Target name

P28482: Mitogen-activated protein kinase 1


  Protein function

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation.

  Database links

Uniprot primary ID P28482
PDB ID 2OJG 1TVO 4N0S 3W55 4FUY 4FUX 2OJI 3I5Z 3D44 3D42 3I60 4QTA 4IZA 3TEI 4O6E 4FV8 4FV9 4FV4 4FV5 4FV6 4FV7 4FV0 4FV1 4FV2 4FV3 1PME 2OJJ 4ZZM 4ZZN 4ZZO 4G6N 4QTE 4IZ7 4IZ5 1WZY 2Y9Q 4G6O 3SA0 4H3Q 4H3P 4NIF 4FMQ
DrugBank ID DB01169 DB01064
BioGrid ID 111580
GuidetoPHARMACOLOGY ID 1495
PharmGKB ID PA30616
KEGG ID hsa:5594
BioCyc
Entrez Gene (Gene ID) 5594
DIP DIP-519N
STRING 9606ENSP00000215832
MINT MINT-144006
IntAct P28482
DMDM 119554
BREDNA 271124
Rectome R-HSA-2559585 R-HSA-445144 R-HSA-2871796 R-HSA-111995 R-HSA-2559580 R-HSA-198753 R-HSA-56547 R-HSA-881907 R-HSA-5654733 R-HSA-5674499 R-HSA-437239 R-HSA-5654727 R-HSA-444257 R-HSA-5654726 R-HSA-982772 R-HSA-5673001 R-HSA-442742 R-HSA-2559582 R-HSA-5663213
SignaLink P28482
BindingDB P28482

  Model Performance Metrics

Fingerprint type F1_CV AUC_CV Accuracy_CV Sensitivity_CV Specificity_CV F1_test AUC_test Accuracy_test Sensitivity_test Specificity_test Download model
FP2 fingerprints 0.903 0.921 0.909 0.839 0.980 0.935 0.950 0.935 0.890 0.985 Download
MACCS fingerprints 0.847 0.916 0.848 0.839 0.857 0.866 0.923 0.865 0.839 0.894 Download
Daylight fingerprints 0.821 0.864 0.846 0.702 0.993 0.863 0.893 0.873 0.759 1.000 Download
ECFP2 fingerprints 0.876 0.931 0.883 0.821 0.945 0.915 0.971 0.916 0.855 0.985 Download
ECFP4 fingerprints 0.904 0.930 0.910 0.844 0.976 0.938 0.953 0.938 0.883 1.000 Download
ECFP6 fingerprints 0.906 0.923 0.913 0.835 0.991 0.930 0.947 0.931 0.869 1.000 Download

  Download datasets

Positive dataset Negative dataset


Copyright @ 2012-2014 Computational Biology & Drug Design Group,
School of Pharmaceutical Sciences, Central South University. All rights reserved.

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