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P63086

- MK01_RAT

UniProt

P63086 - MK01_RAT

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Protein
Mitogen-activated protein kinase 1
Gene
Mapk1, Erk2, Mapk, Prkm1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.1 Publication
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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATP
Binding sitei106 – 1061Inhibitor; via amide nitrogen and carbonyl oxygen
Active sitei147 – 1471Proton acceptor
Binding sitei164 – 1641Inhibitor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379ATP

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. MAP kinase activity Source: UniProtKB
  3. RNA polymerase II carboxy-terminal domain kinase activity Source: Ensembl
  4. kinase activity Source: RGD
  5. mitogen-activated protein kinase kinase kinase binding Source: RGD
  6. protein binding Source: RGD
  7. protein kinase binding Source: RGD
  8. protein serine/threonine kinase activity Source: MGI
  9. transcription factor binding Source: RGD

GO - Biological processi

  1. B cell receptor signaling pathway Source: Ensembl
  2. ERBB signaling pathway Source: Ensembl
  3. ERK1 and ERK2 cascade Source: Ensembl
  4. MAPK cascade Source: RGD
  5. MAPK import into nucleus Source: RGD
  6. T cell receptor signaling pathway Source: Ensembl
  7. apoptotic process Source: UniProtKB-KW
  8. caveolin-mediated endocytosis Source: UniProtKB
  9. cell cycle Source: UniProtKB-KW
  10. cellular response to DNA damage stimulus Source: Ensembl
  11. cellular response to organic substance Source: RGD
  12. cytosine metabolic process Source: Ensembl
  13. intracellular signal transduction Source: RGD
  14. labyrinthine layer blood vessel development Source: Ensembl
  15. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  16. mammary gland epithelial cell proliferation Source: Ensembl
  17. negative regulation of cell differentiation Source: Ensembl
  18. organ morphogenesis Source: Ensembl
  19. peptidyl-serine phosphorylation Source: MGI
  20. peptidyl-threonine phosphorylation Source: UniProtKB
  21. positive regulation of cell migration Source: RGD
  22. positive regulation of cell proliferation Source: RGD
  23. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
  24. positive regulation of transcription, DNA-templated Source: RGD
  25. positive regulation of translation Source: RGD
  26. protein phosphorylation Source: RGD
  27. regulation of Golgi inheritance Source: UniProtKB
  28. regulation of cytoskeleton organization Source: UniProtKB
  29. regulation of early endosome to late endosome transport Source: UniProtKB
  30. regulation of protein stability Source: UniProtKB
  31. regulation of stress-activated MAPK cascade Source: UniProtKB
  32. response to epidermal growth factor Source: UniProtKB
  33. response to estrogen Source: RGD
  34. response to exogenous dsRNA Source: Ensembl
  35. response to toxic substance Source: RGD
  36. sensory perception of pain Source: UniProtKB
  37. signal transduction Source: RGD
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.
ReactomeiREACT_194748. Senescence-Associated Secretory Phenotype (SASP).
REACT_195028. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_195202. FCERI mediated MAPK activation.
REACT_196231. Advanced glycosylation endproduct receptor signaling.
REACT_196390. RSK activation.
REACT_196391. CREB phosphorylation through the activation of Ras.
REACT_196425. Growth hormone receptor signaling.
REACT_196755. Regulation of actin dynamics for phagocytic cup formation.
REACT_198995. Negative regulation of FGFR signaling.
REACT_203770. Oxidative Stress Induced Senescence.
REACT_215142. Oncogene Induced Senescence.
REACT_216489. Regulation of HSF1-mediated heat shock response.
REACT_222166. Signaling by FGFR.

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
ProteomesiUP000002494: Chromosome 11

Organism-specific databases

RGDi70500. Mapk1.

Subcellular locationi

Cytoplasmcytoskeletonspindle By similarity. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasm By similarity
Note: Associated with the spindle during prometaphase and metaphase By similarity. PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention By similarity. Phosphorylation at Ser- 244 and Ser-246 as well as autophosphorylation at Thr-188 promote nuclear localization By similarity.

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. axon Source: RGD
  3. caveola Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytoskeleton Source: UniProtKB
  6. cytosol Source: UniProtKB
  7. dendrite cytoplasm Source: RGD
  8. early endosome Source: UniProtKB
  9. focal adhesion Source: UniProtKB
  10. late endosome Source: UniProtKB
  11. microtubule organizing center Source: UniProtKB-SubCell
  12. mitochondrion Source: UniProtKB
  13. mitotic spindle Source: UniProtKB
  14. nucleoplasm Source: UniProtKB
  15. nucleus Source: UniProtKB
  16. perikaryon Source: RGD
  17. protein complex Source: RGD
  18. pseudopodium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171Q → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-123. 1 Publication
Mutagenesisi123 – 1231H → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-117. 1 Publication
Mutagenesisi155 – 1551L → A: Reduced affinity for DCC. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 358357Mitogen-activated protein kinase 1
PRO_0000186249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei27 – 271Phosphoserine; by SGK1 By similarity
Modified residuei183 – 1831Phosphothreonine; by MAP2K1 and MAP2K2 By similarity
Modified residuei185 – 1851Phosphotyrosine; by MAP2K1 and MAP2K2 By similarity
Modified residuei188 – 1881Phosphothreonine; by autocatalysis By similarity
Modified residuei244 – 2441Phosphoserine By similarity
Modified residuei246 – 2461Phosphoserine By similarity
Modified residuei282 – 2821Phosphoserine By similarity

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.2 Publications
ISGylated By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP63086.
PRIDEiP63086.

2D gel databases

World-2DPAGE0004:P63086.

PTM databases

PhosphoSiteiP63086.

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

GenevestigatoriP63086.

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.5 Publications

Protein-protein interaction databases

BioGridi250505. 12 interactions.
DIPiDIP-29117N.
IntActiP63086. 6 interactions.
MINTiMINT-100037.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123
Beta strandi13 – 164
Turni20 – 223
Beta strandi23 – 319
Beta strandi33 – 4210
Turni43 – 464
Beta strandi47 – 548
Helixi56 – 583
Helixi60 – 7516
Beta strandi86 – 883
Turni93 – 953
Beta strandi99 – 1046
Beta strandi107 – 1093
Helixi110 – 1167
Helixi121 – 14020
Helixi150 – 1523
Beta strandi153 – 1553
Beta strandi161 – 1633
Beta strandi170 – 1723
Helixi174 – 1763
Turni179 – 1813
Helixi182 – 1843
Helixi189 – 1913
Helixi194 – 1985
Beta strandi199 – 2013
Helixi206 – 22116
Helixi231 – 2333
Helixi234 – 2429
Helixi247 – 2515
Helixi256 – 2638
Helixi273 – 2764
Beta strandi278 – 2803
Helixi282 – 29110
Turni296 – 2983
Helixi302 – 3065
Helixi309 – 3113
Turni312 – 3143
Helixi317 – 3193
Helixi329 – 3313
Helixi333 – 3353
Helixi338 – 34811
Helixi350 – 3523
Helixi354 – 3563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3QYIX-ray2.18A1-358[»]
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[»]
ProteinModelPortaliP63086.
SMRiP63086. Positions 10-353.

Miscellaneous databases

EvolutionaryTraceiP63086.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 311289Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 1097Inhibitor-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 76Poly-Ala

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP63086.
KOiK04371.
OMAiVCSAYDR.
OrthoDBiEOG7M3J0K.
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.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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

MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA    50
IKKISPFEHQ TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY 100
IVQDLMETDL YKLLKTQHLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP 150
SNLLLNTTCD LKICDFGLAR VADPDHDHTG FLTEYVATRW YRAPEIMLNS 200
KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG ILGSPSQEDL 250
NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI 300
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA 350
RFQPGYRS 358
Length:358
Mass (Da):41,276
Last modified:January 23, 2007 - v3
Checksum:i3BBCF22471EDBA0B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64300 mRNA. Translation: AAA41124.1.
PIRiA40033.
RefSeqiNP_446294.1. NM_053842.1.
XP_006248720.1. XM_006248658.1.
XP_006248721.1. XM_006248659.1.
XP_006248722.1. XM_006248660.1.
UniGeneiRn.34914.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64300 mRNA. Translation: AAA41124.1 .
PIRi A40033.
RefSeqi NP_446294.1. NM_053842.1.
XP_006248720.1. XM_006248658.1.
XP_006248721.1. XM_006248659.1.
XP_006248722.1. XM_006248660.1.
UniGenei Rn.34914.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ERK X-ray 2.30 A 1-358 [» ]
1GOL X-ray 2.80 A 1-358 [» ]
2ERK X-ray 2.40 A 1-358 [» ]
2FYS X-ray 2.50 A/B 2-358 [» ]
2GPH X-ray 1.90 A 2-358 [» ]
2Z7L X-ray 2.41 A 1-358 [» ]
3C9W X-ray 2.50 A/B 2-358 [» ]
3ERK X-ray 2.10 A 1-358 [» ]
3O71 X-ray 1.95 A 1-358 [» ]
3QYI X-ray 2.18 A 1-358 [» ]
3QYW X-ray 1.50 A 1-358 [» ]
3QYZ X-ray 1.46 A 1-358 [» ]
3R63 X-ray 1.70 A 1-358 [» ]
3ZU7 X-ray 1.97 A 3-358 [» ]
3ZUV X-ray 2.72 A/C 3-358 [» ]
4ERK X-ray 2.20 A 1-358 [» ]
4GSB X-ray 1.80 A 1-358 [» ]
4GT3 X-ray 1.68 A 1-358 [» ]
4GVA X-ray 1.83 A 1-358 [» ]
4I5H X-ray 1.90 A 2-358 [» ]
4N4S X-ray 2.20 A/B 2-358 [» ]
ProteinModelPortali P63086.
SMRi P63086. Positions 10-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250505. 12 interactions.
DIPi DIP-29117N.
IntActi P63086. 6 interactions.
MINTi MINT-100037.

Chemistry

BindingDBi P63086.
ChEMBLi CHEMBL2111356.

PTM databases

PhosphoSitei P63086.

2D gel databases

World-2DPAGE 0004:P63086.

Proteomic databases

PaxDbi P63086.
PRIDEi P63086.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000002533 ; ENSRNOP00000002533 ; ENSRNOG00000001849 .
GeneIDi 116590.
KEGGi rno:116590.

Organism-specific databases

CTDi 5594.
RGDi 70500. Mapk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074298.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P63086.
KOi K04371.
OMAi VCSAYDR.
OrthoDBi EOG7M3J0K.
PhylomeDBi P63086.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 5301.
Reactomei REACT_194748. Senescence-Associated Secretory Phenotype (SASP).
REACT_195028. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_195202. FCERI mediated MAPK activation.
REACT_196231. Advanced glycosylation endproduct receptor signaling.
REACT_196390. RSK activation.
REACT_196391. CREB phosphorylation through the activation of Ras.
REACT_196425. Growth hormone receptor signaling.
REACT_196755. Regulation of actin dynamics for phagocytic cup formation.
REACT_198995. Negative regulation of FGFR signaling.
REACT_203770. Oxidative Stress Induced Senescence.
REACT_215142. Oncogene Induced Senescence.
REACT_216489. Regulation of HSF1-mediated heat shock response.
REACT_222166. Signaling by FGFR.

Miscellaneous databases

EvolutionaryTracei P63086.
NextBioi 304409.
PROi P63086.

Gene expression databases

Genevestigatori P63086.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01770. ERK1ERK2MAPK.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF."
    Boulton T.G., Nye S.H., Robbins D.J., Ip N.Y., Radziejewska E., Morgenbesser S.D., DePinho R.A., Panayotatos N., Cobb M.H., Yancopoulos G.D.
    Cell 65:663-675(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Bienvenut W.V., von Kriegsheim A.F., Kolch W.
    Submitted (AUG-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 69-75; 137-170; 193-201 AND 341-351, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Pheochromocytoma.
  3. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 163-170, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation."
    Seger R., Ahn N.G., Boulton T.G., Yancopoulos G.D., Panayotatos N., Radziejewska E., Ericsson L., Bratlien R.L., Cobb M.H., Krebs E.G.
    Proc. Natl. Acad. Sci. U.S.A. 88:6142-6146(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  5. "PHAS-I as a link between mitogen-activated protein kinase and translation initiation."
    Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J., Sonenberg N., Lawrence J.C. Jr.
    Science 266:653-656(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF EIF4EBP1.
  6. "Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds."
    Luttrell L.M., Roudabush F.L., Choy E.W., Miller W.E., Field M.E., Pierce K.L., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:2449-2454(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  7. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Identification of pY19-caveolin-2 as a positive regulator of insulin-stimulated actin cytoskeleton-dependent mitogenesis."
    Kwon H., Jeong K., Pak Y.
    J. Cell. Mol. Med. 13:1549-1564(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  9. "Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin."
    Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S., Pak Y.
    Biochim. Biophys. Acta 1793:1325-1333(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  10. "The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions."
    Yoon S., Seger R.
    Growth Factors 24:21-44(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. "The ERK signaling cascade--views from different subcellular compartments."
    Yao Z., Seger R.
    BioFactors 35:407-416(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, REVIEW ON SUBCELLULAR LOCATION.
  12. "The ERK cascade: distinct functions within various subcellular organelles."
    Wortzel I., Seger R.
    Genes Cancer 2:195-209(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  13. "Atomic structure of the MAP kinase ERK2 at 2.3-A resolution."
    Zhang F., Strand A., Robbins D., Cobb M.H., Goldsmith E.J.
    Nature 367:704-710(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  14. "Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5'-triphosphate."
    Robinson M.J., Harkins P.C., Zhang J., Baer R., Haycock J.W., Cobb M.H., Goldsmith E.J.
    Biochemistry 35:5641-5646(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP.
  15. "Activation mechanism of the MAP kinase ERK2 by dual phosphorylation."
    Canagarajah B.J., Khokhlatchev A., Cobb M.H., Goldsmith E.J.
    Cell 90:859-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  17. "Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3."
    Liu S., Sun J.P., Zhou B., Zhang Z.Y.
    Proc. Natl. Acad. Sci. U.S.A. 103:5326-5331(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-357, INTERACTION WITH DUSP6.
  18. "Docking interactions induce exposure of activation loop in the MAP kinase ERK2."
    Zhou T., Sun L., Humphreys J., Goldsmith E.J.
    Structure 14:1011-1019(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-357.
  19. "Molecular modeling and crystal structure of ERK2-hypothemycin complexes."
    Rastelli G., Rosenfeld R., Reid R., Santi D.V.
    J. Struct. Biol. 164:18-23(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-358 IN COMPLEX WITH INHIBITOR.
  20. "Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors."
    Katayama N., Orita M., Yamaguchi T., Hisamichi H., Kuromitsu S., Kurihara H., Sakashita H., Matsumoto Y., Fujita S., Niimi T.
    Proteins 73:795-801(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  21. "Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase."
    Ma W., Shang Y., Wei Z., Wen W., Wang W., Zhang M.
    Structure 18:1502-1511(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH DCC, FUNCTION IN PHOSPHORYLATION OF DCC, INTERACTION WITH DCC, MUTAGENESIS OF GLN-117; HIS-123 AND LEU-155.

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: September 3, 2014
This is version 125 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

External Data

Dasty 3

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