss_needle/ |access-date=2022-12-08 |website=www.ebi.ac.uk}}</ref>
|-
|-
![[Mammal|Mammals]]
![[Mammal|Mammals]]
Line 400: Line 400:


== Clinical significance ==
== Clinical significance ==
THAP3 contributes to the presentation of [[X-linked dystonia parkinsonism|X-linked Dystonia-Parkinsonism]], also known as [[X-linked dystonia parkinsonism|Lubag Syndrome]].<ref>{{Cite web |title=THAP3 Gene - GeneCards {{!}} THAP3 Protein {{!}} THAP3 Antibody |url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=THAP3&keywords=THAP3 |access-date=2022-12-08 |website=www.genecards.org}}</ref> This disease is a [[Neurodegenerative disease|neurodegenerative]] movement disorder that predominantly affects males of Filipino descent.<ref name=":1">{{Cite journal |last=Rosales |first=Raymond L. |date=2010-10-30 |title=X-Linked Dystonia Parkinsonism: Clinical Phenotype, Genetics and Therapeutics |url=http://www.e-jmd.org/journal/view.php?doi=10.14802/jmd.10009 |journal=Journal of Movement Disorders |language=English |volume=3 |issue=2 |pages=32–38 |doi=10.14802/jmd.10009 |issn=2005-940X |pmc=4027667 |pmid=24868378}}</ref> Symptoms include [[Tremor|tremors]], [[Hypokinesia|bradykinesia]], [[Spasticity|rigidity]], [[Balance disorder|postural instability]], [[Gait abnormality|shuffling gait]] and [[dystonia]], which typically develops later in life.<ref name=":1" />
THAP3 contributes to the presentation of [[X-linked dystonia parkinsonism|X-linked Dystonia-Parkinsonism]], also known as [[X-linked dystonia parkinsonism|Lubag Syndrome]].<ref>{{Cite web |title=THAP3 Gene - GeneCards {{!}} THAP3 Protein {{!}} THAP3 Antibody |url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=THAP3&keywords=THAP3 |access-date=2022-12-08 |website=www.genecards.org}}</ref> This disease is a [[Neurodegenerative disease|neurodegenerative]] movement disorder that predominantly affects males of Filipino descent.<ref name=":1">{{Cite journal |last=Rosales |first=Raymond L. |date=2010-10-30 |title=X-Linked Dystonia Parkinsonism: Clinical Phenotype, Genetics and Therapeutics |journal=Journal of Movement Disorders |language=English |volume=3 |issue=2 |pages=32–38 |doi=10.14802/jmd.10009 |issn=2005-940X |pmc=4027667 |pmid=24868378}}</ref> Symptoms include [[Tremor|tremors]], [[Hypokinesia|bradykinesia]], [[Spasticity|rigidity]], [[Balance disorder|postural instability]], [[Gait abnormality|shuffling gait]] and [[dystonia]], which typically develops later in life.<ref name=":1" />


== References ==
== References ==

Revision as of 21:29, 17 December 2022

THAP3
Identifiers
AliasesTHAP3, THAP domain containing 3
External IDsOMIM: 612532; MGI: 1917126; HomoloGene: 18413; GeneCards: THAP3; OMA:THAP3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

90326

69876

Ensembl

ENSG00000041988

ENSMUSG00000039759

UniProt

Q8WTV1

Q8BJ25

RefSeq (mRNA)

NM_001145929
NM_175152

RefSeq (protein)

NP_001182681
NP_001182682
NP_612359

NP_001139401
NP_780361

Location (UCSC)Chr 1: 6.62 – 6.64 MbChr 4: 152.07 – 152.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Predicted Tertiary Structure of Homo sapiens THAP3 protein.[5][6]

THAP domain-containing protein 3 (THAP3) is a protein that, in Homo sapiens (humans), is encoded by the THAP3 gene.[7] The THAP3 protein is as known as MGC33488, LOC90326, and THAP domain-containing, apoptosis associated protein 3. This protein contains the Thanatos-associated protein (THAP) domain[8] and a host-cell factor 1C binding motif.[9] These domains allow THAP3 to influence a variety of processes, including transcription and neuronal development.[10] THAP3 is ubiquitously expressed in H. sapiens, though expression is highest in the kidneys.[7]

Gene

The H. sapiens THAP3 gene is a protein-encoding gene that is located on the plus strand of chromosome 1[7] at cytogenetic location 1p36.31.[11] It is 10,727 base pairs long, spanning from genomic coordinates 6,624,868-6,635,595.[11] It contains 6 exons.[12]

Gene neighborhood of Homo sapiens (human) THAP3 gene on chromosome 1.[7]

Expression

In H. sapiens, THAP3 gene is expressed ubiquitously throughout different tissues, and expression is greatest in the kidneys.[13] It has also been determined that expression of THAP3 tends to be slightly higher in organs located in the abdomen and male and female sexual organs, such as the ovaries, testes, prostate, adrenal gland, spleen, liver, and colon, though expression in the kidneys is 1.4-1.5x higher than those organs.[13] THAP3 mRNA is 1.3x. more abundant in H. sapiens fetal brain tissue than in H. sapiens adult kidney tissue.[14]

mRNA

Transcription of the THAP3 gene can result in 11 different mRNA variants, of which 8 are alternatively spliced and 3 are unspliced.[7] Variant 1 is the predominant variant and encodes THAP3 protein isoform 1.[7]

Alternatively spliced Homo sapiens THAP3 mRNA transcript variants![15]Variant
Sequence length (nucleotides) Accession number[7]
1 1358 NM_001195752.2[16]
2 2071 NM_138350.4[17]
3 1361 NM_001195753.2[18]
4 1262 NM_001394496.1[19]
5 2050 NM_001394497.1[20]
6 2047 NM_001394498.1[21]
7 1123 NM_001394499.1[22]
8 1120 NM_001394500.1[23]

Protein

Conceptual translation of Homo sapiens THAP3 aligned mRNA and amino acid sequences. Annotated with start and stop sites of translations, protein domains, and predicted post-translational modification sites.

The H. sapiens THAP3 protein is predicted to have a molecular weight of 26.9 kiloDaltons[24] and a pI of 10.26.[25] The amino acid sequence is isoleucine and tyrosine rich and arginine poor.[24] Characteristics domains of H. sapiens are the THAP domain (THAP) and the hell-cell factor 1C binding motif (HCM).[7]

Isoforms

Due to having 8 alternatively spliced variants, there are 8 THAP3 isoforms.[7]

Isoforms of Homo sapiens THAP3[7]
Isoform Sequence length (amino acids) Accession number Encoded by
1 238 NP_001182681.1[26] Variant 1
2 175 NP_612359.2[27] Variant 2
3 239 NP_001182682.1[28] Variant 3
4 236 NP_001381425.1[29] Variant 4
5 168 NP_001381426.1[30] Variant 5
6 167 NP_001381427.1[31] Variant 6
7 148 NP_001381428.1[32] Variant 7
8 147 NP_001381429.1[33] Variant 8

Structure

Schematic of Homo sapiens THAP3 protein sequence with annotated domains, predicted phosphorylation, glycosylation, and Yin-Yang sites.[34] THAP represents the location of the THAP domain, and HBM represents the HCF1C binding motif. Yellow represents glycosylation sites (with scores over 0.5),[35] green represents phosphorylation sites (with scores over 0.75),[36] and diamond shapes represent Yin-Yang sites.[35]

The predicted H. sapiens THAP3 tertiary structure contains a globular region and an alpha helix.[5][6] The globular region is located near the N-terminus of the sequence and is the structure of the THAP domain. It spans amino acids 4-82.[37] The alpha helix is located from amino acids 186-230 and contains the host-cell factor 1C binding motif.[37]

Regulation

Localization

THAP3 can be localized in the nucleus or mitochondria of H. sapiens cells.[38]

Post-translation modifications

The H. sapiens the THAP3 protein has 30 predicted phosphorylation sites, 28 predicted O-β-glycosylation sites, and 11 predicted Yin-Yang sites.[35][36] Many proteins involved in transcription regulation are influenced by phosphorylation and glycosylation sites, which corroborates THAP3's function.[39]

Homology and evolution

Paralogs

The H. sapiens THAP3 protein, along with several other proteins, is part of the THAP family of proteins.[40] All of these proteins contain the THAP domain and are, thus, paralogs of H. sapiens THAP3.[15]

Paralogs of Homo sapiens THAP3 protein![7]Protein Name
E-Value![15]Percent Identity to THAP3[15]
THAP1[41] 8×10-23 48.00
THAP2[42] 6×10-17 45.24
THAP5[43] 4×10-13 31.96
THAP6[44] 6×10-6 34.44
THAP7[45] 1×10-7 33.33
THAP8[46] 8×10-11 31.96
THAP9[47] 2×10-8 32.99

Orthologs

Multiple sequence alignment of THAP domain in Homo sapiens THAP3 (HSa THAP3; accession number NP 001182681.1[12]) with distant orthologs.[48] Boxing represents the location of the THAP domain in H. sapiens. Bolding and asterisks below groups of sequence indicate that an amino acid is highly conserved at that position. Full sequences include that of Sumatra barb (PTe THAP3), Electric eel (EEl THAP3), Lake whitefish (CCL THAP3), Baby whale (BBr THAP3), Whale shark (ARa THAP3), White-spotted bamboo shark (RTy THAP3), and Thorny skate (CPl THAP3). Accession numbers as in ortholog table.

There are approximately 206 orthlologs of H. sapiens THAP3.[7] Orthologs can be found in a variety of taxomonic classes, including mammals, reptiles, amphibians, bony fishes, and cartilaginous fishes.[15] However, there are no orthologs in bacteria, fungi, protists, archaea, plants, invertebrates, or birds.[15] Additionally, not all orders are represented with in a class. For example, in reptiles, orthologs to H. sapiens THAP3 are found in testudines (turtles or tortoises) and not found in crocodilia (crocodiles and alligators) or squamata (lizards and snakes).[15] Similarly, there are only orthologs in apoda within amphibians.[15] There are no orthologs in anura (frogs) or urodela (salamanders).[15]

In closely related organisms, those diverged 0-160 million years ago (MYA), percent similarity of orthologs ranges from 36-82.9%. THAP3 sequences in rodents are the least conserved compared to H. sapiens. Sequences that diverged 319-353 MYA, those moderately related, have 47.2-68.9% similarity to H. sapiens THAP3, and 41.3-54.1% similarity in organisms that are distantly related, diverged 431-464 MYA.

Orthologs of Homo sapiens THAP3![49]Taxonomic Class
Scientific Name Common Name Taxonomic Order Date of Divergence![50]Accession Number![15]Percent Identity to THAP3![15]Percent Similarity to THAP3[51]
Mammals Marmota flaviventris Yellow-bellied marmot Rodentia 87 XP_027803226.1[52] 29.9 36
Lontra canadensis North American river otter Carnivora 94 XP_032719186.1[53] 59.5 65.8
Eptesicus fuscus Big brown bat Chiroptera 94 XP_028016747.1[54] 65.0 69.6
Balaenoptera musculus Blue whale Cetacea 94 XP_036686252.1[55] 77.5 82.9
Dromiciops gliroides Colocolo opossum Microbiotheria 160 XP_043850206.1[56] 64.6 74.5
Phascolarctos cinereus Koala Diprotodontia 160 XP_020830574.1[57] 65.7 76.4
Reptiles Caretta caretta Loggerhead turtle Testudines 319 XP_048680971.1[58] 36.9 47.2
Gopherus evgoodei Goode's thornscrub tortoise Testudines 319 XP_030393185.1[59] 48.9 58.1
Chelonoidis abingdonii Abingdon Island giant tortoise Testudines 319 XP_032619750.1[60] 48.9 61.4
Mauremys mutica Yellow pond turtle Testudines 319 XP_044852367.1[61] 49.0 60.9
Amphibians Microcaecilia unicolor Microcaecilia unicolor Gymnophiona 353 XP_030041702.1[62] 41.2 56.8
Geotrypetes seraphini Gaboon caecilian Gymnophiona 353 XP_033777236.1[63] 44.2 57.8
Bony Fishes Electrophorus electricus Electric eel Gymnotiformes 431 XP_026873261.2[64] 31.9 41.3
Coregonus clupeaformis Lake whitefish Salmoniformes 431 XP_041712304.2[65] 32.9 47.7
Brienomyrus brachyistius Baby whale Osteoglossiformes 431 XP_048872538.1[66] 33.5 46.3
Puntigrus tetrazona Sumatra barb Cypriniformes 431 XP_043081346.1[67] 34.0 48.1
Cartilaginous Fishes Rhincodon typus Whale shark Orectolobiformes 464 XP_020386430.1[68] 39.0 53.4
Chiloscyllium plagiosum White-spotted bamboo shark Orectolobiformes 464 XP_043531920.1[69] 39.0 53.0
Amblyraja radiata Thorny skate Rajiformes 464 XP_032904038.1[70] 40.2 54.1

Evolution

H. sapiens THAP3 has evolved at a rate similar to H. sapiens fibrinogen alpha, which is involved in the immune system.[15]

Protein interactions

H. sapiens THAP3 interacts with proteins involved in various cellular processes, like transcription regulation and neuronal development.[10] It is also interacts with molecular chaperones during its translation.

Homo sapiens THAP3 Protein Interactions![71]Process
Protein Name Identified By![72]Interaction Type
Transcription Regulation CHAT two hybrid assay Functional
FGFR3 two hybrid assay Functional
HCF1C[73] affinity capture - mass spectrometry Functional
OGT[73] affinity capture - mass spectrometry Functional
PKN1 two hybrid assay Functional
POLR2A two hybrid assay Functional
TARDBP two hybrid assay Functional
Neuronal Development LSAMP two hybrid assay Functional
DNAJB6 two hybrid assay Functional
Protein Folding BAG6 two hybrid assay Developmental

Clinical significance

THAP3 contributes to the presentation of X-linked Dystonia-Parkinsonism, also known as Lubag Syndrome.[74] This disease is a neurodegenerative movement disorder that predominantly affects males of Filipino descent.[75] Symptoms include tremors, bradykinesia, rigidity, postural instability, shuffling gait and dystonia, which typically develops later in life.[75]

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