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UniProtKB/Swiss-Prot entry P27361


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MK03_HUMAN
Primary accession number P27361
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 111)
Name and origin of the protein
Protein name Mitogen-activated protein kinase 3
Synonyms EC 2.7.11.24
Extracellular signal-regulated kinase 1
ERK-1
Insulin-stimulated MAP2 kinase
MAP kinase 1
MAPK 1
p44-ERK1
ERT2
p44-MAPK
Microtubule-associated protein 2 kinase
Gene name
Name: MAPK3
Synonyms: ERK1, PRKM3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
PubMed=7687743 [NCBI, ExPASy, EBI, Israel, Japan]
Charest D.L., Jirik F., Harder K., Pelech S.L., Mordret G.;
"Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1.";
Mol. Cell. Biol. 13:4679-4690(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-15; 33-41; 88-94; 117-131; 212-220; 279-287; 303-318 AND 360-370, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-379.
DOI=10.1016/0006-291X(92)91891-S; PubMed=1540184 [NCBI, ExPASy, EBI, Israel, Japan]
Owaki H., Makar R., Boulton T.G., Cobb M.H., Geppert T.D.;
"Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs.";
Biochem. Biophys. Res. Commun. 182:1416-1422(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-379.
DOI=10.1016/0014-5793(92)80612-K; PubMed=1319925 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez F.A., Raden D.L., Rigby M.R., Davis R.J.;
"Heterogeneous expression of four MAP kinase isoforms in human tissues.";
FEBS Lett. 304:170-178(1992).
[6]
INTERACTION WITH HIV-1 NEF.
PubMed=8794306 [NCBI, ExPASy, EBI, Israel, Japan]
Greenway A.L., Azad A., Mills J., McPhee D.A.;
"Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity.";
J. Virol. 70:6701-6708(1996).
[7]
INTERACTION WITH NISCH.
DOI=10.1074/jbc.M111838200; PubMed=11912194 [NCBI, ExPASy, EBI, Israel, Japan]
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
"Insulin receptor substrate 4 associates with the protein IRAS.";
J. Biol. Chem. 277:19439-19447(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-204, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[10]
FUNCTION, AND INTERACTION WITH HSF4.
DOI=10.1128/MCB.26.8.3282-3294.2006; PubMed=16581800 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Mivechi N.F.;
"Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26.";
Mol. Cell. Biol. 26:3282-3294(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-204, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[16]
VARIANT [LARGE SCALE ANALYSIS] LYS-323.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X60188; CAA42744.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013992; AAH13992.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M84490; AAA36142.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11696; CAA77754.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00018195; -.
PIR A48082; A48082.
RefSeq NP_002737.2; -.
UniGene Hs.861
3D structure databases
PDB
2ZOQ; X-ray; 2.39 A; A/B=1-379.[ExPASy / RCSB / EBI]
PDBsum 2ZOQ; -.
SMR P27361; 28-372, 29-373.
ModBase P27361.
Protein-protein interaction databases
IntAct P27361; 25.
PTM databases
PhosphoSite P27361; -.
Enzyme and pathway databases
BRENDA 2.7.11.24; 247.
Pathway_Interaction_DB alphasynuclein_pathway; Alpha-synuclein signaling.
angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
arf6downstreampathway; Arf6 downstream pathway.
bcr_5pathway; BCR signaling pathway.
anthraxpathway; Cellular roles of Anthrax toxin.
ceramidepathway; Ceramide signaling pathway.
cd8tcrdownstreampathway; Downstream signaling in naive CD8+ T cells.
endothelinpathway; Endothelins.
ephbfwdpathway; EPHB forward signaling.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
fgf_pathway; FGF signaling pathway.
ifngpathway; IFN-gamma pathway.
il2_1pathway; IL2-mediated signaling events.
avb3_integrin_pathway; Integrins in angiogenesis.
trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
avb3_opn_pathway; Osteopontin-mediated events.
ps1pathway; Presenilin action in Notch and Wnt signaling.
tcrraspathway; Ras signaling in the CD4+ TCR pathway.
smad2_3pathway; Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
telomerasepathway; Regulation of Telomerase.
retinoic_acid_pathway; Retinoic acid receptors-mediated signaling.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
s1p_s1p1_pathway; S1P1 pathway.
s1p_s1p2_pathway; S1P2 pathway.
s1p_s1p3_pathway; S1P3 pathway.
s1p_s1p4_pathway; S1P4 pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
prlsignalingeventspathway; Signaling events mediated by PRL.
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
syndecan_1_pathway; Syndecan-1-mediated signaling events.
syndecan_2_pathway; Syndecan-2-mediated signaling events.
trail_pathway; TRAIL signaling pathway.
mapktrkpathway; Trk receptor signaling mediated by the MAPK pathway.
vegfr1_pathway; VEGFR1 specific signals.
lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.
Reactome REACT_11061; Signalling by NGF.
REACT_1788; Transcription.
REACT_498; Signaling by Insulin receptor.
REACT_508; Signal attenuation.
Organism-specific databases
GeneCards GC16M030032; -.
H-InvDB HIX0012930; -.
HGNC HGNC:6877; MAPK3.
GenAtlas MAPK3.
HPA CAB002683; -.
HPA003995; -.
HPA005700; -.
MIM 601795; gene. [NCBI / EBI]
PharmGKB PA30622; -.
Gene expression databases
ArrayExpress P27361; -.
Bgee P27361; -.
CleanEx HS_MAPK3; -.
GermOnline ENSG00000102882; Homo sapiens.
Ontologies
GO
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from HPA).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (non-traceable author statement from UniProtKB).
GO:0004707; Molecular function: MAP kinase activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0007265; Biological process: Ras protein signal transduction (inferred from experiment from Reactome).
QuickGo view.
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 of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
PRINTS PR01770; ERK1ERK2MAPK.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS01351; MAPK; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P27361; -.
Genome annotation databases
Ensembl ENSG00000102882; Homo sapiens. [Contig view]
GeneID 5595; -.
NMPDR fig|9606.3.peg.12045; -.
Phylogenomic databases
HOGENOM P27361; -.
HOVERGEN P27361; -.
OMA P27361; HFRHENI.
Other
DrugBank DB01169; Arsenic trioxide.
DB01064; Isoproterenol.
DB00641; Simvastatin.
DB00605; Sulindac.
NextBio 21714; -.
SOURCE MAPK3; Homo sapiens.
ProtoNet P27361.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; ATP-binding; Cell cycle; Direct protein sequencing; Host-virus interaction; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   379  378     Mitogen-activated protein kinase 3. PRO_0000186251
DOMAIN   42   330  289     Protein kinase. 
NP_BIND   48    56  9     ATP (By similarity). 
MOTIF   202   204  3     TXY. 
ACT_SITE   166   166        Proton acceptor (By similarity). 
BINDING   71    71        ATP (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   202   202        Phosphothreonine. 
MOD_RES   204   204        Phosphotyrosine. 
VARIANT   323   323  1     E -> K. VAR_042253 [3D]
CONFLICT   174   174        I -> S (in Ref. 1; CAA42744). 
Sequence information
Length: 379 AA [This is the length of the unprocessed precursor] Molecular weight: 43136 Da [This is the MW of the unprocessed precursor] CRC64: E6020CE413EC41F7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAAAQGGG GGEPRRTEGV GPGVPGEVEM VKGQPFDVGP RYTQLQYIGE GAYGMVSSAY 

        70         80         90        100        110        120 
DHVRKTRVAI KKISPFEHQT YCQRTLREIQ ILLRFRHENV IGIRDILRAS TLEAMRDVYI 

       130        140        150        160        170        180 
VQDLMETDLY KLLKSQQLSN DHICYFLYQI LRGLKYIHSA NVLHRDLKPS NLLINTTCDL 

       190        200        210        220        230        240 
KICDFGLARI ADPEHDHTGF LTEYVATRWY RAPEIMLNSK GYTKSIDIWS VGCILAEMLS 

       250        260        270        280        290        300 
NRPIFPGKHY LDQLNHILGI LGSPSQEDLN CIINMKARNY LQSLPSKTKV AWAKLFPKSD 

       310        320        330        340        350        360 
SKALDLLDRM LTFNPNKRIT VEEALAHPYL EQYYDPTDEP VAEEPFTFAM ELDDLPKERL 

       370 
KELIFQETAR FQPGVLEAP 

P27361 in FASTA format

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