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P63085 (MK01_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 1

Short name=MAP kinase 1
Short name=MAPK 1
EC=2.7.11.24
Alternative name(s):
ERT1
Extracellular signal-regulated kinase 2
Short name=ERK-2
MAP kinase isoform p42
Short name=p42-MAPK
Mitogen-activated protein kinase 2
Short name=MAP kinase 2
Short name=MAPK 2
Gene names
Name:Mapk1
Synonyms:Erk2, Mapk, Prkm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation By similarity. Ref.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 1of 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 1binding prevents from dephosphorylation and inactivation. The phosphorylated form interacts with PML By similarity. Ref.10 Ref.12 Ref.14

Subcellular location

Cytoplasmcytoskeletonspindle By similarity. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 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.19

ISGylated. Ref.23

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

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

Inferred from direct assay PubMed 9254656. Source: MGI

ERBB signaling pathway

Inferred from electronic annotation. Source: Ensembl

ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

MAPK cascade

Inferred from direct assay PubMed 8626447PubMed 9064344PubMed 9254656. Source: MGI

MAPK import into nucleus

Inferred from electronic annotation. Source: Ensembl

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.21. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 15383658. Source: MGI

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 11854404. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 11854404. Source: UniProtKB

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of translation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 11841548PubMed 14744933PubMed 15284227PubMed 18378670. Source: MGI

regulation of Golgi inheritance

Traceable author statement Ref.21. Source: UniProtKB

regulation of cytoskeleton organization

Traceable author statement Ref.21. Source: UniProtKB

regulation of early endosome to late endosome transport

Traceable author statement Ref.21. Source: UniProtKB

regulation of protein stability

Inferred from sequence or structural similarity. 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.21. Source: UniProtKB

response to epidermal growth factor

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to exogenous dsRNA

Inferred from direct assay PubMed 12872135. Source: MGI

response to lipopolysaccharide

Inferred from direct assay PubMed 12872135. Source: MGI

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Non-traceable author statement PubMed 7889942. Source: UniProtKB

   Cellular_componentGolgi apparatus

Traceable author statement Ref.21. Source: UniProtKB

caveola

Traceable author statement Ref.21. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11726647PubMed 12223545PubMed 12925581. Source: MGI

cytoskeleton

Traceable author statement Ref.21. Source: UniProtKB

cytosol

Traceable author statement Ref.21. Source: UniProtKB

dendrite cytoplasm

Inferred from electronic annotation. Source: Ensembl

early endosome

Traceable author statement Ref.21. Source: UniProtKB

focal adhesion

Traceable author statement Ref.21. Source: UniProtKB

late endosome

Traceable author statement Ref.21. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Traceable author statement Ref.21. Source: UniProtKB

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.21. Source: UniProtKB

perikaryon

Inferred from electronic annotation. Source: Ensembl

pseudopodium

Inferred from direct assay PubMed 12821670. Source: UniProtKB

   Molecular_functionATP 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

kinase activity

Inferred from direct assay PubMed 12808090PubMed 15284227. Source: MGI

phosphotyrosine binding

Inferred from mutant phenotype PubMed 14636584. Source: MGI

protein kinase activity

Inferred from direct assay PubMed 14744933PubMed 18378670. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay PubMed 11854404. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 358357Mitogen-activated protein kinase 1
PRO_0000186248

Regions

Domain23 – 311289Protein kinase
Nucleotide binding29 – 379ATP By similarity
Region103 – 1064Inhibitor-binding By similarity
Region151 – 1522Inhibitor-binding By similarity
Motif183 – 1853TXY
Compositional bias2 – 76Poly-Ala

Sites

Active site1471Proton acceptor By similarity
Binding site521ATP By similarity
Binding site521Inhibitor By similarity
Binding site1061Inhibitor; via amide nitrogen and carbonyl oxygen By similarity
Binding site1121Inhibitor By similarity
Binding site1521Inhibitor By similarity
Binding site1641Inhibitor By similarity
Binding site1651Inhibitor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue271Phosphoserine; by SGK1 By similarity
Modified residue1831Phosphothreonine; by MAP2K1 and MAP2K2 Ref.6 Ref.15 Ref.16 Ref.17 Ref.18
Modified residue1851Phosphotyrosine; by MAP2K1 and MAP2K2 Ref.6 Ref.15 Ref.16 Ref.17 Ref.18
Modified residue1881Phosphothreonine; by autocatalysis By similarity
Modified residue2441Phosphoserine By similarity
Modified residue2461Phosphoserine By similarity
Modified residue2821Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63085 [UniParc].

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

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

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

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

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

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

       310        320        330        340        350 
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA RFQPGYRS 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"ISG15 modulates development of the erythroid lineage."
Maragno A.L., Pironin M., Alcalde H., Cong X., Knobeloch K.P., Tangy F., Zhang D.E., Ghysdael J., Quang C.T.
PLoS ONE 6:E26068-E26068(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
+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.
PIRS16444.
RefSeqNP_001033752.1. NM_001038663.1.
NP_036079.1. NM_011949.3.
XP_006522210.1. XM_006522147.1.
UniGeneMm.196581.

3D structure databases

ProteinModelPortalP63085.
SMRP63085. Positions 10-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204966. 29 interactions.
DIPDIP-661N.
IntActP63085. 21 interactions.
MINTMINT-125264.

Chemistry

BindingDBP63085.
ChEMBLCHEMBL2111454.

PTM databases

PhosphoSiteP63085.

Proteomic databases

PaxDbP63085.
PRIDEP63085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358.
ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358.
ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
GeneID26413.
KEGGmmu:26413.
UCSCuc007yjq.1. mouse.

Organism-specific databases

CTD5594.
MGIMGI:1346858. Mapk1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP63085.
KOK04371.
OMAVCSAYDR.
OrthoDBEOG7M3J0K.
PhylomeDBP63085.
TreeFamTF105097.

Enzyme and pathway databases

ReactomeREACT_105924. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_188257. Signal Transduction.
REACT_98458. Immune System.

Gene expression databases

ArrayExpressP63085.
BgeeP63085.
CleanExMM_MAPK1.
GenevestigatorP63085.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008349. MAPK_ERK1/2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24055:SF111. PTHR24055:SF111. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01770. ERK1ERK2MAPK.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPK1. mouse.
NextBio304409.
PROP63085.
SOURCESearch...

Entry information

Entry nameMK01_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot