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Serine/threonine-protein kinase LATS1 (EC 2.7.11.1) (Large tumor suppressor homolog 1) (WARTS protein kinase) (h-warts)

 LATS1_HUMAN             Reviewed;        1130 AA.
O95835; Q6PKD0;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 173.
RecName: Full=Serine/threonine-protein kinase LATS1;
EC=2.7.11.1;
AltName: Full=Large tumor suppressor homolog 1;
AltName: Full=WARTS protein kinase;
Short=h-warts;
Name=LATS1 {ECO:0000312|EMBL:AAD16882.1};
Synonyms=WARTS {ECO:0000312|EMBL:AAD50272.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD16882.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, AND
INTERACTION WITH CDK1.
TISSUE=Fetal brain {ECO:0000312|EMBL:AAD16882.1};
PubMed=9988268; DOI=10.1038/5960;
Tao W., Zhang S., Turenchalk G.S., Stewart R.A., St John M.A.,
Chen W., Xu T.;
"Human homologue of the Drosophila melanogaster lats tumour suppressor
modulates CDC2 activity.";
Nat. Genet. 21:177-181(1999).
[2] {ECO:0000305, ECO:0000312|EMBL:AAD50272.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
PubMed=10518011; DOI=10.1016/S0014-5793(99)01224-7;
Nishiyama Y., Hirota T., Morisaki T., Hara T., Marumoto T., Iida S.,
Makino K., Yamamoto H., Hiraoka T., Kitamura N., Saya H.;
"A human homolog of Drosophila warts tumor suppressor, h-warts,
localized to mitotic apparatus and specifically phosphorylated during
mitosis.";
FEBS Lett. 459:159-165(1999).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH02767.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Endometrium {ECO:0000312|EMBL:AAH02767.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305}
FUNCTION, AND INTERACTION WITH ZYX.
PubMed=10831611; DOI=10.1083/jcb.149.5.1073;
Hirota T., Morisaki T., Nishiyama Y., Marumoto T., Tada K., Hara T.,
Masuko N., Inagaki M., Hatakeyama K., Saya H.;
"Zyxin, a regulator of actin filament assembly, targets the mitotic
apparatus by interacting with h-warts/LATS1 tumor suppressor.";
J. Cell Biol. 149:1073-1086(2000).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[6] {ECO:0000305}
FUNCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-734.
PubMed=15122335; DOI=10.1038/sj.onc.1207623;
Iida S., Hirota T., Morisaki T., Marumoto T., Hara T., Kuninaka S.,
Honda S., Kosai K., Kawasuji M., Pallas D.C., Saya H.;
"Tumor suppressor WARTS ensures genomic integrity by regulating both
mitotic progression and G1 tetraploidy checkpoint function.";
Oncogene 23:5266-5274(2004).
[7] {ECO:0000305}
FUNCTION, AND INTERACTION WITH LIMK1.
PubMed=15220930; DOI=10.1038/ncb1140;
Yang X., Yu K., Hao Y., Li D.-M., Stewart R.A., Insogna K.L., Xu T.;
"LATS1 tumour suppressor affects cytokinesis by inhibiting LIMK1.";
Nat. Cell Biol. 6:609-617(2004).
[8]
PHOSPHORYLATION AT SER-909 AND THR-1079.
PubMed=15688006; DOI=10.1038/sj.onc.1208445;
Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A.,
Nigg E.A., Sillje H.H.W.;
"The Ste20-like kinase Mst2 activates the human large tumor suppressor
kinase Lats1.";
Oncogene 24:2076-2086(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
FUNCTION, INTERACTION WITH YAP1, AND MUTAGENESIS OF TYR-559.
PubMed=18158288; DOI=10.1074/jbc.M709037200;
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.;
"Tumor suppressor LATS1 is a negative regulator of oncogene YAP.";
J. Biol. Chem. 283:5496-5509(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-278 AND
SER-464, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=20303269; DOI=10.1016/j.cub.2010.02.035;
Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B.,
Longmore G.D.;
"Ajuba LIM proteins are negative regulators of the Hippo signaling
pathway.";
Curr. Biol. 20:657-662(2010).
[17]
INTERACTION WITH MOB1A AND MOB1B.
PubMed=19739119; DOI=10.1002/ijc.24878;
Chow A., Hao Y., Yang X.;
"Molecular characterization of human homologs of yeast MOB1.";
Int. J. Cancer 126:2079-2089(2010).
[18]
FUNCTION, PHOSPHORYLATION AT SER-464, AND MUTAGENESIS OF SER-464.
PubMed=19927127; DOI=10.1038/emboj.2009.342;
Humbert N., Navaratnam N., Augert A., Da Costa M., Martien S.,
Wang J., Martinez D., Abbadie C., Carling D., de Launoit Y., Gil J.,
Bernard D.;
"Regulation of ploidy and senescence by the AMPK-related kinase
NUAK1.";
EMBO J. 29:376-386(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-464 AND
SER-613, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
INTERACTION WITH STK3, AND PHOSPHORYLATION AT THR-1079.
PubMed=28087714; DOI=10.1101/gad.284539.116;
Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S.,
Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.;
"DLG5 connects cell polarity and Hippo signaling protein networks by
linking PAR-1 with MST1/2.";
Genes Dev. 30:2696-2709(2016).
[22]
FUNCTION, AND INTERACTION WITH DCAF13; ESR1 AND DCAF1.
PubMed=28068668; DOI=10.1038/nature20829;
Britschgi A., Duss S., Kim S., Couto J.P., Brinkhaus H., Koren S.,
De Silva D., Mertz K.D., Kaup D., Varga Z., Voshol H., Vissieres A.,
Leroy C., Roloff T., Stadler M.B., Scheel C.H., Miraglia L.J.,
Orth A.P., Bonamy G.M., Reddy V.A., Bentires-Alj M.;
"The Hippo kinases LATS1 and 2 control human breast cell fate via
crosstalk with ERalpha.";
Nature 541:541-545(2017).
[23]
INTERACTION WITH SCRIB.
PubMed=28169360; DOI=10.1038/srep42125;
Liu J., Li J., Li P., Wang Y., Liang Z., Jiang Y., Li J., Feng C.,
Wang R., Chen H., Zhou C., Zhang J., Yang J., Liu P.;
"Loss of DLG5 promotes breast cancer malignancy by inhibiting the
Hippo signaling pathway.";
Sci. Rep. 7:42125-42125(2017).
[24]
VARIANTS [LARGE SCALE ANALYSIS] TRP-96; GLY-204; GLN-237; TRP-370;
SER-531; LEU-641; ILE-669; PRO-806 AND SER-1000.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Negative regulator of YAP1 in the Hippo signaling
pathway that plays a pivotal role in organ size control and tumor
suppression by restricting proliferation and promoting apoptosis.
The core of this pathway is composed of a kinase cascade wherein
STK3/MST2 and STK4/MST1, in complex with its regulatory protein
SAV1, phosphorylates and activates LATS1/2 in complex with its
regulatory protein MOB1, which in turn phosphorylates and
inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of
YAP1 by LATS1 inhibits its translocation into the nucleus to
regulate cellular genes important for cell proliferation, cell
death, and cell migration. Acts as a tumor suppressor which plays
a critical role in maintenance of ploidy through its actions in
both mitotic progression and the G1 tetraploidy checkpoint.
Negatively regulates G2/M transition by down-regulating CDK1
kinase activity. Involved in the control of p53 expression.
Affects cytokinesis by regulating actin polymerization through
negative modulation of LIMK1. May also play a role in endocrine
function. Plays a role in mammary gland epithelial cells
differentiation, both through the Hippo signaling pathway and the
intracellular estrogen receptor signaling pathway by promoting the
degradation of ESR1 (PubMed:28068668).
{ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:10831611,
ECO:0000269|PubMed:15122335, ECO:0000269|PubMed:15220930,
ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:19927127,
ECO:0000269|PubMed:28068668}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:15122335}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Complexes with CDK1 in early mitosis. LATS1-associated
CDK1 has no mitotic cyclin partner and no apparent kinase
activity. Binds phosphorylated ZYX, locating this protein to the
mitotic spindle and suggesting a role for actin regulatory
proteins during mitosis. Binds to and colocalizes with LIMK1 at
the actomyosin contractile ring during cytokinesis. Interacts (via
PPxY motif 2) with YAP1 (via WW domains). Interacts with MOB1A and
MOB1B. Interacts with LIMD1, WTIP and AJUBA. Interacts with ESR1,
DCAF1 and DCAF13; probably recruits DCAF1 and DCAF13 to ESR1 to
promote ESR1 ubiquitination and ubiquitin-mediated proteasomal
degradation (PubMed:28068668). Interacts with STK3/MST2; this
interaction is inhibited in the presence of DLG5
(PubMed:28087714). Interacts with SCRIB in the presence of DLG5
(PubMed:28169360). {ECO:0000269|PubMed:10831611,
ECO:0000269|PubMed:15220930, ECO:0000269|PubMed:18158288,
ECO:0000269|PubMed:19739119, ECO:0000269|PubMed:20303269,
ECO:0000269|PubMed:28068668, ECO:0000269|PubMed:28087714,
ECO:0000269|PubMed:28169360, ECO:0000269|PubMed:9988268}.
-!- INTERACTION:
P06493:CDK1; NbExp=3; IntAct=EBI-444209, EBI-444308;
P24941:CDK2; NbExp=4; IntAct=EBI-444209, EBI-375096;
Q9Y4B6:DCAF1; NbExp=4; IntAct=EBI-444209, EBI-1996353;
P53667:LIMK1; NbExp=5; IntAct=EBI-444209, EBI-444403;
Q9H8S9:MOB1A; NbExp=9; IntAct=EBI-444209, EBI-748229;
Q7L9L4:MOB1B; NbExp=6; IntAct=EBI-444209, EBI-2558745;
P35240:NF2; NbExp=4; IntAct=EBI-444209, EBI-1014472;
P46662:Nf2 (xeno); NbExp=5; IntAct=EBI-444209, EBI-644586;
O60285:NUAK1; NbExp=2; IntAct=EBI-444209, EBI-1046789;
O43255:SIAH2; NbExp=2; IntAct=EBI-444209, EBI-948141;
Q15831:STK11; NbExp=2; IntAct=EBI-444209, EBI-306838;
Q9GZV5:WWTR1; NbExp=5; IntAct=EBI-444209, EBI-747743;
P46937:YAP1; NbExp=9; IntAct=EBI-444209, EBI-1044059;
Q15942:ZYX; NbExp=10; IntAct=EBI-444209, EBI-444225;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:10518011}.
Note=Localizes to the centrosomes throughout interphase but
migrates to the mitotic apparatus, including spindle pole bodies,
mitotic spindle, and midbody, during mitosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:9988268};
IsoId=O95835-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=O95835-2; Sequence=VSP_051604, VSP_051605;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in all adult tissues examined except
for lung and kidney. {ECO:0000269|PubMed:10518011}.
-!- PTM: Autophosphorylated and phosphorylated during M-phase of the
cell cycle. Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079,
which results in its activation. Phosphorylation at Ser-464 by
NUAK1 and NUAK2 leads to decreased protein level and is required
to regulate cellular senescence and cellular ploidy.
{ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:15688006,
ECO:0000269|PubMed:19927127, ECO:0000269|PubMed:9988268}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LATS1ID41127ch6q25.html";
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EMBL; AF104413; AAD16882.1; -; mRNA.
EMBL; AF164041; AAD50272.1; -; mRNA.
EMBL; BC002767; AAH02767.1; -; mRNA.
CCDS; CCDS34551.1; -. [O95835-1]
CCDS; CCDS59040.1; -. [O95835-2]
RefSeq; NP_001257448.1; NM_001270519.1. [O95835-2]
RefSeq; NP_004681.1; NM_004690.3. [O95835-1]
UniGene; Hs.549084; -.
PDB; 4ZRK; X-ray; 2.32 A; E/F/G/H=69-100.
PDB; 5B5W; X-ray; 2.96 A; U=622-704.
PDB; 5BRK; X-ray; 2.30 A; B=602-704.
PDBsum; 4ZRK; -.
PDBsum; 5B5W; -.
PDBsum; 5BRK; -.
ProteinModelPortal; O95835; -.
SMR; O95835; -.
BioGrid; 114563; 106.
CORUM; O95835; -.
DIP; DIP-31516N; -.
IntAct; O95835; 49.
MINT; MINT-2799169; -.
STRING; 9606.ENSP00000253339; -.
BindingDB; O95835; -.
ChEMBL; CHEMBL6167; -.
GuidetoPHARMACOLOGY; 1515; -.
iPTMnet; O95835; -.
PhosphoSitePlus; O95835; -.
BioMuta; LATS1; -.
EPD; O95835; -.
MaxQB; O95835; -.
PaxDb; O95835; -.
PeptideAtlas; O95835; -.
PRIDE; O95835; -.
DNASU; 9113; -.
Ensembl; ENST00000253339; ENSP00000253339; ENSG00000131023. [O95835-1]
Ensembl; ENST00000392273; ENSP00000444678; ENSG00000131023. [O95835-2]
Ensembl; ENST00000543571; ENSP00000437550; ENSG00000131023. [O95835-1]
GeneID; 9113; -.
KEGG; hsa:9113; -.
UCSC; uc003qmu.2; human. [O95835-1]
CTD; 9113; -.
DisGeNET; 9113; -.
EuPathDB; HostDB:ENSG00000131023.12; -.
GeneCards; LATS1; -.
HGNC; HGNC:6514; LATS1.
HPA; HPA031804; -.
MIM; 603473; gene.
neXtProt; NX_O95835; -.
OpenTargets; ENSG00000131023; -.
PharmGKB; PA30301; -.
eggNOG; KOG0605; Eukaryota.
eggNOG; ENOG410XQC0; LUCA.
GeneTree; ENSGT00760000118994; -.
HOGENOM; HOG000040002; -.
HOVERGEN; HBG052311; -.
InParanoid; O95835; -.
KO; K08791; -.
OMA; WQTSLHI; -.
OrthoDB; EOG091G028J; -.
PhylomeDB; O95835; -.
TreeFam; TF351549; -.
Reactome; R-HSA-2028269; Signaling by Hippo.
SignaLink; O95835; -.
SIGNOR; O95835; -.
ChiTaRS; LATS1; human.
GeneWiki; LATS1; -.
GenomeRNAi; 9113; -.
PRO; PR:O95835; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000131023; -.
CleanEx; HS_LATS1; -.
ExpressionAtlas; O95835; baseline and differential.
Genevisible; O95835; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:BHF-UCL.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0035329; P:hippo signaling; IDA:BHF-UCL.
GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0001827; P:inner cell mass cell fate commitment; IEA:Ensembl.
GO; GO:0001828; P:inner cell mass cellular morphogenesis; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0030833; P:regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0046620; P:regulation of organ growth; IBA:GO_Central.
GO; GO:0043254; P:regulation of protein complex assembly; IMP:BHF-UCL.
GO; GO:2000058; P:regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0000819; P:sister chromatid segregation; IDA:UniProtKB.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR028741; LATS1.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like.
PANTHER; PTHR24356:SF138; PTHR24356:SF138; 1.
Pfam; PF00069; Pkinase; 2.
Pfam; PF00627; UBA; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50030; UBA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase; Tumor suppressor.
CHAIN 1 1130 Serine/threonine-protein kinase LATS1.
/FTId=PRO_0000086232.
DOMAIN 100 141 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 705 1010 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 1011 1090 AGC-kinase C-terminal.
NP_BIND 711 719 ATP. {ECO:0000250|UniProtKB:P22612,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 526 655 Interaction with YAP1.
{ECO:0000269|PubMed:18158288}.
MOTIF 373 376 PPxY motif 1.
MOTIF 556 559 PPxY motif 2.
ACT_SITE 828 828 Proton acceptor.
{ECO:0000250|UniProtKB:P22612,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 734 734 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:15122335}.
MOD_RES 246 246 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 464 464 Phosphoserine; by NUAK1 and NUAK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19927127}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 674 674 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 909 909 Phosphoserine; by STK3/MST2.
{ECO:0000269|PubMed:15688006}.
MOD_RES 1079 1079 Phosphothreonine; by STK3/MST2.
{ECO:0000269|PubMed:15688006,
ECO:0000269|PubMed:28087714}.
VAR_SEQ 672 690 GLSQDAQDQMRKMLCQKES -> KPFKMSIFILNHLFAWCL
F (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051604.
VAR_SEQ 691 1130 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051605.
VARIANT 96 96 R -> W (in dbSNP:rs55945045).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040660.
VARIANT 204 204 S -> G (in dbSNP:rs34793526).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040661.
VARIANT 237 237 P -> Q (in dbSNP:rs56149740).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040662.
VARIANT 370 370 R -> W (in dbSNP:rs56348064).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040663.
VARIANT 531 531 P -> S (in dbSNP:rs55874734).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040664.
VARIANT 641 641 F -> L (in dbSNP:rs35163691).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040665.
VARIANT 669 669 M -> I (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040666.
VARIANT 806 806 R -> P (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040667.
VARIANT 1000 1000 G -> S (in dbSNP:rs56412005).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040668.
MUTAGEN 464 464 S->A: Abolishes phosphorylation by NUAK1
and NUAK2. {ECO:0000269|PubMed:19927127}.
MUTAGEN 559 559 Y->F: Loss of interaction with YAP1.
{ECO:0000269|PubMed:18158288}.
MUTAGEN 734 734 K->A: Loss of kinase activity,
autophosphorylation, increased ploidy,
prolonged duration of mitosis and lack of
p53 expression.
{ECO:0000269|PubMed:15122335}.
HELIX 74 85 {ECO:0000244|PDB:4ZRK}.
HELIX 637 671 {ECO:0000244|PDB:5BRK}.
HELIX 675 697 {ECO:0000244|PDB:5BRK}.
SEQUENCE 1130 AA; 126870 MW; 11CFBCD8FD87DCD8 CRC64;
MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA EHNMSKMSTE
DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE VNPQMLQDLQ AAGFDEDMVI
QALQKTNNRS IEAAIEFISK MSYQDPRREQ MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG
SKESLVPQRH GPPLGESVAY HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP
QVRSVTPPPP PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY
PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG TGQTDFMIHQ
NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY TNGSIPQSMM VPNRNSHNME
LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE IPTWQPNIPV RSNSFNNPLG NRASHSANSQ
PSATTVTAIT PAPIQQPVKS MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV
TVMPPVAEAP NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV
DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV LKSHQQRLHR
KKQLENEMMR VGLSQDAQDQ MRKMLCQKES NYIRLKRAKM DKSMFVKIKT LGIGAFGEVC
LARKVDTKAL YATKTLRKKD VLLRNQVAHV KAERDILAEA DNEWVVRLYY SFQDKDNLYF
VMDYIPGGDM MSLLIRMGIF PESLARFYIA ELTCAVESVH KMGFIHRDIK PDNILIDRDG
HIKLTDFGLC TGFRWTHDSK YYQSGDHPRQ DSMDFSNEWG DPSSCRCGDR LKPLERRAAR
QHQRCLAHSL VGTPNYIAPE VLLRTGYTQL CDWWSVGVIL FEMLVGQPPF LAQTPLETQM
KVINWQTSLH IPPQAKLSPE ASDLIIKLCR GPEDRLGKNG ADEIKAHPFF KTIDFSSDLR
QQSASYIPKI THPTDTSNFD PVDPDKLWSD DNEEENVNDT LNGWYKNGKH PEHAFYEFTF
RRFFDDNGYP YNYPKPIEYE YINSQGSEQQ SDEDDQNTGS EIKNRDLVYV


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