STK26_HUMAN
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 03-AUG-2022, entry version 178.
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},
GN MST4 {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; 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}.
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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; 166.
DR DIP; DIP-34049N; -.
DR IntAct; Q9P289; 51.
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; Q9P289; -.
DR PeptideAtlas; Q9P289; -.
DR PRIDE; Q9P289; -.
DR ProteomicsDB; 83756; -. [Q9P289-1]
DR ProteomicsDB; 83757; -. [Q9P289-2]
DR ProteomicsDB; 83758; -. [Q9P289-3]
DR Antibodypedia; 30220; 298 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 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; 1328688at2759; -.
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; 16 hits in 702 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 173 other tissues.
DR ExpressionAtlas; Q9P289; baseline and differential.
DR Genevisible; Q9P289; HS.
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:1903205; P:regulation of hydrogen peroxide-induced cell death; IMP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR CDD; cd06640; STKc_MST4; 1.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035056; STK_MST4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
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
