Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O54992

- MAPK5_MOUSE

UniProt

O54992 - MAPK5_MOUSE

(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)

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

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 kinase activity Source: MGI
  5. 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
Complete GO annotation...

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
Complete GO annotation...

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 PKA1 Publication
Modified residuei182 – 1821Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA2 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

MaxQBiO54992.
PRIDEiO54992.

PTM databases

PhosphoSiteiO54992.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Gene expression databases

BgeeiO54992.
CleanExiMM_MAPKAPK5.
ExpressionAtlasiO54992. baseline and differential.
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 11-364.
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.
GeneTreeiENSGT00760000119016.
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.
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

        10         20         30         40         50
MSEDSDMEKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL
60 70 80 90 100
KILLDRPKAR NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI
110 120 130 140 150
VMEMMEGGEL FHRISQHRHF TEKQASQVTK QIALALQHCH LLNIAHRDLK
160 170 180 190 200
PENLLFKDNS LDAPVKLCDF GFAKVDQGDL MTPQFTPYYV APQVLEAQRR
210 220 230 240 250
HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP FYSKHHSRTI
260 270 280 290 300
PKDMRKKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD
310 320 330 340 350
HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK
360 370 380 390 400
PLHSVNNPIL RKRKLLGTKP KDGIYIHDHE NGTEDSNVAL EKLRDVIAQC
410 420 430 440 450
ILPQAGKGEN EDEKLNEVMQ EAWKYNRECK LLRDALQSFS WNGRGFTDKV
460 470
DRLKLAEVVK QVIEEQTLPH EPQ
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 11-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

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

PTM databases

PhosphoSitei O54992.

Proteomic databases

MaxQBi O54992.
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 ENSGT00760000119016.
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

Bgeei O54992.
CleanExi MM_MAPKAPK5.
ExpressionAtlasi O54992. baseline and differential.
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.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 123 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