THAP3

From Wikipedia, the free encyclopedia
THAP3
Identifiers
AliasesTHAP3, THAP domain containing 3
External IDsOMIM: 612532 MGI: 1917126 HomoloGene: 18413 GeneCards: THAP3
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[edit]

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[edit]

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[edit]

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[edit]

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[edit]

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[edit]

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[edit]

Localization[edit]

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

Post-translation modifications[edit]

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[edit]

Paralogs[edit]

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[edit]

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 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[edit]

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

Protein interactions[edit]

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[edit]

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]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000041988 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039759 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, et al. (August 2021). "Highly accurate protein structure prediction with AlphaFold". Nature. 596 (7873): 583–589. Bibcode:2021Natur.596..583J. doi:10.1038/s41586-021-03819-2. PMC 8371605. PMID 34265844.
  6. ^ a b Varadi M, Anyango S, Deshpande M, Nair S, Natassia C, Yordanova G, et al. (January 2022). "AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models". Nucleic Acids Research. 50 (D1): D439–D444. doi:10.1093/nar/gkab1061. PMC 8728224. PMID 34791371.
  7. ^ a b c d e f g h i j k l "THAP3 THAP domain containing 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-12-08.
  8. ^ Roussigne M, Kossida S, Lavigne AC, Clouaire T, Ecochard V, Glories A, et al. (February 2003). "The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase". Trends in Biochemical Sciences. 28 (2): 66–69. doi:10.1016/S0968-0004(02)00013-0. PMID 12575992.
  9. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 1, mRNA". 2022-04-22.
  10. ^ a b Sabogal A, Lyubimov AY, Corn JE, Berger JM, Rio DC (January 2010). "THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves". Nature Structural & Molecular Biology. 17 (1): 117–123. doi:10.1038/nsmb.1742. PMC 2933787. PMID 20010837.
  11. ^ a b "Entry - *612532 - THAP Doman-Containing Protein 3; THAP3 - OMIM". www.omim.org. Retrieved 2022-12-15.
  12. ^ a b "THAP domain-containing protein 3 isoform 1 [Homo sapiens] - Protein - NCBI". National Center of Biotechnology Information. Retrieved 2022-12-16.
  13. ^ a b Fagerberg L, Hallström BM, Oksvold P, Kampf C, Djureinovic D, Odeberg J, et al. (February 2014). "Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics". Molecular & Cellular Proteomics. 13 (2): 397–406. doi:10.1074/mcp.M113.035600. PMC 3916642. PMID 24309898.
  14. ^ Duff MO, Olson S, Wei X, Garrett SC, Osman A, Bolisetty M, et al. (May 2015). "Genome-wide identification of zero nucleotide recursive splicing in Drosophila". Nature. 521 (7552): 376–379. Bibcode:2015Natur.521..376D. doi:10.1038/nature14475. PMC 4529404. PMID 25970244.
  15. ^ a b c d e f g h i j k "Protein BLAST: search protein databases using a protein query". National Center of Biotechnology Information. Retrieved 2022-12-08.
  16. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 1, mRNA". April 22, 2022 – via NCBI Nucleotide.
  17. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 2, m - Nucleotide - NCBI". www.ncbi.nlm.nih.gov. 22 April 2022.
  18. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 3, m - Nucleotide - NCBI". www.ncbi.nlm.nih.gov. 10 June 2022.
  19. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 4, mRNA". April 22, 2022 – via NCBI Nucleotide.
  20. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 5, mRNA". April 22, 2022 – via NCBI Nucleotide.
  21. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 6, mRNA". April 22, 2022 – via NCBI Nucleotide.
  22. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 7, m - Nucleotide - NCBI". www.ncbi.nlm.nih.gov. 22 April 2022.
  23. ^ "Homo sapiens THAP domain containing 3 (THAP3), transcript variant 8, mRNA". April 22, 2022 – via NCBI Nucleotide.
  24. ^ a b Brendel V, Bucher P, Nourbakhsh IR, Blaisdell BE, Karlin S (March 1992). "Methods and algorithms for statistical analysis of protein sequences". Proceedings of the National Academy of Sciences of the United States of America. 89 (6): 2002–2006. Bibcode:1992PNAS...89.2002B. doi:10.1073/pnas.89.6.2002. PMC 48584. PMID 1549558.
  25. ^ 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).
  26. ^ "THAP domain-containing protein 3 isoform 1 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  27. ^ "THAP domain-containing protein 3 isoform 2 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  28. ^ "THAP domain-containing protein 3 isoform 3 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  29. ^ "THAP domain-containing protein 3 isoform 4 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  30. ^ "THAP domain-containing protein 3 isoform 5 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  31. ^ "THAP domain-containing protein 3 isoform 6 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  32. ^ "THAP domain-containing protein 3 isoform 7 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  33. ^ "THAP domain-containing protein 3 isoform 8 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  34. ^ Liu W, Xie Y, Ma J, Luo X, Nie P, Zuo Z, et al. (October 2015). "IBS: an illustrator for the presentation and visualization of biological sequences". Bioinformatics. 31 (20): 3359–3361. doi:10.1093/bioinformatics/btv362. PMC 4595897. PMID 26069263.
  35. ^ a b c Gupta, R. (2001). Prediction of glycosylation sites in proteomes: from post-translational modifications to protein function. Technical University of Denmark.
  36. ^ a b Blom N, Gammeltoft S, Brunak S (December 1999). "Sequence and structure-based prediction of eukaryotic protein phosphorylation sites". Journal of Molecular Biology. 294 (5): 1351–1362. doi:10.1006/jmbi.1999.3310. PMID 10600390.
  37. ^ a b Wang J, Youkharibache P, Marchler-Bauer A, Lanczycki C, Zhang D, Lu S, et al. (2022). "iCn3D: From Web-Based 3D Viewer to Structural Analysis Tool in Batch Mode". Frontiers in Molecular Biosciences. 9: 831740. doi:10.3389/fmolb.2022.831740. PMC 8892267. PMID 35252351.
  38. ^ "PSORT II Prediction". psort.hgc.jp. Retrieved 2022-12-16.
  39. ^ Filtz TM, Vogel WK, Leid M (February 2014). "Regulation of transcription factor activity by interconnected post-translational modifications". Trends in Pharmacological Sciences. 35 (2): 76–85. doi:10.1016/j.tips.2013.11.005. PMC 3954851. PMID 24388790.
  40. ^ Sanghavi HM, Mallajosyula SS, Majumdar S (March 2019). "Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region". BMC Structural Biology. 19 (1): 4. doi:10.1186/s12900-019-0102-2. PMC 6402169. PMID 30836974.
  41. ^ "THAP1 THAP domain containing 1 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  42. ^ "THAP2 THAP domain containing 2 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  43. ^ "THAP5 THAP domain containing 5 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  44. ^ "THAP6 THAP domain containing 6 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  45. ^ "THAP7 THAP domain containing 7 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  46. ^ "THAP8 THAP domain containing 8 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  47. ^ "THAP9 THAP domain containing 9 [Homo sapiens (human)] - Gene - NCBI". National Center of Biotechnology Information.
  48. ^ Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, Li W, et al. (October 2011). "Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega". Molecular Systems Biology. 7 (1): 539. doi:10.1038/msb.2011.75. PMC 3261699. PMID 21988835.
  49. ^ "THAP domain-containing protein 3 isoform 1 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-12-08.
  50. ^ Kumar S, Suleski M, Craig JM, Kasprowicz AE, Sanderford M, Li M, et al. (August 2022). "TimeTree 5: An Expanded Resource for Species Divergence Times". Molecular Biology and Evolution. 39 (8): msac174. doi:10.1093/molbev/msac174. PMC 9400175. PMID 35932227.
  51. ^ "EMBOSS Needle < Pairwise Sequence Alignment < EMBL-EBI". www.ebi.ac.uk. Retrieved 2022-12-08.
  52. ^ "THAP domain-containing protein 3 isoform X1 [Marmota flaviventris] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  53. ^ "THAP domain-containing protein 3 isoform X1 [Lontra canadensis] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  54. ^ "THAP domain-containing protein 3 isoform X1 [Eptesicus fuscus] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  55. ^ "THAP domain-containing protein 3 isoform X1 [Balaenoptera musculus] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  56. ^ "THAP domain-containing protein 3 isoform X1 [Dromiciops gliroides] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  57. ^ "THAP domain-containing protein 3 isoform X1 [Phascolarctos cinereus] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  58. ^ "THAP domain-containing protein 3 isoform X1 [Caretta caretta] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  59. ^ "THAP domain-containing protein 3 isoform X1 [Gopherus evgoodei] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  60. ^ "THAP domain-containing protein 3 isoform X1 [Chelonoidis abingdonii] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  61. ^ "THAP domain-containing protein 3 isoform X1 [Mauremys mutica] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  62. ^ "THAP domain-containing protein 3 isoform X1 [Microcaecilia unicolor] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  63. ^ "THAP domain-containing protein 3 isoform X1 [Geotrypetes seraphini] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  64. ^ "THAP domain-containing protein 3 isoform X1 [Electrophorus electricus] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  65. ^ "THAP domain-containing protein 3 isoform X1 [Coregonus clupeaformis] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  66. ^ "THAP domain-containing protein 3 isoform X1 [Brienomyrus brachyistius] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  67. ^ "THAP domain-containing protein 3 isoform X1 [Puntigrus tetrazona] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  68. ^ "THAP domain-containing protein 3 isoform X1 [Rhincodon typus] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  69. ^ "THAP domain-containing protein 3 isoform X1 [Chiloscyllium plagiosum] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  70. ^ "THAP domain-containing protein 3 isoform X1 [Amblyraja radiata] - Protein - NCBI". www.ncbi.nlm.nih.gov.
  71. ^ "UniProt". www.uniprot.org. Retrieved 2022-12-16.
  72. ^ "IntAct Portal". www.ebi.ac.uk. Retrieved 2022-12-16.
  73. ^ a b "THAP3 Result Summary | BioGRID". thebiogrid.org. Retrieved 2022-12-16.
  74. ^ "THAP3 Gene - GeneCards | THAP3 Protein | THAP3 Antibody". www.genecards.org. Retrieved 2022-12-08.
  75. ^ a b Rosales RL (October 2010). "X-linked dystonia parkinsonism: clinical phenotype, genetics and therapeutics". Journal of Movement Disorders. 3 (2): 32–38. doi:10.14802/jmd.10009. PMC 4027667. PMID 24868378.
Retrieved from "https://en.wikipedia.org/w/index.php?title=THAP3&oldid=1222544732"