Q9WTY9 (MK13_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 108. History...
Names and origin
|Protein names||Recommended name:|
Mitogen-activated protein kinase 13
Short name=MAP kinase 13
Short name=MAPK 13
Mitogen-activated protein kinase p38 delta
Short name=MAP kinase p38 delta
Stress-activated protein kinase 4
|Organism||Rattus norvegicus (Rat) [Reference proteome]|
|Taxonomic identifier||10116 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus|
|Sequence length||366 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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. Ref.2
ATP + a protein = ADP + a phosphoprotein.
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.
Interacts with MAPK8IP2 By similarity.
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
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 By similarity. Ref.2
Contains 1 protein kinase domain.
|Biological process||Cell cycle|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Biological_process||MAPK cascadecell cycle|
Inferred from electronic annotation. Source: UniProtKB-KWintracellular signal transduction
Inferred from sequence or structural similarity. Source: UniProtKBprotein phosphorylationregulation of transcription, DNA-templated
Inferred from electronic annotation. Source: UniProtKB-KWresponse to stress
Inferred from electronic annotation. Source: UniProtKB-KWtranscription, DNA-templated
Inferred from electronic annotation. Source: UniProtKB-KW
|Molecular_function||ATP bindingMAP kinase activity|
Inferred from sequence or structural similarity. Source: UniProtKB
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 366||366||Mitogen-activated protein kinase 13||PRO_0000186289|
|Domain||25 – 308||284||Protein kinase|
|Nucleotide binding||31 – 39||9||ATP By similarity|
|Motif||180 – 182||3||TXY|
|Active site||150||1||Proton acceptor By similarity|
|Binding site||54||1||ATP By similarity|
Amino acid modifications
|Modified residue||180||1||Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 By similarity|
|Modified residue||182||1||Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 By similarity|
|Modified residue||350||1||Phosphoserine By similarity|
|||"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].
|||"Physiological loading of joints prevents cartilage degradation through CITED2."|
Leong D.J., Li Y.H., Gu X.I., Sun L., Zhou Z., Nasser P., Laudier D.M., Iqbal J., Majeska R.J., Schaffler M.B., Goldring M.B., Cardoso L., Zaidi M., Sun H.B.
FASEB J. 25:182-191(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, FUNCTION.
|||"p38delta mitogen-activated protein kinase regulates skin homeostasis and tumorigenesis."|
Cell Cycle 9:498-505(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
|||"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.
|+||Additional computationally mapped references.|
|AF092534 mRNA. Translation: AAD23376.1.|
3D structure databases
|SMR||Q9WTY9. Positions 1-351. |
Protocols and materials databases
Genome annotation databases
|UCSC||RGD:3045. rat. |
|RGD||3045. Mapk13. |
Enzyme and pathway databases
|BRENDA||22.214.171.124. 5301. |
Gene expression databases
Family and domain databases
|InterPro||IPR011009. Kinase-like_dom. |
|Pfam||PF00069. Pkinase. 1 hit. |
|PRINTS||PR01773. P38MAPKINASE. |
|SMART||SM00220. S_TKc. 1 hit. |
|SUPFAM||SSF56112. SSF56112. 1 hit. |
|PROSITE||PS01351. MAPK. 1 hit. |
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
|Accession||Primary (citable) accession number: Q9WTY9|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families