(data stored in ACNUC13530 zone)

HOVERGEN: MK03_MOUSE

ID   MK03_MOUSE              Reviewed;         380 AA.
AC   Q63844; Q61531; Q8K0X5; Q91YW5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   13-OCT-2009, entry version 101.
DE   RecName: Full=Mitogen-activated protein kinase 3;
DE            EC=2.7.11.24;
DE   AltName: Full=Extracellular signal-regulated kinase 1;
DE            Short=ERK-1;
DE   AltName: Full=Insulin-stimulated MAP2 kinase;
DE   AltName: Full=MAP kinase 1;
DE            Short=MAPK 1;
DE   AltName: Full=p44-ERK1;
DE   AltName: Full=ERT2;
DE   AltName: Full=p44-MAPK;
DE   AltName: Full=Microtubule-associated protein 2 kinase;
DE   AltName: Full=MNK1;
GN   Name=Mapk3; Synonyms=Erk1, Prkm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-65; 89-105; 110-132; 157-209; 213-221; 280-288;
RP   304-319 AND 361-371, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
RL   Submitted (FEB-2008) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-380.
RX   PubMed=8424957; DOI=10.1016/0167-4781(93)90074-N;
RA   Tanner B., Mueckler M.;
RT   "Molecular cloning of a mouse extracellular signal regulated kinase
RT   (erk-1).";
RL   Biochim. Biophys. Acta 1171:319-320(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-19.
RC   TISSUE=Pre-B cell;
RX   MEDLINE=92020947; PubMed=1717989; DOI=10.1073/pnas.88.19.8845;
RA   Crews C.M., Alessandrini A.A., Erikson R.L.;
RT   "Mouse Erk-1 gene product is a serine/threonine protein kinase that
RT   has the potential to phosphorylate tyrosine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8845-8849(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 77-380.
RC   TISSUE=Fetal brain;
RX   MEDLINE=91369479; PubMed=1716439; DOI=10.1089/dna.1991.10.505;
RA   de Miguel C., Kligman D., Patel J., Detera-Wadleigh S.D.;
RT   "Molecular analysis of microtubule-associated protein-2 kinase cDNA
RT   from mouse and rat brain.";
RL   DNA Cell Biol. 10:505-514(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 136-153 AND 191-209, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 171-209.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93185941; PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Novel CDC2-related protein kinases produced in murine hematopoietic
RT   stem cells.";
RL   Gene 124:305-306(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 171-205.
RX   MEDLINE=93092802; PubMed=1459009;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Identification of new protein kinase genes, similar to kinases of the
RT   cdc2 family and expressed in murine hematopoietic stem cells.";
RL   Dokl. Akad. Nauk SSSR 324:893-897(1992).
RN   [9]
RP   INTERACTION WITH MORG1.
RX   PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA   Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA   Bissonette E.A., Weber M.J.;
RT   "Modular construction of a signaling scaffold: MORG1 interacts with
RT   components of the ERK cascade and links ERK signaling to specific
RT   agonists.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
RN   [10]
RP   PHOSPHORYLATION OF SPZ1.
RX   PubMed=15899793; DOI=10.1158/0008-5472.CAN-04-3658;
RA   Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H.;
RT   "bHLH-zip transcription factor Spz1 mediates mitogen-activated protein
RT   kinase cell proliferation, transformation, and tumorigenesis.";
RL   Cancer Res. 65:4041-4050(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RX   PubMed=17389395; DOI=10.1073/pnas.0608638104;
RA   Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
RT   "Multiple reaction monitoring for robust quantitative proteomic
RT   analysis of cellular signaling networks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18973353; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in both the initiation and regulation of
CC       meiosis, mitosis, and postmitotic functions in differentiated
CC       cells by phosphorylating a number of transcription factors such as
CC       ELK-1. Phosphorylates EIF4EBP1; required for initiation of
CC       translation. Phosphorylates microtubule-associated protein 2
CC       (MAP2) and heat shock factor protein 4 (HSF4) (By similarity).
CC       Phosphorylates SPZ1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by tyrosine and threonine
CC       phosphorylation.
CC   -!- SUBUNIT: Interacts with HSF4 and NISCH (By similarity). Interacts
CC       with MORG1.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-203 and Tyr-205, which activates
CC       the enzyme (By similarity). Autophosphorylates on threonine and
CC       tyrosine residues in vitro.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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CC   -!- GENE_FAMILY: HBG014652 [ FAMILY / ALN / TREE ]
DR   EMBL; BC013754; AAH13754.1; -; mRNA.
DR   EMBL; BC029712; AAH29712.1; -; mRNA.
DR   EMBL; S58470; AAB19973.1; -; mRNA.
DR   EMBL; X64605; CAA45889.1; -; mRNA.
DR   IPI; IPI00230277; -.
DR   PIR; S28184; S28184.
DR   RefSeq; NP_036082.1; -.
DR   UniGene; Mm.8385; -.
DR   HSSP; P28482; 1PME.
DR   SMR; Q63844; 29-373, 30-374.
DR   STRING; Q63844; -.
DR   PhosphoSite; Q63844; -.
DR   PRIDE; Q63844; -.
DR   Ensembl; ENSMUST00000050201; ENSMUSP00000101969; ENSMUSG00000063065; Mus musculus.
DR   Ensembl; ENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065; Mus musculus.
DR   GeneID; 26417; -.
DR   KEGG; mmu:26417; -.
DR   NMPDR; fig|10090.3.peg.17639; -.
DR   UCSC; uc009jsm.1; mouse.
DR   CTD; 26417; -.
DR   MGI; MGI:1346859; Mapk3.
DR   HOGENOM; Q63844; -.
DR   HOVERGEN; Q63844; -.
DR   BRENDA; 2.7.11.24; 244.
DR   NextBio; 304429; -.
DR   ArrayExpress; Q63844; -.
DR   Bgee; Q63844; -.
DR   CleanEx; MM_MAPK3; -.
DR   Genevestigator; Q63844; -.
DR   GermOnline; ENSMUSG00000063065; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IMP:MGI.
DR   GO; GO:0001784; F:phosphotyrosine binding; IMP:MGI.
DR   GO; GO:0003700; F:transcription factor activity; EXP:Reactome.
DR   GO; GO:0051216; P:cartilage development; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IDA:MGI.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IDA:MGI.
DR   GO; GO:0051090; P:regulation of transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR   InterPro; IPR008349; Erk_1_2_MAPK.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01770; ERK1ERK2MAPK.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q63844.
DR   SWISS-2DPAGE; Q63844.
KW   Acetylation; ATP-binding; Cell cycle; Direct protein sequencing;
KW   Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   DOMAIN       49    248       PRODOM:2005.1:PD000001  8496
FT   DOMAIN      336    372       PRODOM:2005.1:PD054205  105
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    380       Mitogen-activated protein kinase 3.
FT                                /FTId=PRO_0000186252.
FT   DOMAIN       43    331       Protein kinase.
FT   NP_BIND      49     57       ATP (By similarity).
FT   MOTIF       203    205       TXY.
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   BINDING      72     72       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES     203    203       Phosphothreonine.
FT   MOD_RES     205    205       Phosphotyrosine.
FT   CONFLICT    178    178       T -> P (in Ref. 7; CAA45889 and 8).
SQ   SEQUENCE   380 AA;  43066 MW;  49C14A95B627237F CRC64;
     MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA
     YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY
     IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD
     LKICDFGLAR IADPEHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML
     SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS
     DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE PVAEEPFTFD MELDDLPKER
     LKELIFQETA RFQPGAPEGP
//

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