LATS1_MOUSE
ID LATS1_MOUSE Reviewed; 1129 AA.
AC Q8BYR2; B2RY46; Q9Z0W4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Serine/threonine-protein kinase LATS1;
DE EC=2.7.11.1;
DE AltName: Full=Large tumor suppressor homolog 1;
DE AltName: Full=WARTS protein kinase;
GN Name=Lats1 {ECO:0000312|EMBL:AAD16883.1};
GN Synonyms=Warts {ECO:0000250|UniProtKB:O95835};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-602.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAD16883.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-1129.
RC TISSUE=Brain {ECO:0000312|EMBL:AAD16883.1};
RX PubMed=9988268; DOI=10.1038/5960;
RA Tao W., Zhang S., Turenchalk G.S., Stewart R.A., St John M.A., Chen W.,
RA Xu T.;
RT "Human homologue of the Drosophila melanogaster lats tumour suppressor
RT modulates CDC2 activity.";
RL Nat. Genet. 21:177-181(1999).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=9988269; DOI=10.1038/5965;
RA St John M.A., Tao W., Fei X., Fukumoto R., Carcangiu M.L., Brownstein D.G.,
RA Parlow A.F., McGrath J., Xu T.;
RT "Mice deficient of Lats1 develop soft-tissue sarcomas, ovarian tumours and
RT pituitary dysfunction.";
RL Nat. Genet. 21:182-186(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-463 AND SER-612, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH WWTR1.
RX PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
RA Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
RA Larsen B.G., Rossant J., Wrana J.L.;
RT "The Crumbs complex couples cell density sensing to Hippo-dependent control
RT of the TGF-beta-SMAD pathway.";
RL Dev. Cell 19:831-844(2010).
CC -!- FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway
CC that plays a pivotal role in organ size control and tumor suppression
CC by restricting proliferation and promoting apoptosis. The core of this
CC pathway is composed of a kinase cascade wherein STK3/MST2 and
CC STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates
CC and activates LATS1/2 in complex with its regulatory protein MOB1,
CC which in turn phosphorylates and inactivates YAP1 oncoprotein and
CC WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation
CC into the nucleus to regulate cellular genes important for cell
CC proliferation, cell death, and cell migration (PubMed:21145499). Acts
CC as a tumor suppressor which plays a critical role in maintenance of
CC ploidy through its actions in both mitotic progression and the G1
CC tetraploidy checkpoint. Negatively regulates G2/M transition by down-
CC regulating CDK1 kinase activity. Involved in the control of p53
CC expression. Affects cytokinesis by regulating actin polymerization
CC through negative modulation of LIMK1. May also play a role in endocrine
CC function. Plays a role in mammary gland epithelial cell
CC differentiation, both through the Hippo signaling pathway and the
CC intracellular estrogen receptor signaling pathway by promoting the
CC degradation of ESR1. {ECO:0000250|UniProtKB:O95835,
CC ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:9988269}.
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:0000250|UniProtKB:O95835};
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:0000250|UniProtKB:O95835};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Complexes with CDK1 in early mitosis (By similarity). LATS1-
CC associated CDK1 has no mitotic cyclin partner and no apparent kinase
CC activity (By similarity). Binds phosphorylated ZYX, locating this
CC protein to the mitotic spindle and suggesting a role for actin
CC regulatory proteins during mitosis (By similarity). Binds to and
CC colocalizes with LIMK1 at the actomyosin contractile ring during
CC cytokinesis (By similarity). Interacts (via PPxY motif 2) with YAP1
CC (via WW domains) (By similarity). Interacts with MOB1A and MOB1B.
CC Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with
CC ESR1, DCAF1 and DCAF13; probably recruits DCAF1 and DCAF13 to ESR1 to
CC promote ESR1 ubiquitination and ubiquitin-mediated proteasomal
CC degradation (By similarity). Interacts with STK3/MST2; this interaction
CC is inhibited in the presence of DLG5 (By similarity). Interacts with
CC SCRIB in the presence of DLG5 (By similarity). Interacts with WWTR1/TAZ
CC (PubMed:21145499). {ECO:0000250|UniProtKB:O95835,
CC ECO:0000269|PubMed:21145499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:O95835}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:O95835}. Midbody
CC {ECO:0000250|UniProtKB:O95835}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000250|UniProtKB:O95835}.
CC Note=Localizes to the centrosomes throughout interphase but migrates to
CC the mitotic apparatus, including spindle pole bodies, mitotic spindle,
CC and midbody, during mitosis. {ECO:0000250|UniProtKB:O95835}.
CC -!- PTM: Autophosphorylated and phosphorylated during M-phase of the cell
CC cycle (By similarity). Phosphorylated by STK3/MST2 at Ser-908 and Thr-
CC 1078, which results in its activation (By similarity). Phosphorylation
CC at Ser-463 by NUAK1 and NUAK2 leads to decreased protein level and is
CC required to regulate cellular senescence and cellular ploidy (By
CC similarity). {ECO:0000250|UniProtKB:O95835}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC158092; AAI58093.1; -; mRNA.
DR EMBL; BC158123; AAI58124.1; -; mRNA.
DR EMBL; AK038612; BAC30063.1; -; mRNA.
DR EMBL; AF104414; AAD16883.1; -; mRNA.
DR CCDS; CCDS48494.1; -.
DR RefSeq; NP_034820.1; NM_010690.1.
DR PDB; 5B6B; X-ray; 3.54 A; C/E/G/I/J/L/N/P=621-703.
DR PDB; 6J68; X-ray; 2.50 A; C/D=545-568.
DR PDBsum; 5B6B; -.
DR PDBsum; 6J68; -.
DR AlphaFoldDB; Q8BYR2; -.
DR SMR; Q8BYR2; -.
DR BioGRID; 201113; 8.
DR DIP; DIP-47647N; -.
DR IntAct; Q8BYR2; 2.
DR MINT; Q8BYR2; -.
DR STRING; 10090.ENSMUSP00000132078; -.
DR iPTMnet; Q8BYR2; -.
DR PhosphoSitePlus; Q8BYR2; -.
DR EPD; Q8BYR2; -.
DR jPOST; Q8BYR2; -.
DR MaxQB; Q8BYR2; -.
DR PaxDb; Q8BYR2; -.
DR PeptideAtlas; Q8BYR2; -.
DR PRIDE; Q8BYR2; -.
DR ProteomicsDB; 264917; -.
DR Antibodypedia; 33280; 409 antibodies from 32 providers.
DR DNASU; 16798; -.
DR Ensembl; ENSMUST00000040043; ENSMUSP00000041915; ENSMUSG00000040021.
DR Ensembl; ENSMUST00000165952; ENSMUSP00000132078; ENSMUSG00000040021.
DR Ensembl; ENSMUST00000217931; ENSMUSP00000151533; ENSMUSG00000040021.
DR GeneID; 16798; -.
DR KEGG; mmu:16798; -.
DR UCSC; uc007eig.2; mouse.
DR CTD; 9113; -.
DR MGI; MGI:1333883; Lats1.
DR VEuPathDB; HostDB:ENSMUSG00000040021; -.
DR eggNOG; KOG0608; Eukaryota.
DR GeneTree; ENSGT00940000157684; -.
DR HOGENOM; CLU_004885_1_2_1; -.
DR InParanoid; Q8BYR2; -.
DR OMA; YQSGDHA; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q8BYR2; -.
DR TreeFam; TF351549; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 16798; 2 hits in 80 CRISPR screens.
DR ChiTaRS; Lats1; mouse.
DR PRO; PR:Q8BYR2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BYR2; protein.
DR Bgee; ENSMUSG00000040021; Expressed in undifferentiated genital tubercle and 65 other tissues.
DR Genevisible; Q8BYR2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISO:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; IGI:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0001827; P:inner cell mass cell fate commitment; IGI:MGI.
DR GO; GO:0001828; P:inner cell mass cellular morphogenesis; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030216; P:keratinocyte differentiation; IGI:MGI.
DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046620; P:regulation of organ growth; IBA:GO_Central.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000819; P:sister chromatid segregation; ISS:UniProtKB.
DR CDD; cd05625; STKc_LATS1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028741; LATS1.
DR InterPro; IPR042706; LATS1_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR24356:SF138; PTHR24356:SF138; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Metal-binding; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tumor suppressor.
FT CHAIN 1..1129
FT /note="Serine/threonine-protein kinase LATS1"
FT /id="PRO_0000086233"
FT DOMAIN 100..141
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 704..1009
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1010..1089
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..654
FT /note="Interaction with YAP1"
FT /evidence="ECO:0000250"
FT REGION 1104..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..375
FT /note="PPxY motif 1"
FT MOTIF 555..558
FT /note="PPxY motif 2"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 827
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P22612,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 710..718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22612,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O95835,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 463
FT /note="Phosphoserine; by NUAK1 and NUAK2"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95835"
FT MOD_RES 908
FT /note="Phosphoserine; by STK3/MST2"
FT /evidence="ECO:0000250|UniProtKB:O95835"
FT MOD_RES 1078
FT /note="Phosphothreonine; by STK3/MST2"
FT /evidence="ECO:0000250|UniProtKB:O95835"
FT CONFLICT 940
FT /note="F -> C (in Ref. 3; AAD16883)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="N -> I (in Ref. 3; AAD16883)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="N -> S (in Ref. 3; AAD16883)"
FT /evidence="ECO:0000305"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:6J68"
SQ SEQUENCE 1129 AA; 126258 MW; FCDC2EC8BC2FF2DE CRC64;
MKRGEKPEGY RQMRPKTFPA SNYPGSSRQM LQEIRESLRN LSKPSDASKA EHNLNKMSTE
DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETSSSRSPSE VNPQMFQDLQ AAGFDEDMVI
QALQKTNNRS IEAAVEFISK MSYQDPRREQ MSAAAARPIN ATMKPGNVQH SINRKQSWKG
SKESLVPQRH GPSLGENVVY RSESPNSQAD VGRPLSGSGI AAFAQAHPSN GQRVNPPPPP
QVRSVTPPPP PRGQTPPPRG TTPPPPSWEP SSQTKRYSGN MEYVISRISP VPPGAWQEGY
PPPPLTTSPM NPPSQAQRAI SSVPVGRQPI IMQSTSKFNF TPGRPGVQNG GGQSDFIVHQ
NVPTGSVTRQ PPPPYPLTPA NGQSPSALQT GASAAPPSFA NGNVPQSMMV PNRNSHNMEL
YNINVPGLQT AWPQSSSAPA QSSPSGGHEI PTWQPNIPVR SNSFNNPLGS RASHSANSQP
SATTVTAITP APIQQPVKSM RVLKPELQTA LAPTHPSWMP QPVQTVQPTP FSEGTASSVP
VIPPVAEAPS YQGPPPPYPK HLLHQNPSVP PYESVSKPCK DEQPSLPKED DSEKSADSGD
SGDKEKKQIT TSPITVRKNK KDEERRESRI QSYSPQAFKF FMEQHVENVL KSHQQRLHRK
KQLENEMMRV GLSQDAQDQM RKMLCQKESN YIRLKRAKMD KSMFVKIKTL GIGAFGEVCL
ARKVDTKALY ATKTLRKKDV LLRNQVAHVK AERDILAEAD NEWVVRLYYS FQDKDNLYFV
MDYIPGGDMM SLLIRMGIFP ENLARFYIAE LTCAVESVHK MGFIHRDIKP DNILIDRDGH
IKLTDFGLCT GFRWTHDSKY YQSGDHPRQD SMDFSNEWGD PSNCRCGDRL KPLERRAARQ
HQRCLAHSLV GTPNYIAPEV LLRTGYTQLC DWWSVGVILF EMLVGQPPFL AQTPLETQMK
VINWQTSLHI PPQAKLSPEA SDLIIKLCRG PEDRLGKNGA DEIKAHPFFK TIDFSSDLRQ
QSASYIPKIT HPTDTSNFDP VDPDKLWSDG SEEENISDTL NGWYKNGKHP EHAFYEFTFR
RFFDDNGYPY NYPKPIEYEY IHSQGSEQQS DEDDQHTSSD GNNRDLVYV
