ID LATS2_HUMAN Reviewed; 1088 AA. AC Q9NRM7; B1AM47; Q9P2X1; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 203. DE RecName: Full=Serine/threonine-protein kinase LATS2; DE EC=2.7.11.1; DE AltName: Full=Kinase phosphorylated during mitosis protein; DE AltName: Full=Large tumor suppressor homolog 2; DE AltName: Full=Serine/threonine-protein kinase kpm; DE AltName: Full=Warts-like kinase; GN Name=LATS2 {ECO:0000312|EMBL:BAA92381.1}; Synonyms=KPM; 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, ECO:0000312|EMBL:AAF80561.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-697. RC TISSUE=Myeloid {ECO:0000312|EMBL:AAF80561.1}; RX PubMed=10871863; DOI=10.1038/sj.onc.1203659; RA Hori T., Takaori-Kondo A., Kamikubo Y., Uchiyama T.; RT "Molecular cloning of a novel human protein kinase, kpm, that is homologous RT to warts/lats, a Drosophila tumor suppressor."; RL Oncogene 19:3101-3109(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000305, ECO:0000312|EMBL:BAA92381.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-1088, TISSUE SPECIFICITY, AND VARIANT RP VAL-324. RC TISSUE=Testis {ECO:0000269|PubMed:10673337}; RX PubMed=10673337; DOI=10.1006/geno.1999.6065; RA Yabuta N., Fujii T., Copeland N.G., Gilbert D.J., Jenkins N.A., RA Nishiguchi H., Endo Y., Toji S., Tanaka H., Nishimune Y., Nojima H.; RT "Structure, expression, and chromosome mapping of LATS2, a mammalian RT homologue of the Drosophila tumor suppressor gene lats/warts."; RL Genomics 63:263-270(2000). RN [6] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-697 AND SER-872. RX PubMed=12853976; DOI=10.1038/sj.onc.1206603; RA Li Y., Pei J., Xia H., Ke H., Wang H., Tao W.; RT "Lats2, a putative tumor suppressor, inhibits G1/S transition."; RL Oncogene 22:4398-4405(2003). RN [7] {ECO:0000305} RP SUBCELLULAR LOCATION, INTERACTION WITH AURKA, MUTAGENESIS OF SER-83, AND RP PHOSPHORYLATION AT SER-83. RX PubMed=15147269; DOI=10.1111/j.1356-9597.2004.00732.x; RA Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S., RA Tamai K., Nojima H.; RT "The centrosomal protein Lats2 is a phosphorylation target of Aurora-A RT kinase."; RL Genes Cells 9:383-397(2004). RN [8] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH AR. RX PubMed=15131260; DOI=10.1210/me.2004-0065; RA Powzaniuk M., McElwee-Witmer S., Vogel R.L., Hayami T., Rutledge S.J., RA Chen F., Harada S., Schmidt A., Rodan G.A., Freedman L.P., Bai C.; RT "The LATS2/KPM tumor suppressor is a negative regulator of the androgen RT receptor."; RL Mol. Endocrinol. 18:2011-2023(2004). RN [9] RP PHOSPHORYLATION. RX PubMed=15688006; DOI=10.1038/sj.onc.1208445; RA Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A., Nigg E.A., RA Sillje H.H.W.; RT "The Ste20-like kinase Mst2 activates the human large tumor suppressor RT kinase Lats1."; RL Oncogene 24:2076-2086(2005). RN [10] RP INTERACTION WITH AJUBA. RX PubMed=16413547; DOI=10.1016/j.febslet.2005.12.096; RA Abe Y., Ohsugi M., Haraguchi K., Fujimoto J., Yamamoto T.; RT "LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and RT spindle organization during mitosis."; RL FEBS Lett. 580:782-788(2006). RN [11] RP FUNCTION, AND INTERACTION WITH YAP1. RX PubMed=18158288; DOI=10.1074/jbc.m709037200; RA Hao Y., Chun A., Cheung K., Rashidi B., Yang X.; RT "Tumor suppressor LATS1 is a negative regulator of oncogene YAP."; RL J. Biol. Chem. 283:5496-5509(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP INTERACTION WITH LIMD1; WTIP AND AJUBA. RX PubMed=20303269; DOI=10.1016/j.cub.2010.02.035; RA Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B., RA Longmore G.D.; RT "Ajuba LIM proteins are negative regulators of the Hippo signaling RT pathway."; RL Curr. Biol. 20:657-662(2010). RN [14] RP INTERACTION WITH MOB1A AND MOB1B. RX PubMed=19739119; DOI=10.1002/ijc.24878; RA Chow A., Hao Y., Yang X.; RT "Molecular characterization of human homologs of yeast MOB1."; RL Int. J. Cancer 126:2079-2089(2010). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNAI1, AND PHOSPHORYLATION RP AT THR-1041. RX PubMed=21952048; DOI=10.1038/emboj.2011.357; RA Zhang K., Rodriguez-Aznar E., Yabuta N., Owen R.J., Mingot J.M., Nojima H., RA Nieto M.A., Longmore G.D.; RT "Lats2 kinase potentiates Snail1 activity by promoting nuclear retention RT upon phosphorylation."; RL EMBO J. 31:29-43(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND SER-576, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP INTERACTION WITH WWC1; WWC2 AND WWC3. RX PubMed=24682284; DOI=10.1093/molbev/msu115; RA Wennmann D.O., Schmitz J., Wehr M.C., Krahn M.P., Koschmal N., RA Gromnitza S., Schulze U., Weide T., Chekuri A., Skryabin B.V., Gerke V., RA Pavenstadt H., Duning K., Kremerskothen J.; RT "Evolutionary and Molecular Facts Link the WWC Protein Family to Hippo RT Signaling."; RL Mol. Biol. Evol. 31:1710-1723(2014). RN [19] RP PHOSPHORYLATION BY NUAK2. 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 [20] RP VARIANTS [LARGE SCALE ANALYSIS] GLU-40; LEU-91; VAL-799; GLY-1014 AND RP PRO-1025. 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: 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 LATS2 inhibits its translocation CC into the nucleus to regulate cellular genes important for cell CC proliferation, cell death, and cell migration. Acts as a tumor CC suppressor which plays a critical role in centrosome duplication, CC maintenance of mitotic fidelity and genomic stability. Negatively CC regulates G1/S transition by down-regulating cyclin E/CDK2 kinase CC activity. Negative regulator of the androgen receptor. Phosphorylates CC SNAI1 in the nucleus leading to its nuclear retention and CC stabilization, which enhances its epithelial-mesenchymal transition and CC tumor cell invasion/migration activities. This tumor-promoting activity CC is independent of its effects upon YAP1 or WWTR1/TAZ. CC {ECO:0000269|PubMed:10871863, ECO:0000269|PubMed:12853976, CC ECO:0000269|PubMed:15131260, ECO:0000269|PubMed:18158288, CC ECO:0000269|PubMed:21952048}. 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:10871863}; 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:10871863}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Interacts with and is phosphorylated by AURKA. Binds to AR. CC Interacts with AJUBA during mitosis and this complex regulates CC organization of the spindle apparatus through recruitment of gamma- CC tubulin to the centrosome. Interacts (via PPxY motif) with YAP1 (via WW CC domains). Interacts with MOB1A and MOB1B. Interacts with LIMD1, WTIP CC and AJUBA. Interacts with SNAI1. Interacts with WWC1, WWC2 and WWC3 CC (via their WW domains)(PubMed:24682284). {ECO:0000269|PubMed:15131260, CC ECO:0000269|PubMed:15147269, ECO:0000269|PubMed:16413547, CC ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:19739119, CC ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:21952048, CC ECO:0000269|PubMed:24682284}. CC -!- INTERACTION: CC Q9NRM7; Q96IF1: AJUBA; NbExp=6; IntAct=EBI-3506895, EBI-949782; CC Q9NRM7; Q9Y4B6: DCAF1; NbExp=2; IntAct=EBI-3506895, EBI-1996353; CC Q9NRM7; Q13643: FHL3; NbExp=4; IntAct=EBI-3506895, EBI-741101; CC Q9NRM7; Q9H8S9: MOB1A; NbExp=4; IntAct=EBI-3506895, EBI-748229; CC Q9NRM7; Q7L9L4: MOB1B; NbExp=5; IntAct=EBI-3506895, EBI-2558745; CC Q9NRM7; O43255: SIAH2; NbExp=6; IntAct=EBI-3506895, EBI-948141; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. CC Nucleus. Note=Colocalizes with AURKA at the centrosomes during CC interphase, early prophase and cytokinesis. Migrates to the spindle CC poles during mitosis, and to the midbody during cytokinesis. CC Translocates to the nucleus upon mitotic stress by nocodazole CC treatment. CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart and skeletal CC muscle and at lower levels in all other tissues examined. CC {ECO:0000269|PubMed:10673337, ECO:0000269|PubMed:10871863}. CC -!- PTM: Autophosphorylated and phosphorylated during M-phase and the G1/S- CC phase of the cell cycle. Phosphorylated and activated by STK3/MST2. CC Phosphorylation by NUAK2 may regulate its activity in phosphorylation CC and inactivation YAP1 (PubMed:32845958). {ECO:0000269|PubMed:15147269, CC ECO:0000269|PubMed:15688006, ECO:0000269|PubMed:21952048, CC ECO:0000269|PubMed:32845958}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA92381.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41128/LATS2"; 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; AF207547; AAF80561.1; -; mRNA. DR EMBL; AK314235; BAG36905.1; -; mRNA. DR EMBL; AL161613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356285; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08286.1; -; Genomic_DNA. DR EMBL; AB028019; BAA92381.1; ALT_FRAME; mRNA. DR CCDS; CCDS9294.1; -. DR RefSeq; NP_055387.2; NM_014572.2. DR RefSeq; XP_005266399.1; XM_005266342.1. DR PDB; 4ZRI; X-ray; 2.70 A; C/D=68-99. DR PDBsum; 4ZRI; -. DR AlphaFoldDB; Q9NRM7; -. DR SMR; Q9NRM7; -. DR BioGRID; 117727; 291. DR CORUM; Q9NRM7; -. DR DIP; DIP-43883N; -. DR ELM; Q9NRM7; -. DR IntAct; Q9NRM7; 83. DR MINT; Q9NRM7; -. DR STRING; 9606.ENSP00000372035; -. DR BindingDB; Q9NRM7; -. DR ChEMBL; CHEMBL5907; -. DR DrugCentral; Q9NRM7; -. DR GuidetoPHARMACOLOGY; 1516; -. DR GlyCosmos; Q9NRM7; 1 site, 1 glycan. DR GlyGen; Q9NRM7; 8 sites, 1 O-linked glycan (8 sites). DR iPTMnet; Q9NRM7; -. DR PhosphoSitePlus; Q9NRM7; -. DR BioMuta; LATS2; -. DR DMDM; 212276441; -. DR EPD; Q9NRM7; -. DR jPOST; Q9NRM7; -. DR MassIVE; Q9NRM7; -. DR MaxQB; Q9NRM7; -. DR PaxDb; 9606-ENSP00000372035; -. DR PeptideAtlas; Q9NRM7; -. DR ProteomicsDB; 82392; -. DR Pumba; Q9NRM7; -. DR Antibodypedia; 22361; 374 antibodies from 31 providers. DR DNASU; 26524; -. DR Ensembl; ENST00000382592.5; ENSP00000372035.4; ENSG00000150457.9. DR GeneID; 26524; -. DR KEGG; hsa:26524; -. DR MANE-Select; ENST00000382592.5; ENSP00000372035.4; NM_014572.3; NP_055387.2. DR UCSC; uc001unr.6; human. DR AGR; HGNC:6515; -. DR CTD; 26524; -. DR DisGeNET; 26524; -. DR GeneCards; LATS2; -. DR HGNC; HGNC:6515; LATS2. DR HPA; ENSG00000150457; Low tissue specificity. DR MIM; 604861; gene. DR neXtProt; NX_Q9NRM7; -. DR OpenTargets; ENSG00000150457; -. DR PharmGKB; PA30302; -. DR VEuPathDB; HostDB:ENSG00000150457; -. DR eggNOG; KOG0608; Eukaryota. DR GeneTree; ENSGT00940000159161; -. DR HOGENOM; CLU_004885_1_0_1; -. DR InParanoid; Q9NRM7; -. DR OMA; FNNHQQP; -. DR OrthoDB; 5348633at2759; -. DR PhylomeDB; Q9NRM7; -. DR TreeFam; TF351549; -. DR PathwayCommons; Q9NRM7; -. DR Reactome; R-HSA-2028269; Signaling by Hippo. DR SignaLink; Q9NRM7; -. DR SIGNOR; Q9NRM7; -. DR BioGRID-ORCS; 26524; 32 hits in 1200 CRISPR screens. DR ChiTaRS; LATS2; human. DR GeneWiki; LATS2; -. DR GenomeRNAi; 26524; -. DR Pharos; Q9NRM7; Tchem. DR PRO; PR:Q9NRM7; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9NRM7; Protein. DR Bgee; ENSG00000150457; Expressed in epithelial cell of pancreas and 196 other cell types or tissues. DR ExpressionAtlas; Q9NRM7; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0035329; P:hippo signaling; IDA:BHF-UCL. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0001827; P:inner cell mass cell fate commitment; IEA:Ensembl. DR GO; GO:0001828; P:inner cell mass cellular morphogenesis; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB. DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0046620; P:regulation of organ growth; IBA:GO_Central. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB. DR CDD; cd21777; MobB_LATS2; 1. DR CDD; cd05626; STKc_LATS2; 1. DR CDD; cd14398; UBA_LATS2; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24356:SF149; SERINE_THREONINE-PROTEIN KINASE LATS2; 1. DR Pfam; PF00069; Pkinase; 2. DR Pfam; PF00433; Pkinase_C; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50030; UBA; 1. DR Genevisible; Q9NRM7; HS. 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; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Tumor suppressor. FT CHAIN 1..1088 FT /note="Serine/threonine-protein kinase LATS2" FT /id="PRO_0000086234" FT DOMAIN 98..139 FT /note="UBA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT DOMAIN 668..973 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 974..1052 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT REGION 24..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 271..323 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 383..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 454..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 543..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 994..1022 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1056..1088 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 515..518 FT /note="PPxY motif" FT COMPBIAS 26..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..478 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 551..571 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1062..1080 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 791 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P22612, FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027" FT BINDING 674..682 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P22612, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 697 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:10871863" FT MOD_RES 83 FT /note="Phosphoserine; by AURKA" FT /evidence="ECO:0000269|PubMed:15147269" FT MOD_RES 279 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 576 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1041 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:21952048" FT VARIANT 40 FT /note="G -> E (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040669" FT VARIANT 91 FT /note="S -> L (in dbSNP:rs55842804)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040670" FT VARIANT 324 FT /note="A -> V (in dbSNP:rs558614)" FT /evidence="ECO:0000269|PubMed:10673337" FT /id="VAR_019789" FT VARIANT 363 FT /note="G -> S (in dbSNP:rs2770928)" FT /id="VAR_047077" FT VARIANT 799 FT /note="I -> V (in dbSNP:rs35368391)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040671" FT VARIANT 1014 FT /note="A -> G (in dbSNP:rs45523141)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040672" FT VARIANT 1025 FT /note="L -> P (in dbSNP:rs56116059)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040673" FT MUTAGEN 83 FT /note="S->C: Fails to localize at the centromere during FT interphase." FT /evidence="ECO:0000269|PubMed:15147269" FT MUTAGEN 83 FT /note="S->E: Fails to localize at the centromere during FT interphase." FT /evidence="ECO:0000269|PubMed:15147269" FT MUTAGEN 697 FT /note="K->A: Loss of kinase activity, autophosphorylation FT and tumor suppressor activity." FT /evidence="ECO:0000269|PubMed:10871863, FT ECO:0000269|PubMed:12853976" FT MUTAGEN 872 FT /note="S->A: Loss of tumor suppressor activity." FT /evidence="ECO:0000269|PubMed:12853976" FT CONFLICT 59..61 FT /note="RQQ -> SSK (in Ref. 5; BAA92381)" FT /evidence="ECO:0000305" FT CONFLICT 436 FT /note="T -> S (in Ref. 5; BAA92381)" FT /evidence="ECO:0000305" FT CONFLICT 711 FT /note="A -> V (in Ref. 1; AAF80561)" FT /evidence="ECO:0000305" FT CONFLICT 868 FT /note="C -> S (in Ref. 5; BAA92381)" FT /evidence="ECO:0000305" FT HELIX 74..84 FT /evidence="ECO:0007829|PDB:4ZRI" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:4ZRI" SQ SEQUENCE 1088 AA; 120136 MW; 2866F6B75637AD36 CRC64; MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSVQGLPAG PNSDTSLDAK VLGSKDATRQ QQQMRATPKF GPYQKALREI RYSLLPFANE SGTSAAAEVN RQMLQELVNA GCDQEMAGRA LKQTGSRSIE AALEYISKMG YLDPRNEQIV RVIKQTSPGK GLMPTPVTRR PSFEGTGDSF ASYHQLSGTP YEGPSFGADG PTALEEMPRP YVDYLFPGVG PHGPGHQHQH PPKGYGASVE AAGAHFPLQG AHYGRPHLLV PGEPLGYGVQ RSPSFQSKTP PETGGYASLP TKGQGGPPGA GLAFPPPAAG LYVPHPHHKQ AGPAAHQLHV LGSRSQVFAS DSPPQSLLTP SRNSLNVDLY ELGSTSVQQW PAATLARRDS LQKPGLEAPP RAHVAFRPDC PVPSRTNSFN SHQPRPGPPG KAEPSLPAPN TVTAVTAAHI LHPVKSVRVL RPEPQTAVGP SHPAWVPAPA PAPAPAPAPA AEGLDAKEEH ALALGGAGAF PLDVEYGGPD RRCPPPPYPK HLLLRSKSEQ YDLDSLCAGM EQSLRAGPNE PEGGDKSRKS AKGDKGGKDK KQIQTSPVPV RKNSRDEEKR ESRIKSYSPY AFKFFMEQHV ENVIKTYQQK VNRRLQLEQE MAKAGLCEAE QEQMRKILYQ KESNYNRLKR AKMDKSMFVK IKTLGIGAFG EVCLACKVDT HALYAMKTLR KKDVLNRNQV AHVKAERDIL AEADNEWVVK LYYSFQDKDS LYFVMDYIPG GDMMSLLIRM EVFPEHLARF YIAELTLAIE SVHKMGFIHR DIKPDNILID LDGHIKLTDF GLCTGFRWTH NSKYYQKGSH VRQDSMEPSD LWDDVSNCRC GDRLKTLEQR ARKQHQRCLA HSLVGTPNYI APEVLLRKGY TQLCDWWSVG VILFEMLVGQ PPFLAPTPTE TQLKVINWEN TLHIPAQVKL SPEARDLITK LCCSADHRLG RNGADDLKAH PFFSAIDFSS DIRKQPAPYV PTISHPMDTS NFDPVDEESP WNDASEGSTK AWDTLTSPNN KHPEHAFYEF TFRRFFDDNG YPFRCPKPSG AEASQAESSD LESSDLVDQT EGCQPVYV //