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Q7TSJ6

- LATS2_MOUSE

UniProt

Q7TSJ6 - LATS2_MOUSE

Protein

Serine/threonine-protein kinase LATS2

Gene

Lats2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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 LATS2 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 centrosome duplication, maintenance of mitotic fidelity and genomic stability. Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity. Negative regulator of the androgen receptor. Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities. This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ 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 sitei655 – 6551ATPBy similarityPROSITE-ProRule annotation
    Active sitei749 – 7491Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi632 – 6409ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein localization Source: MGI
    2. G1/S transition of mitotic cell cycle Source: UniProtKB
    3. hippo signaling Source: MGI
    4. hormone-mediated signaling pathway Source: UniProtKB
    5. intracellular signal transduction Source: UniProtKB
    6. keratinocyte differentiation Source: MGI
    7. mitotic nuclear division Source: UniProtKB-KW
    8. negative regulation of canonical Wnt signaling pathway Source: MGI
    9. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    10. protein phosphorylation Source: UniProtKB
    11. regulation of organ growth Source: MGI

    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 LATS2 (EC:2.7.11.1)
    Alternative name(s):
    Kinase phosphorylated during mitosis protein
    Large tumor suppressor homolog 2
    Serine/threonine-protein kinase kpm
    Gene namesi
    Name:Lats2Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1354386. Lats2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication. Cytoplasm 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication. Nucleus By similarity
    Note: Colocalizes with AURKA at the centrosomes during interphase, early prophase and cytokinesis By similarity. Migrates to the spindle poles during mitosis, and to the midbody during cytokinesis. Translocates to the nucleus upon mitotic stress by nocodazole treatment By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10421042Serine/threonine-protein kinase LATS2PRO_0000086235Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei82 – 821Phosphoserine; by AURKABy similarity
    Modified residuei267 – 2671PhosphothreonineBy similarity
    Modified residuei999 – 9991PhosphothreonineBy similarity

    Post-translational modificationi

    Autophosphorylated and phosphorylated during M-phase and the G1/S-phase of the cell cycle. Phosphorylated and activated by STK3/MST2 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ7TSJ6.
    PRIDEiQ7TSJ6.

    PTM databases

    PhosphoSiteiQ7TSJ6.

    Expressioni

    Tissue specificityi

    Expressed at high levels in ovary and testis and at lower levels in all other tissues examined.1 Publication

    Gene expression databases

    ArrayExpressiQ7TSJ6.
    BgeeiQ7TSJ6.
    CleanExiMM_LATS2.
    GenevestigatoriQ7TSJ6.

    Interactioni

    Subunit structurei

    Interacts with and is phosphorylated by AURKA. Binds to AR By similarity. Interacts with AJUBA during mitosis and this complex regulates organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome. Interacts (via PPxY motif) with YAP1 (via WW domains). Interacts with MOB1A and MOB1B By similarity. Interacts with LIMD1, WTIP and AJUBA By similarity. Interacts with SNAI1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ7TSJ6. 124 interactions.
    MINTiMINT-4100233.

    Structurei

    Secondary structure

    1
    1042
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi100 – 11011
    Helixi113 – 12311
    Helixi128 – 13811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2COSNMR-A98-138[»]
    ProteinModelPortaliQ7TSJ6.
    SMRiQ7TSJ6. Positions 91-138, 600-961.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7TSJ6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 13842UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini626 – 931306Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini932 – 101079AGC-kinase C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi472 – 4754PPxY motif

    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.
    InParanoidiQ7TSJ6.
    KOiK08791.
    OMAiGSHIRQD.
    PhylomeDBiQ7TSJ6.
    TreeFamiTF351549.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR028742. LATS2.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    [Graphical view]
    PANTHERiPTHR24356:SF149. PTHR24356:SF149. 1 hit.
    PfamiPF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 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.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7TSJ6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KASTQGLLVG PNSDTSLDAK     50
    VLGSKDASRQ QQMRATPKFG PYQKALREIR YSLLPFANES GTSAAAEVNR 100
    QMLQELVNAG CDQEMAGRAL KQTGSRSIEA ALEYISKMGY LDPRNEQIVR 150
    VIKQTSPGKG LAPTPVTRRP SFEGTGEALP SYHQLGGANY EGPAALEEMP 200
    RQYLDFLFPG AGAGTHGAQA HQHPPKGYST AVEPSAHFPG THYGRGHLLS 250
    EQPGYGVQRS SSFQNKTPPD AYSSMAKAQG GPPASLTFPA HAGLYTASHH 300
    KPAATPPGAH PLHVLGTRGP TFTGESSAQA VLAPSRNSLN ADLYELGSTV 350
    PWSAAPLARR DSLQKQGLEA SRPHVAFRAG PSRTNSFNNP QPEPSLPAPN 400
    TVTAVTAAHI LHPVKSVRVL RPEPQTAVGP SHPAWVAAPT APATESLETK 450
    EGSAGPHPLD VDYGGSERRC PPPPYPKHLL LPSKSEQYSV DLDSLCTSVQ 500
    QSLRGGTEQD RSDKSHKGAK GDKAGRDKKQ IQTSPVPVRK NSRDEEKRES 550
    RIKSYSPYAF KFFMEQHVEN VIKTYQQKVS RRLQLEQEMA KAGLCEAEQE 600
    QMRKILYQKE SNYNRLKRAK MDKSMFVKIK TLGIGAFGEV CLACKLDTHA 650
    LYAMKTLRKK DVLNRNQVAH VKAERDILAE ADNEWVVKLY YSFQDKDSLY 700
    FVMDYIPGGD MMSLLIRMEV FPEHLARFYI AELTLAIESV HKMGFIHRDI 750
    KPDNILIDLD GHIKLTDFGL CTGFRWTHNS KYYQKGNHMR QDSMEPGDLW 800
    DDVSNCRCGD RLKTLEQRAQ KQHQRCLAHS LVGTPNYIAP EVLLRKGYTQ 850
    LCDWWSVGVI LFEMLVGQPP FLAPTPTETQ LKVINWESTL HIPTQVRLSA 900
    EARDLITKLC CAADCRLGRD GADDLKAHPF FNTIDFSRDI RKQPAPYVPT 950
    ISHPMDTSNF DPVDEESPWH EASGESAKAW DTLASPSSKH PEHAFYEFTF 1000
    RRFFDDNGYP FRCPKPSEPA ESADPGDADL EGAAEGCQPV YV 1042
    Length:1,042
    Mass (Da):115,472
    Last modified:October 1, 2003 - v1
    Checksum:i7E0E73A73DB954C0
    GO

    Sequence cautioni

    The sequence BAC26704.1 differs from that shown. Reason: Frameshift at positions 970, 1025 and 1037.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841Q → R in BAA92380. (PubMed:10673337)Curated
    Sequence conflicti279 – 2791Q → R in BAC26704. (PubMed:16141072)Curated
    Sequence conflicti549 – 5491E → K in BAC26704. (PubMed:16141072)Curated
    Sequence conflicti589 – 5891M → V in BAA92380. (PubMed:10673337)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023958 mRNA. Translation: BAA92380.1.
    AK029966 mRNA. Translation: BAC26704.1. Frameshift.
    BC053028 mRNA. Translation: AAH53028.1.
    CCDSiCCDS27158.1.
    RefSeqiNP_056586.2. NM_015771.2.
    UniGeneiMm.347899.

    Genome annotation databases

    EnsembliENSMUST00000022531; ENSMUSP00000022531; ENSMUSG00000021959.
    GeneIDi50523.
    KEGGimmu:50523.
    UCSCiuc007udk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023958 mRNA. Translation: BAA92380.1 .
    AK029966 mRNA. Translation: BAC26704.1 . Frameshift.
    BC053028 mRNA. Translation: AAH53028.1 .
    CCDSi CCDS27158.1.
    RefSeqi NP_056586.2. NM_015771.2.
    UniGenei Mm.347899.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2COS NMR - A 98-138 [» ]
    ProteinModelPortali Q7TSJ6.
    SMRi Q7TSJ6. Positions 91-138, 600-961.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q7TSJ6. 124 interactions.
    MINTi MINT-4100233.

    PTM databases

    PhosphoSitei Q7TSJ6.

    Proteomic databases

    PaxDbi Q7TSJ6.
    PRIDEi Q7TSJ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022531 ; ENSMUSP00000022531 ; ENSMUSG00000021959 .
    GeneIDi 50523.
    KEGGi mmu:50523.
    UCSCi uc007udk.1. mouse.

    Organism-specific databases

    CTDi 26524.
    MGIi MGI:1354386. Lats2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117422.
    HOGENOMi HOG000040002.
    HOVERGENi HBG052311.
    InParanoidi Q7TSJ6.
    KOi K08791.
    OMAi GSHIRQD.
    PhylomeDBi Q7TSJ6.
    TreeFami TF351549.

    Enzyme and pathway databases

    Reactomei REACT_196537. Signaling by Hippo.

    Miscellaneous databases

    ChiTaRSi LATS2. mouse.
    EvolutionaryTracei Q7TSJ6.
    NextBioi 307518.
    PROi Q7TSJ6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7TSJ6.
    Bgeei Q7TSJ6.
    CleanExi MM_LATS2.
    Genevestigatori Q7TSJ6.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR028742. LATS2.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    [Graphical view ]
    PANTHERi PTHR24356:SF149. PTHR24356:SF149. 1 hit.
    Pfami PF00069. Pkinase. 2 hits.
    PF00433. Pkinase_C. 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.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure, expression, and chromosome mapping of LATS2, a mammalian homologue of the Drosophila tumor suppressor gene lats/warts."
      Yabuta N., Fujii T., Copeland N.G., Gilbert D.J., Jenkins N.A., Nishiguchi H., Endo Y., Toji S., Tanaka H., Nishimune Y., Nojima H.
      Genomics 63:263-270(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Testis1 Publication.
    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].
      Strain: C57BL/6J.
      Tissue: Testis.
    3. "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].
      Strain: C57BL/6Imported.
      Tissue: BrainImported.
    4. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    5. "Solution structure of RSGI RUH-038, a UBA domain from mouse LATS2 (large tumor suppressor homolog 2)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 98-138.

    Entry informationi

    Entry nameiLATS2_MOUSE
    AccessioniPrimary (citable) accession number: Q7TSJ6
    Secondary accession number(s): Q8CDJ4, Q9JMI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3