NUAK2_HUMAN
ID NUAK2_HUMAN Reviewed; 628 AA.
AC Q9H093;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=NUAK family SNF1-like kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=Omphalocele kinase 2;
DE AltName: Full=SNF1/AMP kinase-related kinase;
DE Short=SNARK;
GN Name=NUAK2 {ECO:0000312|EMBL:AAH17306.1}; Synonyms=OMPHK2, SNARK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 205-224, FUNCTION, ACTIVITY
RP REGULATION, PHOSPHORYLATION AT THR-208, AND MUTAGENESIS OF THR-208.
RX PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
RA Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J.,
RA Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.;
RT "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily,
RT including MARK/PAR-1.";
RL EMBO J. 23:833-843(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB66825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:CAB66825.1};
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC11234.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma {ECO:0000312|EMBL:BAC11234.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4] {ECO:0000312|EMBL:AAH17306.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph {ECO:0000312|EMBL:AAH17306.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=14575707; DOI=10.1016/j.bbrc.2003.09.184;
RA Suzuki A., Kusakai G., Kishimoto A., Minegichi Y., Ogura T., Esumi H.;
RT "Induction of cell-cell detachment during glucose starvation through F-
RT actin conversion by SNARK, the fourth member of the AMP-activated protein
RT kinase catalytic subunit family.";
RL Biochem. Biophys. Res. Commun. 311:156-161(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-81.
RX PubMed=15345718; DOI=10.1074/jbc.m404334200;
RA Legembre P., Schickel R., Barnhart B.C., Peter M.E.;
RT "Identification of SNF1/AMP kinase-related kinase as an NF-kappaB-regulated
RT anti-apoptotic kinase involved in CD95-induced motility and invasiveness.";
RL J. Biol. Chem. 279:46742-46747(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-523; SER-544 AND
RP SER-547, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP FUNCTION.
RX PubMed=19927127; DOI=10.1038/emboj.2009.342;
RA Humbert N., Navaratnam N., Augert A., Da Costa M., Martien S., Wang J.,
RA Martinez D., Abbadie C., Carling D., de Launoit Y., Gil J., Bernard D.;
RT "Regulation of ploidy and senescence by the AMPK-related kinase NUAK1.";
RL EMBO J. 29:376-386(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP INVOLVEMENT IN ANPH2, VARIANT ANPH2 138-TYR--GLN-145 DELINS GLU,
RP CHARACTERIZATION OF VARIANT ANPH2 138-TYR--GLN-145 DELINS GLU, FUNCTION,
RP AND PHOSPHORYLATION AT THR-208.
RX PubMed=32845958; DOI=10.1084/jem.20191561;
RA Bonnard C., Navaratnam N., Ghosh K., Chan P.W., Tan T.T., Pomp O.,
RA Ng A.Y.J., Tohari S., Changede R., Carling D., Venkatesh B., Altunoglu U.,
RA Kayserili H., Reversade B.;
RT "A loss-of-function NUAK2 mutation in humans causes anencephaly due to
RT impaired Hippo-YAP signaling.";
RL J. Exp. Med. 217:0-0(2020).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-309; LEU-341; ARG-503; VAL-516 AND
RP GLU-541.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Stress-activated kinase involved in tolerance to glucose
CC starvation. Induces cell-cell detachment by increasing F-actin
CC conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via
CC NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required
CC for the increased motility and invasiveness of CD95-activated tumor
CC cells. Phosphorylates LATS1 and LATS2. Plays a key role in neural tube
CC closure during embryonic development through LATS2 phosphorylation and
CC regulation of the nuclear localization of YAP1 a critical downstream
CC regulatory target in the Hippo signaling pathway (PubMed:32845958).
CC {ECO:0000269|PubMed:14575707, ECO:0000269|PubMed:14976552,
CC ECO:0000269|PubMed:15345718, ECO:0000269|PubMed:19927127,
CC ECO:0000269|PubMed:32845958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:14575707, ECO:0000269|PubMed:14976552};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:14575707,
CC ECO:0000269|PubMed:14976552};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14575707, ECO:0000269|PubMed:14976552};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-208.
CC {ECO:0000269|PubMed:14976552}.
CC -!- INTERACTION:
CC Q9H093; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-1181722, EBI-717919;
CC -!- PTM: Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39
CC (PubMed:14976552). Autophosphorylation is also possible at Thr-208
CC (PubMed:32845958). {ECO:0000269|PubMed:14976552,
CC ECO:0000269|PubMed:32845958}.
CC -!- DISEASE: Anencephaly 2 (ANPH2) [MIM:619452]: A form of anencephaly, an
CC extreme neural tube defect resulting in the absence of brain tissues,
CC and death in utero or perinatally. Infants are born with intact spinal
CC cords, cerebellums, and brainstems, but lack formation of neural
CC structures above this level. The skull is only partially formed. ANPH2
CC features may also include frontonasal dysplasia with midline cleft of
CC the upper lip and alveolar ridge, bifid nose, and clinical
CC anophthalmia. ANPH2 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:32845958}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AL136891; CAB66825.1; -; mRNA.
DR EMBL; AK074830; BAC11234.1; -; mRNA.
DR EMBL; BC017306; AAH17306.1; -; mRNA.
DR CCDS; CCDS1453.2; -.
DR RefSeq; NP_112214.2; NM_030952.2.
DR AlphaFoldDB; Q9H093; -.
DR SMR; Q9H093; -.
DR BioGRID; 123581; 21.
DR IntAct; Q9H093; 41.
DR STRING; 9606.ENSP00000356125; -.
DR BindingDB; Q9H093; -.
DR ChEMBL; CHEMBL5698; -.
DR DrugBank; DB11936; Bempedoic acid.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9H093; -.
DR GuidetoPHARMACOLOGY; 2130; -.
DR GlyGen; Q9H093; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H093; -.
DR PhosphoSitePlus; Q9H093; -.
DR BioMuta; NUAK2; -.
DR DMDM; 74761376; -.
DR EPD; Q9H093; -.
DR jPOST; Q9H093; -.
DR MassIVE; Q9H093; -.
DR MaxQB; Q9H093; -.
DR PaxDb; Q9H093; -.
DR PeptideAtlas; Q9H093; -.
DR PRIDE; Q9H093; -.
DR ProteomicsDB; 80220; -.
DR Antibodypedia; 2090; 274 antibodies from 30 providers.
DR DNASU; 81788; -.
DR Ensembl; ENST00000367157.6; ENSP00000356125.5; ENSG00000163545.11.
DR GeneID; 81788; -.
DR KEGG; hsa:81788; -.
DR MANE-Select; ENST00000367157.6; ENSP00000356125.5; NM_030952.3; NP_112214.3.
DR UCSC; uc001hce.4; human.
DR CTD; 81788; -.
DR DisGeNET; 81788; -.
DR GeneCards; NUAK2; -.
DR HGNC; HGNC:29558; NUAK2.
DR HPA; ENSG00000163545; Tissue enhanced (esophagus, vagina).
DR MIM; 608131; gene.
DR MIM; 619452; phenotype.
DR neXtProt; NX_Q9H093; -.
DR OpenTargets; ENSG00000163545; -.
DR PharmGKB; PA142671243; -.
DR VEuPathDB; HostDB:ENSG00000163545; -.
DR eggNOG; KOG0611; Eukaryota.
DR GeneTree; ENSGT00940000158422; -.
DR HOGENOM; CLU_000288_63_42_1; -.
DR InParanoid; Q9H093; -.
DR OMA; NWGYKVP; -.
DR OrthoDB; 1539664at2759; -.
DR PhylomeDB; Q9H093; -.
DR TreeFam; TF324572; -.
DR PathwayCommons; Q9H093; -.
DR SignaLink; Q9H093; -.
DR SIGNOR; Q9H093; -.
DR BioGRID-ORCS; 81788; 12 hits in 1109 CRISPR screens.
DR ChiTaRS; NUAK2; human.
DR GeneWiki; NUAK2; -.
DR GenomeRNAi; 81788; -.
DR Pharos; Q9H093; Tchem.
DR PRO; PR:Q9H093; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H093; protein.
DR Bgee; ENSG00000163545; Expressed in cervix squamous epithelium and 142 other tissues.
DR Genevisible; Q9H093; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0035330; P:regulation of hippo signaling; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; Apoptosis; ATP-binding; Direct protein sequencing;
KW Disease variant; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..628
FT /note="NUAK family SNF1-like kinase 2"
FT /id="PRO_0000247756"
FT DOMAIN 53..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 355..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60285,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O60285,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:15345718"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 208
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000269|PubMed:14976552,
FT ECO:0000269|PubMed:32845958"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZN4"
FT VARIANT 138..145
FT /note="YDYISERQ -> E (in ANPH2; no effect on protein
FT abundance; loss of protein serine/threonine kinase
FT activity; loss of autophosphorylation at T-208; loss of
FT function in regulation of hippo signaling)"
FT /evidence="ECO:0000269|PubMed:32845958"
FT /id="VAR_086106"
FT VARIANT 309
FT /note="T -> S (in dbSNP:rs55745939)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040964"
FT VARIANT 341
FT /note="R -> L (in dbSNP:rs35208615)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040965"
FT VARIANT 503
FT /note="K -> R (in an ovarian Endometrioid carcinoma sample;
FT somatic mutation; dbSNP:rs1271546767)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040966"
FT VARIANT 516
FT /note="A -> V (in dbSNP:rs35070935)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040967"
FT VARIANT 541
FT /note="G -> E (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040968"
FT MUTAGEN 81
FT /note="K->R: Loss of autophosphorylation, kinase activity
FT and of anti-apoptotic activity."
FT /evidence="ECO:0000269|PubMed:15345718"
FT MUTAGEN 208
FT /note="T->A: Prevents phosphorylation and activation by
FT STK11/LKB1 complex."
FT /evidence="ECO:0000269|PubMed:14976552"
SQ SEQUENCE 628 AA; 69612 MW; F76F8B1BF94F4C87 CRC64;
MESLVFARRS GPTPSAAELA RPLAEGLIKS PKPLMKKQAV KRHHHKHNLR HRYEFLETLG
KGTYGKVKKA RESSGRLVAI KSIRKDKIKD EQDLMHIRRE IEIMSSLNHP HIIAIHEVFE
NSSKIVIVME YASRGDLYDY ISERQQLSER EARHFFRQIV SAVHYCHQNR VVHRDLKLEN
ILLDANGNIK IADFGLSNLY HQGKFLQTFC GSPLYASPEI VNGKPYTGPE VDSWSLGVLL
YILVHGTMPF DGHDHKILVK QISNGAYREP PKPSDACGLI RWLLMVNPTR RATLEDVASH
WWVNWGYATR VGEQEAPHEG GHPGSDSARA SMADWLRRSS RPLLENGAKV CSFFKQHAPG
GGSTTPGLER QHSLKKSRKE NDMAQSLHSD TADDTAHRPG KSNLKLPKGI LKKKVSASAE
GVQEDPPELS PIPASPGQAA PLLPKKGILK KPRQRESGYY SSPEPSESGE LLDAGDVFVS
GDPKEQKPPQ ASGLLLHRKG ILKLNGKFSQ TALELAAPTT FGSLDELAPP RPLARASRPS
GAVSEDSILS SESFDQLDLP ERLPEPPLRG CVSVDNLTGL EEPPSEGPGS CLRRWRQDPL
GDSCFSLTDC QEVTATYRQA LRVCSKLT
