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Q8IW41

- MAPK5_HUMAN

UniProt

Q8IW41 - MAPK5_HUMAN

Protein

MAP kinase-activated protein kinase 5

Gene

MAPKAPK5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (13 Sep 2004)
      Previous versions | rss
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    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.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    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 – 511ATPPROSITE-ProRule annotation
    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. MAP kinase kinase activity Source: ProtInc
    3. p53 binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: GOC
    2. MAPK cascade Source: GOC
    3. negative regulation of TOR signaling Source: UniProtKB
    4. protein autophosphorylation Source: UniProtKB
    5. Ras protein signal transduction Source: UniProtKB
    6. regulation of translation Source: UniProtKB
    7. signal transduction Source: ProtInc
    8. 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_169436. Oxidative Stress Induced Senescence.
    SignaLinkiQ8IW41.

    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:
    MAPKAP-K5
    Short name:
    MAPKAPK-5
    Short name:
    MK-5
    Short name:
    MK5
    Alternative name(s):
    p38-regulated/activated protein kinase
    Short name:
    PRAK
    Gene namesi
    Name:MAPKAPK5
    Synonyms:PRAK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6889. 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: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511K → M: Kinase defective mutant, abolishes activity. 1 Publication
    Mutagenesisi182 – 1821T → A: No p38-beta/MAPK11-induced activation. 3 Publications
    Mutagenesisi182 – 1821T → D: Mimicks phosphorylation state and induces constitutive protein kinase activity. 3 Publications
    Mutagenesisi212 – 2121S → D: Mimicks phosphorylation state and displays a slightly higher protein kinase activity. 1 Publication
    Mutagenesisi337 – 3371L → G: Induces constitutive protein kinase activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA30633.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473MAP kinase-activated protein kinase 5PRO_0000086296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151Phosphoserine; by PKABy similarity
    Modified residuei182 – 1821Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA2 Publications
    Modified residuei212 – 2121Phosphoserine1 Publication

    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 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IW41.
    PaxDbiQ8IW41.
    PRIDEiQ8IW41.

    PTM databases

    PhosphoSiteiQ8IW41.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously.1 Publication

    Inductioni

    Directly regulated by MYC: expression is activated by MYC, suggesting the existence of a feedback regulatory loop.1 Publication

    Gene expression databases

    ArrayExpressiQ8IW41.
    BgeeiQ8IW41.
    CleanExiHS_MAPKAPK5.
    GenevestigatoriQ8IW41.

    Organism-specific databases

    HPAiCAB004546.
    HPA015515.

    Interactioni

    Subunit structurei

    Interacts with ERK3/MAPK6 and ERK4/MAPK4 (via FRIEDE motif); the interaction is direct By similarity. Interacts with YWHAE; the interaction prevents phosphorylation of HSP27/HSPB1 leading to disrupt F-actin polymerization. Interacts with SQSTM1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSPB1P047922EBI-1201460,EBI-352682
    MAPK6Q166593EBI-1201460,EBI-1384105
    TP53P046372EBI-1201460,EBI-366083

    Protein-protein interaction databases

    BioGridi114120. 16 interactions.
    IntActiQ8IW41. 18 interactions.
    MINTiMINT-4711647.
    STRINGi9606.ENSP00000202788.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IW41.
    SMRiQ8IW41. Positions 11-473.
    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.
    HOGENOMiHOG000233031.
    HOVERGENiHBG106948.
    InParanoidiQ8IW41.
    KOiK04442.
    OMAiQVTKQIA.
    PhylomeDBiQ8IW41.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IW41-1) [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

    MSEESDMDKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL    50
    KILLDRPKAR NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI 100
    VMEMMEGGEL FHRISQHRHF TEKQASQVTK QIALALRHCH LLNIAHRDLK 150
    PENLLFKDNS LDAPVKLCDF GFAKIDQGDL MTPQFTPYYV APQVLEAQRR 200
    HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP FYSKHHSRTI 250
    PKDMRRKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD 300
    HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK 350
    PLHSVNNPIL RKRKLLGTKP KDSVYIHDHE NGAEDSNVAL EKLRDVIAQC 400
    ILPQAGKGEN EDEKLNEVMQ EAWKYNRECK LLRDTLQSFS WNGRGFTDKV 450
    DRLKLAEIVK QVIEEQTTSH ESQ 473

    Note: No experimental confirmation available.

    Length:473
    Mass (Da):54,220
    Last modified:September 13, 2004 - v2
    Checksum:iF3D9DDC83CC0C49D
    GO
    Isoform 2 (identifier: Q8IW41-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:471
    Mass (Da):54,035
    Checksum:i176FA041A7F28570
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti273 – 2731I → T in CAB53747. (PubMed:17974005)Curated
    Sequence conflicti291 – 2911E → R in AAC39863. (PubMed:9628874)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671M → I.1 Publication
    Corresponds to variant rs34132040 [ dbSNP | Ensembl ].
    VAR_040758
    Natural varianti282 – 2821R → K.1 Publication
    Corresponds to variant rs34843470 [ dbSNP | Ensembl ].
    VAR_040759

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei407 – 4082Missing in isoform 2. 3 PublicationsVSP_011597

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF032437 Genomic DNA. Translation: AAC39863.1.
    AK122767 mRNA. Translation: BAG53717.1.
    CH471054 Genomic DNA. Translation: EAW97981.1.
    BC000833 mRNA. Translation: AAH00833.1.
    BC041049 mRNA. Translation: AAH41049.1.
    BC047284 mRNA. Translation: AAH47284.2.
    AL110301 mRNA. Translation: CAB53747.1.
    CCDSiCCDS44975.1. [Q8IW41-1]
    CCDS44976.1. [Q8IW41-2]
    PIRiT34519.
    RefSeqiNP_003659.2. NM_003668.3. [Q8IW41-2]
    NP_620777.1. NM_139078.2. [Q8IW41-1]
    UniGeneiHs.333120.
    Hs.413901.

    Genome annotation databases

    EnsembliENST00000550735; ENSP00000449667; ENSG00000089022. [Q8IW41-2]
    ENST00000551404; ENSP00000449381; ENSG00000089022. [Q8IW41-1]
    GeneIDi8550.
    KEGGihsa:8550.
    UCSCiuc001tsz.4. human. [Q8IW41-2]
    uc001tta.4. human. [Q8IW41-1]

    Polymorphism databases

    DMDMi52000829.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF032437 Genomic DNA. Translation: AAC39863.1 .
    AK122767 mRNA. Translation: BAG53717.1 .
    CH471054 Genomic DNA. Translation: EAW97981.1 .
    BC000833 mRNA. Translation: AAH00833.1 .
    BC041049 mRNA. Translation: AAH41049.1 .
    BC047284 mRNA. Translation: AAH47284.2 .
    AL110301 mRNA. Translation: CAB53747.1 .
    CCDSi CCDS44975.1. [Q8IW41-1 ]
    CCDS44976.1. [Q8IW41-2 ]
    PIRi T34519.
    RefSeqi NP_003659.2. NM_003668.3. [Q8IW41-2 ]
    NP_620777.1. NM_139078.2. [Q8IW41-1 ]
    UniGenei Hs.333120.
    Hs.413901.

    3D structure databases

    ProteinModelPortali Q8IW41.
    SMRi Q8IW41. Positions 11-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114120. 16 interactions.
    IntActi Q8IW41. 18 interactions.
    MINTi MINT-4711647.
    STRINGi 9606.ENSP00000202788.

    Chemistry

    BindingDBi Q8IW41.
    ChEMBLi CHEMBL3094.
    GuidetoPHARMACOLOGYi 2096.

    PTM databases

    PhosphoSitei Q8IW41.

    Polymorphism databases

    DMDMi 52000829.

    Proteomic databases

    MaxQBi Q8IW41.
    PaxDbi Q8IW41.
    PRIDEi Q8IW41.

    Protocols and materials databases

    DNASUi 8550.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000550735 ; ENSP00000449667 ; ENSG00000089022 . [Q8IW41-2 ]
    ENST00000551404 ; ENSP00000449381 ; ENSG00000089022 . [Q8IW41-1 ]
    GeneIDi 8550.
    KEGGi hsa:8550.
    UCSCi uc001tsz.4. human. [Q8IW41-2 ]
    uc001tta.4. human. [Q8IW41-1 ]

    Organism-specific databases

    CTDi 8550.
    GeneCardsi GC12P112282.
    HGNCi HGNC:6889. MAPKAPK5.
    HPAi CAB004546.
    HPA015515.
    MIMi 606723. gene.
    neXtProti NX_Q8IW41.
    PharmGKBi PA30633.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233031.
    HOVERGENi HBG106948.
    InParanoidi Q8IW41.
    KOi K04442.
    OMAi QVTKQIA.
    PhylomeDBi Q8IW41.
    TreeFami TF312891.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    SignaLinki Q8IW41.

    Miscellaneous databases

    ChiTaRSi MAPKAPK5. human.
    GeneWikii MAPKAPK5.
    GenomeRNAii 8550.
    NextBioi 32036.
    PROi Q8IW41.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IW41.
    Bgeei Q8IW41.
    CleanExi HS_MAPKAPK5.
    Genevestigatori Q8IW41.

    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. "PRAK, a novel protein kinase regulated by the p38 MAP kinase."
      New L., Jiang Y., Zhao M., Liu K., Zhu W., Flood L.J., Kato Y., Parry G.C.N., Han J.
      EMBO J. 17:3372-3384(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), MUTAGENESIS OF THR-182, FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-182, ENZYME REGULATION.
      Tissue: Placenta.
    2. "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] (ISOFORM 2).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Cervix, Pancreas and Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-473 (ISOFORM 2).
      Tissue: Brain.
    6. Cited for: INTERACTION WITH SQSTM1, ENZYME REGULATION, SUBCELLULAR LOCATION.
    7. "Regulation of PRAK subcellular location by p38 MAP kinases."
      New L., Jiang Y., Han J.
      Mol. Biol. Cell 14:2603-2616(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-212, MUTAGENESIS OF THR-182, MUTAGENESIS OF LYS-51; THR-182 AND SER-212.
    8. "14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin polymerization."
      Tak H., Jang E., Kim S.B., Park J., Suk J., Yoon Y.S., Ahn J.K., Lee J.H., Joe C.O.
      Cell. Signal. 19:2379-2387(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1, INTERACTION WITH YWHAE.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5."
      Kostenko S., Johannessen M., Moens U.
      Cell. Signal. 21:712-718(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1.
    12. "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 THR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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] ILE-67 AND LYS-282.
    14. Cited for: FUNCTION IN PHOSPHORYLATION OF TP53.
    15. "The MK5/PRAK kinase and Myc form a negative feedback loop that is disrupted during colorectal tumorigenesis."
      Kress T.R., Cannell I.G., Brenkman A.B., Samans B., Gaestel M., Roepman P., Burgering B.M., Bushell M., Rosenwald A., Eilers M.
      Mol. Cell 41:445-457(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FOXO3, AUTOPHOSPHORYLATION, INDUCTION, MUTAGENESIS OF THR-182 AND LEU-337.
    16. "Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: menage a trois or menage a quatre?"
      Shiryaev A., Moens U.
      Cell. Signal. 22:1185-1192(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiMAPK5_HUMAN
    AccessioniPrimary (citable) accession number: Q8IW41
    Secondary accession number(s): B3KVA5
    , O60491, Q86X46, Q9BVX9, Q9UG86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3