Mitogen-activated protein kinase 13 - Rattus norvegicus (Rat)

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Q9WTY9 (MK13_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 13
Short name=MAP kinase 13
Short name=MAPK 13
EC=2.7.11.24

Alternative name(s):
Mitogen-activated protein kinase p38 delta
Short name=MAP kinase p38 delta
Stress-activated protein kinase 4

Gene names

Name:

Mapk13

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

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	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.
Subunit structure	Interacts with MAPK8IP2 By similarity.
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	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
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Stress response Transcription Transcription regulation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from direct assay PubMed 16879317. Source: RGD MAP 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

Molecule processing

Chain

1 – 366

366

Mitogen-activated protein kinase 13

PRO_0000186289

Regions

Domain

25 – 308

284

Protein kinase

Nucleotide binding

31 – 39

ATP By similarity

Motif

180 – 182

TXY

Sites

Active site

150

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

180

Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 By similarity

Modified residue

182

Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 By similarity

Modified residue

350

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WTY9 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 09F6E65092F2E8D8
Show »

FASTA

366

42,051

        10         20         30         40         50         60 
MSLIRKRGFY KQDINKTAWE LPKTYLAPAH VGSGAYGAVC SAIDKRTGEK VAIKKLSRPF 

        70         80         90        100        110        120 
QSEIFAKRAY RELLLLKHMH HENVIGLLDV YTPATSVRNF QDFYLVMPFM QTDLQKIMGM 

       130        140        150        160        170        180 
EFSEEKVQYL VYQMLKGLKY IHSAGIVHRD LKPGNLAVNE DCELKILDFG LARHTDAEMT 

       190        200        210        220        230        240 
GYVVTRWYRA PEVILSWMHY NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG 

       250        260        270        280        290        300 
VPGAEFVQKL KDKAAKSYIQ SLPQSPKKDF TQLFPRASPQ AVDLLDKMLE LDVDKRLTAA 

       310        320        330        340        350        360 
QALAHPLFEP LRDPEEETEA QQPFDDALER ENLSVDEWKQ HIYKEIANFS PIARKDSRRR 


SGMKLQ

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References

[1]	"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].
[2]	"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.
[3]	"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.
[4]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF092534 mRNA. Translation: AAD23376.1.
IPI	IPI00203497.
UniGene	Rn.207195.
3D structure databases
ProteinModelPortal	Q9WTY9.
SMR	Q9WTY9. Positions 1-351.
ModBase	Search...
PTM databases
PhosphoSite	Q9WTY9.
Proteomic databases
PaxDb	Q9WTY9.
PRIDE	Q9WTY9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:3045. rat.
Organism-specific databases
RGD	3045. Mapk13.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
HOVERGEN	HBG014652.
InParanoid	Q9WTY9.
OrthoDB	EOG4R23V4.
Enzyme and pathway databases
BRENDA	2.7.11.24. 5301.
Gene expression databases
Genevestigator	Q9WTY9.
GermOnline	ENSRNOG00000000515. Rattus norvegicus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR008352. MAPK_p38. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01773. P38MAPKINASE.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MK13_RAT

Accession

Primary (citable) accession number: Q9WTY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents