STK11_RAT
ID STK11_RAT Reviewed; 436 AA.
AC D4AE59; A0A0H2UI02; D4A179;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Serine/threonine-protein kinase STK11 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q15831};
DE AltName: Full=Liver kinase B1 homolog;
DE Short=LKB1;
DE Flags: Precursor;
GN Name=Stk11 {ECO:0000312|RGD:1308653}; Synonyms=Lkb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION IN A COMPLEX WITH STRADA AND CAB39, AND INTERACTION WITH
RP STRADA; STRADB; CAB39 AND CAB39L.
RX PubMed=14511394; DOI=10.1186/1475-4924-2-28;
RA Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Makela T.P.,
RA Alessi D.R., Hardie D.G.;
RT "Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25
RT alpha/beta are upstream kinases in the AMP-activated protein kinase
RT cascade.";
RL J. Biol. 2:28.1-28.16(2003).
RN [4]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX WITH STRADA AND CAB39,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18774945; DOI=10.1042/bj20081447;
RA Towler M.C., Fogarty S., Hawley S.A., Pan D.A., Martin D.M., Morrice N.A.,
RA McCarthy A., Galardo M.N., Meroni S.B., Cigorraga S.B., Ashworth A.,
RA Sakamoto K., Hardie D.G.;
RT "A novel short splice variant of the tumour suppressor LKB1 is required for
RT spermiogenesis.";
RL Biochem. J. 416:1-14(2008).
RN [5]
RP ACETYLATION.
RX PubMed=18687677; DOI=10.1074/jbc.m805711200;
RA Lan F., Cacicedo J.M., Ruderman N., Ido Y.;
RT "SIRT1 modulation of the acetylation status, cytosolic localization, and
RT activity of LKB1. Possible role in AMP-activated protein kinase
RT activation.";
RL J. Biol. Chem. 283:27628-27635(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Tumor suppressor serine/threonine-protein kinase that
CC controls the activity of AMP-activated protein kinase (AMPK) family
CC members, thereby playing a role in various processes such as cell
CC metabolism, cell polarity, apoptosis and DNA damage response. Acts by
CC phosphorylating the T-loop of AMPK family proteins, thus promoting
CC their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1,
CC MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not
CC MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN
CC and possibly p53/TP53. Acts as a key upstream regulator of AMPK by
CC mediating phosphorylation and activation of AMPK catalytic subunits
CC PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition
CC of signaling pathways that promote cell growth and proliferation when
CC energy levels are low, glucose homeostasis in liver, activation of
CC autophagy when cells undergo nutrient deprivation, and B-cell
CC differentiation in the germinal center in response to DNA damage. Also
CC acts as a regulator of cellular polarity by remodeling the actin
CC cytoskeleton. Required for cortical neuron polarization by mediating
CC phosphorylation and activation of BRSK1 and BRSK2, leading to axon
CC initiation and specification. Involved in DNA damage response:
CC interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to
CC participate in transcription activation. Able to phosphorylate
CC p53/TP53; the relevance of such result in vivo is however unclear and
CC phosphorylation may be indirect and mediated by downstream STK11/LKB1
CC kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis
CC via interaction with p53/TP53: translocates to the mitochondrion during
CC apoptosis and regulates p53/TP53-dependent apoptosis pathways.
CC Regulates UV radiation-induced DNA damage response mediated by CDKN1A.
CC In association with NUAK1, phosphorylates CDKN1A in response to UV
CC radiation and contributes to its degradation which is necessary for
CC optimal DNA repair (By similarity). {ECO:0000250|UniProtKB:Q9WTK7,
CC ECO:0000269|PubMed:18774945}.
CC -!- FUNCTION: [Isoform 2]: Has a role in spermiogenesis.
CC {ECO:0000269|PubMed:18774945}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by forming a complex with STRAD (STRADA
CC or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): STRADA
CC (or STRADB)-binding promotes a conformational change of STK11/LKB1 in
CC an active conformation, which is stabilized by CAB39/MO25alpha (or
CC CAB39L/MO25beta) interacting with the STK11/LKB1 activation loop.
CC Sequestration in the nucleus by NR4A1 prevents it from phosphorylating
CC and activating cytoplasmic AMPK (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Catalytic component of a trimeric complex composed of
CC STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CC CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and
CC stimulates its catalytic activity. Found in a ternary complex composed
CC of SMAD4, STK11/LKB1 and STK11IP (By similarity). Interacts with NR4A1,
CC p53/TP53, SMAD4, STK11IP and WDR6 (By similarity). Interacts with
CC NISCH; this interaction may increase STK11 activity (By similarity).
CC Interacts with SIRT1; the interaction deacetylates STK11 (By
CC similarity). Interacts with CDKN1A (By similarity).
CC {ECO:0000250|UniProtKB:Q9WTK7, ECO:0000269|PubMed:14511394,
CC ECO:0000269|PubMed:18774945}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18774945}. Cytoplasm
CC {ECO:0000269|PubMed:18774945}. Membrane {ECO:0000269|PubMed:18774945}.
CC Mitochondrion {ECO:0000250}. Note=A small fraction localizes at
CC membranes. Relocates to the cytoplasm when bound to STRAD (STRADA or
CC STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta).
CC Translocates to the mitochondrion during apoptosis (By similarity).
CC PTEN promotes cytoplasmic localization (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Note=Relocates
CC to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25
CC (CAB39/MO25alpha or CAB39L/MO25beta).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=LKB1(L);
CC IsoId=D4AE59-1; Sequence=Displayed;
CC Name=2; Synonyms=LKB1(S);
CC IsoId=D4AE59-2; Sequence=VSP_055418;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, testis, skeletal muscle
CC and spleen, and weakly in liver and kidney. Isoform 1 is expressed at
CC highest levels in the brain. Isoform 2 is expressed at highest levels
CC in the testis, primarily in postmitotic developing germ cells (at
CC protein level). {ECO:0000269|PubMed:18774945}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in testis from 30 days of
CC age, with significantly increased levels by 60 days; this corresponds
CC to the stage when haploid spermatids appear.
CC {ECO:0000269|PubMed:18774945}.
CC -!- PTM: Phosphorylated by ATM at Thr-366 following ionizing radiation
CC (IR). Phosphorylation at Ser-431 by RPS6KA1 and/or some PKA is required
CC to inhibit cell growth. Phosphorylation at Ser-431 is also required
CC during neuronal polarization to mediate phosphorylation of BRSK1 and
CC BRSK2. Phosphorylation by PKC/PRKCZ at Ser-397 in isoform 2 promotes
CC metformin (or peroxynitrite)-induced nuclear export of STK11 and
CC activation of AMPK. UV radiation -induced phosphorylation at Thr-366
CC mediates CDKN1A degradation. {ECO:0000250|UniProtKB:Q9WTK7}.
CC -!- PTM: Acetylated. Deacetylation at Lys-48 enhances cytoplasmic
CC localization and kinase activity in vitro.
CC {ECO:0000269|PubMed:18687677}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. LKB1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC141331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474029; EDL89333.1; -; Genomic_DNA.
DR RefSeq; NP_001101539.1; NM_001108069.1. [D4AE59-1]
DR RefSeq; XP_006240972.1; XM_006240910.1. [D4AE59-2]
DR RefSeq; XP_008763318.1; XM_008765096.1. [D4AE59-1]
DR AlphaFoldDB; D4AE59; -.
DR SMR; D4AE59; -.
DR IntAct; D4AE59; 1.
DR STRING; 10116.ENSRNOP00000057414; -.
DR iPTMnet; D4AE59; -.
DR PaxDb; D4AE59; -.
DR PeptideAtlas; D4AE59; -.
DR PRIDE; D4AE59; -.
DR Ensembl; ENSRNOT00000060683; ENSRNOP00000057414; ENSRNOG00000014287. [D4AE59-2]
DR GeneID; 314621; -.
DR KEGG; rno:314621; -.
DR UCSC; RGD:1308653; rat. [D4AE59-1]
DR CTD; 6794; -.
DR RGD; 1308653; Stk11.
DR VEuPathDB; HostDB:ENSRNOG00000014287; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000158050; -.
DR HOGENOM; CLU_000288_1_2_1; -.
DR InParanoid; D4AE59; -.
DR OMA; GMFAESE; -.
DR OrthoDB; 856506at2759; -.
DR PhylomeDB; D4AE59; -.
DR TreeFam; TF105322; -.
DR Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:D4AE59; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000014287; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; D4AE59; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0140535; C:intracellular protein-containing complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0030275; F:LRR domain binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0043276; P:anoikis; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; IMP:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0071493; P:cellular response to UV-B; ISO:RGD.
DR GO; GO:0097484; P:dendrite extension; ISO:RGD.
DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0070314; P:G1 to G0 transition; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0051645; P:Golgi localization; ISO:RGD.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:RGD.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:1901610; P:positive regulation of vesicle transport along microtubule; IMP:UniProtKB.
DR GO; GO:0045059; P:positive thymic T cell selection; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0033762; P:response to glucagon; IEP:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0033993; P:response to lipid; IDA:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISS:UniProtKB.
DR CDD; cd14119; STKc_LKB1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039154; LKB1_c.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Autophagy;
KW Cell cycle; Cytoplasm; Differentiation; DNA damage; Kinase; Lipoprotein;
KW Magnesium; Manganese; Membrane; Metal-binding; Methylation; Mitochondrion;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Prenylation;
KW Reference proteome; Serine/threonine-protein kinase; Spermatogenesis;
KW Transferase; Tumor suppressor.
FT CHAIN 1..433
FT /note="Serine/threonine-protein kinase STK11"
FT /id="PRO_0000412651"
FT PROPEP 434..436
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422302"
FT DOMAIN 49..309
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 45..90
FT /note="Sufficient for interaction with SIRT1"
FT /evidence="ECO:0000250"
FT REGION 397..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 189
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 296
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 311
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTK7"
FT MOD_RES 336
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 366
FT /note="Phosphothreonine; by ATM and autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 420
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 431
FT /note="Phosphoserine; by autocatalysis, PKA, PKC/PRKCZ and
FT RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT MOD_RES 433
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT MOD_RES 434
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15831"
FT LIPID 422
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 433
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 374..436
FT /note="QVLEEEVGQNGQSHSLPKAVCVNGTEPQLSSKVKPEGRPGAANPARKVCSSN
FT KIRRLSACKQQ -> VEETAESGLSEDACDTCMWKSQGAGLPGEEPEEGFGAVV (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055418"
SQ SEQUENCE 436 AA; 49246 MW; 3CB4B3D86583CF8A CRC64;
MDVADPQPLG LFPEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY
GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHRNV IQLVDVLYNE
EKQKMYMVME YCVCGMQEML DSVPEKRFPV CQAHGYFRQL IDGLEYLHSQ GIVHKDIKPG
NLLLTTNGTL KISDLGVAEA LHPFAVDDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS
AGVTLYNITT GLYPFEGDNI YKLFENIGRG DFTIPCDCAP PLSDLLRGML EYEPAKRFSI
RQIRQHSWFR KKHPLAEALV PIPPSPDTKD RWRSMTVVPY LEDLHGRAEE EEDEDLFDIE
DGIIYTQDFT VPGQVLEEEV GQNGQSHSLP KAVCVNGTEP QLSSKVKPEG RPGAANPARK
VCSSNKIRRL SACKQQ
