Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O54992

- MAPK5_MOUSE

UniProt

O54992 - MAPK5_MOUSE

Protein

MAP kinase-activated protein kinase 5

Gene

Mapkapk5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.6 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated following phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11, ERK2/MAPK1, ERK3/MAPK6, and ERK4/MAPK4. Activated by stress-related extracellular stimuli; such as H2O2, arsenite, anisomycin TNF alpha and also PMA and the calcium ionophore A23187; but to a lesser extent. In vitro, activated by SQSTM1. Inhibited by diterpenoid alkaloid noroxoaconitine.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511ATPCurated
    Active sitei148 – 1481Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 369ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. mitogen-activated protein kinase binding Source: UniProtKB
    3. p53 binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: MGI
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. negative regulation of TOR signaling Source: UniProtKB
    2. protein autophosphorylation Source: UniProtKB
    3. Ras protein signal transduction Source: UniProtKB
    4. regulation of translation Source: UniProtKB
    5. stress-induced premature senescence Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MAP kinase-activated protein kinase 5 (EC:2.7.11.1)
    Short name:
    MAPK-activated protein kinase 5
    Short name:
    MAPKAP kinase 5
    Short name:
    MAPKAPK-5
    Gene namesi
    Name:Mapkapk5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1333110. Mapkapk5.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Phenotypes are different depending on reports. According to a first report, mice are viable and fertile and do not show changes in tissue morphology and behavior: they exhibit the same susceptibility to LPS-induced endotoxic shock as wild-type animals and do not show the defects in LPS-induced biosynthesis of inflammatory cytokines known to occur with Mapkapk2-deficient animals (PubMed:14560018). According to another report, both homozygous and heterozygous mutant mice are highly susceptible to skin carcinogenesis induced by DMBA (PubMed:17254968). According to a third report, mutant show embryonic lethality around E11 in a C57BL/6 background (PubMed:15538386).3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511K → E: No p38-alpha/MAPK14-, p38-beta/MAPK11-, ERK3/MAPK6-, ERK4/MAPK4-induced activation. 4 Publications
    Mutagenesisi51 – 511K → R or M: Kinase defective mutant, abolishes activity. 4 Publications
    Mutagenesisi115 – 1151S → A: Impairs shuttling to the cytoplasm. 1 Publication
    Mutagenesisi115 – 1151S → D: Mimicks phosphorylation state, lesding to localization to the cytoplasm. 1 Publication
    Mutagenesisi182 – 1821T → A: Impairs protein kinase activity and shuttling to the cytoplasm. 4 Publications
    Mutagenesisi337 – 3371L → A: Constitutive active mutant. In a knockin model, mouse display increased amounts of head dips and open arm time on the maze, compared to littermate controls. In addition, they also explore further into the open arm on the elevated plus maze and are less active in the closed arm compared to littermate controls. Male knockin mice display no differences in anxiety, but their locomotor activity increases compared to non-transgenic littermates. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473MAP kinase-activated protein kinase 5PRO_0000086297Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151Phosphoserine; by PKA2 Publications
    Modified residuei182 – 1821Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA3 Publications
    Modified residuei212 – 2121PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the regulatory phosphorylation site and is located on the T-loop/loop 12, leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization to the cytoplasm. Autophosphorylated.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiO54992.

    PTM databases

    PhosphoSiteiO54992.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.1 Publication

    Gene expression databases

    ArrayExpressiO54992.
    BgeeiO54992.
    CleanExiMM_MAPKAPK5.
    GenevestigatoriO54992.

    Interactioni

    Subunit structurei

    Interacts with SQSTM1 By similarity. Interacts with ERK3/MAPK6 and ERK4/MAPK4 (via FRIEDE motif); the interaction is direct. Interacts with YWHAE; the interaction prevents phosphorylation of HSP27/HSPB1 leading to disrupt F-actin polymerization.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi201309. 2 interactions.
    IntActiO54992. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliO54992.
    SMRiO54992. Positions 11-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 304283Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili409 – 44032Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110339.
    HOGENOMiHOG000233031.
    HOVERGENiHBG106948.
    InParanoidiO54992.
    KOiK04442.
    OMAiQVTKQIA.
    OrthoDBiEOG786H3M.
    PhylomeDBiO54992.
    TreeFamiTF312891.

    Family and domain databases

    Gene3Di4.10.1170.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR027442. MAPKAPK_C.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O54992-1) [UniParc]FASTAAdd to Basket

    Also known as: MK-5 type 1

    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

    MSEDSDMEKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL    50
    KILLDRPKAR NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI 100
    VMEMMEGGEL FHRISQHRHF TEKQASQVTK QIALALQHCH LLNIAHRDLK 150
    PENLLFKDNS LDAPVKLCDF GFAKVDQGDL MTPQFTPYYV APQVLEAQRR 200
    HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP FYSKHHSRTI 250
    PKDMRKKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD 300
    HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK 350
    PLHSVNNPIL RKRKLLGTKP KDGIYIHDHE NGTEDSNVAL EKLRDVIAQC 400
    ILPQAGKGEN EDEKLNEVMQ EAWKYNRECK LLRDALQSFS WNGRGFTDKV 450
    DRLKLAEVVK QVIEEQTLPH EPQ 473
    Length:473
    Mass (Da):54,152
    Last modified:June 1, 1998 - v1
    Checksum:i45441A735075B247
    GO
    Isoform 2 (identifier: O54992-2) [UniParc]FASTAAdd to Basket

    Also known as: MK-5 type 3

    The sequence of this isoform differs from the canonical sequence as follows:
         344-408: DLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTEDSNVALEKLRDVIAQCILPQAGKG → E

    Show »
    Length:409
    Mass (Da):47,103
    Checksum:i7EEAF061669A3F61
    GO
    Isoform 3 (identifier: O54992-3) [UniParc]FASTAAdd to Basket

    Also known as: MK-5 type 4

    The sequence of this isoform differs from the canonical sequence as follows:
         13-161: Missing.

    Show »
    Length:324
    Mass (Da):37,042
    Checksum:i25BF2CB86528174D
    GO
    Isoform 4 (identifier: O54992-4) [UniParc]FASTAAdd to Basket

    Also known as: MK-5 type 5

    The sequence of this isoform differs from the canonical sequence as follows:
         13-161: Missing.
         407-408: Missing.

    Show »
    Length:322
    Mass (Da):36,856
    Checksum:iBADC2B6FEB4AEA4A
    GO
    Isoform 5 (identifier: O54992-5) [UniParc]FASTAAdd to Basket

    Also known as: MK-5 type 2

    The sequence of this isoform differs from the canonical sequence as follows:
         407-408: Missing.

    Show »
    Length:471
    Mass (Da):53,967
    Checksum:iAC171E324E40A3D4
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei13 – 161149Missing in isoform 3 and isoform 4. 1 PublicationVSP_011599Add
    BLAST
    Alternative sequencei344 – 40865DLKVS…QAGKG → E in isoform 2. 1 PublicationVSP_011600Add
    BLAST
    Alternative sequencei407 – 4082Missing in isoform 4 and isoform 5. 1 PublicationVSP_011598

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039840 mRNA. Translation: AAC40047.1.
    AY533679 mRNA. Translation: AAS22330.1.
    AY533680 mRNA. Translation: AAS22331.2.
    AY533681 mRNA. Translation: AAS22332.1.
    AY533682 mRNA. Translation: AAS22333.1.
    AC155316 Genomic DNA. No translation available.
    BC019184 mRNA. Translation: AAH19184.1.
    CCDSiCCDS39248.1. [O54992-1]
    PIRiJC5952.
    RefSeqiNP_034895.1. NM_010765.2. [O54992-1]
    UniGeneiMm.272206.

    Genome annotation databases

    EnsembliENSMUST00000031410; ENSMUSP00000031410; ENSMUSG00000029454. [O54992-1]
    ENSMUST00000111782; ENSMUSP00000107412; ENSMUSG00000029454. [O54992-4]
    ENSMUST00000111783; ENSMUSP00000107413; ENSMUSG00000029454. [O54992-5]
    ENSMUST00000111786; ENSMUSP00000107416; ENSMUSG00000029454. [O54992-3]
    ENSMUST00000153763; ENSMUSP00000119182; ENSMUSG00000029454.
    GeneIDi17165.
    KEGGimmu:17165.
    UCSCiuc008zjq.1. mouse. [O54992-1]
    uc008zjr.1. mouse. [O54992-3]
    uc008zjs.1. mouse. [O54992-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039840 mRNA. Translation: AAC40047.1 .
    AY533679 mRNA. Translation: AAS22330.1 .
    AY533680 mRNA. Translation: AAS22331.2 .
    AY533681 mRNA. Translation: AAS22332.1 .
    AY533682 mRNA. Translation: AAS22333.1 .
    AC155316 Genomic DNA. No translation available.
    BC019184 mRNA. Translation: AAH19184.1 .
    CCDSi CCDS39248.1. [O54992-1 ]
    PIRi JC5952.
    RefSeqi NP_034895.1. NM_010765.2. [O54992-1 ]
    UniGenei Mm.272206.

    3D structure databases

    ProteinModelPortali O54992.
    SMRi O54992. Positions 11-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201309. 2 interactions.
    IntActi O54992. 2 interactions.

    PTM databases

    PhosphoSitei O54992.

    Proteomic databases

    PRIDEi O54992.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031410 ; ENSMUSP00000031410 ; ENSMUSG00000029454 . [O54992-1 ]
    ENSMUST00000111782 ; ENSMUSP00000107412 ; ENSMUSG00000029454 . [O54992-4 ]
    ENSMUST00000111783 ; ENSMUSP00000107413 ; ENSMUSG00000029454 . [O54992-5 ]
    ENSMUST00000111786 ; ENSMUSP00000107416 ; ENSMUSG00000029454 . [O54992-3 ]
    ENSMUST00000153763 ; ENSMUSP00000119182 ; ENSMUSG00000029454 .
    GeneIDi 17165.
    KEGGi mmu:17165.
    UCSCi uc008zjq.1. mouse. [O54992-1 ]
    uc008zjr.1. mouse. [O54992-3 ]
    uc008zjs.1. mouse. [O54992-4 ]

    Organism-specific databases

    CTDi 8550.
    MGIi MGI:1333110. Mapkapk5.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110339.
    HOGENOMi HOG000233031.
    HOVERGENi HBG106948.
    InParanoidi O54992.
    KOi K04442.
    OMAi QVTKQIA.
    OrthoDBi EOG786H3M.
    PhylomeDBi O54992.
    TreeFami TF312891.

    Enzyme and pathway databases

    Reactomei REACT_188970. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    ChiTaRSi MAPKAPK5. mouse.
    NextBioi 291446.
    PROi O54992.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54992.
    Bgeei O54992.
    CleanExi MM_MAPKAPK5.
    Genevestigatori O54992.

    Family and domain databases

    Gene3Di 4.10.1170.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR027442. MAPKAPK_C.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase."
      Ni H., Wang X.S., Diener K., Yao Z.
      Biochem. Biophys. Res. Commun. 243:492-496(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF LYS-51, ENZYME REGULATION, PHOSPHORYLATION BY ERK2/MAPK1 AND MAPK14.
      Tissue: Spleen.
    2. "Novel splice variants of MK5 from mouse heart."
      Benoit M.-J., Moise N., Mamarbachi A.M., Allen B.G.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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).
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    5. "Elimination of protein kinase MK5/PRAK activity by targeted homologous recombination."
      Shi Y., Kotlyarov A., Laabeta K., Gruber A.D., Butt E., Marcus K., Meyer H.E., Friedrich A., Volk H.D., Gaestel M.
      Mol. Cell. Biol. 23:7732-7741(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    6. Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK6, SUBCELLULAR LOCATION, INTERACTION WITH MAPK6, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-182, MUTAGENESIS OF LYS-51 AND THR-182, DISRUPTION PHENOTYPE.
    7. "Activation of MK5/PRAK by the atypical MAP kinase ERK3 defines a novel signal transduction pathway."
      Seternes O.M., Mikalsen T., Johansen B., Michaelsen E., Armstrong C.G., Morrice N.A., Turgeon B., Meloche S., Moens U., Keyse S.M.
      EMBO J. 23:4780-4791(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK6, SUBCELLULAR LOCATION, INTERACTION WITH MAPK6, PHOSPHORYLATION AT THR-182, MUTAGENESIS OF THR-182.
    8. "Characterization of the atypical MAPK ERK4 and its activation of the MAPK-activated protein kinase MK5."
      Kant S., Schumacher S., Singh M.K., Kispert A., Kotlyarov A., Gaestel M.
      J. Biol. Chem. 281:35511-35519(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK4, SUBCELLULAR LOCATION, INTERACTION WITH MAPK4.
    9. "Transgenic mice expressing constitutive active MAPKAPK5 display gender-dependent differences in exploration and activity."
      Gerits N., Van Belle W., Moens U.
      Behav. Brain Funct. 3:58-58(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-337.
    10. Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-51 AND THR-182.
    11. "Modulation of F-actin rearrangement by the cyclic AMP/cAMP-dependent protein kinase (PKA) pathway is mediated by MAPK-activated protein kinase 5 and requires PKA-induced nuclear export of MK5."
      Gerits N., Mikalsen T., Kostenko S., Shiryaev A., Johannessen M., Moens U.
      J. Biol. Chem. 282:37232-37243(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "The Ser(186) phospho-acceptor site within ERK4 is essential for its ability to interact with and activate PRAK/MK5."
      Perander M., Aberg E., Johansen B., Dreyer B., Guldvik I.J., Outzen H., Keyse S.M., Seternes O.M.
      Biochem. J. 411:613-622(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK4.
    13. "Determinants that control the distinct subcellular localization of p38alpha-PRAK and p38beta-PRAK complexes."
      Li Q., Zhang N., Zhang D., Wang Y., Lin T., Wang Y., Zhou H., Ye Z., Zhang F., Lin S.C., Han J.
      J. Biol. Chem. 283:11014-11023(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Activation loop phosphorylation of the atypical MAP kinases ERK3 and ERK4 is required for binding, activation and cytoplasmic relocalization of MK5."
      Deleris P., Rousseau J., Coulombe P., Rodier G., Tanguay P.L., Meloche S.
      J. Cell. Physiol. 217:778-788(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK4 AND MAPK6.
    15. "Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif."
      Aberg E., Torgersen K.M., Johansen B., Keyse S.M., Perander M., Seternes O.M.
      J. Biol. Chem. 284:19392-19401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK4 AND MAPK6.
    16. "The diterpenoid alkaloid noroxoaconitine is a Mapkap kinase 5 (MK5/PRAK) inhibitor."
      Kostenko S., Khan M.T., Sylte I., Moens U.
      Cell. Mol. Life Sci. 68:289-301(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF THR-182.
    17. "Serine residue 115 of MAPK-activated protein kinase MK5 is crucial for its PKA-regulated nuclear export and biological function."
      Kostenko S., Shiryaev A., Gerits N., Dumitriu G., Klenow H., Johannessen M., Moens U.
      Cell. Mol. Life Sci. 68:847-862(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-115, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-115.
    18. "Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced heat shock protein 27 phosphorylation."
      Shiryaev A., Dumitriu G., Moens U.
      J. Mol. Signal. 6:4-4(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1.
    19. "Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1."
      Zheng M., Wang Y.H., Wu X.N., Wu S.Q., Lu B.J., Dong M.Q., Zhang H., Sun P., Lin S.C., Guan K.L., Han J.
      Nat. Cell Biol. 13:263-272(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RHEB, MUTAGENESIS OF LYS-51.

    Entry informationi

    Entry nameiMAPK5_MOUSE
    AccessioniPrimary (citable) accession number: O54992
    Secondary accession number(s): E9QQ45
    , Q6QME4, Q6QME5, Q6QME6, Q6QME7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    The role of p38 MAPK kinases is unclear in phosphorylation and activation of Mapkapk5. According to some reports, it interacts and is phosphorylated by p38-alpha/MAPK14 and p38-beta/MAPK11 (PubMed:9480836). According to other reports, it is not activated by p38-alpha/MAPK14 and p38-beta/MAPK11 (PubMed:14560018). An explanation for these discrepancies, might be that the interaction with p38 MAPK kinases is weak and occurs only under specific conditions.2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3