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Protein

Mitogen-activated protein kinase 3

Gene

Mapk3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATPPROSITE-ProRule annotation
Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: MGI
  3. phosphatase binding Source: MGI
  4. phosphotyrosine binding Source: MGI
  5. protein kinase activity Source: MGI

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. BMP signaling pathway Source: MGI
  3. cartilage development Source: MGI
  4. caveolin-mediated endocytosis Source: UniProtKB
  5. cell cycle Source: UniProtKB-KW
  6. cellular response to DNA damage stimulus Source: MGI
  7. cellular response to mechanical stimulus Source: Ensembl
  8. DNA damage induced protein phosphorylation Source: MGI
  9. interleukin-1-mediated signaling pathway Source: MGI
  10. lipopolysaccharide-mediated signaling pathway Source: MGI
  11. lung morphogenesis Source: MGI
  12. MAPK cascade Source: GOC
  13. negative regulation of apolipoprotein binding Source: BHF-UCL
  14. organ morphogenesis Source: MGI
  15. peptidyl-tyrosine autophosphorylation Source: MGI
  16. phosphorylation Source: MGI
  17. positive regulation of ERK1 and ERK2 cascade Source: MGI
  18. positive regulation of histone acetylation Source: MGI
  19. positive regulation of histone phosphorylation Source: MGI
  20. positive regulation of protein phosphorylation Source: MGI
  21. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  22. protein phosphorylation Source: MGI
  23. regulation of cytoskeleton organization Source: UniProtKB
  24. regulation of early endosome to late endosome transport Source: UniProtKB
  25. regulation of Golgi inheritance Source: UniProtKB
  26. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  27. regulation of stress-activated MAPK cascade Source: UniProtKB
  28. response to epidermal growth factor Source: UniProtKB
  29. response to exogenous dsRNA Source: MGI
  30. response to lipopolysaccharide Source: MGI
  31. sensory perception of pain Source: UniProtKB
  32. signal transduction Source: MGI
  33. trachea formation Source: MGI
  34. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_272921. Regulation of HSF1-mediated heat shock response.
REACT_275222. Thrombin signalling through proteinase activated receptors (PARs).
REACT_277805. ERK1 activation.
REACT_289225. ISG15 antiviral mechanism.
REACT_293022. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_299247. ERKs are inactivated.
REACT_305463. Oxidative Stress Induced Senescence.
REACT_314186. FCERI mediated MAPK activation.
REACT_317434. Growth hormone receptor signaling.
REACT_320943. Activation of the AP-1 family of transcription factors.
REACT_323000. ERK/MAPK targets.
REACT_332023. Negative regulation of FGFR signaling.
REACT_333431. Signal attenuation.
REACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_339798. NCAM signaling for neurite out-growth.
REACT_339940. Oncogene Induced Senescence.
REACT_341193. Signaling by FGFR.
REACT_341392. RNA Polymerase I Promoter Opening.
REACT_342554. Advanced glycosylation endproduct receptor signaling.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.
REACT_350665. Senescence-Associated Secretory Phenotype (SASP).
REACT_353319. Signal transduction by L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 3 (EC:2.7.11.24)
Short name:
MAP kinase 3
Short name:
MAPK 3
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 namesi
Name:Mapk3
Synonyms:Erk1, Prkm3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1346859. Mapk3.

Subcellular locationi

  1. Cytoplasm
  2. Nucleus

  3. 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.By similarity

GO - Cellular componenti

  1. caveola Source: UniProtKB
  2. cytoplasm Source: MGI
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: UniProtKB
  5. early endosome Source: UniProtKB
  6. extracellular vesicular exosome Source: MGI
  7. focal adhesion Source: UniProtKB
  8. Golgi apparatus Source: UniProtKB
  9. late endosome Source: UniProtKB
  10. microtubule cytoskeleton Source: MGI
  11. mitochondrion Source: UniProtKB
  12. nuclear envelope Source: MGI
  13. nucleoplasm Source: MGI
  14. nucleus Source: UniProtKB
  15. pseudopodium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 380379Mitogen-activated protein kinase 3PRO_0000186252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei199 – 1991PhosphothreonineBy similarity
Modified residuei203 – 2031Phosphothreonine; by MAP2K1 and MAP2K23 Publications
Modified residuei205 – 2051Phosphotyrosine; by MAP2K1 and MAP2K23 Publications
Modified residuei208 – 2081Phosphothreonine; by autocatalysisBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ63844.
PaxDbiQ63844.
PRIDEiQ63844.

PTM databases

PhosphoSiteiQ63844.

Expressioni

Gene expression databases

BgeeiQ63844.
CleanExiMM_MAPK3.
ExpressionAtlasiQ63844. baseline and differential.
GenevestigatoriQ63844.

Interactioni

Subunit structurei

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 1 binding prevents from dephosphorylation and inactivation. Interacts with CDKN2AIP.By similarity3 Publications

Protein-protein interaction databases

BioGridi204970. 12 interactions.
DIPiDIP-31078N.
IntActiQ63844. 7 interactions.
MINTiMINT-1524109.

Structurei

3D structure databases

ProteinModelPortaliQ63844.
SMRiQ63844. Positions 25-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 331289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi203 – 2053TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ63844.
KOiK04371.
PhylomeDBiQ63844.
TreeFamiTF105097.

Family and domain databases

InterProiIPR011009. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01770. ERK1ERK2MAPK.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG
60 70 80 90 100
EGAYGMVSSA YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN
110 120 130 140 150
VIGIRDILRA PTLEAMRDVY IVQDLMETDL YKLLKSQQLS NDHICYFLYQ
160 170 180 190 200
ILRGLKYIHS ANVLHRDLKP SNLLINTTCD LKICDFGLAR IADPEHDHTG
210 220 230 240 250
FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML SNRPIFPGKH
260 270 280 290 300
YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS
310 320 330 340 350
DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE PVAEEPFTFD
360 370 380
MELDDLPKER LKELIFQETA RFQPGAPEGP
Length:380
Mass (Da):43,066
Last modified:January 23, 2007 - v5
Checksum:i49C14A95B627237F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781T → P in CAA45889 (PubMed:8444355).Curated
Sequence conflicti178 – 1781T → P no nucleotide entry (PubMed:1459009).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC013754 mRNA. Translation: AAH13754.1.
BC029712 mRNA. Translation: AAH29712.1.
S58470 mRNA. Translation: AAB19973.1.
X64605 mRNA. Translation: CAA45889.1.
CCDSiCCDS21841.1.
PIRiS28184.
RefSeqiNP_036082.1. NM_011952.2.
UniGeneiMm.8385.

Genome annotation databases

EnsembliENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065.
GeneIDi26417.
KEGGimmu:26417.
UCSCiuc009jsm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC013754 mRNA. Translation: AAH13754.1.
BC029712 mRNA. Translation: AAH29712.1.
S58470 mRNA. Translation: AAB19973.1.
X64605 mRNA. Translation: CAA45889.1.
CCDSiCCDS21841.1.
PIRiS28184.
RefSeqiNP_036082.1. NM_011952.2.
UniGeneiMm.8385.

3D structure databases

ProteinModelPortaliQ63844.
SMRiQ63844. Positions 25-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204970. 12 interactions.
DIPiDIP-31078N.
IntActiQ63844. 7 interactions.
MINTiMINT-1524109.

Chemistry

ChEMBLiCHEMBL2111454.

PTM databases

PhosphoSiteiQ63844.

Proteomic databases

MaxQBiQ63844.
PaxDbiQ63844.
PRIDEiQ63844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065.
GeneIDi26417.
KEGGimmu:26417.
UCSCiuc009jsm.1. mouse.

Organism-specific databases

CTDi5595.
MGIiMGI:1346859. Mapk3.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ63844.
KOiK04371.
PhylomeDBiQ63844.
TreeFamiTF105097.

Enzyme and pathway databases

ReactomeiREACT_272921. Regulation of HSF1-mediated heat shock response.
REACT_275222. Thrombin signalling through proteinase activated receptors (PARs).
REACT_277805. ERK1 activation.
REACT_289225. ISG15 antiviral mechanism.
REACT_293022. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_299247. ERKs are inactivated.
REACT_305463. Oxidative Stress Induced Senescence.
REACT_314186. FCERI mediated MAPK activation.
REACT_317434. Growth hormone receptor signaling.
REACT_320943. Activation of the AP-1 family of transcription factors.
REACT_323000. ERK/MAPK targets.
REACT_332023. Negative regulation of FGFR signaling.
REACT_333431. Signal attenuation.
REACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_339798. NCAM signaling for neurite out-growth.
REACT_339940. Oncogene Induced Senescence.
REACT_341193. Signaling by FGFR.
REACT_341392. RNA Polymerase I Promoter Opening.
REACT_342554. Advanced glycosylation endproduct receptor signaling.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.
REACT_350665. Senescence-Associated Secretory Phenotype (SASP).
REACT_353319. Signal transduction by L1.

Miscellaneous databases

ChiTaRSiMapk3. mouse.
NextBioi304429.
PROiQ63844.
SOURCEiSearch...

Gene expression databases

BgeeiQ63844.
CleanExiMM_MAPK3.
ExpressionAtlasiQ63844. baseline and differential.
GenevestigatoriQ63844.

Family and domain databases

InterProiIPR011009. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01770. ERK1ERK2MAPK.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiMK03_MOUSE
AccessioniPrimary (citable) accession number: Q63844
Secondary accession number(s): Q61531, Q8K0X5, Q91YW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 162 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.