Protein Domain : IPR008350

Type:  Family Name:  Mitogen-activated protein (MAP) kinase, ERK3/4
Description:  Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].MAP (Mitogen Activated Protein) kinases participate in kinase cascades, whereby at least 3 protein kinases act in series, culminating in activationof MAP kinase []. MAP kinases are activated by dual phosphorylationon both tyrosine and threonine residues of a conserved TXY motif. ERKs (Extracellularly Regulated Kinases) belong to the family of MAP kinases. ERK 3 (also known as MAPK6) and ERK 4 (also known as MAPK4), however, have no more similarity to ERK 1 and 2 than do the other major classes of MAP kinase, JNK and p38. ERK3 isconstitutively located in the nucleus, despite the lack of a traditional nuclear localisation signal []. It is unique among MAP kinases incontaining in its activation loop only a single phosphorylation site (serine 189) - other MAP kinases have the sequence TXY in this loop, but ERK3contains SEG, with glycine in place of tyrosine. ERK3 has no homologues in nematode or yeast genomes, indicating that it may have arisen from a relatively late gene duplication. Its structure,based on similarity to ERK2, contains segregated alpha and beta regions. Short Name:  MAPK_ERK3/4
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0 Child Features

5 Contains

DB identifier Type Name
IPR000719 Domain Protein kinase domain
IPR011009 Domain Protein kinase-like domain
IPR002290 Domain Serine/threonine/dual specificity protein kinase, catalytic domain
IPR017441 Binding_site Protein kinase, ATP binding site
IPR008271 Active_site Serine/threonine-protein kinase, active site

1 Cross References

Identifier
PR01771

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0004707 IPR008350
GO:0005524 IPR008350
GO:0006468 IPR008350

3 Ontology Annotations

GO Term Gene Name
GO:0004707 IPR008350
GO:0005524 IPR008350
GO:0006468 IPR008350

0 Parent Features

4 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Sialb.0079s0069.1.p PAC:39570818 Sinapis alba 404  
Eruve.1637s0006.1.p PAC:39943607 Eruca vesicaria 372  
Eruve.0594s0020.1.p PAC:39923067 Eruca vesicaria 392  
Sialb.0006s0998.1.p PAC:45666688 Sinapis alba 404  

7 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3291115
            12368087
            12471243
            15078142
            15320712
            10487205
            10657254