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   27-MAR-2024, entry version 176.
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       Q9H093; P31947: SFN; NbExp=2; IntAct=EBI-1181722, EBI-476295;
CC       Q9H093; P62258: YWHAE; NbExp=2; IntAct=EBI-1181722, EBI-356498;
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; CCDS1453.3; -.
DR   RefSeq; NP_112214.2; NM_030952.2.
DR   AlphaFoldDB; Q9H093; -.
DR   SMR; Q9H093; -.
DR   BioGRID; 123581; 48.
DR   IntAct; Q9H093; 41.
DR   STRING; 9606.ENSP00000499251; -.
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   CPTAC; CPTAC-2844; -.
DR   CPTAC; non-CPTAC-2947; -.
DR   EPD; Q9H093; -.
DR   jPOST; Q9H093; -.
DR   MassIVE; Q9H093; -.
DR   MaxQB; Q9H093; -.
DR   PaxDb; 9606-ENSP00000356125; -.
DR   PeptideAtlas; Q9H093; -.
DR   ProteomicsDB; 80220; -.
DR   Antibodypedia; 2090; 296 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   AGR; HGNC:29558; -.
DR   CTD; 81788; -.
DR   DisGeNET; 81788; -.
DR   GeneCards; NUAK2; -.
DR   HGNC; HGNC:29558; NUAK2.
DR   HPA; ENSG00000163545; Tissue enhanced (esophagus, vagina).
DR   MalaCards; NUAK2; -.
DR   MIM; 608131; gene.
DR   MIM; 619452; phenotype.
DR   neXtProt; NX_Q9H093; -.
DR   OpenTargets; ENSG00000163545; -.
DR   Orphanet; 563609; Isolated anencephaly.
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; RPLMKKQ; -.
DR   OrthoDB; 5475340at2759; -.
DR   PhylomeDB; Q9H093; -.
DR   TreeFam; TF324572; -.
DR   PathwayCommons; Q9H093; -.
DR   SignaLink; Q9H093; -.
DR   SIGNOR; Q9H093; -.
DR   BioGRID-ORCS; 81788; 14 hits in 1190 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 144 other cell types or tissues.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; 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:0032007; P:negative regulation of TOR signaling; IBA:GO_Central.
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   CDD; cd14161; STKc_NUAK2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF101; NUAK FAMILY SNF1-LIKE KINASE 1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q9H093; HS.
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
//