Mitogen-activated protein kinase 1 - Rattus norvegicus (Rat)

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P63086 (MK01_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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. Ref.6 Ref.8 Ref.9 Ref.17 Ref.21
Subcellular location	Cytoplasm › cytoskeleton › spindle By similarity. Nucleus By similarity. Cytoplasm › cytoskeleton › centrosome 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
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 process	Apoptosis Cell cycle
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from electronic annotation. Source: Compara ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara MAPK import into nucleus Inferred from direct assay PubMed 12097495. Source: RGD T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara 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 cytosine metabolic process Inferred from electronic annotation. Source: Compara labyrinthine layer blood vessel development Inferred from electronic annotation. Source: Compara lipopolysaccharide-mediated signaling pathway Inferred from electronic annotation. Source: Compara mammary gland epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of cell differentiation Inferred from electronic annotation. Source: Compara organ morphogenesis Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from direct assay PubMed 7768935. Source: MGI 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: Compara positive regulation of transcription, DNA-dependent Inferred from expression pattern PubMed 12097495. Source: RGD positive regulation of translation Inferred from mutant phenotype 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 stress-activated MAPK cascade Traceable author statement Ref.11. Source: UniProtKB response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to epidermal growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB response to estrogen stimulus Inferred from direct assay PubMed 11751611. Source: RGD response to exogenous dsRNA Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from direct assay PubMed 17651772. Source: RGD sensory perception of pain Inferred from mutant phenotype PubMed 11356865. Source: UniProtKB
Cellular_component	Golgi apparatus Traceable author statement Ref.11. Source: UniProtKB axon part Inferred from direct assay PubMed 9714150. Source: RGD caveola Traceable author statement Ref.11. 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 nucleoplasm Inferred from direct assay PubMed 7889942. 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: Compara spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 358

357

Mitogen-activated protein kinase 1

PRO_0000186249

Regions

Domain

23 – 311

289

Protein kinase

Nucleotide binding

29 – 37

ATP

Region

103 – 109

Inhibitor-binding

Motif

183 – 185

TXY

Compositional bias

2 – 7

Poly-Ala

Sites

Active site

147

Proton acceptor

Binding site

ATP

Binding site

106

Inhibitor; via amide nitrogen and carbonyl oxygen

Binding site

164

Inhibitor

Amino acid modifications

Modified residue

N-acetylalanine Ref.2

Modified residue

Phosphoserine; by SGK1 By similarity

Modified residue

183

Phosphothreonine; by MAP2K1 and MAP2K2 By similarity

Modified residue

185

Phosphotyrosine; by MAP2K1 and MAP2K2 By similarity

Modified residue

188

Phosphothreonine; by autocatalysis Ref.7

Modified residue

244

Phosphoserine By similarity

Modified residue

246

Phosphoserine By similarity

Modified residue

282

Phosphoserine By similarity

Experimental info

Mutagenesis

117

Q → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-123. Ref.21

Mutagenesis

123

H → A: Reduced affinity for DCC. Strongly reduced affinity for DCC; when associated with A-117. Ref.21

Mutagenesis

155

L → A: Reduced affinity for DCC. Ref.21

Secondary structure

358

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P63086 [UniParc].

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

358

41,276

        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' referencesShow '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, MASS SPECTROMETRY. Tissue: Pheochromocytoma.
[3]	Lubec G., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 163-170, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183; TYR-185 AND THR-188, MASS SPECTROMETRY. Tissue: Renal collecting duct.
[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.

IPI

IPI00199688.

PIR

A40033.

RefSeq

NP_446294.1. NM_053842.1.

UniGene

Rn.34914.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-357	[»]
2GPH	X-ray	1.90	A	2-357	[»]
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	[»]

ProteinModelPortal

P63086.

SMR

P63086. Positions 10-353.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29117N.

IntAct

P63086. 2 interactions.

MINT

MINT-100037.

PTM databases

PhosphoSite

P63086.

2D gel databases

World-2DPAGE

0004:P63086.

Proteomic databases

PaxDb

P63086.

PRIDE

P63086.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000002533; ENSRNOP00000002533; ENSRNOG00000001849.

GeneID

116590.

KEGG

rno:116590.

Organism-specific databases

CTD

5594.

RGD

70500. Mapk1.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00550000074298.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

P63086.

K04371.

OrthoDB

EOG45HRXM.

Enzyme and pathway databases

BRENDA

2.7.11.24. 5301.

Reactome

REACT_109781. Immune System.
REACT_110573. Disease.
REACT_111984. Signal Transduction.
REACT_79619. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_96538. Developmental Biology.

Gene expression databases

ArrayExpress

P63086.

Genevestigator

P63086.

GermOnline

ENSRNOG00000001849. Rattus norvegicus.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01770. ERK1ERK2MAPK.

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P63086.

ChEMBL

CHEMBL5233.

EvolutionaryTrace

P63086.

NextBio

304409.

Entry information

Entry name

MK01_RAT

Accession

Primary (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:	May 29, 2013
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents