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Reviewed, UniProtKB/Swiss-Prot P63085 (MK01_MOUSE)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

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

Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2) and heat shock factor protein 4 (HSF4) By similarity. Phosphorylates SPZ1.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by phosphorylation on tyrosine and threonine in response to insulin and NGF. Both phosphorylations are required for activity By similarity.

Subunit structure

Interacts with HSF4 and NISCH By similarity. Interacts with MORG1.

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.

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 processCell cycle
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processB cell receptor signaling pathway

Inferred from direct assay. Source: MGI

MAPKKK cascade

Inferred from direct assay. Source: MGI

T cell receptor signaling pathway

Inferred from direct assay. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cytosine metabolic process

Inferred from direct assay. Source: MGI

lipopolysaccharide-mediated signaling pathway

Inferred from direct assay. Source: MGI

negative regulation of cell differentiation

Inferred from genetic interaction. Source: MGI

organ morphogenesis

Inferred from direct assay. Source: MGI

protein amino acid phosphorylation

Inferred from direct assay. Source: MGI

response to DNA damage stimulus

Inferred from direct assay. Source: MGI

response to exogenous dsRNA

Inferred from direct assay. Source: MGI

response to lipopolysaccharide

Inferred from direct assay. Source: MGI

   Cellular componentcytoplasm

Inferred from direct assay. Source: MGI

nucleoplasm

Inferred from Experiment. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

MAP kinase 2 activity

Inferred from direct assay. Source: MGI

phosphotyrosine binding

Inferred from mutant phenotype. Source: MGI

transcription factor activity

Inferred from Experiment. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCL2L11O43521-11EBI-397697,EBI-526416From a different organism.
ELK1P194191EBI-397697,EBI-726632From a different organism.
GSK3BP498411EBI-397697,EBI-373586From a different organism.
Hivep1Q031723EBI-397697,EBI-646850
Mknk1O086052EBI-397697,EBI-646859
Mknk2Q8CDB03EBI-397697,EBI-646209
Rps6ka4Q9Z2B92EBI-397697,EBI-412887

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
Motif183 – 1853TXY
Compositional bias2 – 76Poly-Ala

Sites

Active site1471Proton acceptor By similarity
Binding site521ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1831Phosphothreonine
Modified residue1851Phosphotyrosine
Modified residue1881Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63085-1 [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: 1649458] [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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 54-65; 76-89; 137-146 AND 171-189, MASS SPECTROMETRY.
Tissue: Hippocampus.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 137-146 AND 193-201, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"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: 8444355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-190.
Strain: CBA.
Tissue: Bone marrow.
[7]"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: 1849075] [Abstract]
Cited for: PHOSPHORYLATION AT THR-183 AND TYR-185, PARTIAL PROTEIN SEQUENCE.
[8]"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: 15118098] [Abstract]
Cited for: INTERACTION WITH MORG1.
[9]"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: 15899793] [Abstract]
Cited for: PHOSPHORYLATION OF SPZ1.
[10]"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: 17947660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
Tissue: Mast cell.
[11]"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-183 AND TYR-185, MASS SPECTROMETRY.
[12]"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: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
Tissue: Brain.
[13]"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: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
NP_036079.1.
UniGeneMm.196581

3D structure databases

SMRP63085. Positions 9-353, 10-354.
ModBaseSearch...

Protein-protein interaction databases

IntActP63085.

PTM databases

PhosphoSiteP63085.

Genome annotation databases

EnsemblENSMUSG00000063358. Mus musculus. [Contig view]
GeneID26413.
KEGGmmu:26413.
NMPDRfig|10090.3.peg.30922.

Organism-specific databases

MGIMGI:1346858. Mapk1.

Phylogenomic databases

HOGENOMP63085.
HOVERGENP63085.

Gene expression databases

ArrayExpressP63085.
CleanExMM_MAPK1.
GermOnlineENSMUSG00000063358. Mus musculus.

Family and domain databases

InterProIPR008349. Erk_1_2_MAPK.
IPR003527. MAP_kin_CS.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01770. ERK1ERK2MAPK.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
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 Resources

NextBio304409.
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: November 25, 2008
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents