TMEM128

Last updated

TMEM128
Identifiers
Aliases TMEM128 , transmembrane protein 128
External IDs MGI: 1913559; HomoloGene: 11944; GeneCards: TMEM128; OMA:TMEM128 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

85013

66309

Ensembl

ENSG00000132406

ENSMUSG00000067365

UniProt

Q5BJH2

Q9CZB9

RefSeq (mRNA)

NM_001297551
NM_001297552
NM_032927

NM_025480
NM_001356960

RefSeq (protein)

NP_001284480
NP_001284481
NP_116316

NP_079756
NP_001343889

Location (UCSC) Chr 4: 4.24 – 4.25 Mb Chr 5: 38.42 – 38.43 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

TMEM128, also known as Transmembrane Protein 128, is a protein that in humans is encoded by the TMEM128 gene. TMEM128 has three variants, varying in 5' UTR's and start codon location. [5] TMEM128 contains four transmembrane domains and is localized in the Endoplasmic Reticulum membrane. [6] [7] [8] TMEM128 contains a variety of regulation at the gene, transcript, and protein level. While the function of TMEM128 is poorly understood, it interacts with several proteins associated with the cell cycle, signal transduction, and memory.

Contents

Gene

The TMEM128, or transmembrane protein 128, gene in humans is located on the minus strand at 4p16.3. [9] TMEM128 contains 5 exons total and is 12,701 base pairs long including introns. [5] [9] [10]

Transcripts

There are two isoforms of TMEM128. [11] Isoform 1 being the longest, consists of two variants differing in the 3' UTR region. [11] Variant 1 mRNA is 1,243 base pairs long while Variant 2 mRNA is 1,241 base pairs long. [5] [12] Isoform 2 differs in the 5' UTR region of the protein and uses a different start codon location compared to the first variant. [11] This variant is longer at 1,785 base pairs and has a different N-terminus. [13]

Neighboring genes

TMEM128 is neighbored upstream by LYAR , Ly1 antibody reactive, and downstream by OTOP1, Otopetrin 1. [14]

Protein

Isoform 1

TMEM128 Isoform 1 translates into a protein of 165 amino acids long, containing four transmembrane domains. [6] These domains exist at amino acids 49-69, 81-101, 119-139, and 144-164. [6] Isoform 1 is18,882 Da and has a pI of 6.27. [15] Using compositional analysis, the amino acid composition is similar to the average protein and there are no significant repeats in the protein. [15]

Predicted Secondary Structure for TMEM128 TMEM128 membrane domains.png
Predicted Secondary Structure for TMEM128

Isoform 2

Isoform 2 translates into a protein of 141 amino acids long, also containing four transmembrane domains. [17] [18] Isoform 2 has a different molecular weight and isoelectric point compared to Isoform 1, coming in at 16,093 Da and having a pI of 6.8. [15]

Secondary structure

Secondary structure composition
Type of secondary structureNumber of amino acidsPercent composition
Alpha helix 3420.61%
Extended strand5935.76%
Random coil 7243.64%

Predicted secondary structure composition shows that most of the secondary structure consists of random coils. [19] No disulfide bonds are predicted to be present. [20]

Membrane topology of TMEM128 shows the four transmembrane domains, longer N-terminus, and shorter C terminus.

Tertiary structure

Predicted Tertiary Structure of TMEM128 as predicted by I-TASSER Tertiary Structure of TMEM128.jpg
Predicted Tertiary Structure of TMEM128 as predicted by I-TASSER
Predicted 3-D structure of TMEM128 as predicted by PHYRE2 TMEM128.png
Predicted 3-D structure of TMEM128 as predicted by PHYRE2

Tertiary structure is predicted to have four spiral domains in TMEM128. These domains are the transmembrane sections of the protein. For the above models, it is colored rainbow from N-terminus to C-terminus.

Regulation of expression

Gene level regulation

TMEM128 mRNA expression by tissue type in humans NCBI GEO TMEM128 Differential Expression by Tissue.png
TMEM128 mRNA expression by tissue type in humans

Several promotors/enhancers of TMEM128 exist, with the GH04J00427 promotor located near the start of transcription, the GH04J004540 enhancer located downstream, and GH04J004264 enhancer located upstream of their target gene. [9] [14] TMEM128 sequence also contains many binding sites for various transcription factors, including TATA box, CCAAT binding protein, and cAMP-responsive element binding protein. [23]

Expression of TMEM128 is also regulated at the gene level through differential tissue expression as seen with the image to the left. Red bars represent absolute expression while blue dots represent relative expression. TMEM128 is expressed highly in areas such as the adrenal gland and spinal cord, while is lower in areas such as the liver and bone marrow. [11]

Transcript level regulation

Predicted stem loops for 3' UTR of TMEM128 Secondary structure for 3' UTR of TMEM128.png
Predicted stem loops for 3' UTR of TMEM128
TMEM128 RNA expression in a mouse brain RNA Expression of TMEM128 in a mouse brain.png
TMEM128 RNA expression in a mouse brain

Several miRNAs have binding sites on the 3' UTR of TMEM128 including: [26]

These miRNAs can participate in RNA silencing to prevent the expression of the mRNA.

Analyses of mouse brains show lack of region-specific expression throughout. [25]

Protein level regulation

In terms of protein regulation, TMEM128 contains many different post-translational domains including glycation, [27] phosphorylation, [28] SUMOylation, [29] and O-GlcNAc [30] as seen below:

ModificationAmino acid number
Phosphorylation3, 4, 52, 124, 135, 162
Glycation70, 73, 115
Nuclear export signal [31] 88-95
SUMOylation39-42, 115-118, 161-165
O-GlcNAc3, 4, 34, 35, 123
Acetylation [32] 40, 41, 43, 73

Post-translational modification alters protein structure and can thus alter protein function and viability.

Sub-cellular localization

TMEM128 was found to be located in the Endoplasmic Reticulum membrane, with the N-terminus and C-terminus facing into the cytoplasm. [7] [8]

Evolution

Paralogs

There are no known paralogs of TMEM128. [33]

Orthologs

Orthologs of TMEM128 have not been found outside of Eukaryotes. [33] Inside of Eukaryotes, TMEM128 orthologs have been found in mammals, birds, and several fungi. Mammals contained the highest amount of conservation at no less than 71% conservation. The most distant ortholog detected was the Diversispora epigaea, a fungus. The transmembrane domains of this protein remain the most conserved throughout species, with key amino acids Trp51, Trp139, and Trp142 being conserved in all species with orthologous proteins. All information below was obtained through NCBI BLAST. [33]

Orthologs of TMEM128
Genus and SpeciesCommon NameDate of Divergence (MYA) [34] Accession numberSequence lengthSequence identity
Homo sapiens Human0NP_001284480.1165100%
Rhinopithecus roxellana Golden snub-nosed monkey28.81XP_010355887.216597%
Mus musculus House mouse89NP_001343889.116381%
Microtus ochrogaster Prairie vole89XP_00536602116480%
Ovis aries Sheep94XP_014952114.216583%
Vulpes vulpes Red fox94XP_025854088.116582%
Pteropus vampyrus Large flying fox94XP_011372965.116581%
Orcinus orca Killer whale94XP_004269680.116581%
Monodelphis domestica Gray short-tailed opossum160XP_001371407.317071%
Taeniopygia guttata Zebra finch318XP_002193492.317368%
Alligator sinensis Chinese alligator318XP_006016834.117267%
Pogona vitticeps Central bearded dragon318XP_020633929.116362%
Xenopus laevis African clawed frog351.7NP_001084889.116652%
Orbicella faveolata Mountainous star coral687XP_020610022.117138%
Exaiptasia pallida Sea anenmone687XP_028518835.116936%
Octopus vulgaris Common octopus736XP_029645279.118433%
Brachionus plicatilis N/A736RNA25638.117028%
Crassostrea virginica Eastern oyster736XP_022343076.120028%
Diversispora epigaea N/A1017RHZ70611.117624%

Mutation rate

Divergence of TMEM128 Relative to Fibrinogen Alpha Chain and Cytochrome C Divergence of TMEM128.jpg
Divergence of TMEM128 Relative to Fibrinogen Alpha Chain and Cytochrome C

The evolution rate is at a medium pace, slower than the fibrinogen alpha chain but faster than cytochrome c, suggesting neither positive or negative selection at this locus.

Interacting proteins

TMEM128 has been found via yeast two-hybrid assays to interact with:

Function

The biological function of TMEM128 is still poorly understood. As this is a transmembrane protein, common functions may include receptors, channels, or anchorage. [40] Because TMEM128 has post-translational modification sites, alternative protein states may be present that permit TMEM128 to have different forms. For example, phosphorylation of TMEM128 may make it bind to different substrates through conformational change. [41] TMEM128 also has a variety of interactions with other proteins as discussed above, suggesting it may have a broad range of action.

Clinical significance

Cancer

TMEM128 has been found to show moderate to strong positivity in some patients with carcinoma, with other types of cancer such as melanoma, glioma, breast, ovarian, renal, and pancreatic showing weak to moderate positivity. [42] TMEM128 also has been found to show low cancer specificity. [42]

Skeletal muscle

TMEM128 expression is experimentally associated with presence of the ROR alpha1 protein, as TMEM128 was found in lower quantities when ROR alpha1 was deleted. [43] [44]

Skin

TMEM128 expression was lowered following a null mutation of TAp63 in skin cells. [45] [46]

Cardiac muscle

TMEM128 expression was increased following a Trypanosoma cruzi infection. [47] [48]

Neurological diseases

While it has been associated with several diseases such as Wolf-Hirschhorn Syndrome, no evidence exists for the exact cause of this syndrome and may only be correlation because of location on chromosome 4 [9] [49]

Mutations

Several SNPs have been found in association with TMEM128: [50]

Key SNPs of TMEM128
mRNA positionAmino acid positiondbSNP rs#Reference alleleSNP alleleFunction
16943rs771177507ACMissense
18649rs146625911ACMissense
20455rs1434953873GTMissense
27077rs13135886AGMissense
463139rs757745482TCMissense
466142rs1213450146GANonsense
512158rs202215273GA, TMissense

Related Research Articles

Transmembrane protein 241 is a ubiquitous sugar transporter protein which in humans is encoded by the TMEM241 gene.

The coiled-coil domain containing 142 (CCDC142) is a gene which in humans encodes the CCDC142 protein. The CCDC142 gene is located on chromosome 2, spans 4339 base pairs and contains 9 exons. The gene codes for the coiled-coil domain containing protein 142 (CCDC142), whose function is not yet well understood. There are two known isoforms of CCDC142. CCDC142 proteins produced from these transcripts range in size from 743 to 665 amino acids and contain signals suggesting protein movement between the cytosol and nucleus. Homologous CCDC142 genes are found in many animals including vertebrates and invertebrates but not fungus, plants, protists, archea, or bacteria. Although the function of this protein is not well understood, it contains a coiled-coil domain and a RINT1_TIP1 motif located within the coiled-coil domain.

BEND2 is a protein that in humans is encoded by the BEND2 gene. It is also found in other vertebrates, including mammals, birds, and reptiles. The expression of BEND2 in Homo sapiens is regulated and occurs at high levels in the skeletal muscle tissue of the male testis and in the bone marrow. The presence of the BEN domains in the BEND2 protein indicates that this protein may be involved in chromatin modification and regulation.

<span class="mw-page-title-main">TMEM44</span> Protein-coding gene in the species Homo sapiens

TMEM44 is a protein that in humans is encoded by the TMEM44 gene. DKFZp686O18124 is a synonym of TMEM44.

<span class="mw-page-title-main">C7orf50</span> Mammalian protein found in Homo sapiens

C7orf50 is a gene in humans that encodes a protein known as C7orf50. This gene is ubiquitously expressed in the kidneys, brain, fat, prostate, spleen, among 22 other tissues and demonstrates low tissue specificity. C7orf50 is conserved in chimpanzees, Rhesus monkeys, dogs, cows, mice, rats, and chickens, along with 307 other organisms from mammals to fungi. This protein is predicted to be involved with the import of ribosomal proteins into the nucleus to be assembled into ribosomal subunits as a part of rRNA processing. Additionally, this gene is predicted to be a microRNA (miRNA) protein coding host gene, meaning that it may contain miRNA genes in its introns and/or exons.

<span class="mw-page-title-main">C17orf78</span> Mammalian protein found in Homo sapiens

Uncharacterized protein C17orf78 is a protein encoded by the C17orf78 gene in humans. The name denotes the location of the parent gene, being at the 78th open reading frame, on the 17th human chromosome. The protein is highly expressed in the small intestine, especially the duodenum. The function of C17orf78 is not well defined.

<span class="mw-page-title-main">LSMEM2</span> Protein-coding gene in the species Homo sapiens

Leucine rich single-pass membrane protein 2 is a single-pass membrane protein rich in leucine, that in humans is encoded by the LSMEM2 gene. The LSMEM2 protein is conserved in mammals, birds, and reptiles. In humans, LSMEM2 is found to be highly expressed in the heart, skeletal muscle and tongue.

TMEM275 is a protein that in humans is encoded by the TMEM275 gene. TMEM275 has two, highly-conserved, helical trans-membrane regions. It is predicted to reside within the plasma membrane or the endoplasmic reticulum's membrane.

C2orf74, also known as LOC339804, is a protein encoding gene located on the short arm of chromosome 2 near position 15 (2p15). Isoform 1 of the gene is 19,713 base pairs long. C2orf74 has orthologs in 135 different species, including primarily placental mammals and some marsupials.

<span class="mw-page-title-main">SMIM19</span> Protein-coding gene in the species Homo sapiens

SMIM19, also known as Small Integral Membrane Protein 19, encodes the SMIM19 protein. SMIM19 is a confirmed single-pass transmembrane protein passing from outside to inside, 5' to 3' respectively. SMIM19 has ubiquitously high to medium expression with among varied tissues or organs. The validated function of SMIM19 remains under review because of on sub-cellular localization uncertainty. However, all linked proteins research to interact with SMIM19 are associated with the endoplasmic reticulum (ER), presuming SMIM19 ER association

<span class="mw-page-title-main">FAM214B</span> Protein-coding gene in the species Homo sapiens

The FAM214B, also known as protein family with sequence similarity 214, B (FAM214B) is a protein that, in humans, is encoded by the FAM214B gene located on the human chromosome 9. The protein has 538 amino acids. The gene contain 9 exon. There has been studies that there are low expression of this gene in patients with major depression disorder. In most organisms such as mammals, amphibians, reptiles, and birds, there are high levels of gene expression in the bone marrow and blood. For humans in fetal development, FAM214B is mostly expressed in the brains and bone marrow.

<span class="mw-page-title-main">C6orf136</span> Protein-coding gene in the species Homo sapiens

C6orf136 is a protein in humans encoded by the C6orf136 gene. The gene is conserved in mammals, mollusks, as well some porifera. While the function of the gene is currently unknown, C6orf136 has been shown to be hypermethylated in response to FOXM1 expression in Head Neck Squamous Cell Carcinoma (HNSCC) tissue cells. Additionally, elevated expression of C6orf136 has been associated with improved survival rates in patients with bladder cancer. C6orf136 has three known isoforms.

<span class="mw-page-title-main">FAM120AOS</span> Protein-coding gene in the species Homo sapiens

FAM120AOS, or family with sequence similarity 120A opposite strand, codes for uncharacterized protein FAM120AOS, which currently has no known function. The gene ontology describes the gene to be protein binding. Overall, it appears that the thyroid and the placenta are the two tissues with the highest expression levels of FAM120AOS across a majority of datasets.

<span class="mw-page-title-main">FAM166C</span>

Family with Sequence Similarity 166, member C (FAM166C), is a protein encoded by the FAM166C gene. The protein FAM166C is localized in the nucleus. It has a calculated molecular weight of 23.29 kDa. It also contains DUF2475, a protein of unknown function from amino acid 19–85. The FAM166C protein is nominally expressed in the testis, stomach, and thyroid.

<span class="mw-page-title-main">TBC1D30</span> Protein-coding gene in the species Homo sapiens

TBC1D30 is a gene in the human genome that encodes the protein of the same name. This protein has two domains, one of which is involved in the processing of the Rab protein. Much of the function of this gene is not yet known, but it is expressed mostly in the brain and adrenal cortex.

<span class="mw-page-title-main">TMEM212</span> Protein-coding gene in the species Homo sapiens

Transmembrane protein 212 is a protein that in humans is encoded by the TMEM212 gene. The protein consists of five transmembrane domains and localizes in the plasma membrane and endoplasmic reticulum. TMEM212 has orthologs in vertebrates but not invertebrates. TMEM212 has been associated with sporadic Parkinson's disease, facial processing, and adiposity in African Americans.

<span class="mw-page-title-main">C5orf22</span> Protein-coding gene in the species Homo sapiens

Chromosome 5 open reading frame 22 (c5orf22) is a protein-coding gene of poorly characterized function in Homo sapiens. The primary alias is unknown protein family 0489 (UPF0489).

<span class="mw-page-title-main">KIAA2013</span> Protein-coding gene in the species Homo sapiens

KIAA2013, also known as Q8IYS2 or MGC33867, is a single-pass transmembrane protein encoded by the KIAA2013 gene in humans. The complete function of KIAA2013 has not yet been fully elucidated.

<span class="mw-page-title-main">THAP3</span> Protein in Humans

THAP domain-containing protein 3 (THAP3) is a protein that, in Homo sapiens (humans), is encoded by the THAP3 gene. 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 and a host-cell factor 1C binding motif. These domains allow THAP3 to influence a variety of processes, including transcription and neuronal development. THAP3 is ubiquitously expressed in H. sapiens, though expression is highest in the kidneys.

<span class="mw-page-title-main">C13orf46</span> C13of46 Gene and Protein

Chromosome 13 Open Reading Frame 46 is a protein which in humans is encoded by the C13orf46 gene. In humans, C13orf46 is ubiquitously expressed at low levels in tissues, including the lungs, stomach, prostate, spleen, and thymus. This gene encodes eight alternatively spliced mRNA transcript, which produce five different protein isoforms.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000132406 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000067365 – 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. 1 2 3 "Transmembrane Protein 128, transcript variant 1, mRNA". NCBI. March 1, 2020.
  6. 1 2 3 "transmembrane protein 128 isoform 1 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved April 29, 2020.
  7. 1 2 3 Gutzmann J (2013). "Characterization of Tmem128 – An activity regulated ER protein, interacting with the immediate early gene Arc/Arg3.1". Refubium. doi:10.17169/refubium-14701.
  8. 1 2 "PSORT II Prediction". psort.hgc.jp. Retrieved May 1, 2020.
  9. 1 2 3 4 "TMEM128 Gene - GeneCards | TM128 Protein | TM128 Antibody". www.genecards.org. Retrieved February 7, 2020.
  10. ↑ "Homo sapiens chromosome 4, GRCh38.p13 Primary Assembly". March 2, 2020.
  11. 1 2 3 4 "TMEM128 transmembrane protein 128 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved April 29, 2020.
  12. ↑ "Homo sapiens transmembrane protein 128 (TMEM128), transcript variant 2, mRNA". May 31, 2019.{{cite journal}}: Cite journal requires |journal= (help)
  13. ↑ "Homo sapiens transmembrane protein 128 (TMEM128), transcript variant 3, mRNA". August 3, 2019.
  14. 1 2 "Human hg38 chr4:4,235,542-4,248,223 UCSC Genome Browser v397". genome.ucsc.edu. Retrieved April 30, 2020.
  15. 1 2 3 "SAPS < Sequence Statistics < EMBL-EBI". www.ebi.ac.uk. Retrieved April 29, 2020.
  16. ↑ "Protter - interactive protein feature visualization". wlab.ethz.ch. Retrieved May 2, 2020.
  17. ↑ "Phobius". phobius.sbc.su.se. Retrieved April 29, 2020.
  18. ↑ "transmembrane protein 128 isoform 2 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved April 29, 2020.
  19. ↑ "NPS@ : GOR4 secondary structure prediction". npsa-prabi.ibcp.fr. Retrieved May 2, 2020.
  20. ↑ "DISULFIND - Cysteines Disulfide Bonding State and Connectivity Predictor". disulfind.dsi.unifi.it. Retrieved April 30, 2020.
  21. ↑ "I-TASSER server for protein structure and function prediction". zhanglab.ccmb.med.umich.edu. Retrieved May 2, 2020.
  22. ↑ "PHYRE2 Protein Fold Recognition Server". www.sbg.bio.ic.ac.uk. Retrieved May 2, 2020.
  23. ↑ "Transcription factor binding sites for GXP_149843".
  24. ↑ "miRDB - MicroRNA Target Prediction Database". www.mirdb.org. Retrieved May 3, 2020.
  25. 1 2 "Experiment Detail :: Allen Brain Atlas: Mouse Brain". mouse.brain-map.org. Retrieved May 3, 2020.
  26. ↑ "miRDB - MicroRNA Target Prediction Database". www.mirdb.org. Retrieved May 2, 2020.
  27. ↑ "NetGlycate 1.0 server predication of glycation".
  28. ↑ "Kinase binding site prediction for TMEM128". The CUCKOO Workgroup.
  29. ↑ "SUMOplot Analysis Program Results for TMEM128".
  30. ↑ "YinOYand 1.2 prediction of O-GlcNAc sites for TMEM128".
  31. ↑ "NetNES 1.1 Server". www.cbs.dtu.dk. Retrieved May 1, 2020.
  32. ↑ ":::PAIL - Prediction of Acetylation on Internal Lysines:::". bdmpail.biocuckoo.org. Retrieved May 3, 2020.
  33. 1 2 3 "BLAST: Basic Local Alignment Search Tool". blast.ncbi.nlm.nih.gov. Retrieved April 30, 2020.
  34. ↑ "TimeTree :: The Timescale of Life". www.timetree.org. Retrieved May 2, 2020.
  35. ↑ Grossmann A, Benlasfer N, Birth P, Hegele A, Wachsmuth F, Apelt L, Stelzl U (March 2015). "Phospho-tyrosine dependent protein-protein interaction network". Molecular Systems Biology. 11 (3): 794. doi:10.15252/msb.20145968. PMC   4380928 . PMID   25814554.
  36. ↑ Rolland T, Taşan M, Charloteaux B, Pevzner SJ, Zhong Q, Sahni N, et al. (November 2014). "A proteome-scale map of the human interactome network". Cell. 159 (5): 1212–1226. doi:10.1016/j.cell.2014.10.050. PMC   4266588 . PMID   25416956.
  37. ↑ Passantino R, Cascio C, Deidda I, Galizzi G, Russo D, Spedale G, Guarneri P (March 2013). "Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1833 (3): 529–40. doi: 10.1016/j.bbamcr.2012.10.030 . PMID   23142642.
  38. ↑ Huttlin EL, Bruckner RJ, Paulo JA, Cannon JR, Ting L, Baltier K, et al. (May 2017). "Architecture of the human interactome defines protein communities and disease networks". Nature. 545 (7655): 505–509. Bibcode:2017Natur.545..505H. doi:10.1038/nature22366. PMC   5531611 . PMID   28514442.
  39. 1 2 Luck K, Kim DK, Lambourne L, Spirohn K, Begg BE, Bian W, et al. (April 2020). "A reference map of the human binary protein interactome". Nature. 580 (7803): 402–408. Bibcode:2020Natur.580..402L. doi:10.1038/s41586-020-2188-x. PMC   7169983 . PMID   32296183.
  40. ↑ "Membrane Proteins | BioNinja". ib.bioninja.com.au. Retrieved February 7, 2020.
  41. ↑ "Phosphorylation - US". www.thermofisher.com. Retrieved May 2, 2020.
  42. 1 2 "Expression of TMEM128 in cancer - Summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved May 2, 2020.
  43. ↑ "GDS3720 / ILMN_1248235". www.ncbi.nlm.nih.gov. Retrieved May 2, 2020.
  44. ↑ Raichur S, Fitzsimmons RL, Myers SA, Pearen MA, Lau P, Eriksson N, et al. (July 2010). "Identification and validation of the pathways and functions regulated by the orphan nuclear receptor, ROR alpha1, in skeletal muscle". Nucleic Acids Research. 38 (13): 4296–312. doi:10.1093/nar/gkq180. PMC   2910057 . PMID   20338882.
  45. ↑ "GDS1435 / 107124_at". www.ncbi.nlm.nih.gov. Retrieved May 2, 2020.
  46. ↑ Koster MI, Kim S, Huang J, Williams T, Roop DR (January 2006). "TAp63alpha induces AP-2gamma as an early event in epidermal morphogenesis". Developmental Biology. 289 (1): 253–61. doi:10.1016/j.ydbio.2005.10.041. PMID   16324689.
  47. ↑ "GDS5112 / 1448317_at". www.ncbi.nlm.nih.gov. Retrieved May 2, 2020.
  48. ↑ Silva GK, Costa RS, Silveira TN, Caetano BC, Horta CV, Gutierrez FR, et al. (September 2013). "Apoptosis-associated speck-like protein containing a caspase recruitment domain inflammasomes mediate IL-1β response and host resistance to Trypanosoma cruzi infection". Journal of Immunology. 191 (6): 3373–83. doi: 10.4049/jimmunol.1203293 . PMID   23966627. S2CID   25181644.
  49. ↑ Yang WX, Pan H, Li L, Wu HR, Wang ST, Bao XH, et al. (March 2016). "Analyses of Genotypes and Phenotypes of Ten Chinese Patients with Wolf-Hirschhorn Syndrome by Multiplex Ligation-dependent Probe Amplification and Array Comparative Genomic Hybridization". Chinese Medical Journal. 129 (6): 672–8. doi: 10.4103/0366-6999.177996 . PMC   4804413 . PMID   26960370.
  50. ↑ "SNP linked to Gene (geneID:85013) Via Contig Annotation". www.ncbi.nlm.nih.gov. Retrieved May 2, 2020.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.