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Q8BYR2

- LATS1_MOUSE

UniProt

Q8BYR2 - LATS1_MOUSE

Protein

Serine/threonine-protein kinase LATS1

Gene

Lats1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.By similarity

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei733 – 7331ATPBy similarityPROSITE-ProRule annotation
    Active sitei827 – 8271Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi710 – 7189ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein localization Source: MGI
    2. cytoplasmic sequestering of protein Source: Ensembl
    3. G2/M transition of mitotic cell cycle Source: UniProtKB
    4. hippo signaling Source: MGI
    5. hormone-mediated signaling pathway Source: UniProtKB
    6. keratinocyte differentiation Source: MGI
    7. mitotic nuclear division Source: UniProtKB-KW
    8. negative regulation of canonical Wnt signaling pathway Source: Ensembl
    9. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    10. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    11. protein phosphorylation Source: UniProtKB
    12. regulation of actin filament polymerization Source: UniProtKB
    13. sister chromatid segregation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196537. Signaling by Hippo.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase LATS1 (EC:2.7.11.1)
    Alternative name(s):
    Large tumor suppressor homolog 1
    WARTS protein kinase
    Gene namesi
    Name:Lats1Imported
    Synonyms:WartsBy similarity
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1333883. Lats1.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle By similarity
    Note: Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11291129Serine/threonine-protein kinase LATS1PRO_0000086233Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphothreonine1 Publication
    Modified residuei278 – 2781PhosphoserineBy similarity
    Modified residuei463 – 4631Phosphoserine; alternate2 Publications
    Modified residuei463 – 4631Phosphoserine; by NUAK1 and NUAK2; alternate2 Publications
    Modified residuei612 – 6121Phosphoserine1 Publication
    Modified residuei673 – 6731PhosphoserineBy similarity
    Modified residuei908 – 9081Phosphoserine; by STK3/MST2By similarity
    Modified residuei1078 – 10781Phosphothreonine; by STK3/MST2By similarity

    Post-translational modificationi

    Autophosphorylated and phosphorylated during M-phase of the cell cycle. Phosphorylated by STK3/MST2 at Ser-908 and Thr-1078, which results in its activation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8BYR2.
    PRIDEiQ8BYR2.

    PTM databases

    PhosphoSiteiQ8BYR2.

    Expressioni

    Gene expression databases

    BgeeiQ8BYR2.
    CleanExiMM_LATS1.
    GenevestigatoriQ8BYR2.

    Interactioni

    Subunit structurei

    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 By similarity. Interacts with LIMD1, WTIP and AJUBA By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201113. 1 interaction.
    DIPiDIP-47647N.
    IntActiQ8BYR2. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BYR2.
    SMRiQ8BYR2. Positions 95-142, 625-1118.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini100 – 14142UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini704 – 1009306Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1010 – 108980AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni525 – 654130Interaction with YAP1By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi372 – 3754PPxY motif 1
    Motifi555 – 5584PPxY motif 2

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117422.
    HOGENOMiHOG000040002.
    HOVERGENiHBG052311.
    InParanoidiB2RY46.
    KOiK08791.
    OMAiAGFDEDM.
    OrthoDBiEOG7BZVS1.
    TreeFamiTF351549.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR028741. LATS1/Warts.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PANTHERiPTHR24356:SF138. PTHR24356:SF138. 1 hit.
    PfamiPF00069. Pkinase. 2 hits.
    PF00627. UBA. 1 hit.
    [Graphical view]
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BYR2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRGEKPEGY RQMRPKTFPA SNYPGSSRQM LQEIRESLRN LSKPSDASKA     50
    EHNLNKMSTE DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETSSSRSPSE 100
    VNPQMFQDLQ AAGFDEDMVI QALQKTNNRS IEAAVEFISK MSYQDPRREQ 150
    MSAAAARPIN ATMKPGNVQH SINRKQSWKG SKESLVPQRH GPSLGENVVY 200
    RSESPNSQAD VGRPLSGSGI AAFAQAHPSN GQRVNPPPPP QVRSVTPPPP 250
    PRGQTPPPRG TTPPPPSWEP SSQTKRYSGN MEYVISRISP VPPGAWQEGY 300
    PPPPLTTSPM NPPSQAQRAI SSVPVGRQPI IMQSTSKFNF TPGRPGVQNG 350
    GGQSDFIVHQ NVPTGSVTRQ PPPPYPLTPA NGQSPSALQT GASAAPPSFA 400
    NGNVPQSMMV PNRNSHNMEL YNINVPGLQT AWPQSSSAPA QSSPSGGHEI 450
    PTWQPNIPVR SNSFNNPLGS RASHSANSQP SATTVTAITP APIQQPVKSM 500
    RVLKPELQTA LAPTHPSWMP QPVQTVQPTP FSEGTASSVP VIPPVAEAPS 550
    YQGPPPPYPK HLLHQNPSVP PYESVSKPCK DEQPSLPKED DSEKSADSGD 600
    SGDKEKKQIT TSPITVRKNK KDEERRESRI QSYSPQAFKF FMEQHVENVL 650
    KSHQQRLHRK KQLENEMMRV GLSQDAQDQM RKMLCQKESN YIRLKRAKMD 700
    KSMFVKIKTL GIGAFGEVCL ARKVDTKALY ATKTLRKKDV LLRNQVAHVK 750
    AERDILAEAD NEWVVRLYYS FQDKDNLYFV MDYIPGGDMM SLLIRMGIFP 800
    ENLARFYIAE LTCAVESVHK MGFIHRDIKP DNILIDRDGH IKLTDFGLCT 850
    GFRWTHDSKY YQSGDHPRQD SMDFSNEWGD PSNCRCGDRL KPLERRAARQ 900
    HQRCLAHSLV GTPNYIAPEV LLRTGYTQLC DWWSVGVILF EMLVGQPPFL 950
    AQTPLETQMK VINWQTSLHI PPQAKLSPEA SDLIIKLCRG PEDRLGKNGA 1000
    DEIKAHPFFK TIDFSSDLRQ QSASYIPKIT HPTDTSNFDP VDPDKLWSDG 1050
    SEEENISDTL NGWYKNGKHP EHAFYEFTFR RFFDDNGYPY NYPKPIEYEY 1100
    IHSQGSEQQS DEDDQHTSSD GNNRDLVYV 1129
    Length:1,129
    Mass (Da):126,258
    Last modified:July 27, 2011 - v3
    Checksum:iFCDC2EC8BC2FF2DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti940 – 9401F → C in AAD16883. (PubMed:9988268)Curated
    Sequence conflicti963 – 9631N → I in AAD16883. (PubMed:9988268)Curated
    Sequence conflicti1061 – 10611N → S in AAD16883. (PubMed:9988268)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC158092 mRNA. Translation: AAI58093.1.
    BC158123 mRNA. Translation: AAI58124.1.
    AK038612 mRNA. Translation: BAC30063.1.
    AF104414 mRNA. Translation: AAD16883.1.
    CCDSiCCDS48494.1.
    RefSeqiNP_034820.1. NM_010690.1.
    UniGeneiMm.34083.

    Genome annotation databases

    EnsembliENSMUST00000040043; ENSMUSP00000041915; ENSMUSG00000040021.
    ENSMUST00000165952; ENSMUSP00000132078; ENSMUSG00000040021.
    GeneIDi16798.
    KEGGimmu:16798.
    UCSCiuc007eig.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC158092 mRNA. Translation: AAI58093.1 .
    BC158123 mRNA. Translation: AAI58124.1 .
    AK038612 mRNA. Translation: BAC30063.1 .
    AF104414 mRNA. Translation: AAD16883.1 .
    CCDSi CCDS48494.1.
    RefSeqi NP_034820.1. NM_010690.1.
    UniGenei Mm.34083.

    3D structure databases

    ProteinModelPortali Q8BYR2.
    SMRi Q8BYR2. Positions 95-142, 625-1118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201113. 1 interaction.
    DIPi DIP-47647N.
    IntActi Q8BYR2. 1 interaction.

    PTM databases

    PhosphoSitei Q8BYR2.

    Proteomic databases

    PaxDbi Q8BYR2.
    PRIDEi Q8BYR2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040043 ; ENSMUSP00000041915 ; ENSMUSG00000040021 .
    ENSMUST00000165952 ; ENSMUSP00000132078 ; ENSMUSG00000040021 .
    GeneIDi 16798.
    KEGGi mmu:16798.
    UCSCi uc007eig.2. mouse.

    Organism-specific databases

    CTDi 9113.
    MGIi MGI:1333883. Lats1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117422.
    HOGENOMi HOG000040002.
    HOVERGENi HBG052311.
    InParanoidi B2RY46.
    KOi K08791.
    OMAi AGFDEDM.
    OrthoDBi EOG7BZVS1.
    TreeFami TF351549.

    Enzyme and pathway databases

    Reactomei REACT_196537. Signaling by Hippo.

    Miscellaneous databases

    NextBioi 290674.
    PROi Q8BYR2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BYR2.
    CleanExi MM_LATS1.
    Genevestigatori Q8BYR2.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR028741. LATS1/Warts.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    PANTHERi PTHR24356:SF138. PTHR24356:SF138. 1 hit.
    Pfami PF00069. Pkinase. 2 hits.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-602.
      Strain: C57BL/6J.
      Tissue: Hypothalamus.
    3. "Human homologue of the Drosophila melanogaster lats tumour suppressor modulates CDC2 activity."
      Tao W., Zhang S., Turenchalk G.S., Stewart R.A., St John M.A., Chen W., Xu T.
      Nat. Genet. 21:177-181(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-1129.
      Tissue: BrainImported.
    4. "Mice deficient of Lats1 develop soft-tissue sarcomas, ovarian tumours and pituitary dysfunction."
      St John M.A., Tao W., Fei X., Fukumoto R., Carcangiu M.L., Brownstein D.G., Parlow A.F., McGrath J., Xu T.
      Nat. Genet. 21:182-186(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-463 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLATS1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BYR2
    Secondary accession number(s): B2RY46, Q9Z0W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3