TEKTL1 Gene

Name tektin like 1
Description Predicted to be involved in flagellated sperm motility. Located in extracellular exosome. [provided by Alliance of Genome Resources, Mar 2025]
Summary
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nA careful review of the provided abstracts reveals that none of these studies specifically mention or characterize a gene or protein designated “TEKTL1.” Rather, the collected reports focus on the UFM1 conjugation (ufmylation) system—a ubiquitin‐like modification cascade—in which UFM1 and its associated activating (UBA5), conjugating (UFC1), and ligating (for example, UFL1) enzymes, as well as adaptors such as UFBP1, regulate multiple cellular processes. These processes include the unfolded protein response and endoplasmic reticulum (ER) stress signaling; protection against ER stress–induced apoptosis in secretory cells such as pancreatic β‐cells; and broader roles in heart disease, brain development, vascular remodeling, and immune responses."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFor instance, one study demonstrated that ER stress and the consequent unfolded protein response are activated in cardiomyocytes during ischemic heart disease, suggesting that quality control mechanisms (including those mediated by ubiquitin‐like proteins) are critical for maintaining cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In parallel, the identification of novel UFM1 substrates—such as C20orf116 (later named UFBP1) and CYB5R3—has extended the known roles of ufmylation to processes as diverse as ER-associated protein degradation, autophagy (or ER-phagy), and even protection against stress‐induced apoptosis in protein secretory cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Other reports have linked defects in the UFM1 system to severe developmental and neurological disorders"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "and to altered inflammatory responses and viral defense mechanisms"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": ", further underscoring the system’s broad relevance across tissues."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}, {"type": "fg_f", "ref": "5"}, {"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies have documented the downregulation of components of the UFM1 cascade (often in association with upregulation of other protein modifiers like FAT10) in conditions of protein quality control failure, as seen in liver disease models with Mallory-Denk body formation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ", as well as provided evidence linking ufmylation to the regulation of vascular smooth muscle cell fate and endothelial cell injury in vascular remodeling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Finally, modulation of the UFM1 system has been implied in the heart, where alterations in ufmylation correlate with changes in the expression of novel associated genes, further emphasizing its potential role in cardiac hypertrophy."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "13"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn summary, while these abstracts collectively highlight the multifaceted roles of the UFM1 (ufmylation) system in managing ER stress, protein homeostasis, inflammation, and cellular survival across diverse tissues, they do not provide any details—or functional insights—on a factor named TEKTL1. As such, based on the available scientific literature provided here, no functional role for TEKTL1 is currently described."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}, {"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "\n"}]}]}]}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Asim Azfer, Jianli Niu, Linda M Rogers, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "A novel type of E3 ligase for the Ufm1 conjugation system."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.036814"}], "href": "https://doi.org/10.1074/jbc.M109.036814"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20018847"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20018847"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Katleen Lemaire, Rodrigo F Moura, Mikaela Granvik, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0018517"}], "href": "https://doi.org/10.1371/journal.pone.0018517"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21494687"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21494687"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Ryosuke Ishimura, Afnan H El-Gowily, Daisuke Noshiro, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-022-35501-0"}], "href": "https://doi.org/10.1038/s41467-022-35501-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36543799"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36543799"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Mikko Muona, Ryosuke Ishimura, Anni Laari, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Biallelic Variants in UBA5 Link Dysfunctional UFM1 Ubiquitin-like Modifier Pathway to Severe Infantile-Onset Encephalopathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ajhg.2016.06.020"}], "href": "https://doi.org/10.1016/j.ajhg.2016.06.020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27545674"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27545674"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Jie Zhang, Huabin Zhu, Siyang Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deficiency of Murine UFM1-Specific E3 Ligase Causes Microcephaly and Inflammation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Neurobiol (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s12035-022-02979-0"}], "href": "https://doi.org/10.1007/s12035-022-02979-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35931931"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35931931"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Dale R Balce, Ya-Ting Wang, Michael R McAllaster, et al. "}, {"type": "b", "children": [{"type": "t", "text": "UFMylation inhibits the proinflammatory capacity of interferon-γ-activated macrophages."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.2011763118"}], "href": "https://doi.org/10.1073/pnas.2011763118"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33372156"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33372156"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Xiaolei Hu, Hengyan Zhang, Yuan Song, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitin fold modifier 1 activates NF-κB pathway by down-regulating LZAP expression in the macrophage of diabetic mouse model."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biosci Rep (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BSR20191672"}], "href": "https://doi.org/10.1042/BSR20191672"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31829413"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31829413"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Byung Hak Ha, Hee-Chul Ahn, Sung Hwan Kang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for Ufm1 processing by UfSP1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M708756200"}], "href": "https://doi.org/10.1074/jbc.M708756200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18321862"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18321862"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "H Liu, J Li, B Tillman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ufmylation and FATylation pathways are downregulated in human alcoholic and nonalcoholic steatohepatitis, and mice fed DDC, where Mallory-Denk bodies (MDBs) form."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Mol Pathol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexmp.2014.05.010"}], "href": "https://doi.org/10.1016/j.yexmp.2014.05.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24893112"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24893112"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Ming Su, Zhihong Yue, Hui Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ufmylation Is Activated in Vascular Remodeling and Lipopolysaccharide-Induced Endothelial Cell Injury."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "DNA Cell Biol (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1089/dna.2017.4073"}], "href": "https://doi.org/10.1089/dna.2017.4073"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29461087"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29461087"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Qi Pang, Jie Xiong, Xiao-Lei Hu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "UFM1 Protects Macrophages from oxLDL-Induced Foam Cell Formation Through a Liver X Receptor α Dependent Pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Atheroscler Thromb (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.5551/jat.28829"}], "href": "https://doi.org/10.5551/jat.28829"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26040753"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26040753"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Hu Jiajia, Yang Ziyao, Zheng Jiaqi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Screening UFMylation-associated genes in heart tissues of Ufm1-transgenic mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cardiovasc Disord (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12872-023-03563-7"}], "href": "https://doi.org/10.1186/s12872-023-03563-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37980507"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37980507"}]}]}]}
NCBI Gene ID 126402
API
Download Associations
Predicted Functions View TEKTL1's ARCHS4 Predicted Functions.
Co-expressed Genes View TEKTL1's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View TEKTL1's ARCHS4 Predicted Functions.

Functional Associations

TEKTL1 has 688 functional associations with biological entities spanning 4 categories (functional term, phrase or reference, chemical, cell line, cell type or tissue, gene, protein or microRNA) extracted from 12 datasets.

Click the + buttons to view associations for TEKTL1 from the datasets below.

If available, associations are ranked by standardized value

Dataset Summary
Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles tissue samples with high or low expression of TEKTL1 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
CM4AI KOLF21J CRISPRi Gene Perturbation Atlas gene perturbations changing expression of TEKTL1 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
COMPARTMENTS Curated Protein Localization Evidence Scores 2025 cellular components containing TEKTL1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 cellular components co-occuring with TEKTL1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
GO Cellular Component Annotations 2025 cellular components containing TEKTL1 protein from the curated GO Cellular Component Annotations 2025 dataset.
JASPAR Predicted Human Transcription Factor Targets 2025 transcription factors regulating expression of TEKTL1 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Human Transcription Factor Targets dataset.
JASPAR Predicted Mouse Transcription Factor Targets 2025 transcription factors regulating expression of TEKTL1 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Mouse Transcription Factor Targets 2025 dataset.
Rummagene Transcription Factor Associations 2026 transcription factors regulating expression of TEKTL1 gene from the Rummagene Transcription Factor Associations 2026 dataset.
RummaGEO Drug Perturbation Signatures drug perturbations changing expression of TEKTL1 gene from the RummaGEO Drug Perturbation Signatures dataset.
RummaGEO Gene Perturbation Signatures gene perturbations changing expression of TEKTL1 gene from the RummaGEO Gene Perturbation Signatures dataset.
TISSUES Curated Tissue Protein Expression Evidence Scores 2025 tissues with high expression of TEKTL1 protein from the TISSUES Curated Tissue Protein Expression Evidence Scores 2025 dataset.
TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 tissues co-occuring with TEKTL1 protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset.