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Protein

Mitogen-activated protein kinase 1

Gene

Mapk1

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, 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).By similarity
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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATPPROSITE-ProRule annotation
Binding sitei52 – 521InhibitorBy similarity
Binding sitei106 – 1061Inhibitor; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei112 – 1121InhibitorBy similarity
Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation
Binding sitei152 – 1521InhibitorBy similarity
Binding sitei164 – 1641InhibitorBy similarity
Binding sitei165 – 1651InhibitorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: MGI
  • MAP kinase activity Source: MGI
  • phosphatase binding Source: MGI
  • phosphotyrosine binding Source: MGI
  • protein kinase activity Source: MGI
  • protein serine/threonine kinase activity Source: UniProtKB
  • RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • B cell receptor signaling pathway Source: MGI
  • caveolin-mediated endocytosis Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: MGI
  • cytosine metabolic process Source: MGI
  • ERBB signaling pathway Source: MGI
  • ERK1 and ERK2 cascade Source: MGI
  • labyrinthine layer blood vessel development Source: MGI
  • lipopolysaccharide-mediated signaling pathway Source: MGI
  • long-term synaptic potentiation Source: MGI
  • lung morphogenesis Source: MGI
  • mammary gland epithelial cell proliferation Source: MGI
  • MAPK cascade Source: MGI
  • MAPK import into nucleus Source: Ensembl
  • negative regulation of cell differentiation Source: MGI
  • organ morphogenesis Source: MGI
  • peptidyl-serine phosphorylation Source: UniProtKB
  • peptidyl-threonine phosphorylation Source: UniProtKB
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of peptidyl-threonine phosphorylation Source: MGI
  • positive regulation of transcription, DNA-templated Source: Ensembl
  • positive regulation of translation Source: Ensembl
  • protein phosphorylation Source: MGI
  • regulation of cytoskeleton organization Source: UniProtKB
  • regulation of early endosome to late endosome transport Source: UniProtKB
  • regulation of Golgi inheritance Source: UniProtKB
  • regulation of protein stability Source: UniProtKB
  • regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • regulation of stress-activated MAPK cascade Source: UniProtKB
  • response to epidermal growth factor Source: UniProtKB
  • response to estrogen Source: Ensembl
  • response to exogenous dsRNA Source: MGI
  • response to lipopolysaccharide Source: MGI
  • response to toxic substance Source: Ensembl
  • sensory perception of pain Source: Ensembl
  • T cell receptor signaling pathway Source: MGI
  • trachea formation Source: MGI
  • 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

BRENDAi2.7.11.24. 3474.
ReactomeiREACT_272921. Regulation of HSF1-mediated heat shock response.
REACT_275222. Thrombin signalling through proteinase activated receptors (PARs).
REACT_293022. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_299247. ERKs are inactivated.
REACT_305463. Oxidative Stress Induced Senescence.
REACT_306352. phospho-PLA2 pathway.
REACT_310086. RSK activation.
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_327612. CREB phosphorylation through the activation of Ras.
REACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_339798. NCAM signaling for neurite out-growth.
REACT_339940. Oncogene Induced Senescence.
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_353300. ERK2 activation.
REACT_353319. Signal transduction by L1.
REACT_353475. Recycling pathway of L1.
REACT_357393. Negative regulation of FGFR2 signaling.
REACT_357788. Signaling by FGFR3.
REACT_357826. Negative regulation of FGFR3 signaling.
REACT_357953. Signaling by FGFR1.
REACT_358477. Negative regulation of FGFR4 signaling.
REACT_358608. RHO GTPases Activate WASPs and WAVEs.
REACT_359435. Negative regulation of FGFR1 signaling.
REACT_359980. Signaling by FGFR2.
REACT_361608. Signaling by FGFR4.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 1 (EC:2.7.11.24)
Short name:
MAP kinase 1
Short name:
MAPK 1
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 namesi
Name:Mapk1
Synonyms:Erk2, Mapk, Prkm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1346858. Mapk1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: Ensembl
  • caveola Source: UniProtKB
  • cytoplasm Source: MGI
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: Ensembl
  • early endosome Source: UniProtKB
  • extracellular exosome Source: MGI
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • late endosome Source: UniProtKB
  • microtubule cytoskeleton Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • protein complex Source: Ensembl
  • pseudopodium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 358357Mitogen-activated protein kinase 1PRO_0000186248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei27 – 271Phosphoserine; by SGK1By similarity
Modified residuei183 – 1831Phosphothreonine; by MAP2K1 and MAP2K25 Publications
Modified residuei185 – 1851Phosphotyrosine; by MAP2K1 and MAP2K25 Publications
Modified residuei188 – 1881Phosphothreonine; by autocatalysisBy similarity
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei282 – 2821PhosphoserineBy similarity

Post-translational modificationi

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).By similarity
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP63085.
PaxDbiP63085.
PRIDEiP63085.

PTM databases

PhosphoSiteiP63085.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiP63085.
CleanExiMM_MAPK1.
ExpressionAtlasiP63085. baseline and differential.
GenevisibleiP63085. MM.

Interactioni

Subunit structurei

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 1 of NEK2. Interacts (via phosphorylated form) with TPR (via C-terminal 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 1 binding prevents from dephosphorylation and inactivation. The phosphorylated form interacts with PML (By similarity). Interacts with STYX (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4Q621083EBI-397697,EBI-300895
Dusp6Q9DBB12EBI-397697,EBI-7812384
GSK3BP498412EBI-397697,EBI-373586From a different organism.
Hivep1Q031724EBI-397697,EBI-646850
Mknk2Q8CDB023EBI-397697,EBI-646209
Nupl1Q8R332-13EBI-397697,EBI-646962
PtprrQ621325EBI-397697,EBI-6954051
Rps6ka4Q9Z2B93EBI-397697,EBI-412887

Protein-protein interaction databases

BioGridi204966. 34 interactions.
DIPiDIP-661N.
IntActiP63085. 23 interactions.
MINTiMINT-125264.
STRINGi10090.ENSMUSP00000023462.

Structurei

3D structure databases

ProteinModelPortaliP63085.
SMRiP63085. Positions 10-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 311289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 1064Inhibitor-bindingBy similarity
Regioni151 – 1522Inhibitor-bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 76Poly-Ala

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.
InParanoidiP63085.
KOiK04371.
OMAiRINMEND.
OrthoDBiEOG7M3J0K.
PhylomeDBiP63085.
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.

P63085-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA
60 70 80 90 100
IKKISPFEHQ TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY
110 120 130 140 150
IVQDLMETDL YKLLKTQHLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP
160 170 180 190 200
SNLLLNTTCD LKICDFGLAR VADPDHDHTG FLTEYVATRW YRAPEIMLNS
210 220 230 240 250
KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG ILGSPSQEDL
260 270 280 290 300
NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI
310 320 330 340 350
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA

RFQPGYRS
Length:358
Mass (Da):41,276
Last modified:January 23, 2007 - v3
Checksum:i3BBCF22471EDBA0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27992.1.
PIRiS16444.
RefSeqiNP_001033752.1. NM_001038663.1.
NP_036079.1. NM_011949.3.
XP_006522210.1. XM_006522147.2.
UniGeneiMm.196581.

Genome annotation databases

EnsembliENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358.
ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358.
ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
GeneIDi26413.
KEGGimmu:26413.
UCSCiuc007yjq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27992.1.
PIRiS16444.
RefSeqiNP_001033752.1. NM_001038663.1.
NP_036079.1. NM_011949.3.
XP_006522210.1. XM_006522147.2.
UniGeneiMm.196581.

3D structure databases

ProteinModelPortaliP63085.
SMRiP63085. Positions 10-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204966. 34 interactions.
DIPiDIP-661N.
IntActiP63085. 23 interactions.
MINTiMINT-125264.
STRINGi10090.ENSMUSP00000023462.

Chemistry

BindingDBiP63085.
ChEMBLiCHEMBL2111454.

PTM databases

PhosphoSiteiP63085.

Proteomic databases

MaxQBiP63085.
PaxDbiP63085.
PRIDEiP63085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358.
ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358.
ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
GeneIDi26413.
KEGGimmu:26413.
UCSCiuc007yjq.1. mouse.

Organism-specific databases

CTDi5594.
MGIiMGI:1346858. Mapk1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP63085.
KOiK04371.
OMAiRINMEND.
OrthoDBiEOG7M3J0K.
PhylomeDBiP63085.
TreeFamiTF105097.

Enzyme and pathway databases

BRENDAi2.7.11.24. 3474.
ReactomeiREACT_272921. Regulation of HSF1-mediated heat shock response.
REACT_275222. Thrombin signalling through proteinase activated receptors (PARs).
REACT_293022. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_299247. ERKs are inactivated.
REACT_305463. Oxidative Stress Induced Senescence.
REACT_306352. phospho-PLA2 pathway.
REACT_310086. RSK activation.
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_327612. CREB phosphorylation through the activation of Ras.
REACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_339798. NCAM signaling for neurite out-growth.
REACT_339940. Oncogene Induced Senescence.
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_353300. ERK2 activation.
REACT_353319. Signal transduction by L1.
REACT_353475. Recycling pathway of L1.
REACT_357393. Negative regulation of FGFR2 signaling.
REACT_357788. Signaling by FGFR3.
REACT_357826. Negative regulation of FGFR3 signaling.
REACT_357953. Signaling by FGFR1.
REACT_358477. Negative regulation of FGFR4 signaling.
REACT_358608. RHO GTPases Activate WASPs and WAVEs.
REACT_359435. Negative regulation of FGFR1 signaling.
REACT_359980. Signaling by FGFR2.
REACT_361608. Signaling by FGFR4.

Miscellaneous databases

ChiTaRSiMapk1. mouse.
NextBioi304409.
PROiP63085.
SOURCEiSearch...

Gene expression databases

BgeeiP63085.
CleanExiMM_MAPK1.
ExpressionAtlasiP63085. baseline and differential.
GenevisibleiP63085. MM.

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. "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.
    , 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. 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. 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. 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. Cited for: ISGYLATION.

Entry informationi

Entry nameiMK01_MOUSE
AccessioniPrimary (citable) accession number: P63085
Secondary accession number(s): P27703, Q3V1U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 136 of the entry and version 3 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.