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Q13188

- STK3_HUMAN

UniProt

Q13188 - STK3_HUMAN

Protein

Serine/threonine-protein kinase 3

Gene

STK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (26 Apr 2004)
      Previous versions | rss
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    Functioni

    Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which 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. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 By similarity. Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.By similarity10 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Inhibited by the C-terminal non-catalytic region. Activated by caspase-cleavage. Full activation also requires homodimerization and autophosphorylation of Thr-180, which are inhibited by the proto-oncogene product RAF1. Activated by RASSF1 which acts by preventing its dephosphorylation.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561ATP
    Active sitei146 – 1461Proton acceptorPROSITE-ProRule annotation
    Sitei322 – 3232Cleavage; by caspase-3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi33 – 419ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein dimerization activity Source: UniProtKB
    5. protein kinase activity Source: ProtInc
    6. protein serine/threonine kinase activator activity Source: BHF-UCL
    7. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. hippo signaling Source: UniProtKB
    3. intracellular signal transduction Source: UniProtKB
    4. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
    5. positive regulation of apoptotic process Source: UniProtKB
    6. positive regulation of protein serine/threonine kinase activity Source: GOC
    7. protein phosphorylation Source: UniProtKB
    8. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_118607. Signaling by Hippo.
    SignaLinkiQ13188.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase 3 (EC:2.7.11.1)
    Alternative name(s):
    Mammalian STE20-like protein kinase 2
    Short name:
    MST-2
    STE20-like kinase MST2
    Serine/threonine-protein kinase Krs-1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:STK3
    Synonyms:KRS1, MST2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:11406. STK3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: The caspase-cleaved form cycles between nucleus and cytoplasm By similarity. Phosphorylation at Thr-117 leads to inhibition of nuclear translocation.By similarity1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561K → R: Loss of activity. 1 Publication
    Mutagenesisi322 – 3221D → N: Resistant to proteolytic cleavage. 1 Publication

    Organism-specific databases

    PharmGKBiPA36213.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 491491Serine/threonine-protein kinase 3PRO_0000086689Add
    BLAST
    Chaini1 – 322322Serine/threonine-protein kinase 3 36kDa subunitPRO_0000413713Add
    BLAST
    Chaini323 – 491169Serine/threonine-protein kinase 3 20kDa subunitPRO_0000413714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei15 – 151Phosphoserine1 Publication
    Modified residuei117 – 1171Phosphothreonine; by PKB/AKT12 Publications
    Modified residuei180 – 1801Phosphothreonine; by autocatalysisCurated
    Modified residuei316 – 3161Phosphoserine5 Publications
    Modified residuei336 – 3361Phosphothreonine1 Publication
    Modified residuei384 – 3841Phosphothreonine; by PKB/AKT11 Publication
    Modified residuei444 – 4441Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1.8 Publications
    Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N).1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13188.
    PaxDbiQ13188.
    PRIDEiQ13188.

    2D gel databases

    OGPiQ13188.

    PTM databases

    PhosphoSiteiQ13188.

    Miscellaneous databases

    PMAP-CutDBQ13188.

    Expressioni

    Tissue specificityi

    Expressed at high levels in adult kidney, skeletal and placenta tissues and at very low levels in adult heart, lung and brain tissues.1 Publication

    Inductioni

    Activity increases during mitosis.1 Publication

    Gene expression databases

    ArrayExpressiQ13188.
    BgeeiQ13188.
    CleanExiHS_STK3.
    GenevestigatoriQ13188.

    Organism-specific databases

    HPAiCAB025316.
    HPA007120.

    Interactioni

    Subunit structurei

    Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation By similarity. Interacts with and stabilizes SAV1. Interacts with RAF1, which prevents dimerization and phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) with isoform 1 of NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. Interacts with RASSF2 (via SARAH domain).By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951662EBI-992580,EBI-712001
    GABARAPL1Q9H0R82EBI-992580,EBI-746969
    GABARAPL2P605202EBI-992580,EBI-720116
    MAP1LC3BQ9GZQ85EBI-992580,EBI-373144
    MAP1LC3CQ9BXW42EBI-992580,EBI-2603996
    RASSF1Q9NS23-23EBI-992580,EBI-438698
    RASSF2P5074910EBI-992580,EBI-960081
    RASSF3Q86WH26EBI-992580,EBI-2845202
    RASSF4Q9H2L55EBI-992580,EBI-2933362
    RASSF5Q8WWW07EBI-992580,EBI-367390
    SAV1Q9H4B615EBI-992580,EBI-1017775
    SLMAPQ14BN43EBI-992580,EBI-1043216
    STK4Q1304315EBI-992580,EBI-367376

    Protein-protein interaction databases

    BioGridi112664. 68 interactions.
    DIPiDIP-36128N.
    IntActiQ13188. 61 interactions.
    MINTiMINT-3027356.
    STRINGi9606.ENSP00000377867.

    Structurei

    Secondary structure

    1
    491
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 204
    Helixi23 – 264
    Beta strandi27 – 348
    Beta strandi40 – 467
    Turni47 – 493
    Beta strandi52 – 587
    Helixi64 – 7613
    Beta strandi85 – 917
    Beta strandi94 – 1007
    Helixi107 – 1148
    Helixi120 – 13920
    Helixi149 – 1513
    Beta strandi152 – 1543
    Beta strandi160 – 1623
    Helixi170 – 1723
    Helixi175 – 1828
    Helixi190 – 1956
    Helixi201 – 21616
    Turni220 – 2234
    Helixi226 – 23510
    Helixi244 – 2463
    Helixi249 – 25810
    Helixi263 – 2653
    Helixi269 – 2724
    Helixi276 – 2794
    Helixi284 – 2874
    Helixi288 – 30619
    Helixi436 – 4405
    Helixi445 – 48339

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HKDX-ray1.50A/B/C/D436-484[»]
    4L0NX-ray1.40A/B/C/D/E/F/G/H/I/J436-484[»]
    4LG4X-ray2.42A/B/C/D/E/F16-313[»]
    4LGDX-ray3.05A/B/C/D9-491[»]
    ProteinModelPortaliQ13188.
    SMRiQ13188. Positions 10-302, 386-489.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 278252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini437 – 48448SARAHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili287 – 32842Sequence AnalysisAdd
    BLAST
    Coiled coili442 – 47534Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi308 – 3147Poly-Glu
    Compositional biasi370 – 3756Poly-Glu

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SARAH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234203.
    HOVERGENiHBG108518.
    InParanoidiQ13188.
    KOiK04412.
    OMAiXDEDELD.
    OrthoDBiEOG7TF79T.
    PhylomeDBiQ13188.
    TreeFamiTF354217.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR024205. Mst1_SARAH_domain.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR011524. SARAH_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PfamiPF11629. Mst1_SARAH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50951. SARAH. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13188-1) [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

    MEQPPAPKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG    50
    QVVAIKQVPV ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME 100
    YCGAGSVSDI IRLRNKTLIE DEIATILKST LKGLEYLHFM RKIHRDIKAG 150
    NILLNTEGHA KLADFGVAGQ LTDTMAKRNT VIGTPFWMAP EVIQEIGYNC 200
    VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT FRKPELWSDD 250
    FTDFVKKCLV KNPEQRATAT QLLQHPFIKN AKPVSILRDL ITEAMEIKAK 300
    RHEEQQRELE EEEENSDEDE LDSHTMVKTS VESVGTMRAT STMSEGAQTM 350
    IEHNSTMLES DLGTMVINSE DEEEEDGTMK RNATSPQVQR PSFMDYFDKQ 400
    DFKNKSHENC NQNMHEPFPM SKNVFPDNWK VPQDGDFDFL KNLSLEELQM 450
    RLKALDPMME REIEELRQRY TAKRQPILDA MDAKKRRQQN F 491
    Length:491
    Mass (Da):56,301
    Last modified:April 26, 2004 - v2
    Checksum:i84F598ED3617292C
    GO
    Isoform 2 (identifier: Q13188-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: MEQPPAPK → MLQLMDSGITICLRNGAASVFKKKEWSTQGEENKQD

    Note: No experimental confirmation available.

    Show »
    Length:519
    Mass (Da):59,462
    Checksum:i84CB5FEAA629AE68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 983WIV → YLY in CAA80909. (PubMed:8274451)Curated
    Sequence conflicti121 – 1211D → Y in CAA80909. (PubMed:8274451)Curated
    Sequence conflicti203 – 2031D → G in CAA80909. (PubMed:8274451)Curated
    Sequence conflicti303 – 3031E → D in AAC50386. (PubMed:8566796)Curated
    Sequence conflicti332 – 3343ESV → GEC in AAC50386. (PubMed:8566796)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601V → L in an ovarian clear cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041122
    Natural varianti418 – 4181F → C.
    Corresponds to variant rs36047674 [ dbSNP | Ensembl ].
    VAR_051670

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88MEQPPAPK → MLQLMDSGITICLRNGAASV FKKKEWSTQGEENKQD in isoform 2. 1 PublicationVSP_054167

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26424 mRNA. Translation: AAC50386.1.
    U60206 mRNA. Translation: AAB17261.1.
    AK131363 mRNA. Translation: BAG54769.1.
    AK291837 mRNA. Translation: BAF84526.1.
    AC016877 Genomic DNA. No translation available.
    AP002087 Genomic DNA. No translation available.
    AP003355 Genomic DNA. No translation available.
    AP003467 Genomic DNA. No translation available.
    AP003551 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW91781.1.
    BC010640 mRNA. Translation: AAH10640.1.
    Z25422 mRNA. Translation: CAA80909.1.
    CCDSiCCDS47900.1. [Q13188-1]
    CCDS59108.1. [Q13188-2]
    PIRiI38212.
    RefSeqiNP_001243241.1. NM_001256312.1. [Q13188-2]
    NP_006272.2. NM_006281.3. [Q13188-1]
    UniGeneiHs.492333.

    Genome annotation databases

    EnsembliENST00000419617; ENSP00000390500; ENSG00000104375. [Q13188-1]
    ENST00000523601; ENSP00000429744; ENSG00000104375. [Q13188-2]
    GeneIDi6788.
    KEGGihsa:6788.
    UCSCiuc003yip.4. human. [Q13188-1]

    Polymorphism databases

    DMDMi46577700.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26424 mRNA. Translation: AAC50386.1 .
    U60206 mRNA. Translation: AAB17261.1 .
    AK131363 mRNA. Translation: BAG54769.1 .
    AK291837 mRNA. Translation: BAF84526.1 .
    AC016877 Genomic DNA. No translation available.
    AP002087 Genomic DNA. No translation available.
    AP003355 Genomic DNA. No translation available.
    AP003467 Genomic DNA. No translation available.
    AP003551 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW91781.1 .
    BC010640 mRNA. Translation: AAH10640.1 .
    Z25422 mRNA. Translation: CAA80909.1 .
    CCDSi CCDS47900.1. [Q13188-1 ]
    CCDS59108.1. [Q13188-2 ]
    PIRi I38212.
    RefSeqi NP_001243241.1. NM_001256312.1. [Q13188-2 ]
    NP_006272.2. NM_006281.3. [Q13188-1 ]
    UniGenei Hs.492333.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HKD X-ray 1.50 A/B/C/D 436-484 [» ]
    4L0N X-ray 1.40 A/B/C/D/E/F/G/H/I/J 436-484 [» ]
    4LG4 X-ray 2.42 A/B/C/D/E/F 16-313 [» ]
    4LGD X-ray 3.05 A/B/C/D 9-491 [» ]
    ProteinModelPortali Q13188.
    SMRi Q13188. Positions 10-302, 386-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112664. 68 interactions.
    DIPi DIP-36128N.
    IntActi Q13188. 61 interactions.
    MINTi MINT-3027356.
    STRINGi 9606.ENSP00000377867.

    Chemistry

    BindingDBi Q13188.
    ChEMBLi CHEMBL4708.
    GuidetoPHARMACOLOGYi 2219.

    PTM databases

    PhosphoSitei Q13188.

    Polymorphism databases

    DMDMi 46577700.

    2D gel databases

    OGPi Q13188.

    Proteomic databases

    MaxQBi Q13188.
    PaxDbi Q13188.
    PRIDEi Q13188.

    Protocols and materials databases

    DNASUi 6788.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000419617 ; ENSP00000390500 ; ENSG00000104375 . [Q13188-1 ]
    ENST00000523601 ; ENSP00000429744 ; ENSG00000104375 . [Q13188-2 ]
    GeneIDi 6788.
    KEGGi hsa:6788.
    UCSCi uc003yip.4. human. [Q13188-1 ]

    Organism-specific databases

    CTDi 6788.
    GeneCardsi GC08M099413.
    HGNCi HGNC:11406. STK3.
    HPAi CAB025316.
    HPA007120.
    MIMi 605030. gene.
    neXtProti NX_Q13188.
    PharmGKBi PA36213.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234203.
    HOVERGENi HBG108518.
    InParanoidi Q13188.
    KOi K04412.
    OMAi XDEDELD.
    OrthoDBi EOG7TF79T.
    PhylomeDBi Q13188.
    TreeFami TF354217.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_118607. Signaling by Hippo.
    SignaLinki Q13188.

    Miscellaneous databases

    ChiTaRSi STK3. human.
    GeneWikii STK3.
    GenomeRNAii 6788.
    NextBioi 26504.
    PMAP-CutDB Q13188.
    PROi Q13188.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13188.
    Bgeei Q13188.
    CleanExi HS_STK3.
    Genevestigatori Q13188.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR024205. Mst1_SARAH_domain.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR011524. SARAH_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    Pfami PF11629. Mst1_SARAH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50951. SARAH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a member of the MST subfamily of Ste20-like kinases."
      Creasy C.L., Chernoff J.
      Gene 167:303-306(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    2. "Newly identified stress-responsive protein kinases, Krs-1 and Krs-2."
      Taylor L.K., Wang H.C., Erikson R.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:10099-10104(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Uterus.
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Eye.
    7. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-8; 13-43; 57-69; 85-91; 115-128; 133-141; 149-178; 229-256; 267-298; 329-338; 382-403; 423-451; 462-467 AND 474-485, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma.
    8. "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans."
      Schultz S.J., Nigg E.A.
      Cell Growth Differ. 4:821-830(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-203.
    9. "MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation."
      Lee K.-K., Ohyama T., Yajima N., Tsubuki S., Yonehara S.
      J. Biol. Chem. 276:19276-19285(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-322.
    10. "Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1."
      O'Neill E., Rushworth L., Baccarini M., Kolch W.
      Science 306:2267-2270(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAF1, ENZYME REGULATION.
    11. "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: INTERACTION WITH SAV1, FUNCTION.
    12. Cited for: INTERACTION WITH RASSF1.
    13. "Association of mammalian sterile twenty kinases, Mst1 and Mst2, with hSalvador via C-terminal coiled-coil domains, leads to its stabilization and phosphorylation."
      Callus B.A., Verhagen A.M., Vaux D.L.
      FEBS J. 273:4264-4276(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SAV1, MUTAGENESIS OF LYS-56.
    14. "MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation."
      Praskova M., Xia F., Avruch J.
      Curr. Biol. 18:311-321(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
      Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
      Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STK38 AND MOBKL1B.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Mammalian NDR/LATS protein kinases in hippo tumor suppressor signaling."
      Hergovich A., Hemmings B.A.
      BioFactors 35:338-345(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-316; THR-336 AND SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "RASSF2 associates with and stabilizes the proapoptotic kinase MST2."
      Cooper W.N., Hesson L.B., Matallanas D., Dallol A., von Kriegsheim A., Ward R., Kolch W., Latif F.
      Oncogene 28:2988-2998(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RASSF2, SUBCELLULAR LOCATION.
    22. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "Proapoptotic kinase MST2 coordinates signaling crosstalk between RASSF1A, Raf-1, and Akt."
      Romano D., Matallanas D., Weitsman G., Preisinger C., Ng T., Kolch W.
      Cancer Res. 70:1195-1203(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-117 AND THR-384, INTERACTION WITH PKB/AKT1.
    24. "Mammalian Ste20-like kinase (Mst2) indirectly supports Raf-1/ERK pathway activity via maintenance of protein phosphatase-2A catalytic subunit levels and consequent suppression of inhibitory Raf-1 phosphorylation."
      Kilili G.K., Kyriakis J.M.
      J. Biol. Chem. 285:15076-15087(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction."
      Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M., Schiebel E.
      Nat. Cell Biol. 12:1166-1176(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NEK2.
    26. "Regulation of proapoptotic mammalian ste20-like kinase MST2 by the IGF1-Akt pathway."
      Kim D., Shu S., Coppola M.D., Kaneko S., Yuan Z.Q., Cheng J.Q.
      PLoS ONE 5:E9616-E9616(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-117, INTERACTION WITH PKB/AKT1.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "The tumor suppressor RASSF1A prevents dephosphorylation of the mammalian STE20-like kinases MST1 and MST2."
      Guo C., Zhang X., Pfeifer G.P.
      J. Biol. Chem. 286:6253-6261(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASSF1, ENZYME REGULATION.
    29. "Mammalian MST2 kinase and human Salvador activate and reduce estrogen receptor alpha in the absence of ligand."
      Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.
      J. Mol. Med. 89:181-191(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1.
    30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "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: VARIANT [LARGE SCALE ANALYSIS] LEU-60.

    Entry informationi

    Entry nameiSTK3_HUMAN
    AccessioniPrimary (citable) accession number: Q13188
    Secondary accession number(s): A8K722
    , B3KYA7, Q15445, Q15801, Q96FM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 150 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3