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Protein

Mitogen-activated protein kinase 1

Gene

Mapk1

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. 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 (By similarity).By similarity
Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] consensus sequence. Repress the expression of interferon gamma-induced genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity is independent of kinase activity (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-183 and Tyr-185 in response to external stimuli like insulin or NGF. Both phosphorylations are required for activity. This phosphorylation causes dramatic conformational changes, which enable full activation and interaction of MAPK1/ERK2 with its substrates. Phosphorylation on Ser-27 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52ATPPROSITE-ProRule annotation1 Publication1
Binding sitei106Inhibitor; via amide nitrogen and carbonyl oxygen3 Publications1
Active sitei147Proton acceptor1
Binding sitei164Inhibitor3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi29 – 37ATPPROSITE-ProRule annotation1 Publication9

GO - Molecular functioni

  • ATP binding Source: RGD
  • kinase activity Source: RGD
  • MAP kinase activity Source: UniProtKB
  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • protein kinase binding Source: RGD
  • protein serine/threonine kinase activity Source: MGI
  • RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl
  • transcription factor binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 5301.
ReactomeiR-RNO-111995. phospho-PLA2 pathway.
R-RNO-112409. RAF-independent MAPK1/3 activation.
R-RNO-112411. MAPK1 (ERK2) activation.
R-RNO-1295596. Spry regulation of FGF signaling.
R-RNO-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-RNO-198753. ERK/MAPK targets.
R-RNO-202670. ERKs are inactivated.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-RNO-2559585. Oncogene Induced Senescence.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-375165. NCAM signaling for neurite out-growth.
R-RNO-437239. Recycling pathway of L1.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-444257. RSK activation.
R-RNO-445144. Signal transduction by L1.
R-RNO-450341. Activation of the AP-1 family of transcription factors.
R-RNO-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-RNO-5654726. Negative regulation of FGFR1 signaling.
R-RNO-5654727. Negative regulation of FGFR2 signaling.
R-RNO-5654732. Negative regulation of FGFR3 signaling.
R-RNO-5654733. Negative regulation of FGFR4 signaling.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-5674135. MAP2K and MAPK activation.
R-RNO-5674499. Negative feedback regulation of MAPK pathway.
R-RNO-5675221. Negative regulation of MAPK pathway.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-RNO-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
R-RNO-982772. Growth hormone receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 1 (EC:2.7.11.24)
Short name:
MAP kinase 1
Short name:
MAPK 1
Alternative name(s):
ERT1
Extracellular signal-regulated kinase 2
Short name:
ERK-2
MAP kinase isoform p42
Short name:
p42-MAPK
Mitogen-activated protein kinase 2
Short name:
MAP kinase 2
Short name:
MAPK 2
Gene namesi
Name:Mapk1
Synonyms:Erk2, Mapk, Prkm1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi70500. Mapk1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • caveola Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: RGD
  • early endosome Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • late endosome Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: RGD
  • protein complex Source: RGD
  • pseudopodium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117Q → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-123. 1 Publication1
Mutagenesisi123H → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-117. 1 Publication1
Mutagenesisi155L → A: Reduced affinity for DCC. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001862492 – 358Mitogen-activated protein kinase 1Add BLAST357

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei27Phosphoserine; by SGK1By similarity1
Modified residuei179PhosphothreonineBy similarity1
Modified residuei183PhosphothreonineCombined sources1
Modified residuei185PhosphotyrosineCombined sources1
Modified residuei188Phosphothreonine; by autocatalysisBy similarity1
Modified residuei244PhosphoserineBy similarity1
Modified residuei246PhosphoserineBy similarity1
Modified residuei282PhosphoserineBy similarity1

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme. Phosphorylated upon FLT3 and KIT signaling. Ligand-activated ALK induces tyrosine phosphorylation (By similarity). Dephosphorylated by PTPRJ at Tyr-185 (By similarity). Autophosphorylated on threonine and tyrosine residues in vitro, which correlates with a slow and low level of activation. Phosphorylation on Ser-27 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2 (By similarity).By similarity
ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP63086.
PRIDEiP63086.

2D gel databases

World-2DPAGE0004:P63086.

PTM databases

iPTMnetiP63086.
PhosphoSitePlusiP63086.

Expressioni

Tissue specificityi

Highest levels within the nervous system, expressed in different tissues, mostly in muscle, thymus and heart.

Developmental stagei

Increased expression during development.

Gene expression databases

BgeeiENSRNOG00000001849.
GenevisibleiP63086. RN.

Interactioni

Subunit structurei

Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, MKNK2, DUSP6, MORG1, NISCH, PEA15, SGK1, and isoform 1 of NEK2 (By similarity). Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation (By similarity). MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation (By similarity). Interacts with DCC. The phosphorylated form interacts with PML (By similarity). Interacts with STYX (By similarity).By similarity

GO - Molecular functioni

  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • protein kinase binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi250505. 12 interactors.
DIPiDIP-29117N.
IntActiP63086. 6 interactors.
MINTiMINT-100037.
STRINGi10116.ENSRNOP00000002533.

Chemistry databases

BindingDBiP63086.

Structurei

Secondary structure

1358
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 17Combined sources8
Turni20 – 22Combined sources3
Beta strandi23 – 31Combined sources9
Beta strandi33 – 42Combined sources10
Turni43 – 46Combined sources4
Beta strandi47 – 54Combined sources8
Beta strandi57 – 59Combined sources3
Helixi60 – 75Combined sources16
Beta strandi86 – 88Combined sources3
Turni93 – 95Combined sources3
Beta strandi99 – 104Combined sources6
Beta strandi107 – 109Combined sources3
Helixi110 – 116Combined sources7
Helixi121 – 140Combined sources20
Helixi150 – 152Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi161 – 163Combined sources3
Beta strandi170 – 172Combined sources3
Helixi174 – 176Combined sources3
Turni179 – 181Combined sources3
Helixi182 – 184Combined sources3
Helixi189 – 191Combined sources3
Helixi194 – 196Combined sources3
Turni197 – 199Combined sources3
Helixi206 – 221Combined sources16
Helixi231 – 242Combined sources12
Helixi247 – 251Combined sources5
Helixi256 – 264Combined sources9
Helixi273 – 276Combined sources4
Beta strandi278 – 280Combined sources3
Helixi282 – 291Combined sources10
Turni296 – 298Combined sources3
Helixi302 – 306Combined sources5
Helixi309 – 311Combined sources3
Turni312 – 314Combined sources3
Helixi317 – 319Combined sources3
Helixi329 – 331Combined sources3
Beta strandi333 – 336Combined sources4
Helixi338 – 348Combined sources11
Helixi350 – 352Combined sources3
Helixi354 – 356Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ERKX-ray2.30A1-358[»]
1GOLX-ray2.80A1-358[»]
2ERKX-ray2.40A1-358[»]
2FYSX-ray2.50A/B2-358[»]
2GPHX-ray1.90A2-358[»]
2Z7LX-ray2.41A1-358[»]
3C9WX-ray2.50A/B2-358[»]
3ERKX-ray2.10A1-358[»]
3O71X-ray1.95A1-358[»]
3QYWX-ray1.50A1-358[»]
3QYZX-ray1.46A1-358[»]
3R63X-ray1.70A1-358[»]
3ZU7X-ray1.97A3-358[»]
3ZUVX-ray2.72A/C3-358[»]
4ERKX-ray2.20A1-358[»]
4GSBX-ray1.80A1-358[»]
4GT3X-ray1.68A1-358[»]
4GVAX-ray1.83A1-358[»]
4I5HX-ray1.90A2-358[»]
4N4SX-ray2.20A/B2-358[»]
4QYYX-ray1.65A1-358[»]
4S2ZX-ray1.48A1-358[»]
4S30X-ray2.00A1-358[»]
4S31X-ray1.45A1-358[»]
4S32X-ray1.34A1-358[»]
4S33X-ray1.48A1-358[»]
4S34X-ray2.50A1-358[»]
4XNEX-ray1.80A9-354[»]
4XOYX-ray2.10A8-358[»]
4XOZX-ray1.95A8-358[»]
4XP0X-ray1.46A8-358[»]
4XP2X-ray1.75A8-358[»]
4XP3X-ray1.78A8-358[»]
4XRJX-ray1.69A9-354[»]
4XRLX-ray2.55A9-353[»]
5HD4X-ray1.45A1-358[»]
5HD7X-ray1.69A1-358[»]
5KE0X-ray1.68A1-358[»]
ProteinModelPortaliP63086.
SMRiP63086.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63086.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 311Protein kinasePROSITE-ProRule annotationAdd BLAST289

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 109Inhibitor-binding7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi183 – 185TXY3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 7Poly-Ala6

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

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP63086.
KOiK04371.
OMAiEEAESHH.
OrthoDBiEOG091G08QL.
PhylomeDBiP63086.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01770. ERK1ERK2MAPK.
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA
60 70 80 90 100
IKKISPFEHQ TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY
110 120 130 140 150
IVQDLMETDL YKLLKTQHLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP
160 170 180 190 200
SNLLLNTTCD LKICDFGLAR VADPDHDHTG FLTEYVATRW YRAPEIMLNS
210 220 230 240 250
KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG ILGSPSQEDL
260 270 280 290 300
NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI
310 320 330 340 350
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA

RFQPGYRS
Length:358
Mass (Da):41,276
Last modified:January 23, 2007 - v3
Checksum:i3BBCF22471EDBA0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64300 mRNA. Translation: AAA41124.1.
PIRiA40033.
RefSeqiNP_446294.1. NM_053842.2.
XP_006248720.1. XM_006248658.3.
XP_006248721.1. XM_006248659.3.
XP_008767070.1. XM_008768848.2.
UniGeneiRn.34914.

Genome annotation databases

EnsembliENSRNOT00000002533; ENSRNOP00000002533; ENSRNOG00000001849.
GeneIDi116590.
KEGGirno:116590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64300 mRNA. Translation: AAA41124.1.
PIRiA40033.
RefSeqiNP_446294.1. NM_053842.2.
XP_006248720.1. XM_006248658.3.
XP_006248721.1. XM_006248659.3.
XP_008767070.1. XM_008768848.2.
UniGeneiRn.34914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ERKX-ray2.30A1-358[»]
1GOLX-ray2.80A1-358[»]
2ERKX-ray2.40A1-358[»]
2FYSX-ray2.50A/B2-358[»]
2GPHX-ray1.90A2-358[»]
2Z7LX-ray2.41A1-358[»]
3C9WX-ray2.50A/B2-358[»]
3ERKX-ray2.10A1-358[»]
3O71X-ray1.95A1-358[»]
3QYWX-ray1.50A1-358[»]
3QYZX-ray1.46A1-358[»]
3R63X-ray1.70A1-358[»]
3ZU7X-ray1.97A3-358[»]
3ZUVX-ray2.72A/C3-358[»]
4ERKX-ray2.20A1-358[»]
4GSBX-ray1.80A1-358[»]
4GT3X-ray1.68A1-358[»]
4GVAX-ray1.83A1-358[»]
4I5HX-ray1.90A2-358[»]
4N4SX-ray2.20A/B2-358[»]
4QYYX-ray1.65A1-358[»]
4S2ZX-ray1.48A1-358[»]
4S30X-ray2.00A1-358[»]
4S31X-ray1.45A1-358[»]
4S32X-ray1.34A1-358[»]
4S33X-ray1.48A1-358[»]
4S34X-ray2.50A1-358[»]
4XNEX-ray1.80A9-354[»]
4XOYX-ray2.10A8-358[»]
4XOZX-ray1.95A8-358[»]
4XP0X-ray1.46A8-358[»]
4XP2X-ray1.75A8-358[»]
4XP3X-ray1.78A8-358[»]
4XRJX-ray1.69A9-354[»]
4XRLX-ray2.55A9-353[»]
5HD4X-ray1.45A1-358[»]
5HD7X-ray1.69A1-358[»]
5KE0X-ray1.68A1-358[»]
ProteinModelPortaliP63086.
SMRiP63086.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250505. 12 interactors.
DIPiDIP-29117N.
IntActiP63086. 6 interactors.
MINTiMINT-100037.
STRINGi10116.ENSRNOP00000002533.

Chemistry databases

BindingDBiP63086.
ChEMBLiCHEMBL5233.

PTM databases

iPTMnetiP63086.
PhosphoSitePlusiP63086.

2D gel databases

World-2DPAGE0004:P63086.

Proteomic databases

PaxDbiP63086.
PRIDEiP63086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002533; ENSRNOP00000002533; ENSRNOG00000001849.
GeneIDi116590.
KEGGirno:116590.

Organism-specific databases

CTDi5594.
RGDi70500. Mapk1.

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP63086.
KOiK04371.
OMAiEEAESHH.
OrthoDBiEOG091G08QL.
PhylomeDBiP63086.

Enzyme and pathway databases

BRENDAi2.7.11.24. 5301.
ReactomeiR-RNO-111995. phospho-PLA2 pathway.
R-RNO-112409. RAF-independent MAPK1/3 activation.
R-RNO-112411. MAPK1 (ERK2) activation.
R-RNO-1295596. Spry regulation of FGF signaling.
R-RNO-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-RNO-198753. ERK/MAPK targets.
R-RNO-202670. ERKs are inactivated.
R-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-2559580. Oxidative Stress Induced Senescence.
R-RNO-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-RNO-2559585. Oncogene Induced Senescence.
R-RNO-2871796. FCERI mediated MAPK activation.
R-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-375165. NCAM signaling for neurite out-growth.
R-RNO-437239. Recycling pathway of L1.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-444257. RSK activation.
R-RNO-445144. Signal transduction by L1.
R-RNO-450341. Activation of the AP-1 family of transcription factors.
R-RNO-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-RNO-5654726. Negative regulation of FGFR1 signaling.
R-RNO-5654727. Negative regulation of FGFR2 signaling.
R-RNO-5654732. Negative regulation of FGFR3 signaling.
R-RNO-5654733. Negative regulation of FGFR4 signaling.
R-RNO-5663213. RHO GTPases Activate WASPs and WAVEs.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-5674135. MAP2K and MAPK activation.
R-RNO-5674499. Negative feedback regulation of MAPK pathway.
R-RNO-5675221. Negative regulation of MAPK pathway.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-RNO-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
R-RNO-982772. Growth hormone receptor signaling.

Miscellaneous databases

EvolutionaryTraceiP63086.
PROiP63086.

Gene expression databases

BgeeiENSRNOG00000001849.
GenevisibleiP63086. RN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01770. ERK1ERK2MAPK.
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMK01_RAT
AccessioniPrimary (citable) accession number: P63086
Secondary accession number(s): P27703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.