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O95835

- LATS1_HUMAN

UniProt

O95835 - LATS1_HUMAN

Protein

Serine/threonine-protein kinase LATS1

Gene

LATS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.2 Publications

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei734 – 7341ATP1 PublicationPROSITE-ProRule annotation
    Active sitei828 – 8281Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi711 – 7199ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cytoplasmic sequestering of protein Source: BHF-UCL
    2. G2/M transition of mitotic cell cycle Source: UniProtKB
    3. hippo signaling Source: BHF-UCL
    4. hormone-mediated signaling pathway Source: UniProtKB
    5. keratinocyte differentiation Source: Ensembl
    6. mitotic nuclear division Source: UniProtKB-KW
    7. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
    8. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    9. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    10. protein phosphorylation Source: UniProtKB
    11. regulation of actin filament polymerization Source: UniProtKB
    12. regulation of protein complex assembly Source: BHF-UCL
    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_118607. Signaling by Hippo.
    SignaLinkiO95835.

    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
    Short name:
    h-warts
    Gene namesi
    Name:LATS1Imported
    Synonyms:WARTSImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6514. LATS1.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi464 – 4641S → A: Abolishes phosphorylation by NUAK1 and NUAK2. 1 Publication
    Mutagenesisi559 – 5591Y → F: Loss of interaction with YAP1. 1 Publication
    Mutagenesisi734 – 7341K → A: Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA30301.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11301130Serine/threonine-protein kinase LATS1PRO_0000086232Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphothreonine1 Publication
    Modified residuei278 – 2781Phosphoserine1 Publication
    Modified residuei464 – 4641Phosphoserine; by NUAK1 and NUAK22 Publications
    Modified residuei613 – 6131PhosphoserineBy similarity
    Modified residuei674 – 6741Phosphoserine1 Publication
    Modified residuei909 – 9091Phosphoserine; by STK3/MST21 Publication
    Modified residuei1079 – 10791Phosphothreonine; by STK3/MST21 Publication

    Post-translational modificationi

    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.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95835.
    PaxDbiO95835.
    PRIDEiO95835.

    PTM databases

    PhosphoSiteiO95835.

    Expressioni

    Tissue specificityi

    Expressed in all adult tissues examined except for lung and kidney.1 Publication

    Gene expression databases

    ArrayExpressiO95835.
    BgeeiO95835.
    CleanExiHS_LATS1.
    GenevestigatoriO95835.

    Organism-specific databases

    HPAiHPA031804.

    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. Interacts with LIMD1, WTIP and AJUBA.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDK1P064932EBI-444209,EBI-444308
    LIMK1P536675EBI-444209,EBI-444403
    MOB1AQ9H8S99EBI-444209,EBI-748229
    MOB1BQ7L9L46EBI-444209,EBI-2558745
    NF2P352404EBI-444209,EBI-1014472
    NUAK1O602852EBI-444209,EBI-1046789
    WWTR1Q9GZV55EBI-444209,EBI-747743
    YAP1P469375EBI-444209,EBI-1044059
    ZYXQ1594210EBI-444209,EBI-444225

    Protein-protein interaction databases

    BioGridi114563. 72 interactions.
    DIPiDIP-31516N.
    IntActiO95835. 40 interactions.
    MINTiMINT-2799169.

    Structurei

    3D structure databases

    ProteinModelPortaliO95835.
    SMRiO95835. Positions 95-142, 626-1046.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini100 – 14142UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini705 – 1010306Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1011 – 109080AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni526 – 655130Interaction with YAP1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi373 – 3764PPxY motif 1
    Motifi556 – 5594PPxY 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.
    HOGENOMiHOG000040002.
    HOVERGENiHBG052311.
    InParanoidiO95835.
    KOiK08791.
    OMAiAGFDEDM.
    OrthoDBiEOG7BZVS1.
    PhylomeDBiO95835.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: O95835-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA     50
    EHNMSKMSTE DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE 100
    VNPQMLQDLQ AAGFDEDMVI QALQKTNNRS IEAAIEFISK MSYQDPRREQ 150
    MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG SKESLVPQRH GPPLGESVAY 200
    HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP QVRSVTPPPP 250
    PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY 300
    PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG 350
    TGQTDFMIHQ NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY 400
    TNGSIPQSMM VPNRNSHNME LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE 450
    IPTWQPNIPV RSNSFNNPLG NRASHSANSQ PSATTVTAIT PAPIQQPVKS 500
    MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV TVMPPVAEAP 550
    NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV 600
    DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV 650
    LKSHQQRLHR KKQLENEMMR VGLSQDAQDQ MRKMLCQKES NYIRLKRAKM 700
    DKSMFVKIKT LGIGAFGEVC LARKVDTKAL YATKTLRKKD VLLRNQVAHV 750
    KAERDILAEA DNEWVVRLYY SFQDKDNLYF VMDYIPGGDM MSLLIRMGIF 800
    PESLARFYIA ELTCAVESVH KMGFIHRDIK PDNILIDRDG HIKLTDFGLC 850
    TGFRWTHDSK YYQSGDHPRQ DSMDFSNEWG DPSSCRCGDR LKPLERRAAR 900
    QHQRCLAHSL VGTPNYIAPE VLLRTGYTQL CDWWSVGVIL FEMLVGQPPF 950
    LAQTPLETQM KVINWQTSLH IPPQAKLSPE ASDLIIKLCR GPEDRLGKNG 1000
    ADEIKAHPFF KTIDFSSDLR QQSASYIPKI THPTDTSNFD PVDPDKLWSD 1050
    DNEEENVNDT LNGWYKNGKH PEHAFYEFTF RRFFDDNGYP YNYPKPIEYE 1100
    YINSQGSEQQ SDEDDQNTGS EIKNRDLVYV 1130
    Length:1,130
    Mass (Da):126,870
    Last modified:May 1, 1999 - v1
    Checksum:i11CFBCD8FD87DCD8
    GO
    Isoform 2Curated (identifier: O95835-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         672-690: GLSQDAQDQMRKMLCQKES → KPFKMSIFILNHLFAWCLF
         691-1130: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:690
    Mass (Da):76,193
    Checksum:i7154097947DF44E8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961R → W.1 Publication
    Corresponds to variant rs55945045 [ dbSNP | Ensembl ].
    VAR_040660
    Natural varianti204 – 2041S → G.1 Publication
    Corresponds to variant rs34793526 [ dbSNP | Ensembl ].
    VAR_040661
    Natural varianti237 – 2371P → Q.1 Publication
    Corresponds to variant rs56149740 [ dbSNP | Ensembl ].
    VAR_040662
    Natural varianti370 – 3701R → W.1 Publication
    Corresponds to variant rs56348064 [ dbSNP | Ensembl ].
    VAR_040663
    Natural varianti531 – 5311P → S.1 Publication
    Corresponds to variant rs55874734 [ dbSNP | Ensembl ].
    VAR_040664
    Natural varianti641 – 6411F → L.1 Publication
    Corresponds to variant rs35163691 [ dbSNP | Ensembl ].
    VAR_040665
    Natural varianti669 – 6691M → I in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040666
    Natural varianti806 – 8061R → P in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040667
    Natural varianti1000 – 10001G → S.1 Publication
    Corresponds to variant rs56412005 [ dbSNP | Ensembl ].
    VAR_040668

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei672 – 69019GLSQD…CQKES → KPFKMSIFILNHLFAWCLF in isoform 2. 1 PublicationVSP_051604Add
    BLAST
    Alternative sequencei691 – 1130440Missing in isoform 2. 1 PublicationVSP_051605Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104413 mRNA. Translation: AAD16882.1.
    AF164041 mRNA. Translation: AAD50272.1.
    BC002767 mRNA. Translation: AAH02767.1.
    CCDSiCCDS34551.1. [O95835-1]
    CCDS59040.1. [O95835-2]
    RefSeqiNP_001257448.1. NM_001270519.1. [O95835-2]
    NP_004681.1. NM_004690.3. [O95835-1]
    UniGeneiHs.549084.

    Genome annotation databases

    EnsembliENST00000253339; ENSP00000253339; ENSG00000131023. [O95835-1]
    ENST00000392273; ENSP00000444678; ENSG00000131023. [O95835-2]
    ENST00000543571; ENSP00000437550; ENSG00000131023. [O95835-1]
    GeneIDi9113.
    KEGGihsa:9113.
    UCSCiuc003qmu.2. human. [O95835-1]
    uc003qmw.3. human. [O95835-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    AF104413 mRNA. Translation: AAD16882.1 .
    AF164041 mRNA. Translation: AAD50272.1 .
    BC002767 mRNA. Translation: AAH02767.1 .
    CCDSi CCDS34551.1. [O95835-1 ]
    CCDS59040.1. [O95835-2 ]
    RefSeqi NP_001257448.1. NM_001270519.1. [O95835-2 ]
    NP_004681.1. NM_004690.3. [O95835-1 ]
    UniGenei Hs.549084.

    3D structure databases

    ProteinModelPortali O95835.
    SMRi O95835. Positions 95-142, 626-1046.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114563. 72 interactions.
    DIPi DIP-31516N.
    IntActi O95835. 40 interactions.
    MINTi MINT-2799169.

    Chemistry

    BindingDBi O95835.
    ChEMBLi CHEMBL6167.
    GuidetoPHARMACOLOGYi 1515.

    PTM databases

    PhosphoSitei O95835.

    Proteomic databases

    MaxQBi O95835.
    PaxDbi O95835.
    PRIDEi O95835.

    Protocols and materials databases

    DNASUi 9113.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253339 ; ENSP00000253339 ; ENSG00000131023 . [O95835-1 ]
    ENST00000392273 ; ENSP00000444678 ; ENSG00000131023 . [O95835-2 ]
    ENST00000543571 ; ENSP00000437550 ; ENSG00000131023 . [O95835-1 ]
    GeneIDi 9113.
    KEGGi hsa:9113.
    UCSCi uc003qmu.2. human. [O95835-1 ]
    uc003qmw.3. human. [O95835-2 ]

    Organism-specific databases

    CTDi 9113.
    GeneCardsi GC06M150023.
    HGNCi HGNC:6514. LATS1.
    HPAi HPA031804.
    MIMi 603473. gene.
    neXtProti NX_O95835.
    PharmGKBi PA30301.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000040002.
    HOVERGENi HBG052311.
    InParanoidi O95835.
    KOi K08791.
    OMAi AGFDEDM.
    OrthoDBi EOG7BZVS1.
    PhylomeDBi O95835.
    TreeFami TF351549.

    Enzyme and pathway databases

    Reactomei REACT_118607. Signaling by Hippo.
    SignaLinki O95835.

    Miscellaneous databases

    GeneWikii LATS1.
    GenomeRNAii 9113.
    NextBioi 34157.
    PROi O95835.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95835.
    Bgeei O95835.
    CleanExi HS_LATS1.
    Genevestigatori O95835.

    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. "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] (ISOFORM 1), PHOSPHORYLATION, INTERACTION WITH CDK1.
      Tissue: Fetal brainImported.
    2. "A human homolog of Drosophila warts tumor suppressor, h-warts, localized to mitotic apparatus and specifically phosphorylated during mitosis."
      Nishiyama Y., Hirota T., Morisaki T., Hara T., Marumoto T., Iida S., Makino K., Yamamoto H., Hiraoka T., Kitamura N., Saya H.
      FEBS Lett. 459:159-165(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    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] (ISOFORM 2).
      Tissue: EndometriumImported.
    4. "Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor."
      Hirota T., Morisaki T., Nishiyama Y., Marumoto T., Tada K., Hara T., Masuko N., Inagaki M., Hatakeyama K., Saya H.
      J. Cell Biol. 149:1073-1086(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZYX.
    5. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    6. "Tumor suppressor WARTS ensures genomic integrity by regulating both mitotic progression and G1 tetraploidy checkpoint function."
      Iida S., Hirota T., Morisaki T., Marumoto T., Hara T., Kuninaka S., Honda S., Kosai K., Kawasuji M., Pallas D.C., Saya H.
      Oncogene 23:5266-5274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-734.
    7. "LATS1 tumour suppressor affects cytokinesis by inhibiting LIMK1."
      Yang X., Yu K., Hao Y., Li D.-M., Stewart R.A., Insogna K.L., Xu T.
      Nat. Cell Biol. 6:609-617(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LIMK1.
    8. "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 AT SER-909 AND THR-1079.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "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, MUTAGENESIS OF TYR-559.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246; SER-278 AND SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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.
    17. "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.
    18. Cited for: FUNCTION, PHOSPHORYLATION AT SER-464, MUTAGENESIS OF SER-464.
    19. "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] TRP-96; GLY-204; GLN-237; TRP-370; SER-531; LEU-641; ILE-669; PRO-806 AND SER-1000.

    Entry informationi

    Entry nameiLATS1_HUMAN
    AccessioniPrimary (citable) accession number: O95835
    Secondary accession number(s): Q6PKD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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 6
      Human chromosome 6: 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

    Dasty 3