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P63086 (MK01_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1

Short name=MAP kinase 1
Short name=MAPK 1
EC=2.7.11.24
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 names
Name:Mapk1
Synonyms:Erk2, Mapk, Prkm1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. Ref.21

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. Ref.21

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

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.

Subunit structure

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 1of 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 1binding prevents from dephosphorylation and inactivation By similarity. Interacts with DCC. The phosphorylated form interacts with PML By similarity. Ref.6 Ref.8 Ref.9 Ref.17 Ref.21

Subcellular location

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.

Tissue specificity

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

Developmental stage

Increased expression during development.

Domain

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

Post-translational modification

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. Ref.4 Ref.5

ISGylated By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

ERBB signaling pathway

Inferred from electronic annotation. Source: Ensembl

ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

MAPK cascade

Inferred from mutant phenotype PubMed 17310240. Source: RGD

MAPK import into nucleus

Inferred from direct assay PubMed 12097495. Source: RGD

T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

caveolin-mediated endocytosis

Traceable author statement Ref.11. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to organic substance

Inferred from direct assay PubMed 12487375. Source: RGD

cytosine metabolic process

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from direct assay PubMed 12072413. Source: RGD

labyrinthine layer blood vessel development

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell differentiation

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 7768935. Source: MGI

peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from expression pattern PubMed 15917991. Source: RGD

positive regulation of cell proliferation

Inferred from expression pattern PubMed 15583728. Source: RGD

positive regulation of peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from expression pattern PubMed 12097495. Source: RGD

positive regulation of translation

Inferred from mutant phenotype PubMed 15027896. Source: RGD

protein phosphorylation

Inferred from direct assay PubMed 15027896. Source: RGD

regulation of Golgi inheritance

Traceable author statement Ref.11. Source: UniProtKB

regulation of cytoskeleton organization

Traceable author statement Ref.11. Source: UniProtKB

regulation of early endosome to late endosome transport

Traceable author statement Ref.11. Source: UniProtKB

regulation of protein stability

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of stress-activated MAPK cascade

Traceable author statement Ref.11. Source: UniProtKB

response to epidermal growth factor

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from direct assay PubMed 11751611. Source: RGD

response to exogenous dsRNA

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from direct assay PubMed 17651772. Source: RGD

sensory perception of pain

Inferred from mutant phenotype PubMed 11356865. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 11714707. Source: RGD

   Cellular_componentGolgi apparatus

Traceable author statement Ref.11. Source: UniProtKB

axon

Inferred from direct assay PubMed 9714150. Source: RGD

caveola

Traceable author statement Ref.11. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Traceable author statement Ref.11. Source: UniProtKB

cytosol

Traceable author statement Ref.11. Source: UniProtKB

dendrite cytoplasm

Inferred from direct assay PubMed 9714150. Source: RGD

early endosome

Traceable author statement Ref.11. Source: UniProtKB

focal adhesion

Traceable author statement Ref.11. Source: UniProtKB

late endosome

Traceable author statement Ref.11. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Traceable author statement Ref.11. Source: UniProtKB

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 7889942. Source: UniProtKB

nucleus

Traceable author statement Ref.11. Source: UniProtKB

perikaryon

Inferred from direct assay PubMed 9714150. Source: RGD

protein complex

Inferred from direct assay PubMed 15781236. Source: RGD

pseudopodium

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay PubMed 15027896. Source: RGD

MAP kinase activity

Inferred from direct assay PubMed 7889942. Source: UniProtKB

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: Ensembl

kinase activity

Traceable author statement PubMed 11687663. Source: RGD

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction PubMed 12049732. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 16943189. Source: RGD

protein serine/threonine kinase activity

Inferred from direct assay PubMed 7768935. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 10363932. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 358357Mitogen-activated protein kinase 1
PRO_0000186249

Regions

Domain23 – 311289Protein kinase
Nucleotide binding29 – 379ATP
Region103 – 1097Inhibitor-binding
Motif183 – 1853TXY
Compositional bias2 – 76Poly-Ala

Sites

Active site1471Proton acceptor
Binding site521ATP
Binding site1061Inhibitor; via amide nitrogen and carbonyl oxygen
Binding site1641Inhibitor

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue271Phosphoserine; by SGK1 By similarity
Modified residue1831Phosphothreonine; by MAP2K1 and MAP2K2 By similarity
Modified residue1851Phosphotyrosine; by MAP2K1 and MAP2K2 By similarity
Modified residue1881Phosphothreonine; by autocatalysis By similarity
Modified residue2441Phosphoserine By similarity
Modified residue2461Phosphoserine By similarity
Modified residue2821Phosphoserine By similarity

Experimental info

Mutagenesis1171Q → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-123. Ref.21
Mutagenesis1231H → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-117. Ref.21
Mutagenesis1551L → A: Reduced affinity for DCC. Ref.21

Secondary structure

............................................................................ 358
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63086 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3BBCF22471EDBA0B

FASTA35841,276
        10         20         30         40         50         60 
MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA IKKISPFEHQ 

        70         80         90        100        110        120 
TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY IVQDLMETDL YKLLKTQHLS 

       130        140        150        160        170        180 
NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNTTCD LKICDFGLAR VADPDHDHTG 

       190        200        210        220        230        240 
FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG 

       250        260        270        280        290        300 
ILGSPSQEDL NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI 

       310        320        330        340        350 
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA RFQPGYRS 

« Hide

References

« Hide 'large scale' references
[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]"Structural basis of inhibitor selectivity in MAP kinases."
Wang Z., Canagarajah B.J., Boehm J.C., Kassisa S., Cobb M.H., Young P.R., Abdel-Meguid S., Adams J.L., Goldsmith E.J.
Structure 6:1117-1128(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64300 mRNA. Translation: AAA41124.1.
PIRA40033.
RefSeqNP_446294.1. NM_053842.1.
XP_006248720.1. XM_006248658.1.
XP_006248721.1. XM_006248659.1.
XP_006248722.1. XM_006248660.1.
UniGeneRn.34914.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ERKX-ray2.30A1-358[»]
1GOLX-ray2.80A1-358[»]
2ERKX-ray2.40A1-358[»]
2FYSX-ray2.50A/B2-357[»]
2GPHX-ray1.90A2-357[»]
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[»]
ProteinModelPortalP63086.
SMRP63086. Positions 10-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250505. 12 interactions.
DIPDIP-29117N.
IntActP63086. 5 interactions.
MINTMINT-100037.

Chemistry

BindingDBP63086.
ChEMBLCHEMBL2111356.

PTM databases

PhosphoSiteP63086.

2D gel databases

World-2DPAGE0004:P63086.

Proteomic databases

PaxDbP63086.
PRIDEP63086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002533; ENSRNOP00000002533; ENSRNOG00000001849.
GeneID116590.
KEGGrno:116590.

Organism-specific databases

CTD5594.
RGD70500. Mapk1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP63086.
KOK04371.
OMAVCSAYDR.
OrthoDBEOG7M3J0K.
PhylomeDBP63086.

Enzyme and pathway databases

BRENDA2.7.11.24. 5301.
ReactomeREACT_109458. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_195021. Developmental Biology.

Gene expression databases

GenevestigatorP63086.

Family and domain databases

InterProIPR011009. 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]
PANTHERPTHR24055:SF111. PTHR24055:SF111. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01770. ERK1ERK2MAPK.
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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63086.
NextBio304409.
PROP63086.

Entry information

Entry nameMK01_RAT
AccessionPrimary (citable) accession number: P63086
Secondary accession number(s): P27703
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references