CDC14C Gene

Name cell division cycle 14C
Description This gene represents a retrogene of cell division cycle 14B (CDC14B), which is located on chromosome 9. The introns in the coding sequence have been processed out relative to the CDC14B locus, but there is an intact open reading frame that is missing only some sequence at the N-terminus, including the nuclear localiztion signal, relative to proteins encoded by the CDC14B gene. There is a difference in the subcellular localization of the protein encoded by this gene, relative to its parental gene product. While the parental gene product displays microtubular localization, GFP chimeras of the protein encoded by this gene localize to the endoplasmic reticulum, indicating a possible new functional role for this gene. [provided by RefSeq, Nov 2017]
Summary
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nAlthough none of the provided abstracts explicitly discuss CDC14C, the collective literature instead emphasizes the multifaceted roles of receptor‐type protein tyrosine phosphatases—especially PTPσ and closely related family members—in regulating neural development and axon regeneration. In several studies, PTPσ is shown to function as a receptor for extracellular glycosaminoglycans (such as chondroitin sulfate proteoglycans) that normally inhibit axonal growth. Genetic disruption or pharmacological inhibition of PTPσ in various injury models leads to enhanced axon extension (e.g., in the corticospinal tract, optic nerve, and dorsal root ganglia) via mechanisms that include altered dephosphorylation of substrates like N‐cadherin, p250GAP, and downstream kinases. Structural and biochemical analyses further reveal that PTPσ can interact with multiple ligands—including TrkC and other adhesion molecules—to mediate bidirectional signaling that governs neurite outgrowth and guidance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA second body of work in these abstracts focuses on how these phosphatases contribute to the organization and functional properties of synapses. High‐resolution structural studies, binding assays and loss‐of‐function experiments demonstrate that the extracellular domains of PTPσ (and related LAR‐type phosphatases) are strategically positioned at synaptic contacts, where they engage in trans‐synaptic interactions with proteins such as LRRTMs, neurexins, and TrkC to regulate the composition and signaling of NMDA receptors and other postsynaptic elements. Such interactions not only scaffold synaptic architecture but also fine‐tune receptor phosphorylation dynamics and synaptic plasticity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies extend the impact of receptor protein tyrosine phosphatases beyond classical neural regeneration. In non‐neuronal contexts these enzymes or their homologs regulate diverse biological processes: they modulate immune cell function (for instance, by restraining type I interferon production in plasmacytoid dendritic cells and influencing B cell survival via binding to midkine), affect hematopoietic stem cell engraftment via Rac signaling, and even participate in craniofacial development and intestinal epithelial barrier integrity through dephosphorylation of key substrates such as ezrin. Furthermore, differences in the biochemical properties of mouse versus human isoforms of PTPσ have been characterized, and interactions with intracellular partners (such as NME2) provide further layers of regulation that impact neurite outgrowth."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joanna McLean, Jane Batt, Laurie C Doering, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Enhanced rate of nerve regeneration and directional errors after sciatic nerve injury in receptor protein tyrosine phosphatase sigma knock-out mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "20026462"}], "href": "https://doi.org/20026462"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12097500"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12097500"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Ravi Vijayvargia, Surinder Kaur, M V Krishnasastry "}, {"type": "b", "children": [{"type": "t", "text": "alpha-Hemolysin-induced dephosphorylation of EGF receptor of A431 cells is carried out by rPTPsigma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2004.10.038"}], "href": "https://doi.org/10.1016/j.bbrc.2004.10.038"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15522239"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15522239"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Przemyslaw S Sapieha, Laure Duplan, Noriko Uetani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Receptor protein tyrosine phosphatase sigma inhibits axon regrowth in the adult injured CNS."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Neurosci (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.mcn.2004.10.011"}], "href": "https://doi.org/10.1016/j.mcn.2004.10.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15797710"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15797710"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Noriko Uetani, Mélanie J Chagnon, Timothy E Kennedy, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mammalian motoneuron axon targeting requires receptor protein tyrosine phosphatases sigma and delta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.0386-06.2006"}], "href": "https://doi.org/10.1523/JNEUROSCI.0386-06.2006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16738228"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16738228"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Roberta Siu, Chris Fladd, Daniela Rotin "}, {"type": "b", "children": [{"type": "t", "text": "N-cadherin is an in vivo substrate for protein tyrosine phosphatase sigma (PTPsigma) and participates in PTPsigma-mediated inhibition of axon growth."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00707-06"}], "href": "https://doi.org/10.1128/MCB.00707-06"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17060446"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17060446"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Elizabeth J Fry, Melanie J Chagnon, Rubèn López-Vales, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Corticospinal tract regeneration after spinal cord injury in receptor protein tyrosine phosphatase sigma deficient mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Glia (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/glia.20934"}], "href": "https://doi.org/10.1002/glia.20934"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19780196"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19780196"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Yingjie Shen, Alan P Tenney, Sarah A Busch, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPsigma is a receptor for chondroitin sulfate proteoglycan, an inhibitor of neural regeneration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1178310"}], "href": "https://doi.org/10.1126/science.1178310"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19833921"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19833921"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Mélanie J Chagnon, Chia-Lun Wu, Takanobu Nakazawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Receptor tyrosine phosphatase sigma (RPTPσ) regulates, p250GAP, a novel substrate that attenuates Rac signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2010.06.001"}], "href": "https://doi.org/10.1016/j.cellsig.2010.06.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20550964"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20550964"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Hideto Takahashi, Pamela Arstikaitis, Tuhina Prasad, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Postsynaptic TrkC and presynaptic PTPσ function as a bidirectional excitatory synaptic organizing complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuron (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neuron.2010.12.024"}], "href": "https://doi.org/10.1016/j.neuron.2010.12.024"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21262467"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21262467"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Charlotte H Coles, Yingjie Shen, Alan P Tenney, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteoglycan-specific molecular switch for RPTPσ clustering and neuronal extension."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1200840"}], "href": "https://doi.org/10.1126/science.1200840"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21454754"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21454754"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Li Hou, Jianchuan Wang, Yueyang Zhou, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Biochim Biophys Sin (Shanghai) (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/abbs/gmr095"}], "href": "https://doi.org/10.1093/abbs/gmr095"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22027896"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22027896"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Jae-Hyuk Yi, Yasuhiro Katagiri, Panpan Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Receptor protein tyrosine phosphatase σ binds to neurons in the adult mouse brain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Neurol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.expneurol.2014.02.007"}], "href": "https://doi.org/10.1016/j.expneurol.2014.02.007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24530640"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24530640"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Charlotte H Coles, Nikolaos Mitakidis, Peng Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms6209"}], "href": "https://doi.org/10.1038/ncomms6209"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25385546"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25385546"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Fumio Nakamura, Takako Okada, Maria Shishikura, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein Tyrosine Phosphatase δ Mediates the Sema3A-Induced Cortical Basal Dendritic Arborization through the Activation of Fyn Tyrosine Kinase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.2519-16.2017"}], "href": "https://doi.org/10.1523/JNEUROSCI.2519-16.2017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28637841"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28637841"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Alessandra Sclip, Thomas C Südhof "}, {"type": "b", "children": [{"type": "t", "text": "LAR receptor phospho-tyrosine phosphatases regulate NMDA-receptor responses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.53406"}], "href": "https://doi.org/10.7554/eLife.53406"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31985401"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31985401"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Reiko T Roppongi, Shreya H Dhume, Nirmala Padmanabhan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "LRRTMs Organize Synapses through Differential Engagement of Neurexin and PTPσ."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuron (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neuron.2020.01.003"}], "href": "https://doi.org/10.1016/j.neuron.2020.01.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31995730"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31995730"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Kyungdeok Kim, Wangyong Shin, Muwon Kang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Presynaptic PTPσ regulates postsynaptic NMDA receptor function through direct adhesion-independent mechanisms."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.54224"}], "href": "https://doi.org/10.7554/eLife.54224"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32142410"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32142410"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Javier Emperador-Melero, Giovanni de Nola, Pascal S Kaeser "}, {"type": "b", "children": [{"type": "t", "text": "Intact synapse structure and function after combined knockout of PTPδ, PTPσ, and LAR."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.66638"}], "href": "https://doi.org/10.7554/eLife.66638"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33656439"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33656439"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Sivan Cohen, Or-yam Shoshana, Einat Zelman-Toister, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The cytokine midkine and its receptor RPTPζ regulate B cell survival in a pathway induced by CD74."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.1101468"}], "href": "https://doi.org/10.4049/jimmunol.1101468"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22140262"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22140262"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Katherine Stewart, Noriko Uetani, Wiljan Hendriks, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inactivation of LAR family phosphatase genes Ptprs and Ptprf causes craniofacial malformations resembling Pierre-Robin sequence."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Development (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/dev.094532"}], "href": "https://doi.org/10.1242/dev.094532"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23863482"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23863482"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Ryan Murchie, Cong-Hui Guo, Avinash Persaud, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase σ targets apical junction complex proteins in the intestine and regulates epithelial permeability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1315017111"}], "href": "https://doi.org/10.1073/pnas.1315017111"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24385580"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24385580"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Mamle Quarmyne, Phuong L Doan, Heather A Himburg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein tyrosine phosphatase-σ regulates hematopoietic stem cell-repopulating capacity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI77866"}], "href": "https://doi.org/10.1172/JCI77866"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25415437"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25415437"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Karen M Doody, Stephanie M Stanford, Cristiano Sacchetti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Targeting phosphatase-dependent proteoglycan switch for rheumatoid arthritis therapy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Transl Med (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/scitranslmed.aaa4616"}], "href": "https://doi.org/10.1126/scitranslmed.aaa4616"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25995222"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25995222"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Anna Bunin, Vanja Sisirak, Hiyaa S Ghosh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein Tyrosine Phosphatase PTPRS Is an Inhibitory Receptor on Human and Murine Plasmacytoid Dendritic Cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Immunity (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.immuni.2015.07.009"}], "href": "https://doi.org/10.1016/j.immuni.2015.07.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26231120"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26231120"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Hajime Hamasaki, Masashi Fujitani, Toshihide Yamashita "}, {"type": "b", "children": [{"type": "t", "text": "NME2 associates with PTPσ to transduce signals from chondroitin sulfate proteoglycans."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2016.02.042"}], "href": "https://doi.org/10.1016/j.bbrc.2016.02.042"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26896769"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26896769"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Yasuhiro Katagiri, Ashlea A Morgan, Panpan Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of novel binding sites for heparin in receptor protein-tyrosine phosphatase (RPTPσ): Implications for proteoglycan signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.RA118.003081"}], "href": "https://doi.org/10.1074/jbc.RA118.003081"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29880643"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29880643"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Fucheng Luo, Amanda Phuong Tran, Li Xin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Modulation of proteoglycan receptor PTPσ enhances MMP-2 activity to promote recovery from multiple sclerosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-018-06505-6"}], "href": "https://doi.org/10.1038/s41467-018-06505-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30297691"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30297691"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Christina M Termini, Amara Pang, Destiny M Batton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteoglycans regulate protein tyrosine phosphatase receptor σ organization on hematopoietic stem/progenitor cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Hematol (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.exphem.2021.01.005"}], "href": "https://doi.org/10.1016/j.exphem.2021.01.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33515635"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33515635"}]}]}]}
Synonyms CDC14BRETRO
Proteins CC14C_HUMAN
NCBI Gene ID 168448
API
Download Associations
Predicted Functions View CDC14C's ARCHS4 Predicted Functions.
Co-expressed Genes View CDC14C's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View CDC14C's ARCHS4 Predicted Functions.

Functional Associations

CDC14C has 1,064 functional associations with biological entities spanning 8 categories (molecular profile, organism, functional term, phrase or reference, disease, phenotype or trait, chemical, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 52 datasets.

Click the + buttons to view associations for CDC14C from the datasets below.

If available, associations are ranked by standardized value

Dataset Summary
Achilles Cell Line Gene Essentiality Profiles cell lines with fitness changed by CDC14C gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles tissues with high or low expression of CDC14C gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles tissue samples with high or low expression of CDC14C gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles tissues with high or low expression of CDC14C gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
CCLE Cell Line Gene CNV Profiles cell lines with high or low copy number of CDC14C gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
CCLE Cell Line Gene Expression Profiles cell lines with high or low expression of CDC14C gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
ChEA Transcription Factor Binding Site Profiles transcription factor binding site profiles with transcription factor binding evidence at the promoter of CDC14C gene from the CHEA Transcription Factor Binding Site Profiles dataset.
ChEA Transcription Factor Targets transcription factors binding the promoter of CDC14C gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
ChEA Transcription Factor Targets 2022 transcription factors binding the promoter of CDC14C gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
CM4AI KOLF21J CRISPRi Gene Perturbation Atlas gene perturbations changing expression of CDC14C gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
COMPARTMENTS Curated Protein Localization Evidence Scores cellular components containing CDC14C protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
COMPARTMENTS Curated Protein Localization Evidence Scores 2025 cellular components containing CDC14C protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 cellular components co-occuring with CDC14C protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
COSMIC Cell Line Gene CNV Profiles cell lines with high or low copy number of CDC14C gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
DISEASES Experimental Gene-Disease Association Evidence Scores 2025 diseases associated with CDC14C gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
DISEASES Text-mining Gene-Disease Association Evidence Scores 2025 diseases co-occuring with CDC14C gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
ENCODE Histone Modification Site Profiles histone modification site profiles with high histone modification abundance at CDC14C gene from the ENCODE Histone Modification Site Profiles dataset.
ENCODE Transcription Factor Binding Site Profiles transcription factor binding site profiles with transcription factor binding evidence at the promoter of CDC14C gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
ENCODE Transcription Factor Targets transcription factors binding the promoter of CDC14C gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
GEO Signatures of Differentially Expressed Genes for Diseases disease perturbations changing expression of CDC14C gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.
GEO Signatures of Differentially Expressed Genes for Gene Perturbations gene perturbations changing expression of CDC14C gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.
GEO Signatures of Differentially Expressed Genes for Kinase Perturbations kinase perturbations changing expression of CDC14C gene from the GEO Signatures of Differentially Expressed Genes for Kinase Perturbations dataset.
GEO Signatures of Differentially Expressed Genes for Small Molecules small molecule perturbations changing expression of CDC14C gene from the GEO Signatures of Differentially Expressed Genes for Small Molecules dataset.
GEO Signatures of Differentially Expressed Genes for Transcription Factor Perturbations transcription factor perturbations changing expression of CDC14C gene from the GEO Signatures of Differentially Expressed Genes for Transcription Factor Perturbations dataset.
GEO Signatures of Differentially Expressed Genes for Viral Infections virus perturbations changing expression of CDC14C gene from the GEO Signatures of Differentially Expressed Genes for Viral Infections dataset.
GO Biological Process Annotations 2023 biological processes involving CDC14C gene from the curated GO Biological Process Annotations 2023 dataset.
GO Biological Process Annotations 2025 biological processes involving CDC14C gene from the curated GO Biological Process Annotations2025 dataset.
GO Cellular Component Annotations 2023 cellular components containing CDC14C protein from the curated GO Cellular Component Annotations 2023 dataset.
GO Cellular Component Annotations 2025 cellular components containing CDC14C protein from the curated GO Cellular Component Annotations 2025 dataset.
GO Molecular Function Annotations 2023 molecular functions performed by CDC14C gene from the curated GO Molecular Function Annotations 2023 dataset.
GO Molecular Function Annotations 2025 molecular functions performed by CDC14C gene from the curated GO Molecular Function Annotations 2025 dataset.
GTEx eQTL 2025 SNPs regulating expression of CDC14C gene from the GTEx eQTL 2025 dataset.
GTEx Tissue Gene Expression Profiles 2023 tissues with high or low expression of CDC14C gene relative to other tissues from the GTEx Tissue Gene Expression Profiles 2023 dataset.
GWAS Catalog SNP-Phenotype Associations 2025 phenotypes associated with CDC14C gene in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.
HMDB Metabolites of Enzymes interacting metabolites for CDC14C protein from the curated HMDB Metabolites of Enzymes dataset.
JASPAR Predicted Human Transcription Factor Targets 2025 transcription factors regulating expression of CDC14C gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Human Transcription Factor Targets dataset.
JASPAR Predicted Transcription Factor Targets transcription factors regulating expression of CDC14C gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Transcription Factor Targets dataset.
KEGG Pathways 2026 pathways involving CDC14C protein from the KEGG Pathways 2026 dataset.
Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles cell lines with high or low copy number of CDC14C gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset.
KnockTF Gene Expression Profiles with Transcription Factor Perturbations transcription factor perturbations changing expression of CDC14C gene from the KnockTF Gene Expression Profiles with Transcription Factor Perturbations dataset.
LOCATE Curated Protein Localization Annotations cellular components containing CDC14C protein in low- or high-throughput protein localization assays from the LOCATE Curated Protein Localization Annotations dataset.
LOCATE Predicted Protein Localization Annotations cellular components predicted to contain CDC14C protein from the LOCATE Predicted Protein Localization Annotations dataset.
MGI Mouse Phenotype Associations 2023 phenotypes of transgenic mice caused by CDC14C gene mutations from the MGI Mouse Phenotype Associations 2023 dataset.
Roadmap Epigenomics Histone Modification Site Profiles histone modification site profiles with high histone modification abundance at CDC14C gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset.
Rummagene Transcription Factor Associations 2026 transcription factors regulating expression of CDC14C gene from the Rummagene Transcription Factor Associations 2026 dataset.
RummaGEO Drug Perturbation Signatures drug perturbations changing expression of CDC14C gene from the RummaGEO Drug Perturbation Signatures dataset.
RummaGEO Gene Perturbation Signatures gene perturbations changing expression of CDC14C gene from the RummaGEO Gene Perturbation Signatures dataset.
TCGA Signatures of Differentially Expressed Genes for Tumors tissue samples with high or low expression of CDC14C gene relative to other tissue samples from the TCGA Signatures of Differentially Expressed Genes for Tumors dataset.
TISSUES Curated Tissue Protein Expression Evidence Scores tissues with high expression of CDC14C protein from the TISSUES Curated Tissue Protein Expression Evidence Scores dataset.
TISSUES Curated Tissue Protein Expression Evidence Scores 2025 tissues with high expression of CDC14C protein from the TISSUES Curated Tissue Protein Expression Evidence Scores 2025 dataset.
TISSUES Text-mining Tissue Protein Expression Evidence Scores tissues co-occuring with CDC14C protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores dataset.
TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 tissues co-occuring with CDC14C protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset.