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Draft:ZNF329

  • Comment: This protein is not notable based on the sources provided. Almost all sources are primary (databases or info sheets), and the few secondary references are on other subjects. We need a couple of secondary sources (e.g. books, reviews) that are specifically about ZNF329 to have an article. WeirdNAnnoyed (talk) 10:51, 30 June 2026 (UTC)

Zinc finger 329 protein is a protein that, in humans, is encoded by the zinc finger 329 gene.[1] The protein is a part of the Krüppel C2H2-type zinc finger protein family, and has 12 C2H2 zinc fingers, which characteristically start with a cysteine and end with a histidine.[2]

Gene

The human gene ZNF329 is located on chromosome 19, specifically, its locus location is 19q13.43. The length of the gene is 28,857 nucleotides, and it is on the minus strand. The gene neighborhood is comprised of zinc finger and SCAN domain containing 18 (ZSCAN18), which is downstream, and zinc finger 274 (ZNF274) lies upstream.[3]

Transcripts

There are 12 transcript variants for ZNF329, which differ in nucleotide length. The variants range in mRNA length from 3,438 to 3,871 nucleotides.[4] [5]

Protein

Illustration of the domains of human protein ZNF329. Domain one is color-coded green and has boundaries from amino acid 203-284, domain two is in orange and has boundaries from 314 to 248, domain three in blue has boundaries from 454 to 533.

The ZNF329 protein has a molecular weight of approximately 61.7 kD and an approximate basal isoelectric point of 8.9.[6] There are also two isoforms; X1 has a length of 564 amino acids, while isoform X2 has a length of 541 amino acids. Its amino acid sequence has a higher-than-average level of histidine compared to other human proteins, which is due to the histidine pattern in the zinc fingers. The amino acid sequence has a lower-than-average amount of alanine, valine, and tryptophan, which are all nonpolar hydrophobic amino acids.[7]

  • Conceptual translation of human ZNF329 Part 1.
    Conceptual translation of human ZNF329 Part 1.
  • Conceptual translation of human ZNF329 Part 2.
    Conceptual translation of human ZNF329 Part 2.
  • Conceptual translation of human ZNF329 Part 3.
    Conceptual translation of human ZNF329 Part 3.
Tertiary structure of ZNF329 with blues representing higher confidence levels, while orange and yellow represent lower confidence levels for the structures.

Subcellular localization

localization of ZNF337 is highest in the nucleus (nuclear) at 95.7% followed by 4.3% in the mitochondria (mitochondrial).[8]

Tertiary structure

The tertiary structure is composed primarily of alpha helices and has lacks both positive and negative charge clusters.[9]

Gene level regulation

The ZNF329 gene is expressed both ubiquitously and variably in human tissues. The highest expression was shown in the cerebellum, kidney, and thyroid.[10] Gene expression is near 50th percentile for most tissues, and therefore ZNF329 gene is considered lowly expressed.[11]

Protein level regulation

The post-translational modifications that have been experimentally determined are 6 phosphorylation sites, 3 ubiquitylation sites, and one acetylation site.[12]. Since ZNF329 is localized in the nucleoplasm, it does not undergo N-glycosylation.[13] High-scoring SUMOylation sites were also detected near the beginning of the sequence. [14] The nuclear localization signal used to sort ZNF329 in the nucleoplasm is located at the beginning of the sequence. [15]

Homology and evolution

Paralogs

According to GeneCards database, there are 481 paralogs that exist for ZNF329. The paralogs include zinc finger 180 (ZNF180), zinc finger 135 (ZNF135), zinc finger 420 (ZNF420), and zinc finger 606 (ZNF606).[16]

Orthologs

Phylogenetic tree of 20 placental mammals from 10 different orders.

ZNF329 only has orthologs in placental mammals. The ZNF329 protein first appeared when marsupials and placental mammals diverged, which is roughly between 147 and 164 million years ago.[17] High conservation is shown across the orthologs, especially from the middle to the end of the sequences, notably near where the zinc fingers begin.[18]

Table 1. 20 Orthologs of ZNF329
Genus and Species Common Name Family Order Median Date of Divergence (MYA) Accession Number Sequence Length (aa) Sequence Identity Sequence Similarity
Homo sapiens Humans Hominidae Primata 0 NP_078896.3 541 100% 100%
Macaca mulatta Rhesus macaque Cercopithecidae Primata 28.8 XP_077836321.1 574 97% 97%
Mus musculus House mouse Muridae Rodentia 87 NP_080322.2 522 78% 84%
Sciurus carolinensis Gray squirrel Sciuridae Rodentia 87 XP_047384309.1 532 78% 84%
Ochotona curzoniae Plateau pika Ochotonidae Lagomorpha 87 XP_040834089.1 542 80% 87%
Lepus europaeus European hare Leporidae Lagomorpha 87 XP_062033433.1 598 83% 89%
Erinaceus europaeus European hedgehog Erinaceidae Eulipotyphla 94 XP_060028570.1 536 78% 84%
Condylura cristata Star nosed mole Talpidae Eulipotyphla 94 XP_004695537.1 549 80% 87%
Physeter macrocephalus Sperm whale Physeteridae Artiodactyla 94 XP_007113864.1 541 86% 89%
Bos taurus Cattle Bovidae Artiodactyla 94 NP_001193736.2 538 79% 86%
Felis catus Domestic cat Felidae Carnivora 94 XP_003997391.1 541 85% 90%
Ursus arctos Brown bear Ursidae Carnivora 94 XP_057169886.1 540 87% 90%
Desmodus rotundus Common vampire bat Phyllostomidae Chiroptera 94 XP_045059534.2 539 84% 89%
Pteronotus mesoamericanus Common mustached bat Mormoopidae Chiroptera 94 XP_054423800.1 539 85% 89%
Equus caballus Horse Equidae Perissodactyla 94 XP_070081195.1 538 86% 91%
Equus quagga Plains zebra Equidae Perissodactyla 94 XP_046536570.1 538 85% 90%
Choloepus didactylus Two-toed sloth Choloepodidae Pilosa 99 XP_037674876.1 538 81% 87%
Tamandua tetradactyla Collared anteater Myrmecophagidae Pilosa 99 XP_076986644.1 552 81% 88%
Echinops telfairi Lesser hedgehog tenrec Tenrecidae Afrosoricida 99 XP_045148266.1 531 80% 86%
Tenrec ecaudatus Tailless tenrec Tenrecidae Afrosoricida 99 XP_075392595.1 554 79% 85%

Interacting proteins

Some protein interactants identified through co-expression, protein homology, and text mining, include zinc finger protein 30 (ZFP30), zinc finger protein 225 (ZNF225), zinc finger protein 250 (ZNF250), zinc finger protein 432 (ZNF432), zinc finger protein 549 (ZNF549), and Zinc finger and SCAN domain-containing 18 (ZSCAN 18).[19] The subcellular localizations for these interactants are typically in the nucleoplasm, much like ZNF329. [20] The function of all these interactants is said to be transcriptional regulation.[21]

Clinical significance

ZNF329 is reported to be involved in regulating gene expression in brain tumors.[22][23] ZNF329 is also associated with pathways of cancer progression. [24] ZNF329, as well as other zinc finger proteins, are also a part of the sepsis regulatory network. [25]

References

  1. ^ NCBI Gene https://www.ncbi.nlm.nih.gov/gene/79673
  2. ^ Santa Cruz Biotechnology https://datasheets.scbt.com/sc-377455.pdf
  3. ^ NCBI Gene Neighborhood https://www.ncbi.nlm.nih.gov/gene/79673
  4. ^ NCBI Genome Viewerhttps://www.ncbi.nlm.nih.gov/gdv/browser/gene/?id=79673
  5. ^ The Human Protein Atlas https://www.proteinatlas.org/ENSG00000181894-ZNF329/structure#proteinstructure
  6. ^ Expasy pI and Molecular Weight Toolhttps://web.expasy.org/cgi-bin/compute_pi/pi_tool.cgi
  7. ^ SAPS Compositional Analysis https://www.ebi.ac.uk/jdispatcher/seqstats/saps/summary?jobId=saps-I20260602-020422-0312-62195943-p1m
  8. ^ PSORT II Localization Prediction Tool https://psort.hgc.jp/form2.html
  9. ^ AlphaFold Protein Structure Database https://alphafold.com/entry/AF-Q86UD4-F1?activeTab=summary
  10. ^ NCBI RNA Sequence Data https://www.ncbi.nlm.nih.gov/gene/79673
  11. ^ NCBI GEO Profiles https://www.ncbi.nlm.nih.gov/geoprofiles/?term=ZNF329
  12. ^ PhosphoSitePlus https://www.phosphosite.org/proteinAction.action?id=10242200&showAllSites=true
  13. ^ Glycosylation: mechanisms, biological functions and clinical implications https://www.nature.com/articles/s41392-024-01886-1
  14. ^ SUMOplot Analysis Program www.abcepta.com.
  15. ^ DTU Health Tech https://services.healthtech.dtu.dk/cgi-bin/webface2.cgi?jobid=6A247D2B0011D6C7B60E0229&wait=20
  16. ^ GeneCards: The Human Gene Database https://www.genecards.org/card/ZNF329#Paralogs
  17. ^ Timetree: The Timescale of Life https://timetree.org/
  18. ^ European Bioinformatics Institute: Sequence Analysis Toolhttps://www.ebi.ac.uk/jdispatcher/msa
  19. ^ STRING Database https://string-db.org/cgi/textmining?taskId=bqWWCZjdu7pm&sessionId=bmFcwCf7jw7N&node1=6228699&node2=6228712
  20. ^ The Human Protein Atlas https://www.proteinatlas.org/ENSG00000121413-ZSCAN18/subcellular
  21. ^ STRING Database https://string-db.org/cgi/textmining?taskId=bqWWCZjdu7pm&sessionId=bmFcwCf7jw7N&node1=6228699&node2=6228712
  22. ^ Reconstructing directed gene regulatory network by only gene expression datahttps://pubmed.ncbi.nlm.nih.gov/27556418/
  23. ^ Genome-wide association analyses identify candidate loci for amyloid imaging and plasma biomarkers in adults with Down syndromehttps://alz-journals.onlinelibrary.wiley.com/doi/full/10.1002/alz.70358
  24. ^ Transcriptome Patterns of BRCA1- and BRCA2- Mutated Breast and Ovarian Cancers https://www.mdpi.com/1422-0067/22/3/1266
  25. ^ Reverse Engineering of the Pediatric Sepsis Regulatory Network and Identification of Master Regulators https://www.mdpi.com/2227-9059/9/10/1297


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