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Protein

Mitogen-activated protein kinase 13

Gene

Mapk13

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

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.

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: RGD
  2. MAP kinase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. intracellular signal transduction Source: UniProtKB
  3. MAPK cascade Source: GOC
  4. protein phosphorylation Source: RGD
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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. 5301.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3045. Mapk13.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Mitogen-activated protein kinase 13PRO_0000186289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7By similarity
Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7By similarity
Modified residuei350 – 3501PhosphoserineBy similarity

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9WTY9.
PRIDEiQ9WTY9.

PTM databases

PhosphoSiteiQ9WTY9.

Expressioni

Gene expression databases

GenevestigatoriQ9WTY9.

Interactioni

Subunit structurei

Interacts with MAPK8IP2.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9WTY9.
SMRiQ9WTY9. Positions 1-351.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ9WTY9.
PhylomeDBiQ9WTY9.

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.
[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.

Q9WTY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLIRKRGFY KQDINKTAWE LPKTYLAPAH VGSGAYGAVC SAIDKRTGEK
60 70 80 90 100
VAIKKLSRPF QSEIFAKRAY RELLLLKHMH HENVIGLLDV YTPATSVRNF
110 120 130 140 150
QDFYLVMPFM QTDLQKIMGM EFSEEKVQYL VYQMLKGLKY IHSAGIVHRD
160 170 180 190 200
LKPGNLAVNE DCELKILDFG LARHTDAEMT GYVVTRWYRA PEVILSWMHY
210 220 230 240 250
NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG VPGAEFVQKL
260 270 280 290 300
KDKAAKSYIQ SLPQSPKKDF TQLFPRASPQ AVDLLDKMLE LDVDKRLTAA
310 320 330 340 350
QALAHPLFEP LRDPEEETEA QQPFDDALER ENLSVDEWKQ HIYKEIANFS
360
PIARKDSRRR SGMKLQ
Length:366
Mass (Da):42,051
Last modified:October 31, 1999 - v1
Checksum:i09F6E65092F2E8D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092534 mRNA. Translation: AAD23376.1.
UniGeneiRn.207195.

Genome annotation databases

UCSCiRGD:3045. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092534 mRNA. Translation: AAD23376.1.
UniGeneiRn.207195.

3D structure databases

ProteinModelPortaliQ9WTY9.
SMRiQ9WTY9. Positions 1-351.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9WTY9.

Proteomic databases

PaxDbiQ9WTY9.
PRIDEiQ9WTY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3045. rat.

Organism-specific databases

RGDi3045. Mapk13.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ9WTY9.
PhylomeDBiQ9WTY9.

Enzyme and pathway databases

BRENDAi2.7.11.24. 5301.

Gene expression databases

GenevestigatoriQ9WTY9.

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.
[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]
ProtoNetiSearch...

Publicationsi

  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: PHOSPHORYLATION, FUNCTION.
  3. "p38delta mitogen-activated protein kinase regulates skin homeostasis and tumorigenesis."
    Efimova T.
    Cell Cycle 9:498-505(2009) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.

Entry informationi

Entry nameiMK13_RAT
AccessioniPrimary (citable) accession number: Q9WTY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2001
Last sequence update: October 31, 1999
Last modified: March 3, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.