Biology:Zinc finger protein 226

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Short description: Protein found in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example
Figure 1. Bird's Eye View of the ZNF226 Transcript and Promoters
Figure 2. Human ZNF226 5’ UTR Secondary Structure
Figure 3. Human ZNF226 3' UTR Secondary Structure
Figure 4. A multiple sequence alignment of human ZNF226 and ortholog species with selected regions highlighted.

Zinc finger protein 226 is a protein that in humans is encoded by the ZNF226 gene.[1]

Gene

The zinc finger protein 226 is also known as the Kruppel-associated box protein.[2] Within humans, the ZNF226 gene is found on the plus strand of chromosome19q13, spanning 13,311 nucleotides from 44,165,070 to 44,178,381.[1]

Transcript

Currently, there are 20 different transcript variants encoding ZNF226.[1] All of them have six or seven identified exon regions within ZNF226.[3] The longest identified transcript, ZNF226 transcript variant x4 spans 2,797 base pairs (bp).[3]

Protein

ZNF226 is currently known to have three isoforms within humans: ZNF226 isoform X1, ZNF226 isoform X2, and ZNF226 isoform X3.[1] The ZNF226 isoform X1 protein is the longest known variant, with 803 amino acids.[1] This protein contains the Kruppel associated box A (KRAB-A) domain, which functions as a transcriptional repressor.[4] However, the exact function of the ZNF226 protein is currently unknown. Within isoform X1, there are 18 C2H2 zinc finger structural motif (zf-C2H2) domains, which are known to bind either zinc ions (Zn2+) or nucleic acid (Figure 7–8).[5][6] Within those regions, cysteine and histidine are the primary amino acids that bind to Zn2+ or nucleic acid, although other amino acids have been identified for binding (Figure 7–8). In addition to the KRAB-A domain and zf-C2H2 domains, there are zinc finger double domains which also contain binding sites for ions or nucleic acids.[3]

ZNF226 human and ortholog protein sequences have molecular weights between 89 and 92 kDa.[7] They had isoelectric points (pI) ranging from 8.60 to 9.00.[7] In humans, the zf-C2H2 and zinc finger double domain region of ZNF226 isoform X1 is 59.3 kDa with a theoretical pI of 9.11.[7] With the spacing of cysteine, or C, there is a cysteine every three amino acids. At least one of the amino acids in between the C's are either aspartic acid or glutamic acid.[8] Despite the region's patterns of aspartic acid, it is still considered to have a lesser amount of the amino acid at 1.9%.[8] There is also repetition within the chemical patterns within humans that is characteristic of ZNF226.[8] These repetitions appear most common within the zf-C2H2 and zinc finger double domains of the protein, notably with cysteine and histidine binding sites.[8] Predicted secondary structures of ZNF226 demonstrate a variable number of alpha helices, beta-stranded bridges, and random coils throughout the protein. Using various programs, such as GOR4 and the Chou and Fasman program, there is overall similarity in the predictions of coiled, stranded, and helix regions throughout the protein.[9][10][11]

Regulation

Gene

Promoter

Using the Genomatix software, GXP_7536741 (1142 bp) was identified as the best promoter of ZNF226 (Figure 1).[12] Within the last 500 bp of the promoter, the signal transducer and activator of transcription (V$STAT.01), selenocysteine tRNA activating factor (V$THAP11.01), and cell cycle regulators: cell cycle homology region (V$CHR.01) were conserved among Homo sapiens, Macaca mulatta, Pan troglodytes, and Canis lupus familiaris.[12] In addition, the SPI-1 proto-oncogene; hematopoietic TF PU.1 (V$SPI1.02) was also known for binding to a promoter region within the c-fes proto-oncogene which encodes tyrosine kinase.[13] The TF binding site is also found in two regions within the promoter sequence. The signal transducer and activator of transcription binding site was also conserved in two regions, and is known to have a higher binding specificity.[14] The selenocysteine tRNA activating factor plays a role in embryonic stem cell regeneration.[15] The cell cycle regulators: cell cycle homology region binding site plays an important role in cell survival, where mutations in the transcription factor can lead to apoptosis.[16]

Figure 5. A multiple sequence alignment of human ZNF226 and ortholog species with selected regions highlighted.

thumb|Figure 6. The ZNF226 evolutionary rate in comparison to the cytochrome c and fibrinogen alpha chain proteins|318x318px

Figure 7. ZNF226 zf-C2H2 structural domains highlighted on the conceptual translation
Figure 8. ZNF226 zf-C2H2 structural domains highlighted on the conceptual translation
Figure 9. Sequence logo of ZNF226 zf-C2H2 structural domain DNA binding sites

Tissue distribution

In terms of gene expression, ZNF226 is generally expressed in most tissues.[1] Microarray data illustrates higher expression of ZNF226 within the ovaries.[17] This is further supported by data which depicts a decrease in ZNF226 expression in granulosa cells within individuals with polycystic ovary syndrome.[18] There was also higher expressions of ZNF226 observed within the thyroid compared to other tissues.[1] Evidence of decreased ZNF226 expression is observed with individuals with papillary thyroid cancer.[19]

Within fetuses, there is some level of ZNF226 expression present within all tissues throughout the gestational period of 10 to 20 weeks.[1] However, there is a higher level of ZNF226 expression in the heart at 10 weeks of gestation, and a decreased level of expression within kidneys at 20 weeks gestation.[1]

ZNF226 expression has been observed within epithelial progenitor cells (EPCs) in the peripheral blood (PB) and umbilical cord blood (CB). The gene expression is lower in PB-EPCs when compared to CB-EPCs.[20] PB-EPCs have more tumor suppressor (TP53) expression when compared to CB-EPCs.[20] CB-EPCs have more angiogenic expression, or growth and splitting of vasculature.[20]

Transcript

Using RNAfold, minimum free energy structures were created based on the extended 5’ and 3’ untranslated region (UTR) in human sequences. Unconserved amino acids, miRNA, stem-loop formations, and RNA binding proteins (RBPs) are shown on the diagram (Figure 2–3).

miRNA targeting

Within the 5’ UTR region, both miR-4700-5p and miR-4667-5p were referenced in an experiment which identified certain miRNAs expressed consistently in ERBB2+ breast cancer gene.[21] In addition, miR-8089 was referenced in a study showing certain novel miRNAs found within sepsis patients.[22] miR-4271 was shown to have effects on coronary heart disease binding to the 3' UTR region of the APOC3 gene.[23] Literature on miR-7113-5p shows that this miRNA is a mirtron.[24]

Within the 3’ UTR region, miR-3143 is referenced in a study where miRNAs were expressed consistently in ERBB2+ breast cancer gene.[21] miR-152-5p plays a role in inhibiting DNA methylation of genes involved in metabolic and inflammatory pathways.[25] miR-31-3p is overexpressed in esophageal squamous cell carcinoma (ESCC).[26] One miRNA result, miR-150-5p, was conserved across multiple homologs within the 3’ UTR region more than 3000 bp downstream.[27] The miR-150-5p miRNA plays a role in colorectal cancer (CRC), where a lower expression of the miRNA was associated with a suppression of CRC metastasis.[27]

RNA binding proteins

In terms of some of the RBPs found, PAPBC1 had five binding sites, two of which are highlighted on the 5’ UTR. This protein is known to attach poly-a-tails for proteins that have entered the cytoplasm, preventing them from re-entry into the nucleus. The FUS protein was another one found with a binding site on a predicted stem loop. The gene encodes for a protein which facilitates transportation of the protein into the cytoplasm.[28] Within the 3’ UTR, the RBMY1A1, RBMX, and ACO1 proteins were some of the top scoring RBPs. The RBMY1A1 is a protein known to partake in splicing, and is required for sperm development.[29] The RBMX protein is a homolog of the RBMY protein involved in sperm production.[30] It is also known to promote transcription of a tumor suppressor gene, TXNIP.[30] ACO1 is another RBP known to bind with mRNA to regulate iron levels.[31] By binding to iron responsive elements, it can repress translation of ferritin and inhibit degradation of transferring receptor mRNA when iron levels become low.[31]

Protein

Analysis to predict post-translational modifications of the protein were conducted on. Based on the results of Expasy's Myristoylator in Homo sapiens, Mirounga leonina, and Fukomys damarensis, it can be concluded that ZNF226 is not myristoylated at the N-terminus.[32] Numerous predicted binding sites for post-translational modifications were also identified among the three species. The phosphorylation region at the C-terminus of the protein was also identified as a match for the protein kinase C phosphorylation binding site.[33][34][35][36] S-nitrosylation was another identified modification at C354 (Figure 2). This modification is found in SRG1, a zinc finger protein that plays a role preventing nitric oxide (NO) synthesis.[37] When NO is sustained, s-nitrosylation occurs within the protein, disrupting its transcriptional repression abilities.[37] Acetylation was another modification identified. In the case of promyelocytic leukemia, a condition resulting in the abundance of blood forming cells in the bone marrow, promyelocytic leukemia zinc finger proteins are known to be activated by histone acetyltransferases, or by acetylation of a C-terminus lysine.[38] Acetylation in other zinc finger proteins, such as GATA1, are known to enhance their ability to interact with other proteins.[39] Arginine dimethylation is another identified modification within ZNF226. Arginine methylation of cellular nucleic acid binding protein (CNBP), a zinc finger protein, has shown to impede its ability to bind nucleic acids.[40]

It is predicted that ZNF226 localizes within the nucleus, which aligns with its known functions as a transcription factor.[41] It has also been predicted to localize within the mitochondria.[41]

Homology/evolution

Although there is little information available on the ZNF226 gene, homologs of the gene have been found across eukaryotes and bacteria species. Strict orthologs were only found within mammals (Figure 4). The ZNF226 gene is also closely related to the paralog ZNF234 in humans, and the Zfp111 gene within mice.[1][4] Across the various species in which ZNF226 orthologs and homologs that were identified, conservation of the C2H2 binding sites is apparent (Figure 4–5).[8] In human ZNF226 paralogs, there is also conservation of the C2H2 binding sites, as well as nucleic acid binding sites.[1]

Slow rate evolution is apparent for the ZNF226 protein. It evolves in a manner similar to the cytochrome c protein instead of the fibrinogen alpha chain protein (Figure 6).

Interacting Proteins

Two interactions detected via the two hybrid method occurred with SSBP3 and ATF4, both of which are transcription factors.

ATF4/CREB-2 is a transcription factor which binds to the long terminal repeat of the human T-cell leukemia type1 virus (HTLV-1). It can be an activator of HTLV-1.[42][43][44]

SSBP3/CSDP is found in mice embryonic stem cells to develop into trophoblasts (provide nutrients to embryo).[42][45] ZNF226 is expressed at greater levels within human stem cells.[20]

Function

With ZNF226 being a transcription factor, playing a role in transcriptional repression, the 18 zf-C2H2 binding domains are predicted to bind to the DNA sequence shown in the sequence logo (Figure 7–9).[5][6]

Clinical significance

Associated diseases and conditions

A mutation within ZNF226 gene has been positively correlated with the presence of hepatocellular carcinoma (HCC).[46] A particular SNP (rs2927438) also correlated with an increased expression of ZNF226 in brain frontal cortical tissue and peripheral mononuclear cells, such as T cells and B cells.[47] The promoter region of ZNF226 was found to be hypomethylated in those who were exposed to the Chinese famine.[48] The hypomethylated region in ZNF226 was shown to have a correlation of methylation in the blood and the prefrontal cortex, although the exact function of the protein in the famine is not understood.[48] ZNF226 gene was listed among many other genes with a copy number variation (CNV) that was associated with single common variable immunodeficiency (CVID).

SNPs

Numerous SNPs were identified throughout the ZNF226 gene. Within the GXP_7536741 promoter, there were two SNPs of interest that were found. Listed below are associated transcription factors for both SNPs.

Matrix Matrix Full Name Position Start Position End Strand Matrix Score Function
V$LHX4.01 LIM homeobox 4, Gsh4 58 80 (+) 0.849 Homeodomains play a role in vertebrate development. LIM domains contains two double zinc finger motifs and cysteine-rich regions. Plays a role in neural and lymphoid cell development.[49][50]
V$BRN2.04 POU class 3 homeobox 2 (POU3F2), OTF7 61 79 (-) 0.843 The POU domain has been shown to play a role in neuroendocrine development.[49][51]
V$GSH2.01 Homeodomain transcription factor Gsh-2 61 79 (+) 0.966 Gsh-2 is found to play a role in brain development.[52]
V$LBX2.01 Ladybird homeobox 2 61 79 (-) 0.893 In mice, this TF was shown to play a role in testis and epididymis.[53]
V$CDP.02 Transcriptional repressor CDP 149 171 (-) 0.954 CDP has been studied for its role in regulating the S phase of the cell cycle.[54]
V$HOXC13.01 Homeodomain transcription factor HOXC13 154 170 (-) 0.917 HOXC13 plays a role in regulating keratin expression.[55]
V$NFY.04 Nuclear factor Y (Y-box binding factor) 155 169 (-) 0.938 Plays a role in cell cycle regulation, and binds to the CCAAT box upstream to transcription site.[56]

References

  1. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 "Entrez Gene: Zinc finger protein 226". https://www.ncbi.nlm.nih.gov/gene/7769. 
  2. ↑ "GeneCards entry on ZNF226". 2020. https://www.genecards.org/cgi-bin/carddisp.pl?gene=ZNF226. 
  3. ↑ 3.0 3.1 3.2 "ZNF226 zinc finger protein 226 [Homo sapiens (human) - Gene - NCBI"]. https://www.ncbi.nlm.nih.gov/gene/7769. 
  4. ↑ 4.0 4.1 "Differential expansion of zinc-finger transcription factor loci in homologous human and mouse gene clusters". Genome Research 13 (6A): 1097–110. June 2003. doi:10.1101/gr.963903. PMID 12743021. 
  5. ↑ 5.0 5.1 "Deep sequencing of large library selections allows computational discovery of diverse sets of zinc fingers that bind common targets". Nucleic Acids Research 42 (3): 1497–508. February 2014. doi:10.1093/nar/gkt1034. PMID 24214968. 
  6. ↑ 6.0 6.1 "A systematic survey of the Cys2His2 zinc finger DNA-binding landscape". Nucleic Acids Research 43 (3): 1965–84. February 2015. doi:10.1093/nar/gku1395. PMID 25593323. 
  7. ↑ 7.0 7.1 7.2 "Expasy Compute pI/MW tool". https://web.expasy.org/compute_pi/. 
  8. ↑ 8.0 8.1 8.2 8.3 8.4 "The EMBL-EBI search and sequence analysis tools APIs in 2019". Nucleic Acids Research 47 (W1): W636–W641. July 2019. doi:10.1093/nar/gkz268. PMID 30976793. 
  9. ↑ "NPS@: network protein sequence analysis". Trends in Biochemical Sciences 25 (3): 147–50. March 2000. doi:10.1016/s0968-0004(99)01540-6. PMID 10694887. 
  10. ↑ "I-TASSER server: new development for protein structure and function predictions". Nucleic Acids Research 43 (W1): W174-81. July 2015. doi:10.1093/nar/gkv342. PMID 25883148. 
  11. ↑ "COFACTOR: improved protein function prediction by combining structure, sequence and protein-protein interaction information". Nucleic Acids Research 45 (W1): W291–W299. July 2017. doi:10.1093/nar/gkx366. PMID 28472402. 
  12. ↑ 12.0 12.1 "Genomatix Website". https://www.genomatix.de/?s=63e6c97eb8268448cedfe91b4310fb87. 
  13. ↑ "DNA binding specificities of Spi-1/PU.1 and Spi-B transcription factors and identification of a Spi-1/Spi-B binding site in the c-fes/c-fps promoter". Oncogene 11 (2): 303–13. July 1995. PMID 7624145. 
  14. ↑ "A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain". Genes & Development 9 (8): 984–94. April 1995. doi:10.1101/gad.9.8.984. PMID 7774815. 
  15. ↑ "Ronin/Hcf-1 binds to a hyperconserved enhancer element and regulates genes involved in the growth of embryonic stem cells". Genes & Development 24 (14): 1479–84. July 2010. doi:10.1101/gad.1935210. PMID 20581084. 
  16. ↑ "Cell cycle-dependent regulation of TIAP/m-survivin expression". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1493 (1–2): 188–94. September 2000. doi:10.1016/S0167-4781(00)00142-1. PMID 10978521. 
  17. ↑ "A comprehensive functional analysis of tissue specificity of human gene expression". BMC Biology 6 (1): 49. November 2008. doi:10.1186/1741-7007-6-49. PMID 19014478. 
  18. ↑ "Differential gene expression in granulosa cells from polycystic ovary syndrome patients with and without insulin resistance: identification of susceptibility gene sets through network analysis". The Journal of Clinical Endocrinology and Metabolism 97 (10): E2016-21. October 2012. doi:10.1210/jc.2011-3441. PMID 22904171. 
  19. ↑ "GEO Profiles entry on ZNF226 Papillary Thyroid Cancer". https://www.ncbi.nlm.nih.gov/geo/tools/profileGraph.cgi?ID=GDS1732:233461_x_at. 
  20. ↑ 20.0 20.1 20.2 20.3 "Genetic module and miRNome trait analyses reflect the distinct biological features of endothelial progenitor cells from different anatomic locations". BMC Genomics 13 (1): 447. September 2012. doi:10.1186/1471-2164-13-447. PMID 22943456. 
  21. ↑ 21.0 21.1 "Identification of new microRNAs in paired normal and tumor breast tissue suggests a dual role for the ERBB2/Her2 gene". Cancer Research 71 (1): 78–86. January 2011. doi:10.1158/0008-5472.CAN-10-1869. PMID 21199797. 
  22. ↑ "Characterization and Identification of novel serum microRNAs in sepsis patients with different outcomes". Shock 39 (6): 480–7. June 2013. doi:10.1097/SHK.0b013e3182940cb8. PMID 23612084. 
  23. ↑ "An APOC3 3'UTR variant associated with plasma triglycerides levels and coronary heart disease by creating a functional miR-4271 binding site". Scientific Reports 6 (1): 32700. September 2016. doi:10.1038/srep32700. PMID 27624799. 
  24. ↑ "Discovery of hundreds of mirtrons in mouse and human small RNA data". Genome Research 22 (9): 1634–45. September 2012. doi:10.1101/gr.133553.111. PMID 22955976. 
  25. ↑ "From animal models to patients: the role of placental microRNAs, miR-210, miR-126, and miR-148a/152 in preeclampsia". Clinical Science 134 (8): 1001–1025. April 2020. doi:10.1042/CS20200023. PMID 32337535. 
  26. ↑ "Abrogation of esophageal carcinoma development in miR-31 knockout rats". Proceedings of the National Academy of Sciences of the United States of America 117 (11): 6075–6085. March 2020. doi:10.1073/pnas.1920333117. PMID 32123074. Bibcode: 2020PNAS..117.6075F. 
  27. ↑ 27.0 27.1 "MiR-150-5p suppresses colorectal cancer cell migration and invasion through targeting MUC4". Asian Pacific Journal of Cancer Prevention 15 (15): 6269–73. 2014. doi:10.7314/APJCP.2014.15.15.6269. PMID 25124610. 
  28. ↑ "GeneCards entry on FUS". https://www.genecards.org/cgi-bin/carddisp.pl?gene=FUS. 
  29. ↑ "GeneCards entry on RBMY1A1". https://www.genecards.org/cgi-bin/carddisp.pl?gene=RBMY1A1. 
  30. ↑ 30.0 30.1 "GeneCards entry on RBMX". https://www.genecards.org/cgi-bin/carddisp.pl?gene=RBMX. 
  31. ↑ 31.0 31.1 "GeneCards entry on ACO1". https://www.genecards.org/cgi-bin/carddisp.pl?gene=ACO1. 
  32. ↑ "Expasy Myristoylator tool". https://web.expasy.org/myristoylator/. 
  33. ↑ "GPS 2.1: enhanced prediction of kinase-specific phosphorylation sites with an algorithm of motif length selection". Protein Engineering, Design & Selection 24 (3): 255–60. March 2011. doi:10.1093/protein/gzq094. PMID 21062758. 
  34. ↑ "GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy". Molecular & Cellular Proteomics 7 (9): 1598–608. September 2008. doi:10.1074/mcp.M700574-MCP200. PMID 18463090. 
  35. ↑ "GPS: a comprehensive www server for phosphorylation sites prediction". Nucleic Acids Research 33 (Web Server issue): W184-7. July 2005. doi:10.1093/nar/gki393. PMID 15980451. 
  36. ↑ "Motif Scan tool". https://myhits.sib.swiss/cgi-bin/motif_scan. 
  37. ↑ 37.0 37.1 "S-nitrosylation of the zinc finger protein SRG1 regulates plant immunity". Nature Communications 9 (1): 4226. October 2018. doi:10.1038/s41467-018-06578-3. PMID 30315167. Bibcode: 2018NatCo...9.4226C. 
  38. ↑ "Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein". Molecular and Cellular Biology 25 (13): 5552–66. July 2005. doi:10.1128/MCB.25.13.5552-5566.2005. PMID 15964811. 
  39. ↑ "Zinc finger proteins in cancer progression". Journal of Biomedical Science 23 (1): 53. July 2016. doi:10.1186/s12929-016-0269-9. PMID 27411336. 
  40. ↑ "Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding". FEBS Letters 588 (9): 1542–8. May 2014. doi:10.1016/j.febslet.2014.03.052. PMID 24726729. 
  41. ↑ 41.0 41.1 "PSORT II tool". https://psort.hgc.jp/form2.html. 
  42. ↑ 42.0 42.1 "An atlas of combinatorial transcriptional regulation in mouse and man". Cell 140 (5): 744–52. March 2010. doi:10.1016/j.cell.2010.01.044. PMID 20211142. 
  43. ↑ "NCBI entry on ATF4". https://www.ncbi.nlm.nih.gov/gene/?term=NP_001666. 
  44. ↑ "CREB-2, a cellular CRE-dependent transcription repressor, functions in association with Tax as an activator of the human T-cell leukemia virus type 1 promoter". Journal of Virology 72 (10): 8332–7. October 1998. doi:10.1128/JVI.72.10.8332-8337.1998. PMID 9733879. 
  45. ↑ "Single-stranded DNA binding protein Ssbp3 induces differentiation of mouse embryonic stem cells into trophoblast-like cells". Stem Cell Research & Therapy 7 (1): 79. May 2016. doi:10.1186/s13287-016-0340-1. PMID 27236334. 
  46. ↑ "Whole-genome sequencing of liver cancers identifies etiological influences on mutation patterns and recurrent mutations in chromatin regulators". Nature Genetics 44 (7): 760–4. May 2012. doi:10.1038/ng.2291. PMID 22634756. 
  47. ↑ "An APOE-independent cis-eSNP on chromosome 19q13.32 influences tau levels and late-onset Alzheimer's disease risk". Neurobiology of Aging 66: 178.e1–178.e8. June 2018. doi:10.1016/j.neurobiolaging.2017.12.027. PMID 29395286. 
  48. ↑ 48.0 48.1 "DNA methylation changes related to nutritional deprivation: a genome-wide analysis of population and in vitro data". Clinical Epigenetics 11 (1): 80. May 2019. doi:10.1186/s13148-019-0680-7. PMID 31097004. 
  49. ↑ 49.0 49.1 "Variation in homeodomain DNA binding revealed by high-resolution analysis of sequence preferences". Cell 133 (7): 1266–76. June 2008. doi:10.1016/j.cell.2008.05.024. PMID 18585359. 
  50. ↑ "LIM homeobox transcription factors, a novel subfamily which plays an important role in cancer (review)". Oncology Reports 31 (5): 1975–85. May 2014. doi:10.3892/or.2014.3112. PMID 24676471. 
  51. ↑ "The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain". Cell 73 (1): 193–205. April 1993. doi:10.1016/0092-8674(93)90171-l. PMID 8462099. 
  52. ↑ "Gsh-2, a murine homeobox gene expressed in the developing brain". Mechanisms of Development 50 (2–3): 177–86. April 1995. doi:10.1016/0925-4773(94)00334-j. PMID 7619729. 
  53. ↑ "Expression of the Ladybird-like homeobox 2 transcription factor in the developing mouse testis and epididymis". BMC Developmental Biology 8 (1): 22. February 2008. doi:10.1186/1471-213X-8-22. PMID 18304314. 
  54. ↑ "CDP/Cux stimulates transcription from the DNA polymerase alpha gene promoter". Molecular and Cellular Biology 23 (8): 3013–28. April 2003. doi:10.1128/MCB.23.8.3013-3028.2003. PMID 12665598. 
  55. ↑ "HOXC13 is involved in the regulation of human hair keratin gene expression". The Journal of Biological Chemistry 277 (5): 3718–26. February 2002. doi:10.1074/jbc.M101616200. PMID 11714694. 
  56. ↑ "Arabidopsis thaliana Nuclear Factor Y Transcription Factors" (in English). Frontiers in Plant Science 7: 2045. 2017. doi:10.3389/fpls.2016.02045. PMID 28119722. 



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