Mitogen-activated protein kinase 3 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q63844 (MK03_MOUSE)

Last modified October 13, 2009. Version 101. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase 3
    EC=2.7.11.24
Alternative name(s):
    Extracellular signal-regulated kinase 1
      Short name=ERK-1
    Insulin-stimulated MAP2 kinase
    MAP kinase 1
      Short name=MAPK 1
    p44-ERK1
    ERT2
    p44-MAPK
    Microtubule-associated protein 2 kinase
    MNK1

Gene names

Name:	Mapk3
Synonyms:	Erk1, Prkm3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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 ELK-1. 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 tyrosine and threonine phosphorylation.
Subunit structure	Interacts with HSF4 and NISCH By similarity. Interacts with MORG1.
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-203 and Tyr-205, which activates the enzyme By similarity. Autophosphorylates on threonine and tyrosine residues in vitro.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Hide | Top

Ontologies

Keywords
Biological process	Cell cycle
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cartilage development Inferred from direct assay. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW lipopolysaccharide-mediated signaling pathway Inferred from direct assay. Source: MGI organ morphogenesis Inferred from direct assay. Source: MGI protein amino acid phosphorylation Inferred from direct assay. Source: MGI regulation of transcription factor activity Inferred from mutant phenotype. Source: UniProtKB 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 sensory perception of pain Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from mutant phenotype. Source: MGI phosphotyrosine binding Inferred from mutant phenotype. Source: MGI transcription factor activity Inferred from Experiment. Source: Reactome
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 380

379

Mitogen-activated protein kinase 3

PRO_0000186252

Regions

Domain

43 – 331

289

Protein kinase

Nucleotide binding

49 – 57

ATP By similarity

Motif

203 – 205

TXY

Sites

Active site

167

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.2

Modified residue

203

Phosphothreonine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Modified residue

205

Phosphotyrosine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Experimental info

Sequence conflict

178

T → P in CAA45889. Ref.7

Sequence conflict

178

T → P Ref.8

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q63844-1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 49C14A95B627237F
Show »

FASTA

380

43,066

        10         20         30         40         50         60 
MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA 

        70         80         90        100        110        120 
YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY 

       130        140        150        160        170        180 
IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD 

       190        200        210        220        230        240 
LKICDFGLAR IADPEHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML 

       250        260        270        280        290        300 
SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS 

       310        320        330        340        350        360 
DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE PVAEEPFTFD MELDDLPKER 

       370        380 
LKELIFQETA RFQPGAPEGP

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Strain: FVB/N. Tissue: Kidney and Mammary tumor.
[2]	Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-65; 89-105; 110-132; 157-209; 213-221; 280-288; 304-319 AND 361-371, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[3]	"Molecular cloning of a mouse extracellular signal regulated kinase (erk-1)." Tanner B., Mueckler M. Biochim. Biophys. Acta 1171:319-320(1993) [PubMed: 8424957] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-380.
[4]	"Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine." Crews C.M., Alessandrini A.A., Erikson R.L. Proc. Natl. Acad. Sci. U.S.A. 88:8845-8849(1991) [PubMed: 1717989] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-19. Tissue: Pre-B cell.
[5]	"Molecular analysis of microtubule-associated protein-2 kinase cDNA from mouse and rat brain." de Miguel C., Kligman D., Patel J., Detera-Wadleigh S.D. DNA Cell Biol. 10:505-514(1991) [PubMed: 1716439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-380. Tissue: Fetal brain.
[6]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 136-153 AND 191-209, MASS SPECTROMETRY. Tissue: Hippocampus.
[7]	"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 171-209. Strain: CBA. Tissue: Bone marrow.
[8]	"Identification of new protein kinase genes, similar to kinases of the cdc2 family and expressed in murine hematopoietic stem cells." Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V. Dokl. Akad. Nauk SSSR 324:893-897(1992) [PubMed: 1459009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 171-205.
[9]	"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.
[10]	"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.
[11]	"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-203 AND TYR-205, MASS SPECTROMETRY. Tissue: Mast cell.
[12]	"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-203 AND TYR-205, MASS SPECTROMETRY.
[13]	"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-203 AND TYR-205, MASS SPECTROMETRY. Tissue: Brain.
[14]	"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: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, MASS SPECTROMETRY.
[15]	"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: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
	BC013754 mRNA. Translation: AAH13754.1. BC029712 mRNA. Translation: AAH29712.1. S58470 mRNA. Translation: AAB19973.1. X64605 mRNA. Translation: CAA45889.1.
IPI	IPI00230277.
PIR	S28184.
RefSeq	NP_036082.1.
UniGene	Mm.8385
3D structure databases
HSSP	HSSP built from PDB template 1PME based on UniProtKB P28482.
SMR	Q63844. Positions 29-373, 30-374.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63844.
PTM databases
PhosphoSite	Q63844.
Proteomic databases
PRIDE	Q63844.
Genome annotation databases
Ensembl	ENSMUST00000050201; ENSMUSP00000101969; ENSMUSG00000063065; Mus musculus. [Genome view] ENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065; Mus musculus. [Genome view]
GeneID	26417.
KEGG	mmu:26417.
NMPDR	fig\|10090.3.peg.17639.
UCSC	uc009jsm.1. mouse.
Organism-specific databases
CTD	26417.
MGI	MGI:1346859. Mapk3.
Phylogenomic databases
HOGENOM	Q63844.
HOVERGEN	Q63844.
Enzyme and pathway databases
BRENDA	2.7.11.24. 244.
Gene expression databases
ArrayExpress	Q63844.
Bgee	Q63844.
CleanEx	MM_MAPK3.
Genevestigator	Q63844.
GermOnline	ENSMUSG00000063065. Mus musculus.
Family and domain databases
InterPro	IPR008349. Erk_1_2_MAPK. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01770. ERK1ERK2MAPK.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
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 Resources
NextBio	304429.
SOURCE	Search...

Hide | Top

Entry information

Entry name

MK03_MOUSE

Accession

Primary (citable) accession number: Q63844
Secondary accession number(s): Q61531, Q8K0X5, Q91YW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 101 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

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

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents