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Q63844 (MK03_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 3

Short name=MAP kinase 3
Short name=MAPK 3
EC=2.7.11.24
Alternative name(s):
ERT2
Extracellular signal-regulated kinase 1
Short name=ERK-1
Insulin-stimulated MAP2 kinase
MAP kinase isoform p44
Short name=p44-MAPK
MNK1
Microtubule-associated protein 2 kinase
p44-ERK1
Gene names
Name:Mapk3
Synonyms:Erk1, Prkm3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length380 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, 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. Ref.11 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on Thr-203 and Tyr-205 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. Dephosphorylated and inactivated by DUSP3, DUSP6 and DUSP9.

Subunit structure

Binds both upstream activators and downstream substrates in multimolecular complexes. Found in a complex with at least BRAF, HRAS, MAP2K1/MEK1, MAPK3 and RGS14. Interacts with TPR By similarity. Interacts with ADAM15, ARRB2, CANX, DAPK1 (via death domain), HSF4, IER3, MAP2K1/MEK1, NISCH, and SGK1 By similarity. Interacts with MORG1, PEA15 and MKNK2. MKNK2 isoform 1binding prevents from dephosphorylation and inactivation. Ref.11 Ref.13 Ref.15

Subcellular location

Cytoplasm. Nucleus. Note: Autophosphorylation at Thr-207 promotes nuclear localization By similarity. PEA15-binding redirects the biological outcome of MAPK3 kinase-signaling by sequestering MAPK3 into the cytoplasm. Ref.11 Ref.12

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. Ligand-activated ALK induces tyrosine phosphorylation By similarity. Dephosphorylated by PTPRJ at Tyr-205 By similarity. Autophosphorylated on threonine and tyrosine residues in vitro. Phosphorylated upon FLT3 and KIT signaling By similarity. Ref.9 Ref.10 Ref.14 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 processApoptosis
Cell cycle
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

MAPK cascade

Inferred from direct assay PubMed 15314156. Source: GOC

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cartilage development

Inferred from direct assay PubMed 17644814. Source: MGI

caveolin-mediated endocytosis

Traceable author statement Ref.22. 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

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

interleukin-1-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from direct assay PubMed 12872135. Source: MGI

negative regulation of apolipoprotein binding

Inferred from mutant phenotype PubMed 20037141. Source: BHF-UCL

organ morphogenesis

Inferred from direct assay PubMed 11684667. Source: MGI

peptidyl-tyrosine autophosphorylation

Inferred from electronic annotation. Source: Ensembl

phosphorylation

Traceable author statement PubMed 12223545. Source: MGI

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 11841548PubMed 15383658. Source: MGI

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

Inferred from mutant phenotype PubMed 7889942. Source: UniProtKB

regulation of stress-activated MAPK cascade

Traceable author statement Ref.22. Source: UniProtKB

response to epidermal growth factor

Inferred from sequence or structural similarity. Source: UniProtKB

response to exogenous dsRNA

Inferred from direct assay PubMed 12872135. Source: MGI

response to lipopolysaccharide

Inferred from direct assay PubMed 12872135. Source: MGI

sensory perception of pain

Inferred from mutant phenotype PubMed 11356865. Source: UniProtKB

signal transduction

Traceable author statement PubMed 11684667. Source: MGI

transcription, DNA-templated

Inferred from mutant phenotype PubMed 7889942. Source: UniProtKB

   Cellular_componentGolgi apparatus

Traceable author statement Ref.22. Source: UniProtKB

caveola

Traceable author statement Ref.22. Source: UniProtKB

cytoplasm

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

cytoskeleton

Traceable author statement Ref.22. Source: UniProtKB

cytosol

Traceable author statement Ref.22. Source: UniProtKB

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 cytoskeleton

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Traceable author statement Ref.22. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.22. Source: UniProtKB

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 15314156. Source: MGI

phosphotyrosine binding

Inferred from mutant phenotype PubMed 14636584. Source: MGI

protein kinase activity

Inferred from direct assay PubMed 15383658. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 380379Mitogen-activated protein kinase 3
PRO_0000186252

Regions

Domain43 – 331289Protein kinase
Nucleotide binding49 – 579ATP By similarity
Motif203 – 2053TXY

Sites

Active site1671Proton acceptor By similarity
Binding site721ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue1711Phosphoserine By similarity
Modified residue1991Phosphothreonine By similarity
Modified residue2031Phosphothreonine; by MAP2K1 and MAP2K2 Ref.16 Ref.17 Ref.19
Modified residue2051Phosphotyrosine; by MAP2K1 and MAP2K2 Ref.16 Ref.17 Ref.19
Modified residue2081Phosphothreonine; by autocatalysis By similarity

Experimental info

Sequence conflict1781T → P in CAA45889. Ref.7
Sequence conflict1781T → P no nucleotide entry Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q63844 [UniParc].

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

FASTA38043,066
        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

References

« Hide '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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 171-205.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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-203 AND TYR-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[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-203 AND TYR-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[18]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-203 AND TYR-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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
BC013754 mRNA. Translation: AAH13754.1.
BC029712 mRNA. Translation: AAH29712.1.
S58470 mRNA. Translation: AAB19973.1.
X64605 mRNA. Translation: CAA45889.1.
PIRS28184.
RefSeqNP_036082.1. NM_011952.2.
UniGeneMm.8385.

3D structure databases

ProteinModelPortalQ63844.
SMRQ63844. Positions 25-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204970. 11 interactions.
DIPDIP-31078N.
IntActQ63844. 7 interactions.
MINTMINT-1524109.

Chemistry

ChEMBLCHEMBL2111454.

PTM databases

PhosphoSiteQ63844.

Proteomic databases

PaxDbQ63844.
PRIDEQ63844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065.
GeneID26417.
KEGGmmu:26417.
UCSCuc009jsm.1. mouse.

Organism-specific databases

CTD5595.
MGIMGI:1346859. Mapk3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074298.
HOGENOMHOG000233024.
HOVERGENHBG014652.
KOK04371.
PhylomeDBQ63844.
TreeFamTF105097.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ63844.
BgeeQ63844.
CleanExMM_MAPK3.
GenevestigatorQ63844.

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

ChiTaRSMAPK3. mouse.
NextBio304429.
PROQ63844.
SOURCESearch...

Entry information

Entry nameMK03_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 150 of the entry and version 5 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