P28482 (MK01_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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, PRKM1, PRKM2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	360 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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.39 Ref.41 Ref.42 Ref.53 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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.39 Ref.41 Ref.42 Ref.53
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-185 and Tyr-187 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-29 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. Ref.18 Ref.46
Subunit structure	Binds both upstream activators and downstream substrates in multimolecular complexes. Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine-kinase activity. Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with MORG1, PEA15 and MKNK2 By similarity. MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation By similarity. Interacts with DCC By similarity. The phosphorylated form interacts with PML (isoform PML-4). Ref.8 Ref.12 Ref.18 Ref.19 Ref.23 Ref.28 Ref.32 Ref.33 Ref.35 Ref.36 Ref.38 Ref.39 Ref.44 Ref.46 Ref.53
Subcellular location	Cytoplasm › cytoskeleton › spindle By similarity. Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm. Note: Associated with the spindle during prometaphase and metaphase By similarity. PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention. Phosphorylation at Ser-246 and Ser-248 as well as autophosphorylation at Thr-190 promote nuclear localization. Ref.23 Ref.28 Ref.38 Ref.46
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Phosphorylated upon KIT and FLT3 signaling By similarity. Dually phosphorylated on Thr-185 and Tyr-187, which activates the enzyme. Undergoes regulatory phosphorylation on additional residues such as Ser-246 and Ser-248 in the kinase insert domain (KID) These phosphorylations, which are probably mediated by more than one kinase, are important for binding of MAPK1/ERK2 to importin-7 (IPO7) and its nuclear translocation. In addition, autophosphorylation of Thr-190 was shown to affect the subcellular localization of MAPK1/ERK2 as well. Ligand-activated ALK induces tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-187. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. DUSP3 and DUSP6 dephosphorylate specifically MAPK1/ERK2 and MAPK3/ERK1 whereas DUSP9 dephosphorylates a broader range of MAPKs. Ref.13 Ref.34 Ref.38 Ref.42 Ref.43 Ref.44 Ref.46 Ref.60
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence CAA77753.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Kinase Repressor 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 direct assay PubMed 16314496. Source: UniProtKB Fc-gamma receptor signaling pathway involved in phagocytosis Traceable author statement. Source: Reactome JAK-STAT cascade involved in growth hormone signaling pathway Traceable author statement. Source: Reactome MAPK import into nucleus Inferred from electronic annotation. Source: Compara MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Ras protein signal transduction Traceable author statement. Source: Reactome T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome activation of MAPK activity Traceable author statement. Source: Reactome activation of MAPKK activity Traceable author statement. Source: Reactome apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axon guidance Traceable author statement. Source: Reactome caveolin-mediated endocytosis Traceable author statement Ref.48. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytosine metabolic process Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome induction of apoptosis Traceable author statement PubMed 10958679. Source: ProtInc innate immune response Traceable author statement. Source: Reactome insulin receptor signaling pathway Traceable author statement. Source: Reactome 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 neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome organ morphogenesis Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from direct assay PubMed 15850461. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-threonine phosphorylation Inferred from direct assay PubMed 16314496. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of translation Inferred from electronic annotation. Source: Compara regulation of Golgi inheritance Traceable author statement Ref.48. Source: UniProtKB regulation of cytoskeleton organization Traceable author statement Ref.48. Source: UniProtKB regulation of early endosome to late endosome transport Traceable author statement Ref.48. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome regulation of stress-activated MAPK cascade Traceable author statement Ref.48. Source: UniProtKB response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to epidermal growth factor stimulus Inferred from direct assay Ref.39. Source: UniProtKB response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to exogenous dsRNA Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara stress-activated MAPK cascade Traceable author statement. Source: Reactome synaptic transmission Traceable author statement. Source: Reactome toll-like receptor 10 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 5 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 9 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR1:TLR2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR6:TLR2 signaling pathway Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Traceable author statement Ref.48. Source: UniProtKB axon part Inferred from electronic annotation. Source: Compara caveola Traceable author statement Ref.48. Source: UniProtKB cytosol Traceable author statement Ref.48. Source: UniProtKB dendrite cytoplasm Inferred from electronic annotation. Source: Compara early endosome Traceable author statement Ref.48. Source: UniProtKB focal adhesion Traceable author statement Ref.48. Source: UniProtKB late endosome Traceable author statement Ref.48. Source: UniProtKB microtubule cytoskeleton Inferred from direct assay. Source: HPA microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Traceable author statement Ref.48. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome perikaryon Inferred from electronic annotation. Source: Compara pseudopodium Inferred from electronic annotation. Source: Compara spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Traceable author statement PubMed 10706854. Source: ProtInc RNA polymerase II carboxy-terminal domain kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DUSP1	P28562	3	EBI-959949,EBI-975493

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 360

359

Mitogen-activated protein kinase 1

PRO_0000186247

Regions

Domain

25 – 313

289

Protein kinase

Nucleotide binding

31 – 39

9

ATP By similarity

DNA binding

259 – 277

19

Ref.41

Region

105 – 108

4

Inhibitor-binding

Region

153 – 154

2

Inhibitor-binding

Motif

185 – 187

3

TXY

Motif

318 – 322

5

Cytoplasmic retention motif

Motif

327 – 333

7

Nuclear translocation motif

Compositional bias

2 – 9

8

Poly-Ala

Sites

Active site

149

1

Proton acceptor By similarity

Binding site

54

1

ATP By similarity

Binding site

54

1

Inhibitor

Binding site

108

1

Inhibitor; via amide nitrogen and carbonyl oxygen

Binding site

114

1

Inhibitor

Binding site

154

1

Inhibitor

Binding site

166

1

Inhibitor

Binding site

167

1

Inhibitor

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Modified residue

29

1

Phosphoserine; by SGK1 Ref.44

Modified residue

185

1

Phosphothreonine; by MAP2K1 and MAP2K2 Ref.40 Ref.49 Ref.54

Modified residue

187

1

Phosphotyrosine; by MAP2K1 and MAP2K2 Ref.40 Ref.43 Ref.49 Ref.54 Ref.60

Modified residue

190

1

Phosphothreonine; by autocatalysis Ref.46

Modified residue

246

1

Phosphoserine Ref.38

Modified residue

248

1

Phosphoserine Ref.38

Modified residue

284

1

Phosphoserine Ref.45

Experimental info

Mutagenesis

54

1

K → R: Does not inhibit interaction with MAP2K1. Ref.39

Mutagenesis

176 – 179

4

Missing: Inhibits homodimerization and interaction with TPR. Ref.39

Mutagenesis

185

1

T → A: Inhibits interaction with TPR; when associated with A-187. Ref.39

Mutagenesis

187

1

Y → A: Inhibits interaction with TPR; when associated with A-185. Ref.39

Mutagenesis

234

1

L → A: Inhibits interaction with TPR. Ref.39

Mutagenesis

318

1

D → A: Loss of dephosphorylation by PTPRJ. Ref.39 Ref.43

Mutagenesis

318

1

D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-321. Ref.39 Ref.43

Mutagenesis

321

1

D → N: Inhibits interaction with MAP2K1 but not with TPR; when associated with N-318. Ref.39

Sequence conflict

91

1

R → Q in CAA77752. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

360

Helix Strand Turn

Details...

Beta strand

12 – 19

8

Turn

22 – 24

3

Beta strand

25 – 33

9

Beta strand

38 – 44

7

Turn

45 – 48

4

Beta strand

49 – 56

8

Beta strand

59 – 61

3

Helix

62 – 77

16

Beta strand

88 – 90

3

Turn

95 – 97

3

Beta strand

101 – 106

6

Beta strand

109 – 111

3

Helix

112 – 118

7

Helix

123 – 142

20

Helix

152 – 154

3

Beta strand

155 – 157

3

Beta strand

163 – 165

3

Helix

168 – 170

3

Helix

176 – 178

3

Turn

181 – 185

5

Helix

191 – 193

3

Helix

196 – 200

5

Beta strand

202 – 205

4

Helix

208 – 223

16

Helix

233 – 244

12

Helix

249 – 252

4

Beta strand

253 – 255

3

Helix

258 – 266

9

Helix

275 – 278

4

Beta strand

279 – 282

4

Helix

284 – 293

10

Helix

298 – 300

3

Helix

304 – 308

5

Helix

311 – 313

3

Turn

314 – 316

3

Helix

319 – 321

3

Turn

335 – 337

3

Helix

340 – 351

12

Helix

352 – 354

3

Turn

356 – 358

3

Sequences

	Sequence		Length	Mass (Da)
	P28482 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E85D0B2A5D2D724E	FASTA	360	41,390
	10 20 30 40 50 60 MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR VAIKKISPFE 70 80 90 100 110 120 HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD VYIVQDLMET DLYKLLKTQH 130 140 150 160 170 180 LSNDHICYFL YQILRGLKYI HSANVLHRDL KPSNLLLNTT CDLKICDFGL ARVADPDHDH 190 200 210 220 230 240 TGFLTEYVAT RWYRAPEIML NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI 250 260 270 280 290 300 LGILGSPSQE DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK 310 320 330 340 350 360 RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE TARFQPGYRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs." Owaki H., Makar R., Boulton T.G., Cobb M.H., Geppert T.D. Biochem. Biophys. Res. Commun. 182:1416-1422(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Heterogeneous expression of four MAP kinase isoforms in human tissues." Gonzalez F.A., Raden D.L., Rigby M.R., Davis R.J. FEBS Lett. 304:170-178(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15, ACETYLATION AT ALA-2. Tissue: Platelet.
[6]	"ERF: an ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation." Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G., Mavrothalassitis G.J. EMBO J. 14:4781-4793(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ERF.
[7]	"3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region." Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G. , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R. Mol. Cell. Biol. 16:868-876(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPKAPK3.
[8]	"Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity." Greenway A.L., Azad A., Mills J., McPhee D.A. J. Virol. 70:6701-6708(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 NEF.
[9]	"MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase." Ni H., Wang X.S., Diener K., Yao Z. Biochem. Biophys. Res. Commun. 243:492-496(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPKAPK5.
[10]	"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB." Deak M., Clifton A.D., Lucocq J.M., Alessi D.R. EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KA5/MSK1.
[11]	"Antigen receptor signaling induces MAP kinase-mediated phosphorylation and degradation of the BCL-6 transcription factor." Niu H., Ye B.H., Dalla-Favera R. Genes Dev. 12:1953-1961(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF BCL6.
[12]	"Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase." Camps M., Nichols A., Gillieron C., Antonsson B., Muda M., Chabert C., Boschert U., Arkinstall S. Science 280:1262-1265(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DUSP6, FUNCTION.
[13]	"Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway." Todd J.L., Tanner K.G., Denu J.M. J. Biol. Chem. 274:13271-13280(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION BY DUSP3.
[14]	"ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry." Cruzalegui F.H., Cano E., Treisman R. Oncogene 18:7948-7957(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ELK1.
[15]	"Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation." Brondello J.M., Pouyssegur J., McKenzie F.R. Science 286:2514-2517(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF DUSP1.
[16]	"The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells." Scheper G.C., Morrice N.A., Kleijn M., Proud C.G. Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS MKNK2 KINASE.
[17]	"Growth factors can activate ATF2 via a two-step mechanism: phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69 through RalGDS-Src-p38." Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P., Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A., van Dam H. EMBO J. 21:3782-3793(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ATF2.
[18]	"IEX-1: a new ERK substrate involved in both ERK survival activity and ERK activation." Garcia J., Ye Y., Arranz V., Letourneux C., Pezeron G., Porteu F. EMBO J. 21:5151-5163(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF IER3, INTERACTION WITH IER3, ENZYME REGULATION.
[19]	"Insulin receptor substrate 4 associates with the protein IRAS." Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E. J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NISCH.
[20]	"EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2." Wu Y., Chen Z., Ullrich A. Biol. Chem. 384:1215-1226(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2.
[21]	"Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446." Masuda K., Shima H., Katagiri C., Kikuchi K. J. Biol. Chem. 278:32448-32456(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF DUSP16.
[22]	"Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK." Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R. Nat. Cell Biol. 5:647-654(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CASP9.
[23]	"Nek2A specifies the centrosomal localization of Erk2." Lou Y., Xie W., Zhang D.F., Yao J.H., Luo Z.F., Wang Y.Z., Shi Y.Y., Yao X.B. Biochem. Biophys. Res. Commun. 321:495-501(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK2.
[24]	"Signal transduction via the stem cell factor receptor/c-Kit." Ronnstrand L. Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[25]	"Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin." Mitsushima M., Suwa A., Amachi T., Ueda K., Kioka N. J. Biol. Chem. 279:34570-34577(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SORBS3.
[26]	"MCL1 is phosphorylated in the PEST region and stabilized upon ERK activation in viable cells, and at additional sites with cytotoxic okadaic acid or taxol." Domina A.M., Vrana J.A., Gregory M.A., Hann S.R., Craig R.W. Oncogene 23:5301-5315(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MCL1.
[27]	"Phosphorylation of Grb10 by mitogen-activated protein kinase: identification of Ser150 and Ser476 of human Grb10zeta as major phosphorylation sites." Langlais P., Wang C., Dong L.Q., Carroll C.A., Weintraub S.T., Liu F. Biochemistry 44:8890-8897(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GRB10.
[28]	"Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK." Chen C.H., Wang W.J., Kuo J.C., Tsai H.C., Lin J.R., Chang Z.F., Chen R.H. EMBO J. 24:294-304(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK1, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
[29]	"Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces Pin-1 binding in cytoplasm and cell death." Hong J.W., Ryu M.S., Lim I.K. J. Biol. Chem. 280:21256-21263(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF BTG2.
[30]	"Regulation of Raf-1 by direct feedback phosphorylation." Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z., Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K. Mol. Cell 17:215-224(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RAF1.
[31]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[32]	"ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA." Fujishiro S.H., Tanimura S., Mure S., Kashimoto Y., Watanabe K., Kohno M. Biochem. Biophys. Res. Commun. 368:162-167(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF2.
[33]	"Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26." Hu Y., Mivechi N.F. Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSF4.
[34]	"ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation." Degoutin J., Vigny M., Gouzi J.Y. FEBS Lett. 581:727-734(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[35]	"Mutations of beta-arrestin 2 that limit self-association also interfere with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs." Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R., Kolch W., Houslay M.D., Milligan G. Biochem. J. 413:51-60(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARRB2.
[36]	"Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma." Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R. Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADAM15.
[37]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[38]	"Identification and characterization of a general nuclear translocation signal in signaling proteins." Chuderland D., Konson A., Seger R. Mol. Cell 31:850-861(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-246 AND SER-248, INTERACTION WITH IPO7, SUBCELLULAR LOCATION.
[39]	"Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction." Vomastek T., Iwanicki M.P., Burack W.R., Tiwari D., Kumar D., Parsons J.T., Weber M.J., Nandicoori V.K. Mol. Cell. Biol. 28:6954-6966(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TPR, INTERACTION WITH TPR, MUTAGENESIS OF LYS-54; 176-PRO--ASP-179; THR-185; TYR-187; LEU-234; ASP-318 AND ASP-321.
[40]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[41]	"Profiling the human protein-DNA interactome reveals ERK2 as a transcriptional repressor of interferon signaling." Hu S., Xie Z., Onishi A., Yu X., Jiang L., Lin J., Rho H.-S., Woodard C., Wang H., Jeong J.-S., Long S., He X., Wade H., Blackshaw S., Qian J., Zhu H. Cell 139:610-622(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, DNA-BINDING.
[42]	"The D816V mutation of c-Kit circumvents a requirement for Src family kinases in c-Kit signal transduction." Sun J., Pedersen M., Ronnstrand L. J. Biol. Chem. 284:11039-11047(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN KIT SIGNALING PATHWAY, PHOSPHORYLATION.
[43]	"Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases." Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P., Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G. J. Biol. Chem. 284:22048-22058(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-187, DEPHOSPHORYLATION BY PTPRJ AT TYR-187, MUTAGENESIS OF ASP-318.
[44]	"Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration." Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J., Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M., Hur G.M. J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-29 BY SGK1, INTERACTION WITH SGK1.
[45]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, MASS SPECTROMETRY.
[46]	"A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy." Lorenz K., Schmitt J.P., Schmitteckert E.M., Lohse M.J. Nat. Med. 15:75-83(2009) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION AT THR-190, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
[47]	"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.
[48]	"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.
[49]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[50]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[51]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[52]	"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.
[53]	"Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover." Lim J.H., Liu Y., Reineke E., Kao H.Y. J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PML.
[54]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY.
[55]	"A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase." Fox T., Coll J.T., Xie X., Ford P.J., Germann U.A., Porter M.D., Pazhanisamy S., Fleming M.A., Galullo V., Su M.S., Wilson K.P. Protein Sci. 7:2249-2255(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[56]	"Identification of a selective ERK inhibitor and structural determination of the inhibitor-ERK2 complex." Ohori M., Kinoshita T., Okubo M., Sato K., Yamazaki A., Arakawa H., Nishimura S., Inamura N., Nakajima H., Neya M., Miyake H., Fujii T. Biochem. Biophys. Res. Commun. 336:357-363(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[57]	"Crystal structure of human ERK2 complexed with a pyrazolo[3,4-c]pyridazine derivative." Kinoshita T., Warizaya M., Ohori M., Sato K., Neya M., Fujii T. Bioorg. Med. Chem. Lett. 16:55-58(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[58]	"Role of a cysteine residue in the active site of ERK and the MAPKK family." Ohori M., Kinoshita T., Yoshimura S., Warizaya M., Nakajima H., Miyake H. Biochem. Biophys. Res. Commun. 353:633-637(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[59]	"Flipped out: structure-guided design of selective pyrazolylpyrrole ERK inhibitors." Aronov A.M., Baker C., Bemis G.W., Cao J., Chen G., Ford P.J., Germann U.A., Green J., Hale M.R., Jacobs M., Janetka J.W., Maltais F., Martinez-Botella G., Namchuk M.N., Straub J., Tang Q., Xie X. J. Med. Chem. 50:1280-1287(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
[60]	"Structural basis of substrate recognition by hematopoietic tyrosine phosphatase." Critton D.A., Tortajada A., Stetson G., Peti W., Page R. Biochemistry 47:13336-13345(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 186-191, PHOSPHORYLATION AT TYR-187.
[61]	"Structure-guided design of potent and selective pyrimidylpyrrole inhibitors of extracellular signal-regulated kinase (ERK) using conformational control." Aronov A.M., Tang Q., Martinez-Botella G., Bemis G.W., Cao J., Chen G., Ewing N.P., Ford P.J., Germann U.A., Green J., Hale M.R., Jacobs M., Janetka J.W., Maltais F., Markland W., Namchuk M.N., Nanthakumar S., Poondru S. , Straub J., ter Haar E., Xie X. J. Med. Chem. 52:6362-6368(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
+	Additional computationally mapped references.

Web resources

Wikipedia

Extracellular signal-regulated kinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M84489 mRNA. Translation: AAA58459.1.
Z11694 mRNA. Translation: CAA77752.1.
Z11695 mRNA. Translation: CAA77753.1. Different initiation.
AP000555 Genomic DNA. No translation available.
BC017832 mRNA. Translation: AAH17832.1.

IPI

IPI00003479.

PIR

JQ1400.

RefSeq

NP_002736.3. NM_002745.4.
NP_620407.1. NM_138957.2.

UniGene

Hs.431850.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PME	X-ray	2.00	A	1-360	[»]
1TVO	X-ray	2.50	A	1-360	[»]
1WZY	X-ray	2.50	A	1-360	[»]
2OJG	X-ray	2.00	A	2-359	[»]
2OJI	X-ray	2.60	A	2-359	[»]
2OJJ	X-ray	2.40	A	2-359	[»]
2Y9Q	X-ray	1.55	A	1-360	[»]
3D42	X-ray	2.46	B	184-191	[»]
3D44	X-ray	1.90	B	186-191	[»]
3I5Z	X-ray	2.20	A	1-360	[»]
3I60	X-ray	2.50	A	1-360	[»]
3SA0	X-ray	1.59	A	1-360	[»]
3TEI	X-ray	2.40	A	1-360	[»]
3W55	X-ray	3.00	A	1-360	[»]
4FMQ	X-ray	2.10	A	1-360	[»]
4FUX	X-ray	2.20	A	1-360	[»]
4FUY	X-ray	2.00	A	1-360	[»]
4FV0	X-ray	2.10	A	1-360	[»]
4FV1	X-ray	1.99	A	1-360	[»]
4FV2	X-ray	2.00	A	1-360	[»]
4FV3	X-ray	2.20	A	1-360	[»]
4FV4	X-ray	2.50	A	1-360	[»]
4FV5	X-ray	2.40	A	1-360	[»]
4FV6	X-ray	2.50	A	1-360	[»]
4FV7	X-ray	1.90	A	1-360	[»]
4FV8	X-ray	2.00	A	1-360	[»]
4FV9	X-ray	2.11	A	1-360	[»]
4G6N	X-ray	2.00	A	1-360	[»]
4G6O	X-ray	2.20	A	1-360	[»]
4H3P	X-ray	2.30	A/D	1-360	[»]
4H3Q	X-ray	2.20	A	1-360	[»]
4IZ5	X-ray	3.19	A/B/C/D	8-360	[»]
4IZ7	X-ray	1.80	A/C	8-360	[»]
4IZA	X-ray	1.93	A/C	8-360	[»]

ProteinModelPortal

P28482.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-519N.

IntAct

P28482. 28 interactions.

MINT

MINT-144006.

STRING

9606.ENSP00000215832.

PTM databases

PhosphoSite

P28482.

Polymorphism databases

DMDM

119554.

2D gel databases

OGP

P28482.

Proteomic databases

PaxDb

P28482.

PeptideAtlas

P28482.

PRIDE

P28482.

Protocols and materials databases

DNASU

5594.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215832; ENSP00000215832; ENSG00000100030.
ENST00000398822; ENSP00000381803; ENSG00000100030.

GeneID

5594.

KEGG

hsa:5594.

UCSC

uc002zvn.3. human.

Organism-specific databases

CTD

5594.

GeneCards

GC22M022108.

HGNC

HGNC:6871. MAPK1.

HPA

CAB004229.
HPA003995.
HPA005700.
HPA030069.

MIM

176948. gene.

neXtProt

NX_P28482.

Orphanet

261330. Distal 22q11.2 microdeletion syndrome.

PharmGKB

PA30616.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

P28482.

KO

K04371.

OMA

FEVAPRY.

OrthoDB

EOG45HRXM.

PhylomeDB

P28482.

Enzyme and pathway databases

BRENDA

2.7.11.24. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
arf6downstreampathway. Arf6 downstream pathway.
bcr_5pathway. BCR signaling pathway.
bmppathway. BMP receptor signaling.
anthraxpathway. Cellular roles of Anthrax toxin.
ceramidepathway. Ceramide signaling pathway.
pi3kcibpathway. Class IB PI3K non-lipid kinase events.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
endothelinpathway. Endothelins.
ephbfwdpathway. EPHB forward signaling.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
fgf_pathway. FGF signaling pathway.
ifngpathway. IFN-gamma pathway.
il2_1pathway. IL2-mediated signaling events.
avb3_integrin_pathway. Integrins in angiogenesis.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
avb3_opn_pathway. Osteopontin-mediated events.
ps1pathway. Presenilin action in Notch and Wnt signaling.
tcrraspathway. Ras signaling in the CD4+ TCR pathway.
smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
s1p_s1p1_pathway. S1P1 pathway.
s1p_s1p2_pathway. S1P2 pathway.
s1p_s1p3_pathway. S1P3 pathway.
s1p_s1p4_pathway. S1P4 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
prlsignalingeventspathway. Signaling events mediated by PRL.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_1_pathway. Syndecan-1-mediated signaling events.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
trail_pathway. TRAIL signaling pathway.
mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.
vegfr1_pathway. VEGFR1 specific signals.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

SignaLink

P28482.

Gene expression databases

ArrayExpress

P28482.

Bgee

P28482.

CleanEx

HS_MAPK1.

Genevestigator

P28482.

GermOnline

ENSG00000100030. Homo sapiens.

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

P28482.

ChEMBL

CHEMBL4040.

ChiTaRS

MAPK1. human.

DrugBank

DB01169. Arsenic trioxide.

EvolutionaryTrace

P28482.

GenomeRNAi

5594.

NextBio

21708.

SOURCE

Search...

Entry information

Entry name

MK01_HUMAN

Accession

Primary (citable) accession number: P28482

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 157 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.