ID STK26_HUMAN Reviewed; 416 AA. AC Q9P289; B2RAU2; Q3ZB77; Q8NC04; Q9BXC3; Q9BXC4; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 2. DT 27-MAR-2024, entry version 187. DE RecName: Full=Serine/threonine-protein kinase 26 {ECO:0000305}; DE EC=2.7.11.1 {ECO:0000269|PubMed:11641781, ECO:0000269|PubMed:29232556}; DE AltName: Full=MST3 and SOK1-related kinase {ECO:0000303|PubMed:11741893}; DE AltName: Full=Mammalian STE20-like protein kinase 4 {ECO:0000303|PubMed:11641781}; DE Short=MST-4 {ECO:0000305}; DE Short=STE20-like kinase MST4 {ECO:0000305}; DE AltName: Full=Serine/threonine-protein kinase MASK {ECO:0000305}; GN Name=STK26 {ECO:0000312|HGNC:HGNC:18174}; GN Synonyms=MASK {ECO:0000303|PubMed:11741893}, MST4 GN {ECO:0000303|PubMed:11641781}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11641781; DOI=10.1038/sj.onc.1204818; RA Lin J.-L., Chen H.-C., Fang H.-I., Robinson D., Kung H.-J., Shih H.-M.; RT "MST4, a new Ste20-related kinase that mediates cell growth and RT transformation via modulating ERK pathway."; RL Oncogene 20:6559-6569(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Fetal brain; RX PubMed=11306563; DOI=10.1074/jbc.m009323200; RA Qian Z., Lin C., Espinosa R., LeBeau M., Rosner M.R.; RT "Cloning and characterization of MST4, a novel Ste20-like kinase."; RL J. Biol. Chem. 276:22439-22445(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11741893; DOI=10.1074/jbc.m110882200; RA Dan I., Ong S.E., Watanabe N.M., Blagoev B., Nielsen M.M., Kajikawa E., RA Kristiansen T.Z., Mann M., Pandey A.; RT "Cloning of MASK, a novel member of the mammalian germinal center kinase RT III subfamily, with apoptosis-inducing properties."; RL J. Biol. Chem. 277:5929-5939(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-178, INTERACTION WITH GOLGA2, RP AND ACTIVITY REGULATION. RX PubMed=15037601; DOI=10.1083/jcb.200310061; RA Preisinger C., Short B., De Corte V., Bruyneel E., Haas A., Kopajtich R., RA Gettemans J., Barr F.A.; RT "YSK1 is activated by the Golgi matrix protein GM130 and plays a role in RT cell migration through its substrate 14-3-3zeta."; RL J. Cell Biol. 164:1009-1020(2004). RN [10] RP INTERACTION WITH PDCD10, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17360971; DOI=10.1091/mbc.e06-07-0608; RA Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X., RA Ma D.; RT "PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and RT transformation via modulation of the ERK pathway."; RL Mol. Biol. Cell 18:1965-1978(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-178, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-304 AND SER-306, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP INTERACTION WITH PDCD10. RX PubMed=19370760; DOI=10.1002/humu.20996; RA Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E., RA Schulte-Merker S., Felbor U.; RT "Functional analyses of human and zebrafish 18-amino acid in-frame deletion RT pave the way for domain mapping of the cerebral cavernous malformation 3 RT protein."; RL Hum. Mutat. 30:1003-1011(2009). RN [14] RP INTERACTION WITH CTTNBP2NL. RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200; RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., RA Aebersold R., Raught B., Gingras A.C.; RT "A PP2A phosphatase high density interaction network identifies a novel RT striatin-interacting phosphatase and kinase complex linked to the cerebral RT cavernous malformation 3 (CCM3) protein."; RL Mol. Cell. Proteomics 8:157-171(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-4; THR-178 AND SER-300, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP INTERACTION WITH PDCD10 AND GOLGA2, AND SUBCELLULAR LOCATION. RX PubMed=20332113; DOI=10.1242/jcs.061341; RA Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.; RT "CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell RT orientation."; RL J. Cell Sci. 123:1274-1284(2010). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-4; SER-300; SER-304 AND SER-306, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; THR-178; SER-325; THR-327 RP AND THR-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] RP FUNCTION, INTERACTION WITH RIPOR1, AND SUBCELLULAR LOCATION. RX PubMed=27807006; DOI=10.1242/jcs.198614; RA Mardakheh F.K., Self A., Marshall C.J.; RT "RHO binding to FAM65A regulates Golgi reorientation during cell RT migration."; RL J. Cell Sci. 129:4466-4479(2016). RN [25] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-53. RX PubMed=29232556; DOI=10.1016/j.ccell.2017.11.005; RA Huang T., Kim C.K., Alvarez A.A., Pangeni R.P., Wan X., Song X., Shi T., RA Yang Y., Sastry N., Horbinski C.M., Lu S., Stupp R., Kessler J.A., RA Nishikawa R., Nakano I., Sulman E.P., Lu X., James C.D., Yin X.M., Hu B., RA Cheng S.Y.; RT "MST4 phosphorylation of ATG4B regulates autophagic activity, RT tumorigenicity, and radioresistance in glioblastoma."; RL Cancer Cell 32:840-855(2017). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-300 IN COMPLEX WITH QUINAZOLIN RP INHIBITOR, AND SUBUNIT. RX PubMed=20730082; DOI=10.1371/journal.pone.0011905; RA Record C.J., Chaikuad A., Rellos P., Das S., Pike A.C., Fedorov O., RA Marsden B.D., Knapp S., Lee W.H.; RT "Structural comparison of human mammalian ste20-like kinases."; RL PLoS ONE 5:E11905-E11905(2010). RN [27] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-9; TRP-36 AND CYS-45. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Serine/threonine-protein kinase that acts as a mediator of CC cell growth (PubMed:11641781, PubMed:17360971). Modulates apoptosis CC (PubMed:11641781, PubMed:17360971). In association with STK24 CC negatively regulates Golgi reorientation in polarized cell migration CC upon RHO activation (PubMed:27807006). Phosphorylates ATG4B at 'Ser- CC 383', thereby increasing autophagic flux (PubMed:29232556). CC {ECO:0000269|PubMed:11641781, ECO:0000269|PubMed:17360971, CC ECO:0000269|PubMed:27807006, ECO:0000269|PubMed:29232556}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:11641781, ECO:0000269|PubMed:29232556}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11641781}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q9Y4P1}; CC -!- ACTIVITY REGULATION: Interaction with Golgi matrix protein GOLGA2 leads CC to autophosphorylation on Thr-178, possibly as a consequence of CC stabilization of dimer formation. May also be activated by C-terminal CC cleavage. {ECO:0000269|PubMed:15037601}. CC -!- SUBUNIT: Homodimer (PubMed:20730082). Interacts with PDCD10 CC (PubMed:17360971, PubMed:19370760, PubMed:20332113). Interacts with CC GOLGA2 (PubMed:15037601, PubMed:20332113). Interacts with CTTNBP2NL CC (PubMed:18782753). Interacts with RIPOR1 (via C-terminus); this CC interaction occurs in a PDCD10-dependent and Rho-independent manner CC (PubMed:27807006). Interacts with PDCD10; this interaction is required CC for the association of STK26 with RIPOR1 (PubMed:27807006). CC {ECO:0000269|PubMed:15037601, ECO:0000269|PubMed:17360971, CC ECO:0000269|PubMed:18782753, ECO:0000269|PubMed:19370760, CC ECO:0000269|PubMed:20332113, ECO:0000269|PubMed:20730082, CC ECO:0000269|PubMed:27807006}. CC -!- INTERACTION: CC Q9P289; Q9Y376: CAB39; NbExp=6; IntAct=EBI-618239, EBI-306905; CC Q9P289; P13569: CFTR; NbExp=6; IntAct=EBI-618239, EBI-349854; CC Q9P289; Q9P2B4: CTTNBP2NL; NbExp=5; IntAct=EBI-618239, EBI-1774273; CC Q9P289; Q08379: GOLGA2; NbExp=6; IntAct=EBI-618239, EBI-618309; CC Q9P289; Q9BUL8: PDCD10; NbExp=8; IntAct=EBI-618239, EBI-740195; CC Q9P289; Q9P289: STK26; NbExp=4; IntAct=EBI-618239, EBI-618239; CC Q9P289; Q5VSL9: STRIP1; NbExp=3; IntAct=EBI-618239, EBI-1773588; CC Q9P289-1; Q9Y376: CAB39; NbExp=10; IntAct=EBI-15996971, EBI-306905; CC Q9P289-1; Q9BUL8: PDCD10; NbExp=10; IntAct=EBI-15996971, EBI-740195; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17360971, CC ECO:0000269|PubMed:27807006}. Golgi apparatus CC {ECO:0000269|PubMed:15037601, ECO:0000269|PubMed:27807006}. CC Note=Colocalized with RIPOR1 in the Golgi of serum-starved cells and CC relocated to cytoplasmic punctae, probably vesicular compartments, CC along with RIPOR1 upon serum stimulation in a Rho- and PDCD10-dependent CC manner (PubMed:27807006). {ECO:0000269|PubMed:27807006}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9P289-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P289-2; Sequence=VSP_041469; CC Name=3; Synonyms=MST4a; CC IsoId=Q9P289-3; Sequence=VSP_041470; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF231012; AAK38484.1; -; mRNA. DR EMBL; AF344882; AAK29620.1; -; mRNA. DR EMBL; AF344883; AAK29621.1; -; mRNA. DR EMBL; AB040057; BAA92785.2; -; mRNA. DR EMBL; BT020099; AAV38902.1; -; mRNA. DR EMBL; AK075107; BAC11406.1; -; mRNA. DR EMBL; AK314356; BAG36989.1; -; mRNA. DR EMBL; AL109749; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471107; EAX11786.1; -; Genomic_DNA. DR EMBL; CH471107; EAX11787.1; -; Genomic_DNA. DR EMBL; BC098315; AAH98315.1; -; mRNA. DR EMBL; BC103503; AAI03504.1; -; mRNA. DR CCDS; CCDS14631.1; -. [Q9P289-1] DR CCDS; CCDS43995.1; -. [Q9P289-3] DR CCDS; CCDS48168.1; -. [Q9P289-2] DR RefSeq; NP_001035917.1; NM_001042452.1. [Q9P289-3] DR RefSeq; NP_001035918.1; NM_001042453.1. [Q9P289-2] DR RefSeq; NP_057626.2; NM_016542.3. [Q9P289-1] DR PDB; 3GGF; X-ray; 2.35 A; A/B=1-300. DR PDB; 3W8I; X-ray; 2.40 A; B=346-416. DR PDB; 4FZA; X-ray; 3.15 A; B=18-297. DR PDB; 4FZD; X-ray; 3.25 A; B=18-297, C=323-327. DR PDB; 4FZF; X-ray; 3.64 A; B=18-297. DR PDB; 4GEH; X-ray; 1.95 A; B/D=325-413. DR PDB; 5XY9; X-ray; 2.30 A; C/D=314-325. DR PDB; 5YF4; X-ray; 1.90 A; B=320-335. DR PDB; 7B36; X-ray; 2.11 A; A/C=1-300. DR PDBsum; 3GGF; -. DR PDBsum; 3W8I; -. DR PDBsum; 4FZA; -. DR PDBsum; 4FZD; -. DR PDBsum; 4FZF; -. DR PDBsum; 4GEH; -. DR PDBsum; 5XY9; -. DR PDBsum; 5YF4; -. DR PDBsum; 7B36; -. DR AlphaFoldDB; Q9P289; -. DR SMR; Q9P289; -. DR BioGRID; 119722; 230. DR DIP; DIP-34049N; -. DR IntAct; Q9P289; 52. DR MINT; Q9P289; -. DR STRING; 9606.ENSP00000377867; -. DR BindingDB; Q9P289; -. DR ChEMBL; CHEMBL5941; -. DR DrugBank; DB07853; 2-[4-[4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl]iminocyclohexa-2,5-dien-1-yl]acetonitrile. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q9P289; -. DR GlyGen; Q9P289; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9P289; -. DR PhosphoSitePlus; Q9P289; -. DR SwissPalm; Q9P289; -. DR BioMuta; STK26; -. DR DMDM; 73621232; -. DR EPD; Q9P289; -. DR jPOST; Q9P289; -. DR MassIVE; Q9P289; -. DR MaxQB; Q9P289; -. DR PaxDb; 9606-ENSP00000377867; -. DR PeptideAtlas; Q9P289; -. DR ProteomicsDB; 83756; -. [Q9P289-1] DR ProteomicsDB; 83757; -. [Q9P289-2] DR ProteomicsDB; 83758; -. [Q9P289-3] DR Pumba; Q9P289; -. DR Antibodypedia; 30220; 344 antibodies from 37 providers. DR DNASU; 51765; -. DR Ensembl; ENST00000394334.7; ENSP00000377867.2; ENSG00000134602.16. [Q9P289-1] DR Ensembl; ENST00000394335.6; ENSP00000377868.2; ENSG00000134602.16. [Q9P289-2] DR Ensembl; ENST00000496850.1; ENSP00000419702.1; ENSG00000134602.16. [Q9P289-3] DR GeneID; 51765; -. DR KEGG; hsa:51765; -. DR MANE-Select; ENST00000394334.7; ENSP00000377867.2; NM_016542.4; NP_057626.2. DR UCSC; uc004ewk.2; human. [Q9P289-1] DR AGR; HGNC:18174; -. DR CTD; 51765; -. DR DisGeNET; 51765; -. DR GeneCards; STK26; -. DR HGNC; HGNC:18174; STK26. DR HPA; ENSG00000134602; Tissue enhanced (bone marrow, epididymis). DR MIM; 300547; gene. DR neXtProt; NX_Q9P289; -. DR OpenTargets; ENSG00000134602; -. DR VEuPathDB; HostDB:ENSG00000134602; -. DR eggNOG; KOG0201; Eukaryota. DR GeneTree; ENSGT00940000157904; -. DR HOGENOM; CLU_000288_63_23_1; -. DR InParanoid; Q9P289; -. DR OrthoDB; 152877at2759; -. DR PhylomeDB; Q9P289; -. DR PathwayCommons; Q9P289; -. DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins. DR SignaLink; Q9P289; -. DR SIGNOR; Q9P289; -. DR BioGRID-ORCS; 51765; 18 hits in 777 CRISPR screens. DR ChiTaRS; STK26; human. DR EvolutionaryTrace; Q9P289; -. DR GeneWiki; MST4; -. DR GenomeRNAi; 51765; -. DR Pharos; Q9P289; Tchem. DR PRO; PR:Q9P289; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9P289; Protein. DR Bgee; ENSG00000134602; Expressed in germinal epithelium of ovary and 175 other cell types or tissues. DR ExpressionAtlas; Q9P289; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0012506; C:vesicle membrane; TAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB. DR GO; GO:0030033; P:microvillus assembly; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB. DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IMP:UniProtKB. DR CDD; cd06640; STKc_MST4; 1. DR Gene3D; 1.10.12.70; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR046409; PDC10_dimerisation_sf. DR InterPro; IPR048288; PDCD10_N. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR035056; STK_MST4. DR PANTHER; PTHR48012:SF7; SERINE_THREONINE-PROTEIN KINASE 26; 1. DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1. DR Pfam; PF20929; PDCD10_N; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q9P289; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding; KW Cytoplasm; Golgi apparatus; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CHAIN 2..416 FT /note="Serine/threonine-protein kinase 26" FT /id="PRO_0000086404" FT DOMAIN 24..274 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 297..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 144 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 30..38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 53 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000305|PubMed:29232556" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 178 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:15037601, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 306 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99JT2" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 327 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 328 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 15..91 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041469" FT VAR_SEQ 200..261 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11306563" FT /id="VSP_041470" FT VARIANT 9 FT /note="Q -> R (in dbSNP:rs56035648)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040844" FT VARIANT 36 FT /note="G -> W (in a gastric adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040845" FT VARIANT 45 FT /note="R -> C (in dbSNP:rs56044451)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040846" FT MUTAGEN 53 FT /note="K->E: Abolished serine/threonine-protein kinase FT activity." FT /evidence="ECO:0000269|PubMed:29232556" FT HELIX 20..23 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 24..31 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:4FZD" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:7B36" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 49..56 FT /evidence="ECO:0007829|PDB:7B36" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:4FZD" FT HELIX 61..63 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 64..76 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:3GGF" FT HELIX 107..111 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 118..137 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:3GGF" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:7B36" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:4FZD" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:4FZA" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:4FZA" FT HELIX 188..191 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 199..214 FT /evidence="ECO:0007829|PDB:7B36" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 224..233 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:4FZA" FT HELIX 245..254 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 272..277 FT /evidence="ECO:0007829|PDB:7B36" FT HELIX 282..296 FT /evidence="ECO:0007829|PDB:7B36" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:5YF4" FT HELIX 346..350 FT /evidence="ECO:0007829|PDB:3W8I" FT HELIX 352..355 FT /evidence="ECO:0007829|PDB:4GEH" FT HELIX 357..366 FT /evidence="ECO:0007829|PDB:4GEH" FT TURN 367..370 FT /evidence="ECO:0007829|PDB:3W8I" FT HELIX 372..391 FT /evidence="ECO:0007829|PDB:4GEH" FT HELIX 395..409 FT /evidence="ECO:0007829|PDB:4GEH" SQ SEQUENCE 416 AA; 46529 MW; 3E31B7E3CBDA5768 CRC64; MAHSPVAVQV PGMQNNIADP EELFTKLERI GKGSFGEVFK GIDNRTQQVV AIKIIDLEEA EDEIEDIQQE ITVLSQCDSS YVTKYYGSYL KGSKLWIIME YLGGGSALDL LRAGPFDEFQ IATMLKEILK GLDYLHSEKK IHRDIKAANV LLSEQGDVKL ADFGVAGQLT DTQIKRNTFV GTPFWMAPEV IQQSAYDSKA DIWSLGITAI ELAKGEPPNS DMHPMRVLFL IPKNNPPTLV GDFTKSFKEF IDACLNKDPS FRPTAKELLK HKFIVKNSKK TSYLTELIDR FKRWKAEGHS DDESDSEGSD SESTSRENNT HPEWSFTTVR KKPDPKKVQN GAEQDLVQTL SCLSMIITPA FAELKQQDEN NASRNQAIEE LEKSIAVAEA ACPGITDKMV KKLIEKFQKC SADESP //