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Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1) (LKB1) (hLKB1) (Renal carcinoma antigen NY-REN-19)

 STK11_HUMAN             Reviewed;         433 AA.
Q15831; B2RBX7; E7EW76;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 196.
RecName: Full=Serine/threonine-protein kinase STK11;
EC=2.7.11.1;
AltName: Full=Liver kinase B1;
Short=LKB1;
Short=hLKB1;
AltName: Full=Renal carcinoma antigen NY-REN-19;
Flags: Precursor;
Name=STK11; Synonyms=LKB1, PJS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN PJS.
TISSUE=Liver;
PubMed=9425897; DOI=10.1038/ng0198-38;
Jenne D.E., Reimann H., Nezu J., Friedl W., Loff S., Jeschke R.,
Mueller O., Back W., Zimmer M.;
"Peutz-Jeghers syndrome is caused by mutations in a novel serine
threonine kinase.";
Nat. Genet. 18:38-43(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9537235;
Bignell G.R., Barfoot R., Seal S., Collins N., Warren W.,
Stratton M.R.;
"Low frequency of somatic mutations in the LKB1/Peutz-Jeghers syndrome
gene in sporadic breast cancer.";
Cancer Res. 58:1384-1386(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Uterus;
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).
[7]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[8]
INVOLVEMENT IN LUNG CANCER.
PubMed=11212897; DOI=10.1023/A:1006442024874;
Sobottka S.B., Haase M., Fitze G., Hahn M., Schackert H.K.,
Schackert G.;
"Frequent loss of heterozygosity at the 19p13.3 locus without
LKB1/STK11 mutations in human carcinoma metastases to the brain.";
J. Neurooncol. 49:187-195(2000).
[9]
IDENTIFICATION IN A TERNARY COMPLEX COMPOSED OF SMAD4 AND STK11IP, AND
INTERACTION WITH SMAD4 AND STK11IP.
PubMed=11741830; DOI=10.1093/hmg/10.25.2869;
Smith D.P., Rayter S.I., Niederlander C., Spicer J., Jones C.M.,
Ashworth A.;
"LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers
syndrome kinase LKB1.";
Hum. Mol. Genet. 10:2869-2877(2001).
[10]
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, FUNCTION, MUTAGENESIS OF
LYS-78 AND THR-189, AND PHOSPHORYLATION AT THR-189.
PubMed=11430832; DOI=10.1016/S1097-2765(01)00258-1;
Karuman P., Gozani O., Odze R.D., Zhou X.C., Zhu H., Shaw R.,
Brien T.P., Bozzuto C.D., Ooi D., Cantley L.C., Yuan J.;
"The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent
cell death.";
Mol. Cell 7:1307-1319(2001).
[11]
INVOLVEMENT IN LUNG CANCER.
PubMed=12097271;
Sanchez-Cespedes M., Parrella P., Esteller M., Nomoto S., Trink B.,
Engles J.M., Westra W.H., Herman J.G., Sidransky D.;
"Inactivation of LKB1/STK11 is a common event in adenocarcinomas of
the lung.";
Cancer Res. 62:3659-3662(2002).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STRADA,
PHOSPHORYLATION AT THR-336 AND THR-363, AND CHARACTERIZATION OF
VARIANT SPORADIC CANCER TYR-176.
PubMed=12805220; DOI=10.1093/emboj/cdg292;
Baas A.F., Boudeau J., Sapkota G.P., Smit L., Medema R., Morrice N.A.,
Alessi D.R., Clevers H.C.;
"Activation of the tumour suppressor kinase LKB1 by the STE20-like
pseudokinase STRAD.";
EMBO J. 22:3062-3072(2003).
[13]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-194, IDENTIFICATION
IN A COMPLEX WITH STRADA AND CAB39, AND INTERACTION WITH STRADA;
STRADB; CAB39 AND CAB39L.
PubMed=14517248; DOI=10.1093/emboj/cdg490;
Boudeau J., Baas A.F., Deak M., Morrice N.A., Kieloch A.,
Schutkowski M., Prescott A.R., Clevers H.C., Alessi D.R.;
"MO25alpha/beta interact with STRADalpha/beta enhancing their ability
to bind, activate and localize LKB1 in the cytoplasm.";
EMBO J. 22:5102-5114(2003).
[14]
FUNCTION IN CELL POLARITY.
PubMed=15016379; DOI=10.1016/S0092-8674(04)00114-X;
Baas A.F., Kuipers J., van der Wel N.N., Batlle E., Koerten H.K.,
Peters P.J., Clevers H.C.;
"Complete polarization of single intestinal epithelial cells upon
activation of LKB1 by STRAD.";
Cell 116:457-466(2004).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-194.
PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,
Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,
Alessi D.R.;
"LKB1 is a master kinase that activates 13 kinases of the AMPK
subfamily, including MARK/PAR-1.";
EMBO J. 23:833-843(2004).
[16]
INVOLVEMENT IN LUNG CANCER.
PubMed=15021901; DOI=10.1038/sj.onc.1207502;
Carretero J., Medina P.P., Pio R., Montuenga L.M.,
Sanchez-Cespedes M.;
"Novel and natural knockout lung cancer cell lines for the LKB1/STK11
tumor suppressor gene.";
Oncogene 23:4037-4040(2004).
[17]
FUNCTION.
PubMed=15733851; DOI=10.1016/j.febslet.2005.01.042;
Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,
Alessi D.R.;
"Identification of the sucrose non-fermenting related kinase SNRK, as
a novel LKB1 substrate.";
FEBS Lett. 579:1417-1423(2005).
[18]
FUNCTION, INTERACTION WITH PTEN, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT PJS ASN-176.
PubMed=15987703; DOI=10.1093/hmg/ddi225;
Mehenni H., Lin-Marq N., Buchet-Poyau K., Reymond A., Collart M.A.,
Picard D., Antonarakis S.E.;
"LKB1 interacts with and phosphorylates PTEN: a functional link
between two proteins involved in cancer predisposing syndromes.";
Hum. Mol. Genet. 14:2209-2219(2005).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53.
PubMed=17108107; DOI=10.1158/0008-5472.CAN-06-0999;
Zeng P.Y., Berger S.L.;
"LKB1 is recruited to the p21/WAF1 promoter by p53 to mediate
transcriptional activation.";
Cancer Res. 66:10701-10708(2006).
[20]
INTERACTION WITH WDR6.
PubMed=17216128; DOI=10.1007/s11010-006-9402-5;
Xie X., Wang Z., Chen Y.;
"Association of LKB1 with a WD-repeat protein WDR6 is implicated in
cell growth arrest and p27(Kip1) induction.";
Mol. Cell. Biochem. 301:115-122(2007).
[21]
INVOLVEMENT IN LUNG CANCER.
PubMed=17711506; DOI=10.1111/j.1349-7006.2007.00585.x;
Onozato R., Kosaka T., Achiwa H., Kuwano H., Takahashi T., Yatabe Y.,
Mitsudomi T.;
"LKB1 gene mutations in Japanese lung cancer patients.";
Cancer Sci. 98:1747-1751(2007).
[22]
INVOLVEMENT IN LUNG CANCER.
PubMed=17676035; DOI=10.1038/nature06030;
Ji H., Ramsey M.R., Hayes D.N., Fan C., McNamara K., Kozlowski P.,
Torrice C., Wu M.C., Shimamura T., Perera S.A., Liang M.C., Cai D.,
Naumov G.N., Bao L., Contreras C.M., Li D., Chen L., Krishnamurthy J.,
Koivunen J., Chirieac L.R., Padera R.F., Bronson R.T., Lindeman N.I.,
Christiani D.C., Lin X., Shapiro G.I., Janne P.A., Johnson B.E.,
Meyerson M., Kwiatkowski D.J., Castrillon D.H., Bardeesy N.,
Sharpless N.E., Wong K.K.;
"LKB1 modulates lung cancer differentiation and metastasis.";
Nature 448:807-810(2007).
[23]
INVOLVEMENT IN LUNG CANCER.
PubMed=17384680; DOI=10.1038/sj.onc.1210418;
Matsumoto S., Iwakawa R., Takahashi K., Kohno T., Nakanishi Y.,
Matsuno Y., Suzuki K., Nakamoto M., Shimizu E., Minna J.D., Yokota J.;
"Prevalence and specificity of LKB1 genetic alterations in lung
cancers.";
Oncogene 26:5911-5918(2007).
[24]
INVOLVEMENT IN LUNG CANCER.
PubMed=18594528; DOI=10.1038/sj.bjc.6604469;
Koivunen J.P., Kim J., Lee J., Rogers A.M., Park J.O., Zhao X.,
Naoki K., Okamoto I., Nakagawa K., Yeap B.Y., Meyerson M., Wong K.K.,
Richards W.G., Sugarbaker D.J., Johnson B.E., Janne P.A.;
"Mutations in the LKB1 tumour suppressor are frequently detected in
tumours from Caucasian but not Asian lung cancer patients.";
Br. J. Cancer 99:245-252(2008).
[25]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-428, AND
MUTAGENESIS OF SER-428.
PubMed=18321849; DOI=10.1074/jbc.M708208200;
Song P., Xie Z., Wu Y., Xu J., Dong Y., Zou M.H.;
"Protein kinase Czeta-dependent LKB1 serine 428 phosphorylation
increases LKB1 nucleus export and apoptosis in endothelial cells.";
J. Biol. Chem. 283:12446-12455(2008).
[26]
INTERACTION WITH SIRT1, ACETYLATION AT LYS-44; LYS-48; LYS-96; LYS-97;
LYS-296; LYS-311; LYS-416; LYS-423 AND LYS-431, AND MUTAGENESIS OF
LYS-44; LYS-48; LYS-96 AND LYS-97.
PubMed=18687677; DOI=10.1074/jbc.M805711200;
Lan F., Cacicedo J.M., Ruderman N., Ido Y.;
"SIRT1 modulation of the acetylation status, cytosolic localization,
and activity of LKB1. Possible role in AMP-activated protein kinase
activation.";
J. Biol. Chem. 283:27628-27635(2008).
[27]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
PHOSPHORYLATION AT SER-428, AND MUTAGENESIS OF SER-428.
PubMed=18854309; DOI=10.1074/jbc.M806153200;
Denison F.C., Hiscock N.J., Carling D., Woods A.;
"Characterization of an alternative splice variant of LKB1.";
J. Biol. Chem. 284:67-76(2009).
[28]
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).
[29]
INVOLVEMENT IN LUNG CANCER.
PubMed=20559149; DOI=10.1097/JTO.0b013e3181e05016;
Gao B., Sun Y., Zhang J., Ren Y., Fang R., Han X., Shen L., Liu X.Y.,
Pao W., Chen H., Ji H.;
"Spectrum of LKB1, EGFR, and KRAS mutations in Chinese lung
adenocarcinomas.";
J. Thorac. Oncol. 5:1130-1135(2010).
[30]
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).
[31]
FUNCTION.
PubMed=21317932; DOI=10.1038/onc.2011.19;
Hou X., Liu J.E., Liu W., Liu C.Y., Liu Z.Y., Sun Z.Y.;
"A new role of NUAK1: directly phosphorylating p53 and regulating cell
proliferation.";
Oncogene 30:2933-2942(2011).
[32]
REVIEW ON FUNCTION.
PubMed=21396365; DOI=10.1016/j.febslet.2011.03.010;
Alexander A., Walker C.L.;
"The role of LKB1 and AMPK in cellular responses to stress and
damage.";
FEBS Lett. 585:952-957(2011).
[33]
REVIEW ON INVOLVEMENT IN LUNG CANCER.
PubMed=21380642; DOI=10.1007/s13238-011-1021-6;
Gao Y., Ge G., Ji H.;
"LKB1 in lung cancerigenesis: a serine/threonine kinase as tumor
suppressor.";
Protein Cell 2:99-107(2011).
[34]
ENZYME REGULATION, INTERACTION WITH NR4A1, AND SUBCELLULAR LOCATION.
PubMed=22983157; DOI=10.1038/nchembio.1069;
Zhan Y.Y., Chen Y., Zhang Q., Zhuang J.J., Tian M., Chen H.Z.,
Zhang L.R., Zhang H.K., He J.P., Wang W.J., Wu R., Wang Y., Shi C.,
Yang K., Li A.Z., Xin Y.Z., Li T.Y., Yang J.Y., Zheng Z.H., Yu C.D.,
Lin S.C., Chang C., Huang P.Q., Lin T., Wu Q.;
"The orphan nuclear receptor Nur77 regulates LKB1 localization and
activates AMPK.";
Nat. Chem. Biol. 8:897-904(2012).
[35]
INTERACTION WITH NISCH, AND SUBCELLULAR LOCATION.
PubMed=23572524; DOI=10.1074/jbc.M112.418103;
Jain P., Baranwal S., Dong S., Struckhoff A.P., Worthylake R.A.,
Alahari S.K.;
"Integrin-binding protein nischarin interacts with tumor suppressor
liver kinase B1 (LKB1) to regulate cell migration of breast epithelial
cells.";
J. Biol. Chem. 288:15495-15509(2013).
[36]
SUBCELLULAR LOCATION (ISOFORM 2), AND PHOSPHORYLATION AT SER-399
(ISOFORM 2).
PubMed=23612973; DOI=10.1074/jbc.M112.443580;
Zhu H., Moriasi C.M., Zhang M., Zhao Y., Zou M.H.;
"Phosphorylation of serine 399 in LKB1 protein short form by protein
kinase Czeta is required for its nucleocytoplasmic transport and
consequent AMP-activated protein kinase (AMPK) activation.";
J. Biol. Chem. 288:16495-16505(2013).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-401, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[38]
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).
[39]
FUNCTION, AND INTERACTION WITH CDKN1A.
PubMed=25329316; DOI=10.1371/journal.pgen.1004721;
Esteve-Puig R., Gil R., Gonzalez-Sanchez E., Bech-Serra J.J.,
Grueso J., Hernandez-Losa J., Moline T., Canals F., Ferrer B.,
Cortes J., Bastian B., Cajal S.R.Y., Martin-Caballero J., Flores J.M.,
Vivancos A., Garcia-Patos V., Recio J.A.;
"A mouse model uncovers LKB1 as an UVB-induced DNA damage sensor
mediating CDKN1A (p21WAF1/CIP1) degradation.";
PLoS Genet. 10:E1004721-E1004721(2014).
[40]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 43-347 IN COMPLEX WITH
STRADA AND CAB39, ENZYME REGULATION, CHARACTERIZATION OF VARIANTS
SPORADIC CANCER MET-66; GLY-86; ARG-123; SER-157; ASP-163; PRO-170;
SER-171; ARG-174; TYR-176; ASN-177; GLU-181; GLN-199; THR-205;
PHE-216; VAL-223; PRO-230; PRO-232; ARG-245; PRO-250; HIS-272;
TYR-277; GLN-285 AND SER-315, AND MUTAGENESIS OF ARG-74; ASP-194 AND
PHE-204.
PubMed=19892943; DOI=10.1126/science.1178377;
Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.;
"Structure of the LKB1-STRAD-MO25 complex reveals an allosteric
mechanism of kinase activation.";
Science 326:1707-1711(2009).
[41]
VARIANTS PJS 50-LEU--ASP-53 DEL; ASN-176 AND CYS-308, CHARACTERIZATION
OF VARIANTS PJS PRO-67; ASN-176 AND CYS-308, AND MUTAGENESIS OF
LYS-78.
PubMed=9837816; DOI=10.1086/302159;
Mehenni H., Gehrig C., Nezu J., Oku A., Shimane M., Rossier C.,
Guex N., Blouin J.L., Scott H.S., Antonarakis S.E.;
"Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence
for allelic and locus heterogeneity.";
Am. J. Hum. Genet. 63:1641-1650(1998).
[42]
VARIANT TGCT ASP-163.
PubMed=9605748;
Avizienyte E., Roth S., Loukola A., Hemminki A., Lothe R.A.,
Stenwig A.E., Fossaa S.D., Salovaara R., Aaltonen L.A.;
"Somatic mutations in LKB1 are rare in sporadic colorectal and
testicular tumors.";
Cancer Res. 58:2087-2090(1998).
[43]
VARIANTS COLORECTAL CANCER SER-171; LYS-199; ASN-208; ASP-215; LEU-354
AND MET-367.
PubMed=9731485;
Dong S.M., Kim K.M., Kim S.Y., Shin M.S., Na E.Y., Lee S.H.,
Park W.S., Yoo N.J., Jang J.J., Yoon C.Y., Kim J.W., Kim S.Y.,
Yang Y.M., Kim S.H., Kim C.S., Lee J.Y.;
"Frequent somatic mutations in serine/threonine kinase 11/Peutz-
Jeghers syndrome gene in left-sided colon cancer.";
Cancer Res. 58:3787-3790(1998).
[44]
VARIANT COLORECTAL CANCER HIS-314.
PubMed=9809980;
Resta N., Simone C., Mareni C., Montera M., Gentile M., Susca F.,
Gristina R., Pozzi S., Bertario L., Bufo P., Carlomagno N.,
Ingrosso M., Rossini F.P., Tenconi R., Guanti G.;
"STK11 mutations in Peutz-Jeghers syndrome and sporadic colon
cancer.";
Cancer Res. 58:4799-4801(1998).
[45]
VARIANT PJS ASN-247 DEL.
PubMed=9760200; DOI=10.1007/s004390050801;
Nakagawa H., Koyama K., Miyoshi Y., Ando H., Baba S., Watatani M.,
Yasutomi M., Matsuura N., Monden M., Nakamura Y.;
"Nine novel germline mutations of STK11 in ten families with Peutz-
Jeghers syndrome.";
Hum. Genet. 103:168-172(1998).
[46]
VARIANT GASTRIC CARCINOMA LEU-324.
PubMed=9683800;
Park W.S., Moon Y.W., Yang Y.M., Kim Y.S., Kim Y.D., Fuller B.G.,
Vortmeyer A.O., Fogt F., Lubensky I.A., Zhuang Z.;
"Mutations of the STK11 gene in sporadic gastric carcinoma.";
Int. J. Oncol. 13:601-604(1998).
[47]
VARIANTS PJS PRO-67 AND 303-ILE--GLN-306 DELINS ASN.
PubMed=9428765; DOI=10.1038/34432;
Hemminki A., Markie D., Tomlinson I., Avizienyte E., Roth S.,
Loukola A., Bignell G., Warren W., Aminoff M., Hoeglund P.,
Jaervinen H., Kristo P., Pelin K., Ridanpaeae M., Salovaara R.,
Toro T., Bodmer W., Olschwang S., Olsen A.S., Stratton M.R.,
de la Chapelle A., Aaltonen L.A.;
"A serine/threonine kinase gene defective in Peutz-Jeghers syndrome.";
Nature 391:184-187(1998).
[48]
VARIANT LUNG CANCER VAL-194.
PubMed=10079245; DOI=10.1016/S0002-9440(10)65314-X;
Avizienyte E., Loukola A., Roth S., Hemminki A., Tarkkanen M.,
Salovaara R., Arola J., Butzow R., Husgafvel-Pursiainen K.,
Kokkola A., Jarvinen H., Aaltonen L.A.;
"LKB1 somatic mutations in sporadic cancers.";
Am. J. Pathol. 154:677-681(1999).
[49]
VARIANTS PJS 162-ASN--MET-164; ASN-194 AND LYS-297.
PubMed=10408777;
DOI=10.1002/(SICI)1098-1004(1999)13:6<476::AID-HUMU7>3.0.CO;2-2;
Westerman A.M., Entius M.M., Boor P.P.C., Koole R., de Baar E.,
Offerhaus G.J.A., Lubinski J., Lindhout D., Halley D.J.J.,
de Rooij F.W.M., Wilson J.H.P.;
"Novel mutations in the LKB1/STK11 gene in Dutch Peutz-Jeghers
families.";
Hum. Mutat. 13:476-481(1999).
[50]
CHARACTERIZATION OF VARIANT TGCT ASP-163.
PubMed=9887330; DOI=10.1093/hmg/8.1.45;
Ylikorkala A., Avizienyte E., Tomlinson I.P., Tiainen M., Roth S.,
Loukola A., Hemminki A., Johansson M., Sistonen P., Markie D.,
Neale K., Phillips R., Zauber P., Twama T., Sampson J., Jaervinen H.,
Maekelae T.P., Aaltonen L.A.;
"Mutations and impaired function of LKB1 in familial and non-familial
Peutz-Jeghers syndrome and a sporadic testicular cancer.";
Hum. Mol. Genet. 8:45-51(1999).
[51]
VARIANT OVARIAN CARCINOMA LEU-281.
PubMed=10429654; DOI=10.1111/j.1349-7006.1999.tb00793.x;
Nishioka Y., Kobayashi K., Sagae S., Sugimura M., Ishioka S.,
Nagata M., Terasawa K., Tokino T., Kudo R.;
"Mutational analysis of STK11 gene in ovarian carcinomas.";
Jpn. J. Cancer Res. 90:629-632(1999).
[52]
VARIANTS MELANOMA ASP-49 AND ARG-135.
PubMed=10201537; DOI=10.1046/j.1523-1747.1999.00551.x;
Rowan A., Bataille V., MacKie R., Healy E., Bicknell D., Bodmer W.,
Tomlinson I.;
"Somatic mutations in the Peutz-Jeghers (LKB1/STKII) gene in sporadic
malignant melanomas.";
J. Invest. Dermatol. 112:509-511(1999).
[53]
VARIANT MELANOMA TYR-194.
PubMed=10208439; DOI=10.1038/sj.onc.1202486;
Guldberg P., thor Straten P., Ahrenkiel V., Seremet T., Kirkin A.F.,
Zeuthen J.;
"Somatic mutation of the Peutz-Jeghers syndrome gene, LKB1/STK11, in
malignant melanoma.";
Oncogene 18:1777-1780(1999).
[54]
VARIANTS PJS CYS-239 AND SER-315.
PubMed=12372054; DOI=10.1034/j.1399-0004.2002.620405.x;
Scott R.J., Crooks R., Meldrum C.J., Thomas L., Smith C.J.A.,
Mowat D., McPhillips M., Spigelman A.D.;
"Mutation analysis of the STK11/LKB1 gene and clinical characteristics
of an Australian series of Peutz-Jeghers syndrome patients.";
Clin. Genet. 62:282-287(2002).
[55]
VARIANTS CERVICAL CANCER LYS-14; PRO-160 AND LEU-231, AND VARIANT
CERVICAL CARCINOMA MET-66.
PubMed=12533684;
Kuragaki C., Enomoto T., Ueno Y., Sun H., Fujita M., Nakashima R.,
Ueda Y., Wada H., Murata Y., Toki T., Konishi I., Fujii S.;
"Mutations in the STK11 gene characterize minimal deviation
adenocarcinoma of the uterine cervix.";
Lab. Invest. 83:35-45(2003).
[56]
VARIANT [LARGE SCALE ANALYSIS] LYS-87.
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).
[57]
VARIANT PJS GLY-16.
PubMed=21411391; DOI=10.1016/j.clinre.2010.11.008;
Liu L., Du X., Nie J.;
"A novel de novo mutation in LKB1 gene in a Chinese Peutz Jeghers
syndrome patient significantly diminished p53 activity.";
Clin. Res. Hepatol. Gastroenterol. 35:221-226(2011).
-!- FUNCTION: Tumor suppressor serine/threonine-protein kinase that
controls the activity of AMP-activated protein kinase (AMPK)
family members, thereby playing a role in various processes such
as cell metabolism, cell polarity, apoptosis and DNA damage
response. Acts by phosphorylating the T-loop of AMPK family
proteins, thus promoting their activity: phosphorylates PRKAA1,
PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2,
SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-
AMPK family proteins such as STRADA, PTEN and possibly p53/TP53.
Acts as a key upstream regulator of AMPK by mediating
phosphorylation and activation of AMPK catalytic subunits PRKAA1
and PRKAA2 and thereby regulates processes including: inhibition
of signaling pathways that promote cell growth and proliferation
when energy levels are low, glucose homeostasis in liver,
activation of autophagy when cells undergo nutrient deprivation,
and B-cell differentiation in the germinal center in response to
DNA damage. Also acts as a regulator of cellular polarity by
remodeling the actin cytoskeleton. Required for cortical neuron
polarization by mediating phosphorylation and activation of BRSK1
and BRSK2, leading to axon initiation and specification. Involved
in DNA damage response: interacts with p53/TP53 and recruited to
the CDKN1A/WAF1 promoter to participate in transcription
activation. Able to phosphorylate p53/TP53; the relevance of such
result in vivo is however unclear and phosphorylation may be
indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also
acts as a mediator of p53/TP53-dependent apoptosis via interaction
with p53/TP53: translocates to the mitochondrion during apoptosis
and regulates p53/TP53-dependent apoptosis pathways. In vein
endothelial cells, inhibits PI3K/Akt signaling activity and thus
induces apoptosis in response to the oxidant peroxynitrite (in
vitro). Regulates UV radiation-induced DNA damage response
mediated by CDKN1A. In association with NUAK1, phosphorylates
CDKN1A in response to UV radiation and contributes to its
degradation which is necessary for optimal DNA repair
(PubMed:25329316). {ECO:0000269|PubMed:11430832,
ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248,
ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15016379,
ECO:0000269|PubMed:15733851, ECO:0000269|PubMed:15987703,
ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:18321849,
ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:25329316}.
-!- FUNCTION: Isoform 2: Has a role in spermiogenesis. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:14976552}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- ENZYME REGULATION: Activated by forming a complex with STRAD
(STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CAB39L/MO25beta): STRADA (or STRADB)-binding promotes a
conformational change of STK11/LKB1 in an active conformation,
which is stabilized by CAB39/MO25alpha (or CAB39L/MO25beta)
interacting with the STK11/LKB1 activation loop. Sequestration in
the nucleus by NR4A1 prevents it from phosphorylating and
activating cytoplasmic AMPK. {ECO:0000269|PubMed:19892943,
ECO:0000269|PubMed:22983157}.
-!- SUBUNIT: Catalytic component of a trimeric complex composed of
STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25
(CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers
STK11/LKB1 in the cytoplasm and stimulates its catalytic activity.
Found in a ternary complex composed of SMAD4, STK11/LKB1 and
STK11IP. Interacts with p53/TP53, SMAD4, STK11IP and WDR6.
Interacts with NR4A1. Interacts with NISCH; this interaction may
increase STK11 activity. Interacts with PTEN; leading to PTEN
phosphorylation. Interacts with SIRT1; the interaction
deacetylates STK11. Interacts with CDKN1A.
{ECO:0000269|PubMed:11741830, ECO:0000269|PubMed:12805220,
ECO:0000269|PubMed:14517248, ECO:0000269|PubMed:15987703,
ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17216128,
ECO:0000269|PubMed:18687677, ECO:0000269|PubMed:19892943,
ECO:0000269|PubMed:22983157, ECO:0000269|PubMed:23572524,
ECO:0000269|PubMed:25329316}.
-!- INTERACTION:
Q9Y376:CAB39; NbExp=12; IntAct=EBI-306838, EBI-306905;
Q16543:CDC37; NbExp=3; IntAct=EBI-306838, EBI-295634;
Q9BT78:COPS4; NbExp=2; IntAct=EBI-306838, EBI-742413;
Q13451:FKBP5; NbExp=4; IntAct=EBI-306838, EBI-306914;
P07900:HSP90AA1; NbExp=2; IntAct=EBI-306838, EBI-296047;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-306838, EBI-352572;
O95835:LATS1; NbExp=2; IntAct=EBI-306838, EBI-444209;
Q96L34:MARK4; NbExp=2; IntAct=EBI-306838, EBI-302319;
P26927:MST1; NbExp=2; IntAct=EBI-306838, EBI-6929133;
Q7RTN6:STRADA; NbExp=12; IntAct=EBI-306838, EBI-1109114;
Q7RTN6-1:STRADA; NbExp=3; IntAct=EBI-306838, EBI-15787241;
Q9C0K7:STRADB; NbExp=6; IntAct=EBI-306838, EBI-306893;
Q8NFZ5:TNIP2; NbExp=5; IntAct=EBI-306838, EBI-359372;
Q9NNW5:WDR6; NbExp=3; IntAct=EBI-306838, EBI-1568315;
P63104:YWHAZ; NbExp=6; IntAct=EBI-306838, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Membrane {ECO:0000250}.
Mitochondrion. Note=A small fraction localizes at membranes (By
similarity). Relocates to the cytoplasm when bound to STRAD
(STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CAB39L/MO25beta). Translocates to the mitochondrion during
apoptosis. Translocates to the cytoplasm in response to metformin
or peroxynitrite treatment. PTEN promotes cytoplasmic
localization. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000269|PubMed:23612973}. Cytoplasm
{ECO:0000269|PubMed:23612973}. Note=Predominantly nuclear, but
translocates to the cytoplasm in response to metformin or
peroxynitrite treatment.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LKB1(L);
IsoId=Q15831-1; Sequence=Displayed;
Name=2; Synonyms=LKB1(S);
IsoId=Q15831-2; Sequence=VSP_041746;
Note=Contains a phosphoserine at position 399.
{ECO:0000269|PubMed:23612973};
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Strongest expression
in testis and fetal liver.
-!- PTM: Phosphorylated by ATM at Thr-363 following ionizing radiation
(IR). Phosphorylation at Ser-428 by RPS6KA1 and/or some PKA is
required to inhibit cell growth. Phosphorylation at Ser-428 is
also required during neuronal polarization to mediate
phosphorylation of BRSK1 and BRSK2 (By similarity).
Phosphorylation by PKC/PRKCZ at Ser-428 promotes peroxynitrite-
induced nuclear export of STK11, leading to PTEN activation and
subsequent inhibition of AKT signaling. Phosphorylation by
PKC/PRKCZ at Ser-399 in isoform 2 promotes metformin (or
peroxynitrite)-induced nuclear export of STK11 and activation of
AMPK. UV radiation-induced phosphorylation at Thr-363 mediates
CDKN1A degradation (By similarity). {ECO:0000250|UniProtKB:Q9WTK7,
ECO:0000269|PubMed:11430832, ECO:0000269|PubMed:12805220,
ECO:0000269|PubMed:18321849, ECO:0000269|PubMed:18854309}.
-!- PTM: Acetylated. Deacetylation at Lys-48 enhances cytoplasmic
localization and kinase activity in vitro.
{ECO:0000269|PubMed:18687677}.
-!- DISEASE: Peutz-Jeghers syndrome (PJS) [MIM:175200]: An autosomal
dominant disorder characterized by melanocytic macules of the
lips, multiple gastrointestinal hamartomatous polyps and an
increased risk for various neoplasms, including gastrointestinal
cancer. {ECO:0000269|PubMed:10408777, ECO:0000269|PubMed:12372054,
ECO:0000269|PubMed:15987703, ECO:0000269|PubMed:21411391,
ECO:0000269|PubMed:9425897, ECO:0000269|PubMed:9428765,
ECO:0000269|PubMed:9760200, ECO:0000269|PubMed:9837816}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common
malignancy in males representing 95% of all testicular neoplasms.
TGCTs have various pathologic subtypes including: unclassified
intratubular germ cell neoplasia, seminoma (including cases with
syncytiotrophoblastic cells), spermatocytic seminoma, embryonal
carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
{ECO:0000269|PubMed:9605748, ECO:0000269|PubMed:9887330}. Note=The
gene represented in this entry may be involved in disease
pathogenesis.
-!- DISEASE: Note=Defects in STK11 are associated with some sporadic
cancers, especially lung cancers. Frequently mutated and
inactivated in non-small cell lung cancer (NSCLC). Defects promote
lung cancerigenesis process, especially lung cancer progression
and metastasis. Confers lung adenocarcinoma the ability to trans-
differentiate into squamous cell carcinoma. Also able to promotes
lung cancer metastasis, via both cancer-cell autonomous and non-
cancer-cell autonomous mechanisms.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. LKB1 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/STK11ID292.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=PJS entry;
URL="https://en.wikipedia.org/wiki/PJS";
-----------------------------------------------------------------------
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EMBL; U63333; AAB05809.1; -; mRNA.
EMBL; AF035625; AAC39527.1; -; mRNA.
EMBL; AF032984; AAB97833.1; -; Genomic_DNA.
EMBL; AF055327; AAC15742.1; -; Genomic_DNA.
EMBL; AF055320; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AF055321; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AF055322; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AF055323; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AF055324; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AF055325; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AF055326; AAC15742.1; JOINED; Genomic_DNA.
EMBL; AK314858; BAG37374.1; -; mRNA.
EMBL; AC011544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69540.1; -; Genomic_DNA.
EMBL; BC007981; AAH07981.1; -; mRNA.
EMBL; BC019334; AAH19334.1; -; mRNA.
CCDS; CCDS45896.1; -. [Q15831-1]
RefSeq; NP_000446.1; NM_000455.4. [Q15831-1]
RefSeq; XP_005259675.1; XM_005259618.3. [Q15831-2]
UniGene; Hs.515005; -.
PDB; 2WTK; X-ray; 2.65 A; C/F=43-347.
PDB; 4ZDR; X-ray; 2.90 A; A/B=333-340.
PDB; 5WXN; X-ray; 2.93 A; C/D=331-343.
PDBsum; 2WTK; -.
PDBsum; 4ZDR; -.
PDBsum; 5WXN; -.
ProteinModelPortal; Q15831; -.
SMR; Q15831; -.
BioGrid; 112670; 93.
CORUM; Q15831; -.
DIP; DIP-31317N; -.
IntAct; Q15831; 112.
MINT; MINT-204048; -.
STRING; 9606.ENSP00000324856; -.
BindingDB; Q15831; -.
ChEMBL; CHEMBL5606; -.
GuidetoPHARMACOLOGY; 2212; -.
iPTMnet; Q15831; -.
PhosphoSitePlus; Q15831; -.
BioMuta; STK11; -.
DMDM; 3024670; -.
EPD; Q15831; -.
MaxQB; Q15831; -.
PaxDb; Q15831; -.
PeptideAtlas; Q15831; -.
PRIDE; Q15831; -.
DNASU; 6794; -.
Ensembl; ENST00000326873; ENSP00000324856; ENSG00000118046. [Q15831-1]
GeneID; 6794; -.
KEGG; hsa:6794; -.
UCSC; uc002lrl.2; human. [Q15831-1]
CTD; 6794; -.
DisGeNET; 6794; -.
EuPathDB; HostDB:ENSG00000118046.14; -.
GeneCards; STK11; -.
GeneReviews; STK11; -.
HGNC; HGNC:11389; STK11.
HPA; CAB016231; -.
HPA; CAB022105; -.
HPA; HPA017254; -.
HPA; HPA067481; -.
MalaCards; STK11; -.
MIM; 175200; phenotype.
MIM; 273300; phenotype.
MIM; 602216; gene.
neXtProt; NX_Q15831; -.
OpenTargets; ENSG00000118046; -.
Orphanet; 2869; Peutz-Jeghers syndrome.
PharmGKB; PA36198; -.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00530000063214; -.
HOGENOM; HOG000007002; -.
HOVERGEN; HBG054467; -.
InParanoid; Q15831; -.
KO; K07298; -.
OMA; DPQQLGM; -.
OrthoDB; EOG091G0BNP; -.
PhylomeDB; Q15831; -.
TreeFam; TF105322; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q15831; -.
SIGNOR; Q15831; -.
ChiTaRS; STK11; human.
EvolutionaryTrace; Q15831; -.
GeneWiki; STK11; -.
GenomeRNAi; 6794; -.
PRO; PR:Q15831; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000118046; -.
CleanEx; HS_STK11; -.
ExpressionAtlas; Q15831; baseline and differential.
Genevisible; Q15831; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0036398; C:TCR signalosome; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0030275; F:LRR domain binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:MGI.
GO; GO:0043276; P:anoikis; IMP:BHF-UCL.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
GO; GO:0097484; P:dendrite extension; IEA:Ensembl.
GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0051645; P:Golgi localization; IEA:Ensembl.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IEA:Ensembl.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:ParkinsonsUK-UCL.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0051896; P:regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0036399; P:TCR signalosome assembly; IEA:Ensembl.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
GO; GO:0001944; P:vasculature development; ISS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Autophagy; Cell cycle; Complete proteome; Cytoplasm;
Differentiation; Disease mutation; DNA damage; Kinase; Lipoprotein;
Magnesium; Manganese; Membrane; Metal-binding; Methylation;
Mitochondrion; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
Polymorphism; Prenylation; Reference proteome;
Serine/threonine-protein kinase; Spermatogenesis; Transferase;
Tumor suppressor.
CHAIN 1 430 Serine/threonine-protein kinase STK11.
/FTId=PRO_0000086699.
PROPEP 431 433 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000422300.
DOMAIN 49 309 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 55 63 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 45 90 Sufficient for interaction with SIRT1.
{ECO:0000269|PubMed:18687677}.
ACT_SITE 176 176 Proton acceptor.
BINDING 78 78 ATP. {ECO:0000305}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 48 48 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 96 96 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 189 189 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:11430832}.
MOD_RES 296 296 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 311 311 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WTK7}.
MOD_RES 336 336 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12805220}.
MOD_RES 363 363 Phosphothreonine; by ATM and
autocatalysis.
{ECO:0000269|PubMed:12805220}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 416 416 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 423 423 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
MOD_RES 428 428 Phosphoserine; by autocatalysis, PKA,
PKC/PRKCZ and RPS6KA1.
{ECO:0000269|PubMed:18321849,
ECO:0000269|PubMed:18854309}.
MOD_RES 430 430 Cysteine methyl ester. {ECO:0000250}.
MOD_RES 431 431 N6-acetyllysine.
{ECO:0000269|PubMed:18687677}.
LIPID 418 418 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 430 430 S-farnesyl cysteine. {ECO:0000250}.
VAR_SEQ 371 433 QVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAP
NPARKACSASSKIRRLSACKQQ -> GEEASEAGLRAERGL
QKSEGSDLSGEEASRPAPQ (in isoform 2).
{ECO:0000305}.
/FTId=VSP_041746.
VARIANT 14 14 E -> K (in cervical cancer; somatic
mutation). {ECO:0000269|PubMed:12533684}.
/FTId=VAR_065627.
VARIANT 16 16 E -> G (in PJS).
{ECO:0000269|PubMed:21411391}.
/FTId=VAR_065628.
VARIANT 49 49 Y -> D (in melanoma; sporadic malignant;
somatic mutation; dbSNP:rs137853080).
{ECO:0000269|PubMed:10201537}.
/FTId=VAR_033138.
VARIANT 50 53 Missing (in PJS).
{ECO:0000269|PubMed:9837816}.
/FTId=VAR_071057.
VARIANT 66 66 V -> M (in cervical carcinoma; somatic
mutation). {ECO:0000269|PubMed:12533684,
ECO:0000269|PubMed:19892943}.
/FTId=VAR_065629.
VARIANT 67 67 L -> P (in PJS; abolishes kinase
activity, leading to loss of
autophosphorylation; dbSNP:rs137853077).
{ECO:0000269|PubMed:9428765,
ECO:0000269|PubMed:9837816}.
/FTId=VAR_006202.
VARIANT 86 86 R -> G (in sporadic cancer; somatic
mutation; no effect on kinase activity
nor in heterotrimeric complex assembly
with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065630.
VARIANT 87 87 R -> K (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041139.
VARIANT 123 123 Q -> R (in sporadic cancer; somatic
mutation; no effect on kinase activity
nor in heterotrimeric complex assembly
with STRADA and CAB39;
dbSNP:rs764449808).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065631.
VARIANT 135 135 G -> R (in melanoma; sporadic malignant;
somatic mutation; dbSNP:rs137853081).
{ECO:0000269|PubMed:10201537}.
/FTId=VAR_033139.
VARIANT 157 157 F -> S (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065632.
VARIANT 160 160 L -> P (in cervical cancer; somatic
mutation). {ECO:0000269|PubMed:12533684}.
/FTId=VAR_065633.
VARIANT 162 164 DGL -> NDM (in PJS).
/FTId=VAR_007920.
VARIANT 163 163 G -> D (in TGCT; a tumor with seminoma
and teratoma components; associated with
severely impaired but detectable kinase
activity; somatic mutation; impairs
heterotrimeric complex assembly with
STRADA and CAB39; predominantly nuclear
localization; dbSNP:rs137853078).
{ECO:0000269|PubMed:19892943,
ECO:0000269|PubMed:9605748,
ECO:0000269|PubMed:9887330}.
/FTId=VAR_033140.
VARIANT 170 170 Q -> P (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065634.
VARIANT 171 171 G -> S (in colorectal cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943,
ECO:0000269|PubMed:9731485}.
/FTId=VAR_065635.
VARIANT 174 174 H -> R (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065636.
VARIANT 176 176 D -> N (in PJS; loss of kinase activity,
leading to greatly reduced
autophosphorylation; fails to
phosphorylate PTEN in vitro; no
significant effect on nucleocytoplasmic
localization; dbSNP:rs730881979).
{ECO:0000269|PubMed:15987703,
ECO:0000269|PubMed:9837816}.
/FTId=VAR_071058.
VARIANT 176 176 D -> Y (in sporadic cancer; somatic
mutation; Loss of kinase activity).
{ECO:0000269|PubMed:12805220,
ECO:0000269|PubMed:19892943}.
/FTId=VAR_065637.
VARIANT 177 177 I -> N (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065638.
VARIANT 181 181 N -> E (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39; requires
2 nucleotide substitutions).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065639.
VARIANT 194 194 D -> N (in PJS; dbSNP:rs121913315).
{ECO:0000269|PubMed:10408777}.
/FTId=VAR_007921.
VARIANT 194 194 D -> V (in lung cancer; somatic mutation;
dbSNP:rs121913316).
{ECO:0000269|PubMed:10079245}.
/FTId=VAR_065640.
VARIANT 194 194 D -> Y (in melanoma; sporadic malignant;
somatic mutation; dbSNP:rs121913315).
{ECO:0000269|PubMed:10208439}.
/FTId=VAR_033141.
VARIANT 199 199 E -> K (in colorectal cancer; somatic
mutation; impaired kinase activity;
dbSNP:rs121913317).
{ECO:0000269|PubMed:9731485}.
/FTId=VAR_065641.
VARIANT 199 199 E -> Q (in sporadic cancer; somatic
mutation; does not affect kinase
activity). {ECO:0000269|PubMed:19892943}.
/FTId=VAR_065642.
VARIANT 205 205 A -> T (in sporadic cancer; somatic
mutation; no effect heterotrimeric
complex assembly with STRADA and CAB39;
dbSNP:rs730881981).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065643.
VARIANT 208 208 D -> N (in colorectal cancer; somatic
mutation; no effect heterotrimeric
complex assembly with STRADA and CAB39).
{ECO:0000269|PubMed:9731485}.
/FTId=VAR_065644.
VARIANT 215 215 G -> D (in colorectal cancer; somatic
mutation). {ECO:0000269|PubMed:9731485}.
/FTId=VAR_065645.
VARIANT 216 216 S -> F (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065646.
VARIANT 223 223 E -> V (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065647.
VARIANT 230 230 T -> P (in sporadic cancer; somatic
mutation; no effect heterotrimeric
complex assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065648.
VARIANT 231 231 F -> L (in cervical cancer; somatic
mutation). {ECO:0000269|PubMed:12533684}.
/FTId=VAR_065649.
VARIANT 232 232 S -> P (in sporadic cancer; somatic
mutation; no effect heterotrimeric
complex assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065650.
VARIANT 239 239 W -> C (in PJS; late onset suggests
reduced penetrance; dbSNP:rs137853082).
{ECO:0000269|PubMed:12372054}.
/FTId=VAR_033142.
VARIANT 245 245 L -> R (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065651.
VARIANT 247 247 Missing (in PJS).
{ECO:0000269|PubMed:9760200}.
/FTId=VAR_006203.
VARIANT 250 250 T -> P (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065652.
VARIANT 272 272 Y -> H (in sporadic cancer; somatic
mutation; no effect on kinase activity
nor in heterotrimeric complex assembly
with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065653.
VARIANT 277 277 D -> Y (in sporadic cancer; somatic
mutation; no effect on kinase activity
nor in heterotrimeric complex assembly
with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065654.
VARIANT 281 281 P -> L (in ovarian carcinoma; somatic
mutation; dbSNP:rs121913322).
{ECO:0000269|PubMed:10429654}.
/FTId=VAR_065655.
VARIANT 285 285 L -> Q (in sporadic cancer; somatic
mutation; impairs heterotrimeric complex
assembly with STRADA and CAB39).
{ECO:0000269|PubMed:19892943}.
/FTId=VAR_065656.
VARIANT 297 297 R -> K (in PJS).
{ECO:0000269|PubMed:10408777}.
/FTId=VAR_007922.
VARIANT 303 306 IRQH -> N (in PJS).
/FTId=VAR_033143.
VARIANT 308 308 W -> C (in PJS; abolishes kinase
activity, leading to loss of
autophosphorylation).
{ECO:0000269|PubMed:9837816}.
/FTId=VAR_071059.
VARIANT 314 314 P -> H (in colorectal cancer; no effect
heterotrimeric complex assembly with
STRADA and CAB39).
{ECO:0000269|PubMed:9809980}.
/FTId=VAR_065657.
VARIANT 315 315 P -> S (in PJS; pathogenicity uncertain;
no effect heterotrimeric complex assembly
with STRADA and CAB39;
dbSNP:rs786202431).
{ECO:0000269|PubMed:12372054,
ECO:0000269|PubMed:19892943}.
/FTId=VAR_033144.
VARIANT 324 324 P -> L (in gastric carcinoma; no effect
heterotrimeric complex assembly with
STRADA and CAB39; dbSNP:rs367807476).
{ECO:0000269|PubMed:9683800}.
/FTId=VAR_065658.
VARIANT 354 354 F -> L (in colorectal cancer; somatic
mutation; dbSNP:rs59912467).
{ECO:0000269|PubMed:9731485}.
/FTId=VAR_065659.
VARIANT 367 367 T -> M (in colorectal cancer; somatic
mutation; dbSNP:rs587782835).
{ECO:0000269|PubMed:9731485}.
/FTId=VAR_065660.
MUTAGEN 44 44 K->R: No effect on kinase activity.
{ECO:0000269|PubMed:18687677}.
MUTAGEN 48 48 K->Q: No effect on basal
nucleocytoplasmic localization, but fails
to translocate to the cytoplasm when
coexpressed with SIRT1.
{ECO:0000269|PubMed:18687677}.
MUTAGEN 48 48 K->R: Enhanced phosphorylation at Thr-336
and Ser-428, enhanced cytoplasmic
localization and increased kinase
activity. {ECO:0000269|PubMed:18687677}.
MUTAGEN 74 74 R->A: Impaired formation of a
heterotrimeric complex with STRADA and
CAB39; when associated with A-204.
{ECO:0000269|PubMed:19892943}.
MUTAGEN 78 78 K->I: Loss of kinase activity, leading to
greatly reduced autophosphorylation.
{ECO:0000269|PubMed:11430832,
ECO:0000269|PubMed:9837816}.
MUTAGEN 78 78 K->M: Loss of kinase activity, leading to
reduced autophosphorylation and acting as
a dominant-negative mutant.
{ECO:0000269|PubMed:11430832,
ECO:0000269|PubMed:9837816}.
MUTAGEN 96 96 K->R: No effect on kinase activity.
{ECO:0000269|PubMed:18687677}.
MUTAGEN 97 97 K->R: No effect on kinase activity.
{ECO:0000269|PubMed:18687677}.
MUTAGEN 189 189 T->A: Reduced phosphorylation.
{ECO:0000269|PubMed:11430832}.
MUTAGEN 194 194 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:14517248,
ECO:0000269|PubMed:14976552,
ECO:0000269|PubMed:19892943}.
MUTAGEN 204 204 F->A: No effect. Impaired formation of a
heterotrimeric complex with STRADA and
CAB39; when associated with A-74.
{ECO:0000269|PubMed:19892943}.
MUTAGEN 428 428 S->A,E: No effect on kinase activity.
{ECO:0000269|PubMed:18321849,
ECO:0000269|PubMed:18854309}.
MUTAGEN 428 428 S->A: Inhibits peroxynitrite-induced
nuclear export of STK11, and consequent
PTEN phosphorylation and inhibition of
PI3K/Akt signaling.
{ECO:0000269|PubMed:18321849,
ECO:0000269|PubMed:18854309}.
STRAND 54 57 {ECO:0000244|PDB:2WTK}.
STRAND 62 68 {ECO:0000244|PDB:2WTK}.
TURN 69 71 {ECO:0000244|PDB:2WTK}.
STRAND 74 80 {ECO:0000244|PDB:2WTK}.
HELIX 82 87 {ECO:0000244|PDB:2WTK}.
HELIX 91 102 {ECO:0000244|PDB:2WTK}.
STRAND 113 118 {ECO:0000244|PDB:2WTK}.
STRAND 125 130 {ECO:0000244|PDB:2WTK}.
STRAND 133 135 {ECO:0000244|PDB:2WTK}.
HELIX 136 142 {ECO:0000244|PDB:2WTK}.
HELIX 150 169 {ECO:0000244|PDB:2WTK}.
HELIX 179 181 {ECO:0000244|PDB:2WTK}.
STRAND 182 184 {ECO:0000244|PDB:2WTK}.
STRAND 190 192 {ECO:0000244|PDB:2WTK}.
HELIX 217 219 {ECO:0000244|PDB:2WTK}.
HELIX 222 225 {ECO:0000244|PDB:2WTK}.
STRAND 231 233 {ECO:0000244|PDB:2WTK}.
HELIX 234 250 {ECO:0000244|PDB:2WTK}.
HELIX 260 269 {ECO:0000244|PDB:2WTK}.
STRAND 276 278 {ECO:0000244|PDB:2WTK}.
HELIX 280 289 {ECO:0000244|PDB:2WTK}.
TURN 294 296 {ECO:0000244|PDB:2WTK}.
HELIX 300 305 {ECO:0000244|PDB:2WTK}.
HELIX 307 310 {ECO:0000244|PDB:2WTK}.
HELIX 334 336 {ECO:0000244|PDB:4ZDR}.
HELIX 339 341 {ECO:0000244|PDB:2WTK}.
SEQUENCE 433 AA; 48636 MW; 6DF4C37AB7A89569 CRC64;
MEVVDPQQLG MFTEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY
GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHKNV IQLVDVLYNE
EKQKMYMVME YCVCGMQEML DSVPEKRFPV CQAHGYFCQL IDGLEYLHSQ GIVHKDIKPG
NLLLTTGGTL KISDLGVAEA LHPFAADDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS
AGVTLYNITT GLYPFEGDNI YKLFENIGKG SYAIPGDCGP PLSDLLKGML EYEPAKRFSI
RQIRQHSWFR KKHPPAEAPV PIPPSPDTKD RWRSMTVVPY LEDLHGADED EDLFDIEDDI
IYTQDFTVPG QVPEEEASHN GQRRGLPKAV CMNGTEAAQL STKSRAEGRA PNPARKACSA
SSKIRRLSAC KQQ


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