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UniProtKB/Swiss-Prot entry P28482


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

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Entry information
Entry name MK01_HUMAN
Primary accession number P28482
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 103)
Name and origin of the protein
Protein name Mitogen-activated protein kinase 1
Synonyms EC 2.7.11.24
Extracellular signal-regulated kinase 2
ERK-2
Mitogen-activated protein kinase 2
MAP kinase 2
MAPK 2
p42-MAPK
ERT1
Gene name
Name: MAPK1
Synonyms: ERK2, PRKM1, PRKM2
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].
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[4]
PROTEIN SEQUENCE OF 2-15, AND ACETYLATION AT ALA-2.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[5]
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).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, 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).
[8]
INTERACTION WITH ARHGEF2.
DOI=10.1016/j.bbrc.2008.01.066; PubMed=18211802 [NCBI, ExPASy, EBI, Israel, Japan]
Fujishiro S.H., Tanimura S., Mure S., Kashimoto Y., Watanabe K., Kohno M.;
"ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA.";
Biochem. Biophys. Res. Commun. 368:162-167(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-187, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, 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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, 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).
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
M84489; AAA58459.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11694; CAA77752.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11695; CAA77753.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017832; AAH17832.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ1400; JQ1400.
RefSeq NP_002736.3; -.
NP_620407.1; -.
UniGene Hs.431850
3D structure databases
PDB
1PME; X-ray; 2.00 A; A=1-360.[ExPASy / RCSB / EBI]
1TVO; X-ray; 2.50 A; A=1-360.[ExPASy / RCSB / EBI]
1WZY; X-ray; 2.50 A; A=1-360.[ExPASy / RCSB / EBI]
2E14; X-ray; 3.00 A; A=1-360.[ExPASy / RCSB / EBI]
2OJG; X-ray; 2.00 A; A=1-360.[ExPASy / RCSB / EBI]
2OJI; X-ray; 2.60 A; A=1-360.[ExPASy / RCSB / EBI]
2OJJ; X-ray; 2.40 A; A=1-360.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1PME; -.
1TVO; -.
1WZY; -.
2E14; -.
2OJG; -.
2OJI; -.
2OJJ; -.
ModBase P28482.
Protein-protein interaction databases
DIP DIP:519N; -.
IntAct P28482; -.
PTM databases
PhosphoSite P28482; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune System.
2D gel databases
OGP P28482; -.
Organism-specific databases
H-InvDB HIX0016281; -.
HGNC HGNC:6871; MAPK1.
GenAtlas MAPK1.
HPA CAB004229; -.
MIM 176948; gene. [NCBI / EBI]
Orphanet 567; Monosomy 22q11.
PharmGKB PA30616; -.
GeneCards P28482.
Gene expression databases
ArrayExpress P28482; -.
CleanEx HS_MAPK1; -.
GermOnline ENSG00000100030; 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 (inferred from electronic annotation from InterPro).
GO:0004707; Molecular function: MAP kinase activity (traceable author statement from ProtInc).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0006917; Biological process: induction of apoptosis (traceable author statement from ProtInc).
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 electronic annotation from InterPro).
GO:0007265; Biological process: Ras protein signal transduction (inferred from experiment from Reactome).
GO:0007268; Biological process: synaptic transmission (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR008349; Erk_1_2_MAPK.
IPR003527; MAP_kin_CS.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
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).
BLOCKS P28482.
ProtoNet P28482.
Proteomic databases
PeptideAtlas P28482; -.
Genome annotation databases
Ensembl ENSG00000100030; Homo sapiens. [Contig view]
GeneID 5594; -.
KEGG hsa:5594; -.
Phylogenomic databases
HOGENOM P28482; -.
HOVERGEN P28482; -.
Other
DrugBank DB01169; Arsenic trioxide.
LinkHub P28482; -.
NextBio 21708; -.
SOURCE MAPK1; Homo sapiens.
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; 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   360  359     Mitogen-activated protein kinase 1. PRO_0000186247
DOMAIN   25   313  289     Protein kinase. 
NP_BIND   31    39  9     ATP (By similarity). 
MOTIF   185   187  3     TXY. 
COMPBIAS   2     9  8     Poly-Ala. 
ACT_SITE   149   149        Proton acceptor (By similarity). 
BINDING   54    54        ATP (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   185   185        Phosphothreonine. 
MOD_RES   187   187        Phosphotyrosine. 
MOD_RES   190   190        Phosphothreonine (By similarity). 
CONFLICT   91    91        R -> Q (in Ref. 2; CAA77752). 
STRAND   25    30  6      
STRAND   39    44  6      
TURN   45    47  3      
STRAND   49    56  8      
HELIX   62    77  16      
STRAND   88    90  3      
TURN   95    97  3      
STRAND   101   106  6      
HELIX   112   118  7      
HELIX   123   142  20      
HELIX   152   154  3      
STRAND   155   157  3      
STRAND   163   165  3      
HELIX   176   178  3      
HELIX   191   193  3      
HELIX   196   198  3      
TURN   199   201  3      
HELIX   208   223  16      
HELIX   233   244  12      
HELIX   249   253  5      
HELIX   258   265  8      
HELIX   275   278  4      
HELIX   284   293  10      
TURN   298   300  3      
HELIX   304   308  5      
HELIX   311   313  3      
TURN   314   316  3      
HELIX   319   321  3      
HELIX   340   350  11      
HELIX   352   354  3      
TURN   356   358  3      
Sequence information
Length: 360 AA [This is the length of the unprocessed precursor] Molecular weight: 41390 Da [This is the MW of the unprocessed precursor] CRC64: E85D0B2A5D2D724E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR VAIKKISPFE 

        70         80         90        100        110        120 
HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD VYIVQDLMET DLYKLLKTQH 

       130        140        150        160        170        180 
LSNDHICYFL YQILRGLKYI HSANVLHRDL KPSNLLLNTT CDLKICDFGL ARVADPDHDH 

       190        200        210        220        230        240 
TGFLTEYVAT RWYRAPEIML NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI 

       250        260        270        280        290        300 
LGILGSPSQE DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK 

       310        320        330        340        350        360 
RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE TARFQPGYRS 

P28482 in FASTA format

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View entry in raw text format (no links)
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