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O15264

- MK13_HUMAN

UniProt

O15264 - MK13_HUMAN

Protein

Mitogen-activated protein kinase 13

Gene

MAPK13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 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 such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by phosphorylation on threonine and tyrosine by dual specificity kinases, MAP2K3/MKK3, MAP2K6/MKK6, MAP2K4/MKK4 and MAP2K7/MKK7. Activation by ultraviolet radiation, hyperosmotic shock, anisomycin or by TNF-alpha is mediated by MAP2K3/MKK3. Inhibited by dual specificity phosphatase DUSP1.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541ATPPROSITE-ProRule annotation
    Active sitei150 – 1501Proton 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
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: BHF-UCL

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. intracellular signal transduction Source: UniProtKB
    3. MAPK cascade Source: GOC
    4. neurotrophin TRK receptor signaling pathway Source: Reactome
    5. peptidyl-serine phosphorylation Source: BHF-UCL
    6. positive regulation of inflammatory response Source: BHF-UCL
    7. positive regulation of interleukin-6 production Source: BHF-UCL
    8. Ras protein signal transduction Source: Reactome
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. response to osmotic stress Source: UniProtKB
    11. response to stress Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 2681.
    ReactomeiREACT_12065. p38MAPK events.
    REACT_25299. DSCAM interactions.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiO15264.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 13 (EC:2.7.11.24)
    Short name:
    MAP kinase 13
    Short name:
    MAPK 13
    Alternative name(s):
    Mitogen-activated protein kinase p38 delta
    Short name:
    MAP kinase p38 delta
    Stress-activated protein kinase 4
    Gene namesi
    Name:MAPK13
    Synonyms:PRKM13, SAPK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6875. MAPK13.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801T → A: Loss of kinase activity. 1 Publication
    Mutagenesisi182 – 1821Y → A: Loss of kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA30620.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 365365Mitogen-activated protein kinase 13PRO_0000186286Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 471Phosphoserine1 Publication
    Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K71 Publication
    Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K71 Publication
    Modified residuei350 – 3501Phosphoserine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO15264.
    PaxDbiO15264.
    PRIDEiO15264.

    PTM databases

    PhosphoSiteiO15264.

    Expressioni

    Tissue specificityi

    Expressed in testes, pancreas, small intestine, lung and kidney. Abundant in macrophages, also present in neutrophils, CD4+ T-cells, and endothelial cells.2 Publications

    Gene expression databases

    ArrayExpressiO15264.
    BgeeiO15264.
    CleanExiHS_MAPK13.
    GenevestigatoriO15264.

    Organism-specific databases

    HPAiCAB025854.
    HPA007667.

    Interactioni

    Subunit structurei

    Interacts with MAPK8IP2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FPR1P214623EBI-2116951,EBI-2869495
    PRKD1Q151396EBI-2116951,EBI-1181072

    Protein-protein interaction databases

    BioGridi111589. 14 interactions.
    IntActiO15264. 90 interactions.
    MINTiMINT-1183220.
    STRINGi9606.ENSP00000211287.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 85
    Beta strandi9 – 146
    Beta strandi17 – 226
    Beta strandi25 – 339
    Beta strandi35 – 4410
    Turni45 – 473
    Beta strandi50 – 567
    Helixi63 – 7816
    Beta strandi88 – 914
    Beta strandi95 – 973
    Beta strandi104 – 1085
    Beta strandi111 – 1133
    Helixi114 – 1174
    Helixi124 – 14320
    Helixi153 – 1553
    Beta strandi156 – 1583
    Beta strandi164 – 1663
    Helixi191 – 1944
    Helixi204 – 21815
    Beta strandi222 – 2265
    Helixi228 – 23912
    Helixi244 – 2474
    Helixi253 – 2619
    Helixi270 – 2734
    Helixi279 – 28810
    Turni293 – 2953
    Helixi299 – 3035
    Helixi306 – 3083
    Turni309 – 3113
    Helixi314 – 3163
    Turni327 – 3304
    Helixi335 – 34814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3COIX-ray2.09A2-352[»]
    4EXUX-ray1.70A1-352[»]
    4EYJX-ray2.10A1-352[»]
    4EYMX-ray2.35A1-352[»]
    ProteinModelPortaliO15264.
    SMRiO15264. Positions 2-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15264.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 308284Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi180 – 1823TXY

    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

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiO15264.
    KOiK04441.
    OMAiEHPYFDN.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiO15264.
    TreeFamiTF105100.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15264-1) [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

    MSLIRKKGFY KQDVNKTAWE LPKTYVSPTH VGSGAYGSVC SAIDKRSGEK    50
    VAIKKLSRPF QSEIFAKRAY RELLLLKHMQ HENVIGLLDV FTPASSLRNF 100
    YDFYLVMPFM QTDLQKIMGM EFSEEKIQYL VYQMLKGLKY IHSAGVVHRD 150
    LKPGNLAVNE DCELKILDFG LARHADAEMT GYVVTRWYRA PEVILSWMHY 200
    NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG VPGTEFVQKL 250
    NDKAAKSYIQ SLPQTPRKDF TQLFPRASPQ AADLLEKMLE LDVDKRLTAA 300
    QALTHPFFEP FRDPEEETEA QQPFDDSLEH EKLTVDEWKQ HIYKEIVNFS 350
    PIARKDSRRR SGMKL 365
    Length:365
    Mass (Da):42,090
    Last modified:January 1, 1998 - v1
    Checksum:i52E749EDB2973DDF
    GO
    Isoform 2 (identifier: O15264-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         204-256: VDIWSVGCIM...VQKLNDKAAK → GQILHPVPAT...DGRAGPHPSL
         257-364: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:257
    Mass (Da):28,779
    Checksum:iBDCA13CF80344118
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 142DV → EL in AAC51374. (PubMed:9207191)Curated
    Sequence conflicti39 – 391V → W in AAC51374. (PubMed:9207191)Curated
    Sequence conflicti56 – 561L → P in AAC51758. (PubMed:9295308)Curated
    Sequence conflicti166 – 1661I → V in AAC51758. (PubMed:9295308)Curated
    Sequence conflicti224 – 2241K → R in AAC51758. (PubMed:9295308)Curated
    Sequence conflicti224 – 2241K → R in AAD23377. (PubMed:10066767)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411S → L.1 Publication
    Corresponds to variant rs55776345 [ dbSNP | Ensembl ].
    VAR_042267
    Natural varianti282 – 2821A → V.1 Publication
    Corresponds to variant rs55990045 [ dbSNP | Ensembl ].
    VAR_042268
    Natural varianti300 – 3001A → T.1 Publication
    Corresponds to variant rs41270090 [ dbSNP | Ensembl ].
    VAR_042269

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei204 – 25653VDIWS…DKAAK → GQILHPVPATDPQEGFHSAV PTGQPPGCGPAGEDAGARRG QAPDGRAGPHPSL in isoform 2. 1 PublicationVSP_056558Add
    BLAST
    Alternative sequencei257 – 364108Missing in isoform 2. 1 PublicationVSP_056559Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10488 mRNA. Translation: CAA71512.1.
    U93232 mRNA. Translation: AAB87639.1.
    AF015256 mRNA. Translation: AAC51758.1.
    AF004709 mRNA. Translation: AAC51374.1.
    AF092535 mRNA. Translation: AAD23377.1.
    AF100546 mRNA. Translation: AAF36772.1.
    BT007221 mRNA. Translation: AAP35885.1.
    CR536490 mRNA. Translation: CAG38729.1.
    Z95152 Genomic DNA. Translation: CAB08438.1.
    CH471081 Genomic DNA. Translation: EAX03874.1.
    CH471081 Genomic DNA. Translation: EAX03875.1.
    BC000433 mRNA. Translation: AAH00433.1.
    BC001641 mRNA. Translation: AAH01641.1.
    BC004428 mRNA. Translation: AAH04428.1.
    BC085196 mRNA. Translation: AAH85196.1.
    CCDSiCCDS4818.1.
    PIRiJC5528.
    RefSeqiNP_002745.1. NM_002754.4.
    UniGeneiHs.178695.

    Genome annotation databases

    EnsembliENST00000211287; ENSP00000211287; ENSG00000156711.
    ENST00000373766; ENSP00000362871; ENSG00000156711.
    GeneIDi5603.
    KEGGihsa:5603.
    UCSCiuc003ols.4. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10488 mRNA. Translation: CAA71512.1 .
    U93232 mRNA. Translation: AAB87639.1 .
    AF015256 mRNA. Translation: AAC51758.1 .
    AF004709 mRNA. Translation: AAC51374.1 .
    AF092535 mRNA. Translation: AAD23377.1 .
    AF100546 mRNA. Translation: AAF36772.1 .
    BT007221 mRNA. Translation: AAP35885.1 .
    CR536490 mRNA. Translation: CAG38729.1 .
    Z95152 Genomic DNA. Translation: CAB08438.1 .
    CH471081 Genomic DNA. Translation: EAX03874.1 .
    CH471081 Genomic DNA. Translation: EAX03875.1 .
    BC000433 mRNA. Translation: AAH00433.1 .
    BC001641 mRNA. Translation: AAH01641.1 .
    BC004428 mRNA. Translation: AAH04428.1 .
    BC085196 mRNA. Translation: AAH85196.1 .
    CCDSi CCDS4818.1.
    PIRi JC5528.
    RefSeqi NP_002745.1. NM_002754.4.
    UniGenei Hs.178695.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3COI X-ray 2.09 A 2-352 [» ]
    4EXU X-ray 1.70 A 1-352 [» ]
    4EYJ X-ray 2.10 A 1-352 [» ]
    4EYM X-ray 2.35 A 1-352 [» ]
    ProteinModelPortali O15264.
    SMRi O15264. Positions 2-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111589. 14 interactions.
    IntActi O15264. 90 interactions.
    MINTi MINT-1183220.
    STRINGi 9606.ENSP00000211287.

    Chemistry

    BindingDBi O15264.
    ChEMBLi CHEMBL2939.
    GuidetoPHARMACOLOGYi 1502.

    PTM databases

    PhosphoSitei O15264.

    Proteomic databases

    MaxQBi O15264.
    PaxDbi O15264.
    PRIDEi O15264.

    Protocols and materials databases

    DNASUi 5603.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000211287 ; ENSP00000211287 ; ENSG00000156711 .
    ENST00000373766 ; ENSP00000362871 ; ENSG00000156711 .
    GeneIDi 5603.
    KEGGi hsa:5603.
    UCSCi uc003ols.4. human.

    Organism-specific databases

    CTDi 5603.
    GeneCardsi GC06P036095.
    HGNCi HGNC:6875. MAPK13.
    HPAi CAB025854.
    HPA007667.
    MIMi 602899. gene.
    neXtProti NX_O15264.
    PharmGKBi PA30620.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi O15264.
    KOi K04441.
    OMAi EHPYFDN.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi O15264.
    TreeFami TF105100.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    Reactomei REACT_12065. p38MAPK events.
    REACT_25299. DSCAM interactions.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki O15264.

    Miscellaneous databases

    EvolutionaryTracei O15264.
    GeneWikii MAPK13.
    GenomeRNAii 5603.
    NextBioi 21772.
    PROi O15264.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15264.
    Bgeei O15264.
    CleanExi HS_MAPK13.
    Genevestigatori O15264.

    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. "Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases."
      Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.
      EMBO J. 16:3563-3571(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION.
      Tissue: Pituitary.
    2. "Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta."
      Jiang Y., Gram H., Zhao M., New L., Gu J., Feng L., Di Padova F., Ulevitch R.J., Han J.
      J. Biol. Chem. 272:30122-30128(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-180 AND TYR-182, MUTAGENESIS OF THR-180 AND TYR-182, ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase."
      Wang X.S., Diener K., Manthey C.L., Wang S.-W., Rosenzweig B., Bray J., Delaney J., Cole C., Zukowski M., Yao Z.
      J. Biol. Chem. 272:23668-23674(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles."
      Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R.
      Biochem. Biophys. Res. Commun. 235:533-538(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Murine p38-delta mitogen-activated protein kinase, a developmentally regulated protein kinase that is activated by stress and proinflammatory cytokines."
      Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R., Tan T.-H.
      J. Biol. Chem. 274:7095-7102(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "Structure and polymorphism of two stress-activated protein kinase genes centromeric of the MHC: SAPK2a and SAPK4."
      Herbison C.E., Sayer D.C., Bellgard M., Allcock R.J.N., Christiansen F.T., Price P.
      DNA Seq. 10:229-243(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Lung and Pancreas.
    12. Cited for: FUNCTION IN PHOSPHORYLATION OF STMN1.
    13. "Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages."
      Hale K.K., Trollinger D., Rihanek M., Manthey C.L.
      J. Immunol. 162:4246-4252(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Fibroblast growth factor homologous factors are intracellular signaling proteins."
      Schoorlemmer J., Goldfarb M.
      Curr. Biol. 11:793-797(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK8IP2.
    15. "A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta."
      Knebel A., Morrice N., Cohen P.
      EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    16. "Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells."
      Buee-Scherrer V., Goedert M.
      FEBS Lett. 515:151-154(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
    17. "Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly."
      Feijoo C., Campbell D.G., Jakes R., Goedert M., Cuenda A.
      J. Cell Sci. 118:397-408(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
    18. "Activation of PKCdelta and p38delta MAPK during okadaic acid dependent keratinocyte apoptosis."
      Kraft C.A., Efimova T., Eckert R.L.
      Arch. Dermatol. Res. 299:71-83(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN KERATINOCYTE APOPTOSIS.
    19. "p38MAPK delta controls c-Myb degradation in response to stress."
      Pani E., Ferrari S.
      Blood Cells Mol. Dis. 40:388-394(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MYB.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    21. "MKP-1 inhibits high NaCl-induced activation of p38 but does not inhibit the activation of TonEBP/OREBP: opposite roles of p38alpha and p38delta."
      Zhou X., Ferraris J.D., Dmitrieva N.I., Liu Y., Burg M.B.
      Proc. Natl. Acad. Sci. U.S.A. 105:5620-5625(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION BY DUSP1, FUNCTION.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Human p38 delta MAP kinase mediates UV irradiation induced up-regulation of the gene expression of chemokine BRAK/CXCL14."
      Ozawa S., Ito S., Kato Y., Kubota E., Hata R.
      Biochem. Biophys. Res. Commun. 396:1060-1064(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "p38delta mitogen-activated protein kinase regulates skin homeostasis and tumorigenesis."
      Efimova T.
      Cell Cycle 9:498-505(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    25. "Mechanisms and functions of p38 MAPK signalling."
      Cuadrado A., Nebreda A.R.
      Biochem. J. 429:403-417(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Crystal structure of p38delta kinase."
      New York structural genomix research consortium (NYSGXRC)
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-352.
    28. "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] LEU-41; VAL-282 AND THR-300.

    Entry informationi

    Entry nameiMK13_HUMAN
    AccessioniPrimary (citable) accession number: O15264
    Secondary accession number(s): O14739
    , O15124, Q5U4A5, Q6FI46, Q9UNU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 155 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 6
      Human chromosome 6: 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