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Q9Y6E0

- STK24_HUMAN

UniProt

Q9Y6E0 - STK24_HUMAN

Protein

Serine/threonine-protein kinase 24

Gene

STK24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Mg2+ or Mn2+ or Co2+ or Zn2+.1 Publication

    Kineticsi

    1. KM=12.8 µM for manganese ions1 Publication
    2. KM=34.9 µM for cobalt ions1 Publication
    3. KM=22.7 µM for magnesium ions1 Publication
    4. KM=4.1 µM for zinc ions1 Publication

    Vmax=2623.1 pmol/min/mg enzyme for manganese ions1 Publication

    Vmax=1746.1 pmol/min/mg enzyme for cobalt ions1 Publication

    Vmax=129.1 pmol/min/mg enzyme for magnesium ions1 Publication

    Vmax=22.3 pmol/min/mg enzyme for zinc ions1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651ATP
    Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation
    Metal bindingi161 – 1611Magnesium
    Metal bindingi174 – 1741Magnesium
    Sitei325 – 3262Cleavage; by caspase-3, caspase-7 and caspase-8

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 509ATP
    Nucleotide bindingi112 – 1143ATP

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    3. execution phase of apoptosis Source: UniProtKB
    4. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
    5. negative regulation of cell migration Source: UniProtKB
    6. protein autophosphorylation Source: UniProtKB
    7. protein phosphorylation Source: UniProtKB
    8. regulation of axon regeneration Source: UniProtKB
    9. 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

    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_995. Apoptotic execution phase.
    SignaLinkiQ9Y6E0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase 24 (EC:2.7.11.1)
    Alternative name(s):
    Mammalian STE20-like protein kinase 3
    Short name:
    MST-3
    STE20-like kinase MST3
    Cleaved into the following 2 chains:
    Alternative name(s):
    Mammalian STE20-like protein kinase 3 N-terminal
    Short name:
    MST3/N
    Alternative name(s):
    Mammalian STE20-like protein kinase 3 C-terminal
    Short name:
    MST3/C
    Gene namesi
    Name:STK24
    Synonyms:MST3, STK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:11403. STK24.

    Subcellular locationi

    Cytoplasm. Nucleus. Membrane
    Note: The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB-SubCell
    5. nucleolus Source: HPA
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181T → A: Loss of phosphorylation by PKA. 1 Publication
    Mutagenesisi65 – 651K → A: Loss of activity and autophosphorylation. 1 Publication
    Mutagenesisi190 – 1901T → A: Loss of activity and autophosphorylation. 1 Publication
    Mutagenesisi321 – 3211D → N: Loss of proteolytic cleavage by caspases. 1 Publication

    Organism-specific databases

    PharmGKBiPA36210.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Serine/threonine-protein kinase 24PRO_0000086711Add
    BLAST
    Chaini1 – 325325Serine/threonine-protein kinase 24 36 kDa subunitPRO_0000413618Add
    BLAST
    Chaini326 – 443118Serine/threonine-protein kinase 24 12 kDa subunitPRO_0000413619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphothreonine; by PKA1 Publication
    Modified residuei190 – 1901Phosphothreonine; by autocatalysis3 Publications
    Modified residuei320 – 3201Phosphoserine1 Publication

    Post-translational modificationi

    Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis.1 Publication
    Isoform B is activated by phosphorylation by PKA. Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-190 and phosphorylation at this site is essential for its function. Manganese, magnesium and cobalt-dependent autophosphorylation is mainly on threonine residues while zinc-dependent autophosphorylation is on both serine and threonine residues.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6E0.
    PaxDbiQ9Y6E0.
    PRIDEiQ9Y6E0.

    PTM databases

    PhosphoSiteiQ9Y6E0.

    Expressioni

    Tissue specificityi

    Isoform A is ubiquitous. Isoform B is expressed in brain with high expression in hippocampus and cerebral cortex.

    Gene expression databases

    ArrayExpressiQ9Y6E0.
    BgeeiQ9Y6E0.
    CleanExiHS_STK24.
    HS_STK3.
    GenevestigatoriQ9Y6E0.

    Organism-specific databases

    HPAiHPA026435.
    HPA026502.

    Interactioni

    Subunit structurei

    Monomer. Interacts with CTTNBP2NL.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTTNBP2NLQ9P2B44EBI-740175,EBI-1774273
    PDCD10Q9BUL87EBI-740175,EBI-740195
    STRNO438153EBI-740175,EBI-1046642
    TRAF3IP3Q9Y2282EBI-740175,EBI-765817

    Protein-protein interaction databases

    BioGridi114011. 65 interactions.
    DIPiDIP-40608N.
    IntActiQ9Y6E0. 33 interactions.
    MINTiMINT-3088034.
    STRINGi9606.ENSP00000365730.

    Structurei

    Secondary structure

    1
    443
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 343
    Beta strandi36 – 449
    Beta strandi46 – 5510
    Turni56 – 583
    Beta strandi61 – 688
    Turni69 – 713
    Helixi76 – 8813
    Beta strandi97 – 1037
    Beta strandi106 – 1127
    Beta strandi116 – 1183
    Helixi119 – 1235
    Beta strandi124 – 1263
    Helixi130 – 14920
    Helixi159 – 1613
    Beta strandi162 – 1643
    Beta strandi166 – 1683
    Beta strandi170 – 1723
    Helixi180 – 1834
    Beta strandi186 – 1883
    Helixi195 – 1973
    Helixi200 – 2034
    Helixi211 – 22616
    Turni230 – 2334
    Helixi236 – 24510
    Helixi257 – 26610
    Helixi271 – 2733
    Helixi277 – 2804
    Helixi284 – 2896
    Helixi293 – 2964
    Helixi297 – 30913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A7FX-ray1.55A27-315[»]
    3A7GX-ray2.00A/B27-315[»]
    3A7HX-ray1.96A/B27-315[»]
    3A7IX-ray1.45A27-315[»]
    3A7JX-ray1.50A27-315[»]
    3CKWX-ray1.96A31-323[»]
    3CKXX-ray2.70A31-323[»]
    3ZHPX-ray2.90C/D31-301[»]
    ProteinModelPortaliQ9Y6E0.
    SMRiQ9Y6E0. Positions 27-350, 372-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6E0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 286251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni335 – 38652Nuclear export signal (NES)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi278 – 29215Bipartite nuclear localization signalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234203.
    HOVERGENiHBG108518.
    KOiK08838.
    OMAiGSDDWIF.
    PhylomeDBiQ9Y6E0.
    TreeFamiTF354217.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PfamiPF00069. 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.
    [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 B (identifier: Q9Y6E0-1) [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

    MDSRAQLWGL ALNKRRATLP HPGGSTNLKA DPEELFTKLE KIGKGSFGEV    50
    FKGIDNRTQK VVAIKIIDLE EAEDEIEDIQ QEITVLSQCD SPYVTKYYGS 100
    YLKDTKLWII MEYLGGGSAL DLLEPGPLDE TQIATILREI LKGLDYLHSE 150
    KKIHRDIKAA NVLLSEHGEV KLADFGVAGQ LTDTQIKRNT FVGTPFWMAP 200
    EVIKQSAYDS KADIWSLGIT AIELARGEPP HSELHPMKVL FLIPKNNPPT 250
    LEGNYSKPLK EFVEACLNKE PSFRPTAKEL LKHKFILRNA KKTSYLTELI 300
    DRYKRWKAEQ SHDDSSSEDS DAETDGQASG GSDSGDWIFT IREKDPKNLE 350
    NGALQPSDLD RNKMKDIPKR PFSQCLSTII SPLFAELKEK SQACGGNLGS 400
    IEELRGAIYL AEEACPGISD TMVAQLVQRL QRYSLSGGGT SSH 443
    Length:443
    Mass (Da):49,308
    Last modified:November 1, 1999 - v1
    Checksum:i4A9FF1F6B6A88A97
    GO
    Isoform A (identifier: Q9Y6E0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MDSRAQLWGLALNKRRATLPHPGGST → MAHSPVQSGLPGMQ

    Note: Initiator Met-1 is removed. Contains a phosphoserine at position 4. Contains a N-acetylalanine at position 2.

    Show »
    Length:431
    Mass (Da):47,913
    Checksum:i26D863FDFEDF90AD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti414 – 4141A → V.2 Publications
    Corresponds to variant rs55953606 [ dbSNP | Ensembl ].
    VAR_041148
    Natural varianti426 – 4261L → I.1 Publication
    Corresponds to variant rs55897869 [ dbSNP | Ensembl ].
    VAR_041149

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626MDSRA…PGGST → MAHSPVQSGLPGMQ in isoform A. 2 PublicationsVSP_004874Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF024636 mRNA. Translation: AAB82560.1.
    AF083420 mRNA. Translation: AAD42039.1.
    AL356423, AL137249 Genomic DNA. Translation: CAI13114.1.
    AL137249, AL356423 Genomic DNA. Translation: CAI39453.1.
    CH471085 Genomic DNA. Translation: EAX08986.1.
    BC035578 mRNA. Translation: AAH35578.1.
    CCDSiCCDS32001.1. [Q9Y6E0-2]
    CCDS9488.1. [Q9Y6E0-1]
    RefSeqiNP_001027467.2. NM_001032296.3. [Q9Y6E0-2]
    NP_003567.2. NM_003576.4. [Q9Y6E0-1]
    UniGeneiHs.508514.

    Genome annotation databases

    EnsembliENST00000376547; ENSP00000365730; ENSG00000102572. [Q9Y6E0-1]
    ENST00000397517; ENSP00000380651; ENSG00000102572. [Q9Y6E0-2]
    GeneIDi8428.
    KEGGihsa:8428.
    UCSCiuc001vnm.1. human. [Q9Y6E0-1]

    Polymorphism databases

    DMDMi13626607.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF024636 mRNA. Translation: AAB82560.1 .
    AF083420 mRNA. Translation: AAD42039.1 .
    AL356423 , AL137249 Genomic DNA. Translation: CAI13114.1 .
    AL137249 , AL356423 Genomic DNA. Translation: CAI39453.1 .
    CH471085 Genomic DNA. Translation: EAX08986.1 .
    BC035578 mRNA. Translation: AAH35578.1 .
    CCDSi CCDS32001.1. [Q9Y6E0-2 ]
    CCDS9488.1. [Q9Y6E0-1 ]
    RefSeqi NP_001027467.2. NM_001032296.3. [Q9Y6E0-2 ]
    NP_003567.2. NM_003576.4. [Q9Y6E0-1 ]
    UniGenei Hs.508514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A7F X-ray 1.55 A 27-315 [» ]
    3A7G X-ray 2.00 A/B 27-315 [» ]
    3A7H X-ray 1.96 A/B 27-315 [» ]
    3A7I X-ray 1.45 A 27-315 [» ]
    3A7J X-ray 1.50 A 27-315 [» ]
    3CKW X-ray 1.96 A 31-323 [» ]
    3CKX X-ray 2.70 A 31-323 [» ]
    3ZHP X-ray 2.90 C/D 31-301 [» ]
    ProteinModelPortali Q9Y6E0.
    SMRi Q9Y6E0. Positions 27-350, 372-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114011. 65 interactions.
    DIPi DIP-40608N.
    IntActi Q9Y6E0. 33 interactions.
    MINTi MINT-3088034.
    STRINGi 9606.ENSP00000365730.

    Chemistry

    BindingDBi Q9Y6E0.
    ChEMBLi CHEMBL5082.
    GuidetoPHARMACOLOGYi 2217.

    PTM databases

    PhosphoSitei Q9Y6E0.

    Polymorphism databases

    DMDMi 13626607.

    Proteomic databases

    MaxQBi Q9Y6E0.
    PaxDbi Q9Y6E0.
    PRIDEi Q9Y6E0.

    Protocols and materials databases

    DNASUi 8428.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376547 ; ENSP00000365730 ; ENSG00000102572 . [Q9Y6E0-1 ]
    ENST00000397517 ; ENSP00000380651 ; ENSG00000102572 . [Q9Y6E0-2 ]
    GeneIDi 8428.
    KEGGi hsa:8428.
    UCSCi uc001vnm.1. human. [Q9Y6E0-1 ]

    Organism-specific databases

    CTDi 8428.
    GeneCardsi GC13M099103.
    HGNCi HGNC:11403. STK24.
    HPAi HPA026435.
    HPA026502.
    MIMi 604984. gene.
    neXtProti NX_Q9Y6E0.
    PharmGKBi PA36210.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234203.
    HOVERGENi HBG108518.
    KOi K08838.
    OMAi GSDDWIF.
    PhylomeDBi Q9Y6E0.
    TreeFami TF354217.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_995. Apoptotic execution phase.
    SignaLinki Q9Y6E0.

    Miscellaneous databases

    ChiTaRSi STK24. human.
    EvolutionaryTracei Q9Y6E0.
    GeneWikii STK24.
    GenomeRNAii 8428.
    NextBioi 31540.
    PROi Q9Y6E0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6E0.
    Bgeei Q9Y6E0.
    CleanExi HS_STK24.
    HS_STK3.
    Genevestigatori Q9Y6E0.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    Pfami 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements."
      Schinkmann K., Blenis J.
      J. Biol. Chem. 272:28695-28703(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    2. "Identification of a human brain-specific isoform of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent protein kinase."
      Zhou T.-H., Ling K., Guo J., Zhou H., Wu Y.-L., Jing Q., Ma L., Pei G.
      J. Biol. Chem. 275:2513-2519(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PHOSPHORYLATION AT THR-18, MUTAGENESIS OF THR-18, VARIANT VAL-414.
      Tissue: Brain.
    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. "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 A).
      Tissue: Skin.
    6. Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-65 AND ASP-321.
    7. "Identification and characterization of the nuclear import and export signals of the mammalian Ste20-like protein kinase 3."
      Lee W.S., Hsu C.Y., Wang P.L., Huang C.Y., Chang C.H., Yuan C.J.
      FEBS Lett. 572:41-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL.
    8. "Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3."
      Lu T.J., Huang C.Y., Yuan C.J., Lee Y.C., Leu T.H., Chang W.C., Lu T.L., Jeng W.Y., Lai M.D.
      J. Inorg. Biochem. 99:1306-1313(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3."
      Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J., Hemmings B.A.
      Mol. Cell. Biol. 25:11019-11029(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST."
      Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D.
      J. Biol. Chem. 281:38405-38417(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-190, MUTAGENESIS OF THR-190.
    12. "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-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Mammalian sterile 20-like kinase 3 (MST3) mediates oxidative-stress-induced cell death by modulating JNK activation."
      Chen C.B., Ng J.K., Choo P.H., Wu W., Porter A.G.
      Biosci. Rep. 29:405-415(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-190.
    14. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
      Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
      Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTTNBP2NL.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Mst3b, an Ste20-like kinase, regulates axon regeneration in mature CNS and PNS pathways."
      Lorber B., Howe M.L., Benowitz L.I., Irwin N.
      Nat. Neurosci. 12:1407-1414(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Mammalian Ste20-like protein kinase 3 induces a caspase-independent apoptotic pathway."
      Lin C.Y., Wu H.Y., Wang P.L., Yuan C.J.
      Int. J. Biochem. Cell Biol. 42:98-105(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structures of human MST3 kinase in complex with adenine, ADP and Mn2+."
      Ko T.P., Jeng W.Y., Liu C.I., Lai M.D., Wu C.L., Chang W.J., Shr H.L., Lu T.J., Wang A.H.
      Acta Crystallogr. D 66:145-154(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-315 IN COMPLEX WITH ADENINE; ADP AND MANGANESE IONS, SUBUNIT, PHOSPHORYLATION AT THR-190.
    22. "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] VAL-414 AND ILE-426.

    Entry informationi

    Entry nameiSTK24_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6E0
    Secondary accession number(s): O14840, Q5JV92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 144 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

    3D-structure, 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. 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