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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 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, 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 additionnal cytosolic and nuclear targets, thereby extending the specificity of the cascade. 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.38 Ref.47 Ref.48 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.38 Ref.47 Ref.48
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. Dephospphorylated and inactivated by DUSP3, DUSP6 and DUSP9. Inactivated by pyrimidylpyrrole inhibitors. Ref.18 Ref.53
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. Ref.8 Ref.12 Ref.18 Ref.19 Ref.23 Ref.28 Ref.33 Ref.38 Ref.41 Ref.42 Ref.44 Ref.50 Ref.53
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm. Note: 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.44 Ref.53
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.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 Ref.43 Ref.44 Ref.45 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.64
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	ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome MyD88-independent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Ras protein signal transduction Traceable author statement. Source: Reactome Toll 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 axon guidance Traceable author statement. Source: Reactome cell cycle Inferred from electronic annotation. Source: UniProtKB-KW epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome induction of apoptosis Traceable author statement. Source: ProtInc innate immune response Traceable author statement. Source: Reactome insulin receptor signaling pathway Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome positive regulation of peptidyl-threonine phosphorylation Inferred from direct assay. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome stress-activated MAPK cascade Traceable author statement. Source: Reactome synaptic transmission Traceable author statement. Source: Reactome toll-like receptor 1 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: Reactome microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
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. Source: ProtInc RNA polymerase II carboxy-terminal domain kinase activity Inferred from sequence or structural similarity. Source: UniProtKB phosphatase binding Inferred from physical interaction Ref.49. 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.47

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 Ref.46

Modified residue

29

1

Phosphoserine; by SGK1 Ref.50

Modified residue

63

1

Phosphothreonine Ref.52

Modified residue

181

1

Phosphothreonine Ref.52

Modified residue

185

1

Phosphothreonine; by MAP2K1 and MAP2K2 Ref.32 Ref.37 Ref.40 Ref.43 Ref.45 Ref.52 Ref.54

Modified residue

187

1

Phosphotyrosine; by MAP2K1 and MAP2K2 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37 Ref.40 Ref.43 Ref.45 Ref.49 Ref.51 Ref.52 Ref.54 Ref.64

Modified residue

190

1

Phosphothreonine; by autocatalysis Ref.53

Modified residue

202

1

Phosphoserine Ref.43 Ref.52

Modified residue

246

1

Phosphoserine Ref.44

Modified residue

248

1

Phosphoserine Ref.44

Modified residue

284

1

Phosphoserine Ref.52

Experimental info

Mutagenesis

318

1

D → A: Loss of dephosphorylation by PTPRJ. Ref.49

Sequence conflict

91

1

R → Q in CAA77752. Ref.2

Secondary structure

1

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360

Helix Strand Turn

Details...

Beta strand

25 – 30

6

Beta strand

39 – 44

6

Turn

45 – 47

3

Beta strand

49 – 56

8

Helix

62 – 77

16

Beta strand

88 – 90

3

Turn

95 – 97

3

Beta strand

101 – 106

6

Helix

112 – 118

7

Helix

123 – 142

20

Helix

152 – 154

3

Beta strand

155 – 157

3

Beta strand

163 – 165

3

Helix

176 – 178

3

Helix

191 – 193

3

Helix

196 – 198

3

Turn

199 – 201

3

Helix

208 – 223

16

Helix

233 – 244

12

Helix

249 – 253

5

Helix

258 – 265

8

Helix

275 – 278

4

Helix

284 – 293

10

Turn

298 – 300

3

Helix

304 – 308

5

Helix

311 – 313

3

Turn

314 – 316

3

Helix

319 – 321

3

Helix

340 – 350

11

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: 1540184] [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: 1319925] [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: 10591208] [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: 15489334] [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: 12665801] [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: 7588608] [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: 8622688] [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: 8794306] [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: 9480836] [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: 9687510] [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: 9649500] [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: 9596579] [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: 10224087] [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: 10637505] [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: 10617468] [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: 11154262] [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: 12110590] [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: 12356731] [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: 11912194] [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: 12974390] [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: 12794087] [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: 12792650] [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: 15358203] [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: 15526160] [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: 15184391] [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: 15241487] [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: 15952796] [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: 15616583] [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: 15788397] [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: 15664191] [Abstract] Cited for: FUNCTION IN THE PHOSPHORYLATION OF RAF1.
[31]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[32]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[33]	"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: 18211802] [Abstract] Cited for: INTERACTION WITH ARHGEF2.
[34]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[35]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, MASS SPECTROMETRY.
[36]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[37]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[38]	"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: 16581800] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSF4.
[39]	"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: 17274988] [Abstract] Cited for: PHOSPHORYLATION.
[40]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[41]	"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: 18435604] [Abstract] Cited for: INTERACTION WITH ARRB2.
[42]	"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: 18296648] [Abstract] Cited for: INTERACTION WITH ADAM15.
[43]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185; TYR-187 AND SER-202, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[44]	"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: 18760948] [Abstract] Cited for: PHOSPHORYLATION AT SER-246 AND SER-248, INTERACTION WITH IPO7, SUBCELLULAR LOCATION.
[45]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[46]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[47]	"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: 19879846] [Abstract] Cited for: FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, DNA-BINDING.
[48]	"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: 19265199] [Abstract] Cited for: FUNCTION IN KIT SIGNALING PATHWAY, PHOSPHORYLATION.
[49]	"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: 19494114] [Abstract] Cited for: PHOSPHORYLATION AT TYR-187, DEPHOSPHORYLATION BY PTPRJ AT TYR-187, MUTAGENESIS OF ASP-318.
[50]	"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: 19447520] [Abstract] Cited for: PHOSPHORYLATION AT SER-29 BY SGK1, INTERACTION WITH SGK1.
[51]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[52]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63; THR-181; THR-185; TYR-187; SER-202 AND SER-284, MASS SPECTROMETRY.
[53]	"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: 19060905] [Abstract] Cited for: AUTOPHOSPHORYLATION AT THR-190, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
[54]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[55]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]	"The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions." Yoon S., Seger R. Growth Factors 24:21-44(2006) [PubMed: 16393692] [Abstract] Cited for: REVIEW ON FUNCTION.
[57]	"The ERK signaling cascade--views from different subcellular compartments." Yao Z., Seger R. BioFactors 35:407-416(2009) [PubMed: 19565474] [Abstract] Cited for: REVIEW ON FUNCTION, REVIEW ON SUBCELLULAR LOCATION.
[58]	"The ERK cascade: distinct functions within various subcellular organelles." Wortzel I., Seger R. Genes Cancer 2:195-209(2011) [PubMed: 21779493] [Abstract] Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
[59]	"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: 9827991] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[60]	"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: 16139248] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[61]	"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: 16242327] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[62]	"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: 17194451] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[63]	"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: 17300186] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
[64]	"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: 19053285] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 186-191, PHOSPHORYLATION AT TYR-187.
[65]	"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: 19827834] [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

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	[»]
2E14	X-ray	3.00	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	[»]
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	[»]

ProteinModelPortal

P28482.

SMR

P28482. Positions 10-360.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-519N.

IntAct

P28482. 25 interactions.

MINT

MINT-144006.

STRING

P28482.

PTM databases

PhosphoSite

P28482.

Polymorphism databases

DMDM

119554.

2D gel databases

OGP

P28482.

Proteomic databases

PeptideAtlas

P28482.

PRIDE

P28482.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

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

GeneID

5594.

KEGG

hsa:5594.

UCSC

uc002zvn.1. human.

Organism-specific databases

CTD

5594.

GeneCards

GC22M022108.

H-InvDB

HIX0016281.

HGNC

HGNC:6871. MAPK1.

HPA

CAB004229.
HPA003995.
HPA005700.
HPA030069.

MIM

176948. gene.

neXtProt

NX_P28482.

Orphanet

567. Monosomy 22q11.

PharmGKB

PA30616.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10833.

HOGENOM

HBG755340.

HOVERGEN

HBG014652.

InParanoid

P28482.

OMA

YISTELM.

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_13685. Neuronal System.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

Bgee

P28482.

CleanEx

HS_MAPK1.

Genevestigator

P28482.

GermOnline

ENSG00000100030. Homo sapiens.

Family and domain databases

InterPro

IPR008349. Erk_1_2_MAPK.
IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K04371.

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

DrugBank

DB01169. Arsenic trioxide.

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:	January 25, 2012
This is version 142 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.