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Serine/threonine-protein kinase 26 (EC 2.7.11.1) (MST3 and SOK1-related kinase) (Mammalian STE20-like protein kinase 4) (MST-4) (STE20-like kinase MST4) (Serine/threonine-protein kinase MASK)

 STK26_HUMAN             Reviewed;         416 AA.
Q9P289; B2RAU2; Q3ZB77; Q8NC04; Q9BXC3; Q9BXC4;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
27-SEP-2017, entry version 150.
RecName: Full=Serine/threonine-protein kinase 26 {ECO:0000305};
EC=2.7.11.1 {ECO:0000269|PubMed:11641781};
AltName: Full=MST3 and SOK1-related kinase {ECO:0000303|PubMed:11741893};
AltName: Full=Mammalian STE20-like protein kinase 4 {ECO:0000303|PubMed:11641781};
Short=MST-4 {ECO:0000305};
Short=STE20-like kinase MST4 {ECO:0000305};
AltName: Full=Serine/threonine-protein kinase MASK {ECO:0000305};
Name=STK26 {ECO:0000312|HGNC:HGNC:18174};
Synonyms=MASK {ECO:0000303|PubMed:11741893},
MST4 {ECO:0000303|PubMed:11641781};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=11641781; DOI=10.1038/sj.onc.1204818;
Lin J.-L., Chen H.-C., Fang H.-I., Robinson D., Kung H.-J.,
Shih H.-M.;
"MST4, a new Ste20-related kinase that mediates cell growth and
transformation via modulating ERK pathway.";
Oncogene 20:6559-6569(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
TISSUE=Fetal brain;
PubMed=11306563; DOI=10.1074/jbc.M009323200;
Qian Z., Lin C., Espinosa R., LeBeau M., Rosner M.R.;
"Cloning and characterization of MST4, a novel Ste20-like kinase.";
J. Biol. Chem. 276:22439-22445(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11741893; DOI=10.1074/jbc.M110882200;
Dan I., Ong S.E., Watanabe N.M., Blagoev B., Nielsen M.M.,
Kajikawa E., Kristiansen T.Z., Mann M., Pandey A.;
"Cloning of MASK, a novel member of the mammalian germinal center
kinase III subfamily, with apoptosis-inducing properties.";
J. Biol. Chem. 277:5929-5939(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-178, INTERACTION WITH
GOLGA2, AND ENZYME REGULATION.
PubMed=15037601; DOI=10.1083/jcb.200310061;
Preisinger C., Short B., De Corte V., Bruyneel E., Haas A.,
Kopajtich R., Gettemans J., Barr F.A.;
"YSK1 is activated by the Golgi matrix protein GM130 and plays a role
in cell migration through its substrate 14-3-3zeta.";
J. Cell Biol. 164:1009-1020(2004).
[10]
INTERACTION WITH PDCD10, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17360971; DOI=10.1091/mbc.E06-07-0608;
Ma X., Zhao H., Shan J., Long F., Chen Y., Chen Y., Zhang Y., Han X.,
Ma D.;
"PDCD10 interacts with Ste20-related kinase MST4 to promote cell
growth and transformation via modulation of the ERK pathway.";
Mol. Biol. Cell 18:1965-1978(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-178, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-304 AND
SER-306, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
INTERACTION WITH PDCD10.
PubMed=19370760; DOI=10.1002/humu.20996;
Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E.,
Schulte-Merker S., Felbor U.;
"Functional analyses of human and zebrafish 18-amino acid in-frame
deletion pave the way for domain mapping of the cerebral cavernous
malformation 3 protein.";
Hum. Mutat. 30:1003-1011(2009).
[14]
INTERACTION WITH CTTNBP2NL.
PubMed=18782753; DOI=10.1074/mcp.M800266-MCP200;
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
Aebersold R., Raught B., Gingras A.C.;
"A PP2A phosphatase high density interaction network identifies a
novel striatin-interacting phosphatase and kinase complex linked to
the cerebral cavernous malformation 3 (CCM3) protein.";
Mol. Cell. Proteomics 8:157-171(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; THR-178 AND SER-300, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
INTERACTION WITH PDCD10 AND GOLGA2, AND SUBCELLULAR LOCATION.
PubMed=20332113; DOI=10.1242/jcs.061341;
Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J.;
"CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and
cell orientation.";
J. Cell Sci. 123:1274-1284(2010).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4; SER-300; SER-304 AND SER-306, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; THR-178; SER-325;
THR-327 AND THR-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
FUNCTION, INTERACTION WITH RIPOR1, AND SUBCELLULAR LOCATION.
PubMed=27807006; DOI=10.1242/jcs.198614;
Mardakheh F.K., Self A., Marshall C.J.;
"RHO binding to FAM65A regulates Golgi reorientation during cell
migration.";
J. Cell Sci. 129:4466-4479(2016).
[25]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-300 IN COMPLEX WITH
QUINAZOLIN INHIBITOR, AND SUBUNIT.
PubMed=20730082; DOI=10.1371/journal.pone.0011905;
Record C.J., Chaikuad A., Rellos P., Das S., Pike A.C., Fedorov O.,
Marsden B.D., Knapp S., Lee W.H.;
"Structural comparison of human mammalian ste20-like kinases.";
PLoS ONE 5:E11905-E11905(2010).
[26]
VARIANTS [LARGE SCALE ANALYSIS] ARG-9; TRP-36 AND CYS-45.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Mediator of cell growth (PubMed:11641781,
PubMed:17360971). Modulates apoptosis (PubMed:11641781,
PubMed:17360971). In association with STK24 negatively regulates
Golgi reorientation in polarized cell migration upon RHO
activation (PubMed:27807006). {ECO:0000269|PubMed:11641781,
ECO:0000269|PubMed:17360971, ECO:0000269|PubMed:27807006}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11641781}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Interaction with Golgi matrix protein GOLGA2
leads to autophosphorylation on Thr-178, possibly as a consequence
of stabilization of dimer formation. May also be activated by C-
terminal cleavage. {ECO:0000269|PubMed:15037601}.
-!- SUBUNIT: Homodimer (PubMed:20730082). Interacts with PDCD10
(PubMed:17360971, PubMed:19370760, PubMed:20332113). Interacts
with GOLGA2 (PubMed:15037601, PubMed:20332113). Interacts with
CTTNBP2NL (PubMed:18782753). Interacts with RIPOR1 (via C-
terminus); this interaction occurs in a PDCD10-dependent and Rho-
independent manner (PubMed:27807006). Interacts with PDCD10; this
interaction is required for the association of STK26 with RIPOR1
(PubMed:27807006). {ECO:0000269|PubMed:15037601,
ECO:0000269|PubMed:17360971, ECO:0000269|PubMed:18782753,
ECO:0000269|PubMed:19370760, ECO:0000269|PubMed:20332113,
ECO:0000269|PubMed:20730082, ECO:0000269|PubMed:27807006}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-618239, EBI-618239;
Q9Y376:CAB39; NbExp=6; IntAct=EBI-618239, EBI-306905;
Q9P2B4:CTTNBP2NL; NbExp=4; IntAct=EBI-618239, EBI-1774273;
Q08379:GOLGA2; NbExp=4; IntAct=EBI-618239, EBI-618309;
Q9BUL8:PDCD10; NbExp=9; IntAct=EBI-618239, EBI-740195;
Q5VSL9:STRIP1; NbExp=2; IntAct=EBI-618239, EBI-1773588;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17360971,
ECO:0000269|PubMed:27807006}. Golgi apparatus
{ECO:0000269|PubMed:15037601, ECO:0000269|PubMed:27807006}.
Note=Colocalized with RIPOR1 in the Golgi of serum-starved cells
and relocated to cytoplasmic punctae, probably vesicular
compartments, along with RIPOR1 upon serum stimulation in a
Rho- and PDCD10-dependent manner (PubMed:27807006).
{ECO:0000269|PubMed:27807006}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9P289-1; Sequence=Displayed;
Name=2;
IsoId=Q9P289-2; Sequence=VSP_041469;
Name=3; Synonyms=MST4a;
IsoId=Q9P289-3; Sequence=VSP_041470;
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF231012; AAK38484.1; -; mRNA.
EMBL; AF344882; AAK29620.1; -; mRNA.
EMBL; AF344883; AAK29621.1; -; mRNA.
EMBL; AB040057; BAA92785.2; -; mRNA.
EMBL; BT020099; AAV38902.1; -; mRNA.
EMBL; AK075107; BAC11406.1; -; mRNA.
EMBL; AK314356; BAG36989.1; -; mRNA.
EMBL; AL109749; CAI42079.1; -; Genomic_DNA.
EMBL; CH471107; EAX11786.1; -; Genomic_DNA.
EMBL; CH471107; EAX11787.1; -; Genomic_DNA.
EMBL; BC098315; AAH98315.1; -; mRNA.
EMBL; BC103503; AAI03504.1; -; mRNA.
CCDS; CCDS14631.1; -. [Q9P289-1]
CCDS; CCDS43995.1; -. [Q9P289-3]
CCDS; CCDS48168.1; -. [Q9P289-2]
RefSeq; NP_001035917.1; NM_001042452.1. [Q9P289-3]
RefSeq; NP_001035918.1; NM_001042453.1. [Q9P289-2]
RefSeq; NP_057626.2; NM_016542.3. [Q9P289-1]
UniGene; Hs.444247; -.
PDB; 3GGF; X-ray; 2.35 A; A/B=1-300.
PDB; 3W8I; X-ray; 2.40 A; B=346-416.
PDB; 4FZA; X-ray; 3.15 A; B=18-297.
PDB; 4FZD; X-ray; 3.25 A; B=18-297, C=323-327.
PDB; 4FZF; X-ray; 3.64 A; B=18-297.
PDB; 4GEH; X-ray; 1.95 A; B/D=325-413.
PDBsum; 3GGF; -.
PDBsum; 3W8I; -.
PDBsum; 4FZA; -.
PDBsum; 4FZD; -.
PDBsum; 4FZF; -.
PDBsum; 4GEH; -.
ProteinModelPortal; Q9P289; -.
SMR; Q9P289; -.
BioGrid; 119722; 79.
DIP; DIP-34049N; -.
IntAct; Q9P289; 32.
STRING; 9606.ENSP00000377867; -.
BindingDB; Q9P289; -.
ChEMBL; CHEMBL5941; -.
GuidetoPHARMACOLOGY; 2287; -.
iPTMnet; Q9P289; -.
PhosphoSitePlus; Q9P289; -.
SwissPalm; Q9P289; -.
BioMuta; MST4; -.
DMDM; 73621232; -.
EPD; Q9P289; -.
MaxQB; Q9P289; -.
PaxDb; Q9P289; -.
PeptideAtlas; Q9P289; -.
PRIDE; Q9P289; -.
DNASU; 51765; -.
Ensembl; ENST00000394334; ENSP00000377867; ENSG00000134602. [Q9P289-1]
Ensembl; ENST00000394335; ENSP00000377868; ENSG00000134602. [Q9P289-2]
Ensembl; ENST00000496850; ENSP00000419702; ENSG00000134602. [Q9P289-3]
GeneID; 51765; -.
KEGG; hsa:51765; -.
UCSC; uc004ewk.2; human. [Q9P289-1]
CTD; 51765; -.
DisGeNET; 51765; -.
EuPathDB; HostDB:ENSG00000134602.15; -.
GeneCards; STK26; -.
HGNC; HGNC:18174; STK26.
HPA; HPA059921; -.
MIM; 300547; gene.
neXtProt; NX_Q9P289; -.
OpenTargets; ENSG00000134602; -.
eggNOG; KOG0201; Eukaryota.
eggNOG; ENOG410XP9G; LUCA.
GeneTree; ENSGT00810000125395; -.
HOGENOM; HOG000234203; -.
HOVERGEN; HBG108518; -.
InParanoid; Q9P289; -.
KO; K08838; -.
PhylomeDB; Q9P289; -.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
SignaLink; Q9P289; -.
SIGNOR; Q9P289; -.
EvolutionaryTrace; Q9P289; -.
GeneWiki; MST4; -.
GenomeRNAi; 51765; -.
PMAP-CutDB; Q9P289; -.
PRO; PR:Q9P289; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000134602; -.
ExpressionAtlas; Q9P289; baseline and differential.
Genevisible; Q9P289; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0012506; C:vesicle membrane; TAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0030033; P:microvillus assembly; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:1903205; P:regulation of hydrogen peroxide-induced cell death; IMP:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
CDD; cd06640; STKc_MST4; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR035056; STK_MST4.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Complete proteome; Cytoplasm; Golgi apparatus; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CHAIN 2 416 Serine/threonine-protein kinase 26.
/FTId=PRO_0000086404.
DOMAIN 24 274 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 178 178 Phosphothreonine; by autocatalysis.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15037601}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JT2}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 327 327 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 15 91 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041469.
VAR_SEQ 200 261 Missing (in isoform 3).
{ECO:0000303|PubMed:11306563}.
/FTId=VSP_041470.
VARIANT 9 9 Q -> R (in dbSNP:rs56035648).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040844.
VARIANT 36 36 G -> W (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040845.
VARIANT 45 45 R -> C (in dbSNP:rs56044451).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040846.
HELIX 20 23 {ECO:0000244|PDB:3GGF}.
STRAND 24 32 {ECO:0000244|PDB:3GGF}.
STRAND 34 43 {ECO:0000244|PDB:3GGF}.
TURN 44 46 {ECO:0000244|PDB:3GGF}.
STRAND 49 56 {ECO:0000244|PDB:3GGF}.
TURN 58 60 {ECO:0000244|PDB:4FZD}.
HELIX 63 74 {ECO:0000244|PDB:3GGF}.
STRAND 85 91 {ECO:0000244|PDB:3GGF}.
STRAND 94 100 {ECO:0000244|PDB:3GGF}.
STRAND 104 106 {ECO:0000244|PDB:3GGF}.
HELIX 107 111 {ECO:0000244|PDB:3GGF}.
HELIX 118 132 {ECO:0000244|PDB:3GGF}.
STRAND 138 142 {ECO:0000244|PDB:3GGF}.
HELIX 147 149 {ECO:0000244|PDB:3GGF}.
STRAND 150 152 {ECO:0000244|PDB:3GGF}.
STRAND 158 161 {ECO:0000244|PDB:3GGF}.
TURN 162 164 {ECO:0000244|PDB:4FZD}.
TURN 172 174 {ECO:0000244|PDB:4FZA}.
TURN 176 178 {ECO:0000244|PDB:4FZA}.
HELIX 188 191 {ECO:0000244|PDB:3GGF}.
HELIX 199 214 {ECO:0000244|PDB:3GGF}.
TURN 218 221 {ECO:0000244|PDB:3GGF}.
HELIX 224 233 {ECO:0000244|PDB:3GGF}.
STRAND 241 243 {ECO:0000244|PDB:4FZA}.
HELIX 245 254 {ECO:0000244|PDB:3GGF}.
HELIX 259 261 {ECO:0000244|PDB:3GGF}.
HELIX 265 269 {ECO:0000244|PDB:3GGF}.
HELIX 272 277 {ECO:0000244|PDB:3GGF}.
HELIX 281 284 {ECO:0000244|PDB:3GGF}.
HELIX 285 296 {ECO:0000244|PDB:3GGF}.
HELIX 346 350 {ECO:0000244|PDB:3W8I}.
HELIX 352 355 {ECO:0000244|PDB:4GEH}.
HELIX 357 366 {ECO:0000244|PDB:4GEH}.
TURN 367 370 {ECO:0000244|PDB:3W8I}.
HELIX 372 391 {ECO:0000244|PDB:4GEH}.
HELIX 395 409 {ECO:0000244|PDB:4GEH}.
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


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