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P47812

- MK14_XENLA

UniProt

P47812 - MK14_XENLA

Protein

Mitogen-activated protein kinase 14

Gene

mapk14

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. mapk14a is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. MPK2 is activated by upstream MAPKK/MAPKKK and stimulates MAPKAP kinase 2 to phosphorylate small heat shock proteins. Does not phosphorylate myelin basic protein or MAPKAP kinase 1.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541ATPPROSITE-ProRule annotation
    Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. p38MAPK cascade Source: UniProtKB
    3. positive regulation of myoblast differentiation Source: UniProtKB
    4. positive regulation of myoblast fusion Source: UniProtKB
    5. positive regulation of myotube differentiation Source: UniProtKB
    6. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 6726.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 14 (EC:2.7.11.24)
    Short name:
    MAP kinase 14
    Short name:
    MAPK 14
    Alternative name(s):
    Mitogen-activated Mitogen-activated protein kinase 2
    Short name:
    MAP kinase 2
    Short name:
    MPK2
    Gene namesi
    Name:mapk14
    Synonyms:mpk2
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-1018624. mapk14.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 361361Mitogen-activated protein kinase 14PRO_0000186299Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811PhosphothreonineBy similarity
    Modified residuei183 – 1831PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP47812.

    Interactioni

    Protein-protein interaction databases

    BioGridi98234. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP47812.
    SMRiP47812. Positions 9-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 309285Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi181 – 1833TXY

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG014652.
    KOiK04441.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01773. P38MAPKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P47812-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSNQSYVFY RQELNKTLWE VPDRYQNLTP VGSGAYGSVC SSFDTRTALR    50
    IAVKKLSRPF QSIIHAKRTY RELRLLKHMK HENVIGLLDV FSPAKSFEEF 100
    NDVYLVTHLM GADLNNIVKC QKLTDDHVQF LIYQILRGLK YIHSAGIIHR 150
    DLKPSNLAVN EDCELKILDF GLARHTDEEM TGYVATRWYR APEIMLNWMH 200
    YNQTVDIWSV GCIMAELLTG RTLFPGTDHI DQLKLILRLV GTPEPELLQK 250
    ISSEAARNYI QSLPYMPKMN FEDVFLGANP QAVDLLEKML VLDTDKRITA 300
    AEALAHSYFA QYHDPDDEPI AEPYDQSFES RELDIEEWKR LTYEEVTCFV 350
    PPPLDSEEME S 361
    Length:361
    Mass (Da):41,719
    Last modified:February 1, 1996 - v1
    Checksum:iF2B2E6C40800A70D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80751 mRNA. Translation: CAA56727.1.
    BC056064 mRNA. Translation: AAH56064.1.
    PIRiA54805.
    RefSeqiNP_001080300.1. NM_001086831.1.
    UniGeneiXl.1245.

    Genome annotation databases

    GeneIDi379992.
    KEGGixla:379992.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80751 mRNA. Translation: CAA56727.1 .
    BC056064 mRNA. Translation: AAH56064.1 .
    PIRi A54805.
    RefSeqi NP_001080300.1. NM_001086831.1.
    UniGenei Xl.1245.

    3D structure databases

    ProteinModelPortali P47812.
    SMRi P47812. Positions 9-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 98234. 1 interaction.

    Proteomic databases

    PRIDEi P47812.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 379992.
    KEGGi xla:379992.

    Organism-specific databases

    CTDi 1432.
    Xenbasei XB-GENE-1018624. mapk14.

    Phylogenomic databases

    HOVERGENi HBG014652.
    KOi K04441.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 6726.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    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 ]
    PRINTSi PR01773. P38MAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins."
      Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., Zamanillo D., Hunt T., Nebreda A.R.
      Cell 78:1027-1037(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Spleen.

    Entry informationi

    Entry nameiMK14_XENLA
    AccessioniPrimary (citable) accession number: P47812
    Secondary accession number(s): Q5D076
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3