Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P47812 (MK14_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 14

Short name=MAP kinase 14
Short name=MAPK 14
EC=2.7.11.24
Alternative name(s):
Mitogen-activated Mitogen-activated protein kinase 2
Short name=MAP kinase 2
Short name=MPK2
Gene names
Name:mapk14
Synonyms:mpk2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation.

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Mitogen-activated protein kinase 14
PRO_0000186299

Regions

Domain25 – 309285Protein kinase
Nucleotide binding31 – 399ATP By similarity
Motif181 – 1833TXY

Sites

Active site1511Proton acceptor By similarity
Binding site541ATP By similarity

Amino acid modifications

Modified residue1811Phosphothreonine By similarity
Modified residue1831Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P47812 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: F2B2E6C40800A70D

FASTA36141,719
        10         20         30         40         50         60 
MSSNQSYVFY RQELNKTLWE VPDRYQNLTP VGSGAYGSVC SSFDTRTALR IAVKKLSRPF 

        70         80         90        100        110        120 
QSIIHAKRTY RELRLLKHMK HENVIGLLDV FSPAKSFEEF NDVYLVTHLM GADLNNIVKC 

       130        140        150        160        170        180 
QKLTDDHVQF LIYQILRGLK YIHSAGIIHR DLKPSNLAVN EDCELKILDF GLARHTDEEM 

       190        200        210        220        230        240 
TGYVATRWYR APEIMLNWMH YNQTVDIWSV GCIMAELLTG RTLFPGTDHI DQLKLILRLV 

       250        260        270        280        290        300 
GTPEPELLQK ISSEAARNYI QSLPYMPKMN FEDVFLGANP QAVDLLEKML VLDTDKRITA 

       310        320        330        340        350        360 
AEALAHSYFA QYHDPDDEPI AEPYDQSFES RELDIEEWKR LTYEEVTCFV PPPLDSEEME 


S 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80751 mRNA. Translation: CAA56727.1.
BC056064 mRNA. Translation: AAH56064.1.
PIRA54805.
RefSeqNP_001080300.1. NM_001086831.1.
UniGeneXl.1245.

3D structure databases

ProteinModelPortalP47812.
SMRP47812. Positions 9-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid98234. 1 interaction.

Proteomic databases

PRIDEP47812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID379992.
KEGGxla:379992.

Organism-specific databases

CTD1432.
XenbaseXB-GENE-1018624. mapk14.

Phylogenomic databases

HOVERGENHBG014652.
KOK04441.

Enzyme and pathway databases

BRENDA2.7.11.24. 6726.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01773. P38MAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMK14_XENLA
AccessionPrimary (citable) accession number: P47812
Secondary accession number(s): Q5D076
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families