P63085 (MK01_MOUSE) 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, Mapk, Prkm1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.9 Ref.10 Ref.11 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.9 Ref.10 Ref.11
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, DUSP6, NISCH, SGK1, and isoform 1 of NEK2. Interacts (via phosphorylated form) with TPR (via C-terminus region and phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases following EGF stimulation 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. Interacts with DCC By similarity. Interacts with MORG1, PEA15 and MKNK2. MKNK2 isoform 1 binding prevents from dephosphorylation and inactivation. The phosphorylated form interacts with PML By similarity. Ref.10 Ref.12 Ref.14
Subcellular location	Cytoplasm › cytoskeleton › spindle By similarity. Nucleus. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm. Note: Associated with the spindle during prometaphase and metaphase By similarity. PEA15-binding and phosphorylated DAPK1 promote its cytoplasmic retention. Phosphorylation at Ser-244 and Ser-246 as well as autophosphorylation at Thr-188 promote nuclear localization By similarity. Ref.10 Ref.11
Tissue specificity	Widely expressed.
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. Ligand-activated ALK induces tyrosine phosphorylation By similarity. Dephosphorylated by PTPRJ at Tyr-185 By similarity. Phosphorylated upon FLT3 and KIT signaling By similarity. Ref.6 Ref.7 Ref.8 Ref.13 Ref.20
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from direct assay PubMed 9254656. Source: MGI ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara MAPK import into nucleus Inferred from electronic annotation. Source: Compara T cell receptor signaling pathway Inferred from direct assay PubMed 9064344. Source: MGI apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW caveolin-mediated endocytosis Traceable author statement Ref.22. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytosine metabolic process Inferred from direct assay PubMed 15284227. Source: MGI labyrinthine layer blood vessel development Inferred from mutant phenotype PubMed 14622137. Source: MGI lipopolysaccharide-mediated signaling pathway Inferred from direct assay PubMed 12872135. Source: MGI mammary gland epithelial cell proliferation Inferred from direct assay PubMed 18604197. Source: MGI negative regulation of cell differentiation Inferred from genetic interaction PubMed 14970190. Source: MGI organ morphogenesis Inferred from direct assay PubMed 11684667. Source: MGI peptidyl-serine phosphorylation Inferred from direct assay PubMed 18084034. Source: MGI 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 electronic annotation. Source: Compara 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.22. Source: UniProtKB regulation of cytoskeleton organization Traceable author statement Ref.22. Source: UniProtKB regulation of early endosome to late endosome transport Traceable author statement Ref.22. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Non-traceable author statement PubMed 7889942. Source: UniProtKB regulation of stress-activated MAPK cascade Traceable author statement Ref.22. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay PubMed 15383658. Source: MGI response to epidermal growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to exogenous dsRNA Inferred from direct assay PubMed 12872135. Source: MGI response to toxin Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Non-traceable author statement PubMed 7889942. Source: UniProtKB
Cellular_component	Golgi apparatus Traceable author statement Ref.22. Source: UniProtKB axon part Inferred from electronic annotation. Source: Compara caveola Traceable author statement Ref.22. Source: UniProtKB cytoskeleton Traceable author statement Ref.22. Source: UniProtKB cytosol Traceable author statement Ref.22. Source: UniProtKB dendrite cytoplasm Inferred from electronic annotation. Source: Compara early endosome Traceable author statement Ref.22. Source: UniProtKB focal adhesion Traceable author statement Ref.22. Source: UniProtKB late endosome Traceable author statement Ref.22. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Traceable author statement Ref.22. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome perikaryon Inferred from electronic annotation. Source: Compara pseudopodium Inferred from direct assay PubMed 12821670. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from direct assay PubMed 12223545PubMed 15314156PubMed 15896720PubMed 18084034PubMed 8626447PubMed 9064344PubMed 9254656. Source: MGI RNA polymerase II carboxy-terminal domain kinase activity Inferred from direct assay PubMed 12721286. Source: UniProtKB phosphotyrosine binding Inferred from mutant phenotype PubMed 14636584. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dlg4	Q62108	3	EBI-397697,EBI-300895
GSK3B	P49841	2	EBI-397697,EBI-373586	From a different organism.
Hivep1	Q03172	4	EBI-397697,EBI-646850
Mknk2	Q8CDB0	23	EBI-397697,EBI-646209
Nupl1	Q8R332-1	3	EBI-397697,EBI-646962
Rps6ka4	Q9Z2B9	3	EBI-397697,EBI-412887

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 358	357	Mitogen-activated protein kinase 1		PRO_0000186248
Regions
	Domain	23 – 311	289	Protein kinase
	Nucleotide binding	29 – 37	9	ATP By similarity
	Region	103 – 106	4	Inhibitor-binding By similarity
	Region	151 – 152	2	Inhibitor-binding By similarity
	Motif	183 – 185	3	TXY
	Compositional bias	2 – 7	6	Poly-Ala
Sites
	Active site	147	1	Proton acceptor By similarity
	Binding site	52	1	ATP By similarity
	Binding site	52	1	Inhibitor By similarity
	Binding site	106	1	Inhibitor; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	112	1	Inhibitor By similarity
	Binding site	152	1	Inhibitor By similarity
	Binding site	164	1	Inhibitor By similarity
	Binding site	165	1	Inhibitor By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	27	1	Phosphoserine; by SGK1 By similarity
	Modified residue	183	1	Phosphothreonine; by MAP2K1 and MAP2K2 Ref.6 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
	Modified residue	185	1	Phosphotyrosine; by MAP2K1 and MAP2K2 Ref.6 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
	Modified residue	188	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	244	1	Phosphoserine By similarity
	Modified residue	246	1	Phosphoserine By similarity
	Modified residue	282	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63085 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3BBCF22471EDBA0B	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation." Her J.-H., Wu J.-S., Rall T.B., Sturgill T.W., Weber M.J. Nucleic Acids Res. 19:3743-3743(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss. Tissue: Fibroblast.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Brain, Head, Thymus and Urinary bladder.
[3]	"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: Eye.
[4]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-65; 76-89; 137-162; 171-189; 193-201 AND 260-268, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"Novel CDC2-related protein kinases produced in murine hematopoietic stem cells." Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V. Gene 124:305-306(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-190. Strain: CBA. Tissue: Bone marrow.
[6]	"Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase)." Payne D.M., Rossomando A.J., Martino P., Erickson A.K., Her J.-H., Shabanowitz J., Hunt D.F., Weber M.J., Sturgill T.W. EMBO J. 10:885-892(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-183 AND TYR-185, PARTIAL PROTEIN SEQUENCE.
[7]	"Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells." Zhang S., Mantel C., Broxmeyer H.E. J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
[8]	"Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways." Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C., Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J., Kanakura Y., Berdel W.E., Serve H. Blood 96:3907-3914(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
[9]	"Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells." Ku H., Meier K.E. J. Biol. Chem. 275:11333-11340(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PXN.
[10]	"PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase." Formstecher E., Ramos J.W., Fauquet M., Calderwood D.A., Hsieh J.C., Canton B., Nguyen X.T., Barnier J.V., Camonis J., Ginsberg M.H., Chneiweiss H. Dev. Cell 1:239-250(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PEA15, SUBCELLULAR LOCATION, FUNCTION OF THE MAPK ERK CASCADE.
[11]	"Molecular interpretation of ERK signal duration by immediate early gene products." Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J. Nat. Cell Biol. 4:556-564(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FOS, SUBCELLULAR LOCATION.
[12]	"Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists." Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E., Bissonette E.A., Weber M.J. Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MORG1.
[13]	"bHLH-zip transcription factor Spz1 mediates mitogen-activated protein kinase cell proliferation, transformation, and tumorigenesis." Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H. Cancer Res. 65:4041-4050(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION OF SPZ1.
[14]	"Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties." Parra J.L., Buxade M., Proud C.G. J. Biol. Chem. 280:37623-37633(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MKNK2.
[15]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY. Tissue: Mast cell.
[16]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY. Tissue: Brain.
[17]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY. Tissue: Liver.
[18]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[20]	"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling." Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P. J. Biol. Chem. 286:10918-10929(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
[21]	"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.
[22]	"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.
[23]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58712 mRNA. Translation: CAA41548.1. AK035386 mRNA. Translation: BAC29053.1. AK048127 mRNA. Translation: BAC33251.1. AK087925 mRNA. Translation: BAC40044.1. AK132241 mRNA. Translation: BAE21053.1. BC058258 mRNA. Translation: AAH58258.1. D10939 mRNA. Translation: BAA01733.1.
IPI	IPI00119663.
PIR	S16444.
RefSeq	NP_001033752.1. NM_001038663.1. NP_036079.1. NM_011949.3.
UniGene	Mm.196581.
3D structure databases
ProteinModelPortal	P63085.
SMR	P63085. Positions 10-353.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-661N.
IntAct	P63085. 16 interactions.
MINT	MINT-125264.
PTM databases
PhosphoSite	P63085.
Proteomic databases
PaxDb	P63085.
PRIDE	P63085.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358. ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358. ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
GeneID	26413.
KEGG	mmu:26413.
UCSC	uc009jsn.1. mouse.
Organism-specific databases
CTD	5594.
MGI	MGI:1346858. Mapk1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074298.
HOGENOM	HOG000233024.
HOVERGEN	HBG014652.
InParanoid	P63085.
KO	K04371.
OMA	FEVAPRY.
OrthoDB	EOG45HRXM.
Enzyme and pathway databases
Reactome	REACT_105924. TRAF6 Mediated Induction of proinflammatory cytokines. REACT_107772. Immune System. REACT_115202. Signal Transduction.
Gene expression databases
ArrayExpress	P63085.
Bgee	P63085.
CleanEx	MM_MAPK1.
Genevestigator	P63085.
GermOnline	ENSMUSG00000063358. Mus musculus.
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	P63085.
ChEMBL	CHEMBL2207.
ChiTaRS	MAPK1. mouse.
NextBio	304409.
SOURCE	Search...

Entry information

Entry name

MK01_MOUSE

Accession

Primary (citable) accession number: P63085
Secondary accession number(s): P27703, Q3V1U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 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