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Q9NRM7

- LATS2_HUMAN

UniProt

Q9NRM7 - LATS2_HUMAN

Protein

Serine/threonine-protein kinase LATS2

Gene

LATS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      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.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei697 – 6971ATP1 PublicationPROSITE-ProRule annotation
    Active sitei791 – 7911Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi674 – 782109ATPBy similarityPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

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

    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_118607. Signaling by Hippo.
    SignaLinkiQ9NRM7.

    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
    Warts-like kinase
    Gene namesi
    Name:LATS2Imported
    Synonyms:KPM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:6515. LATS2.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831S → C: Fails to localize at the centromere during interphase. 1 Publication
    Mutagenesisi83 – 831S → E: Fails to localize at the centromere during interphase. 1 Publication
    Mutagenesisi697 – 6971K → A: Loss of kinase activity, autophosphorylation and tumor suppressor activity. 2 Publications
    Mutagenesisi872 – 8721S → A: Loss of tumor suppressor activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA30302.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10881088Serine/threonine-protein kinase LATS2PRO_0000086234Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Phosphoserine; by AURKA2 Publications
    Modified residuei279 – 2791Phosphothreonine2 Publications
    Modified residuei1041 – 10411Phosphothreonine2 Publications

    Post-translational modificationi

    Autophosphorylated and phosphorylated during M-phase and the G1/S-phase of the cell cycle. Phosphorylated and activated by STK3/MST2.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRM7.
    PaxDbiQ9NRM7.
    PRIDEiQ9NRM7.

    PTM databases

    PhosphoSiteiQ9NRM7.

    Expressioni

    Tissue specificityi

    Expressed at high levels in heart and skeletal muscle and at lower levels in all other tissues examined.2 Publications

    Gene expression databases

    BgeeiQ9NRM7.
    CleanExiHS_LATS2.
    GenevestigatoriQ9NRM7.

    Organism-specific databases

    HPAiHPA039191.

    Interactioni

    Subunit structurei

    Interacts with and is phosphorylated by AURKA. Binds to AR. 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. Interacts with LIMD1, WTIP and AJUBA. Interacts with SNAI1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AJUBAQ96IF16EBI-3506895,EBI-949782
    MOB1AQ9H8S94EBI-3506895,EBI-748229
    MOB1BQ7L9L43EBI-3506895,EBI-2558745

    Protein-protein interaction databases

    BioGridi117727. 144 interactions.
    IntActiQ9NRM7. 8 interactions.
    MINTiMINT-1772003.
    STRINGi9606.ENSP00000372035.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRM7.
    SMRiQ9NRM7. Positions 92-139, 640-1042.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini98 – 13942UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini668 – 973306Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini974 – 105279AGC-kinase C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi515 – 5184PPxY 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.
    HOGENOMiHOG000040002.
    HOVERGENiHBG052311.
    InParanoidiQ9NRM7.
    KOiK08791.
    OMAiGSHIRQD.
    OrthoDBiEOG7BZVS1.
    PhylomeDBiQ9NRM7.
    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.

    Q9NRM7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSVQGLPAG PNSDTSLDAK     50
    VLGSKDATRQ QQQMRATPKF GPYQKALREI RYSLLPFANE SGTSAAAEVN 100
    RQMLQELVNA GCDQEMAGRA LKQTGSRSIE AALEYISKMG YLDPRNEQIV 150
    RVIKQTSPGK GLMPTPVTRR PSFEGTGDSF ASYHQLSGTP YEGPSFGADG 200
    PTALEEMPRP YVDYLFPGVG PHGPGHQHQH PPKGYGASVE AAGAHFPLQG 250
    AHYGRPHLLV PGEPLGYGVQ RSPSFQSKTP PETGGYASLP TKGQGGPPGA 300
    GLAFPPPAAG LYVPHPHHKQ AGPAAHQLHV LGSRSQVFAS DSPPQSLLTP 350
    SRNSLNVDLY ELGSTSVQQW PAATLARRDS LQKPGLEAPP RAHVAFRPDC 400
    PVPSRTNSFN SHQPRPGPPG KAEPSLPAPN TVTAVTAAHI LHPVKSVRVL 450
    RPEPQTAVGP SHPAWVPAPA PAPAPAPAPA AEGLDAKEEH ALALGGAGAF 500
    PLDVEYGGPD RRCPPPPYPK HLLLRSKSEQ YDLDSLCAGM EQSLRAGPNE 550
    PEGGDKSRKS AKGDKGGKDK KQIQTSPVPV RKNSRDEEKR ESRIKSYSPY 600
    AFKFFMEQHV ENVIKTYQQK VNRRLQLEQE MAKAGLCEAE QEQMRKILYQ 650
    KESNYNRLKR AKMDKSMFVK IKTLGIGAFG EVCLACKVDT HALYAMKTLR 700
    KKDVLNRNQV AHVKAERDIL AEADNEWVVK LYYSFQDKDS LYFVMDYIPG 750
    GDMMSLLIRM EVFPEHLARF YIAELTLAIE SVHKMGFIHR DIKPDNILID 800
    LDGHIKLTDF GLCTGFRWTH NSKYYQKGSH VRQDSMEPSD LWDDVSNCRC 850
    GDRLKTLEQR ARKQHQRCLA HSLVGTPNYI APEVLLRKGY TQLCDWWSVG 900
    VILFEMLVGQ PPFLAPTPTE TQLKVINWEN TLHIPAQVKL SPEARDLITK 950
    LCCSADHRLG RNGADDLKAH PFFSAIDFSS DIRKQPAPYV PTISHPMDTS 1000
    NFDPVDEESP WNDASEGSTK AWDTLTSPNN KHPEHAFYEF TFRRFFDDNG 1050
    YPFRCPKPSG AEASQAESSD LESSDLVDQT EGCQPVYV 1088
    Length:1,088
    Mass (Da):120,136
    Last modified:November 4, 2008 - v2
    Checksum:i2866F6B75637AD36
    GO

    Sequence cautioni

    The sequence BAA92381.1 differs from that shown. Reason: Frameshift at positions 512 and 526.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 613RQQ → SSK in BAA92381. (PubMed:10673337)Curated
    Sequence conflicti436 – 4361T → S in BAA92381. (PubMed:10673337)Curated
    Sequence conflicti711 – 7111A → V in AAF80561. (PubMed:10871863)Curated
    Sequence conflicti868 – 8681C → S in BAA92381. (PubMed:10673337)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040669
    Natural varianti91 – 911S → L.1 Publication
    Corresponds to variant rs55842804 [ dbSNP | Ensembl ].
    VAR_040670
    Natural varianti324 – 3241A → V.1 Publication
    Corresponds to variant rs558614 [ dbSNP | Ensembl ].
    VAR_019789
    Natural varianti363 – 3631G → S.
    Corresponds to variant rs2770928 [ dbSNP | Ensembl ].
    VAR_047077
    Natural varianti799 – 7991I → V.1 Publication
    Corresponds to variant rs35368391 [ dbSNP | Ensembl ].
    VAR_040671
    Natural varianti1014 – 10141A → G.1 Publication
    Corresponds to variant rs45523141 [ dbSNP | Ensembl ].
    VAR_040672
    Natural varianti1025 – 10251L → P.1 Publication
    Corresponds to variant rs56116059 [ dbSNP | Ensembl ].
    VAR_040673

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207547 mRNA. Translation: AAF80561.1.
    AK314235 mRNA. Translation: BAG36905.1.
    AL161613, AL356285 Genomic DNA. Translation: CAH71526.1.
    AL356285, AL161613 Genomic DNA. Translation: CAI15861.1.
    CH471075 Genomic DNA. Translation: EAX08286.1.
    AB028019 mRNA. Translation: BAA92381.1. Frameshift.
    CCDSiCCDS9294.1.
    RefSeqiNP_055387.2. NM_014572.2.
    XP_005266399.1. XM_005266342.1.
    UniGeneiHs.78960.

    Genome annotation databases

    EnsembliENST00000382592; ENSP00000372035; ENSG00000150457.
    GeneIDi26524.
    KEGGihsa:26524.
    UCSCiuc001unr.4. human.

    Polymorphism databases

    DMDMi212276441.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207547 mRNA. Translation: AAF80561.1 .
    AK314235 mRNA. Translation: BAG36905.1 .
    AL161613 , AL356285 Genomic DNA. Translation: CAH71526.1 .
    AL356285 , AL161613 Genomic DNA. Translation: CAI15861.1 .
    CH471075 Genomic DNA. Translation: EAX08286.1 .
    AB028019 mRNA. Translation: BAA92381.1 . Frameshift.
    CCDSi CCDS9294.1.
    RefSeqi NP_055387.2. NM_014572.2.
    XP_005266399.1. XM_005266342.1.
    UniGenei Hs.78960.

    3D structure databases

    ProteinModelPortali Q9NRM7.
    SMRi Q9NRM7. Positions 92-139, 640-1042.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117727. 144 interactions.
    IntActi Q9NRM7. 8 interactions.
    MINTi MINT-1772003.
    STRINGi 9606.ENSP00000372035.

    Chemistry

    BindingDBi Q9NRM7.
    ChEMBLi CHEMBL5907.
    GuidetoPHARMACOLOGYi 1516.

    PTM databases

    PhosphoSitei Q9NRM7.

    Polymorphism databases

    DMDMi 212276441.

    Proteomic databases

    MaxQBi Q9NRM7.
    PaxDbi Q9NRM7.
    PRIDEi Q9NRM7.

    Protocols and materials databases

    DNASUi 26524.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382592 ; ENSP00000372035 ; ENSG00000150457 .
    GeneIDi 26524.
    KEGGi hsa:26524.
    UCSCi uc001unr.4. human.

    Organism-specific databases

    CTDi 26524.
    GeneCardsi GC13M021547.
    H-InvDB HIX0022357.
    HGNCi HGNC:6515. LATS2.
    HPAi HPA039191.
    MIMi 604861. gene.
    neXtProti NX_Q9NRM7.
    PharmGKBi PA30302.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000040002.
    HOVERGENi HBG052311.
    InParanoidi Q9NRM7.
    KOi K08791.
    OMAi GSHIRQD.
    OrthoDBi EOG7BZVS1.
    PhylomeDBi Q9NRM7.
    TreeFami TF351549.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.
    SignaLinki Q9NRM7.

    Miscellaneous databases

    ChiTaRSi LATS2. human.
    GeneWikii LATS2.
    GenomeRNAii 26524.
    NextBioi 48850.
    PROi Q9NRM7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NRM7.
    CleanExi HS_LATS2.
    Genevestigatori Q9NRM7.

    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. "Molecular cloning of a novel human protein kinase, kpm, that is homologous to warts/lats, a Drosophila tumor suppressor."
      Hori T., Takaori-Kondo A., Kamikubo Y., Uchiyama T.
      Oncogene 19:3101-3109(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-697.
      Tissue: MyeloidImported.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] OF 42-1088, TISSUE SPECIFICITY, VARIANT VAL-324.
      Tissue: Testis1 Publication.
    6. "Lats2, a putative tumor suppressor, inhibits G1/S transition."
      Li Y., Pei J., Xia H., Ke H., Wang H., Tao W.
      Oncogene 22:4398-4405(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-697 AND SER-872.
    7. "The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase."
      Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S., Tamai K., Nojima H.
      Genes Cells 9:383-397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AURKA, MUTAGENESIS OF SER-83, PHOSPHORYLATION AT SER-83.
    8. Cited for: FUNCTION, INTERACTION WITH AR.
    9. "The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1."
      Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A., Nigg E.A., Sillje H.H.W.
      Oncogene 24:2076-2086(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    10. "LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis."
      Abe Y., Ohsugi M., Haraguchi K., Fujimoto J., Yamamoto T.
      FEBS Lett. 580:782-788(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AJUBA.
    11. "Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
      Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
      J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YAP1.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Ajuba LIM proteins are negative regulators of the Hippo signaling pathway."
      Das Thakur M., Feng Y., Jagannathan R., Seppa M.J., Skeath J.B., Longmore G.D.
      Curr. Biol. 20:657-662(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIMD1; WTIP AND AJUBA.
    14. "Molecular characterization of human homologs of yeast MOB1."
      Chow A., Hao Y., Yang X.
      Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MOB1A AND MOB1B.
    15. "Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation."
      Zhang K., Rodriguez-Aznar E., Yabuta N., Owen R.J., Mingot J.M., Nojima H., Nieto M.A., Longmore G.D.
      EMBO J. 31:29-43(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNAI1, PHOSPHORYLATION AT THR-1041.
    16. "Patterns of somatic mutation in human cancer genomes."
      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.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-40; LEU-91; VAL-799; GLY-1014 AND PRO-1025.

    Entry informationi

    Entry nameiLATS2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRM7
    Secondary accession number(s): B1AM47, Q9P2X1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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