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Using integrative analysis of over 3825 human phosphoproteomic studies, the work identifies major KIF21A phosphosites (S853, S1212, S1239) and examines co-regulation to infer kinase associations. S853 connects to cytoskeletal organization, while S1239 shows tumor-specific CDK18 correlations across cancers. Enrichment and pan-cancer results implicate cytoskeleton regulation, cell cycle control, and carcinogenesis, supported by gene-level validation of KIF21A-related regulators.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":40,"@type":76,"position":81},"https://docshare.wps.com/document/research-report/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/deciphering-site-specific-regulatory-networks-of-the-kinesin-protein-kif21a-through-integrative-phosphoproteomic-analysis/353309/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/deciphering-site-specific-regulatory-networks-of-the-kinesin-protein-kif21a-through-integrative-phosphoproteomic-analysis/353309.png","ImageObject",300,407,{"name":92,"@type":93},"awa","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-09-23","2026-09-22",true,{"@type":102,"interactionType":103,"userInteractionCount":8},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What dataset and analysis strategy were used to study KIF21A phosphorylation sites?","Question",{"text":112,"@type":113},"The study integrates more than 3825 human phosphoproteomics studies, then characterizes site-specific phosphorylation of KIF21A and analyzes co-regulation patterns to infer kinase associations and functional networks.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"Which KIF21A phosphosites are identified as predominant, and what do they suggest?",{"text":117,"@type":113},"The predominant phosphosites are S853, S1212, and S1239. S853 is strongly associated with cytoskeletal organization and cortical microtubule stabilization complexes, while S1239 shows tumor-specific correlations with CDK18 across multiple cancer types.",{"name":119,"@type":110,"acceptedAnswer":120},"How do the results connect KIF21A to cancer biology?",{"text":121,"@type":113},"Functional enrichment of co-regulated phosphoproteins highlights cytoskeleton regulation, cell cycle regulation, and carcinogenesis. 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Rai 1, Ayadathil Sujina 1, Mukhtar Ahmed 2, Sreeshma Ravindran Kammarambath 1, Suhail Subair 1, Athira Perunelly Gopalakrishnan 1, Apoorva Pai Kalasa Anil Kumar 1, Levin John 3, Rajesh Raju 1, * and Akhina Palollathil 1, *  \nAcademic Editor: Michael T. Wolfinger  \nReceived: 30 April 2026  \nRevised: 30 May 2026  \nAccepted: 7 June 2026  \nPublished: 18 July 2026  \nCopyright: © 2026 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.  \n1 Centre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore 575018, India; [shanmithabrai.ciods@yenepoya.edu.in](shanmithabrai.ciods@yenepoya.edu.in) (S.B.R.); [sujinaa.ciods@yenepoya.edu.in](sujinaa.ciods@yenepoya.edu.in) (A.S.)  \n2 Department of Zoology, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia; [mahmed1@ksu.edu.sa](mahmed1@ksu.edu.sa)  \n3 Institute for Regeneration and Repair, University of Edinburgh, Edinburgh EH16 4UU, UK; [vblevinjohn@gmail.com](vblevinjohn@gmail.com)  \n* Correspondence: rajrrnbt@gmail.com or [rajeshraju@yenepoya.edu.in](rajeshraju@yenepoya.edu.in) (R.R.);  \n[akhinap.ciods@yenepoya.edu.in](akhinap.ciods@yenepoya.edu.in) (A.P.)  \nAbstract  \nKIF21A, a member of the Kinesin-4 family of motor proteins, is involved in the regulation of microtubule dynamics and intracellular transport, with emerging evidence suggesting its potential role in cancer progression. In this study, we performed an integrative analysis of over 3825 human phosphoproteomics studies to characterize site-specific phosphorylation of KIF21A. Three predominant phosphosites were identified in KIF21A (S853, S1212, and S1239) with the highest detection frequency across phosphoproteomics studies, and were analyzed for co-regulation patterns to identify potential kinase associations and functional networks. Phosphosite S853 showed a strong association with cytoskeletal organization and cortical microtubule stabilization complexes (CMSCs) components, including KANK1 (S186), PHLDB2 (S513, S42) and CLASP1 (S600, S572, S646), indicating its role in cytoskeletal organization. Upstream kinase analysis identified potential regulators, such as PAK2, RPS6KA1/A3, RPS6KB1, CHEK1/2 and CDK18/16 with site-specific variability in their associations with KIF21A predominant sites. Interestingly, phosphosite-specific correlation analysis between KIF21A and candidate kinases revealed that the KIF21AS1239 phosphosite exhibited tumor-specific correlations with CDK18 across multiple cancer types. Functional enrichment revealed that co-regulated phosphoproteins were involved in cytoskeleton regulation, cell cycle regulation, and carcinogenesis. Pan-cancer analysis demonstrated dysregulated expression of KIF21A in multiple tumor types, with stageassociated upregulation in selected cancers. Gene-level validation further supported these findings, showing consistent positive correlations between KIF21A and key regulators such as CTNND1 and PTK2, as well as other cytoskeleton and cancer-associated genes. Overall, this study highlights site-specific phosphorylation as a key regulatory mechanism of KIF21A and suggests its involvement in cytoskeleton-associated signaling networks in cancer.  \nKeywords: KANK; CMSC; microtubule stabilization; WD-40 repeats; KIF21A; co-regulation  \n1. Introduction  \nKinesin superfamily proteins (KIFs) comprise a wide range of motor proteins that depend on microtubules and use ATP hydrolysis to move organelles, protein complexes, and mRNA around cells [1,2] . To date, more than 45 members in KIFs have been identified and are collectively classified into 14 distinct classes [3] . These include C-terminal kinesins, C-1 kinesin, and C-2 kinesin, a single class of M-","cbCaikV5X7r1uE0H","https://ap.wps.com/l/cbCaikV5X7r1uE0H","pdf",21338577,25,"English","# Introduction\n## Kinesin superfamily and Kinesin-4 overview\n## KIF21A structure and regulatory mechanisms\n## Disease relevance and prior findings","[{\"question\":\"What dataset and analysis strategy were used to study KIF21A phosphorylation sites?\",\"answer\":\"The study integrates more than 3825 human phosphoproteomics studies, then characterizes site-specific phosphorylation of KIF21A and analyzes co-regulation patterns to infer kinase associations and functional networks.\"},{\"question\":\"Which KIF21A phosphosites are identified as predominant, and what do they suggest?\",\"answer\":\"The predominant phosphosites are S853, S1212, and S1239. S853 is strongly associated with cytoskeletal organization and cortical microtubule stabilization complexes, while S1239 shows tumor-specific correlations with CDK18 across multiple cancer types.\"},{\"question\":\"How do the results connect KIF21A to cancer biology?\",\"answer\":\"Functional enrichment of co-regulated phosphoproteins highlights cytoskeleton regulation, cell cycle regulation, and carcinogenesis. Pan-cancer analysis shows dysregulated KIF21A expression across tumor types, with selected cancers showing stage-associated upregulation, further supported by gene-level validation of key regulators.\"}]","Deciphering Site-Specific Regulatory Networks of the Kinesin Protein KIF21A Through Integrative Phosphoproteomic Analysis | PDF",1790104635,63]