(data stored in ACNUC13530 zone)

HOVERGEN: MK03_RAT

ID   MK03_RAT                Reviewed;         380 AA.
AC   P21708; Q4PIY8; Q62686; Q9JJ13;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   03-NOV-2009, entry version 115.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   MEDLINE=93013050; PubMed=1327976; DOI=10.1016/0378-1119(92)90109-3;
RA   Marquardt B., Stabel S.;
RT   "Sequence of a rat cDNA encoding the ERK1-MAP kinase.";
RL   Gene 120:297-299(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=20283605; PubMed=10748187; DOI=10.1074/jbc.M910060199;
RA   Yung Y., Yao Z., Hanoch T., Seger R.;
RT   "ERK1b, a 46-kDa ERK isoform that is differentially regulated by
RT   MEK.";
RL   J. Biol. Chem. 275:15799-15808(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-65; 96-132; 157-209; 213-221; 280-357 AND
RP   361-380 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   ALA-2, PHOSPHORYLATION AT THR-203 AND TYR-205, AND MASS SPECTROMETRY.
RC   TISSUE=Pheochromocytoma;
RA   Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL   Submitted (AUG-2006) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-380 (ISOFORM 1).
RA   Maisonpierre P.C., le Beau M.M., Espinosa R. III, Ip N.Y.,
RA   Belluscio L., la Monte S.M., Squinto S., Furth M.E., Yancopoulos G.D.;
RL   Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 73-84 AND 183-190, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-380 (ISOFORM 1), AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   MEDLINE=90312137; PubMed=2164259; DOI=10.1126/science.2164259;
RA   Boulton T.G., Yancopoulos G.D., Gregory J.S., Slaughter C., Moomaw C.,
RA   Hsu J., Cobb M.H.;
RT   "An insulin-stimulated protein kinase similar to yeast kinases
RT   involved in cell cycle control.";
RL   Science 249:64-67(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-380 (ISOFORM 1).
RC   TISSUE=Brain cortex;
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   [8]
RP   PROTEIN SEQUENCE OF 43-64 AND 167-185, AND CHARACTERIZATION.
RX   MEDLINE=91105092; PubMed=1846291; DOI=10.1021/bi00215a038;
RA   Boulton T.G., Gregory J.S., Cobb M.H.;
RT   "Purification and properties of extracellular signal-regulated kinase
RT   1, an insulin-stimulated microtubule-associated protein 2 kinase.";
RL   Biochemistry 30:278-286(1991).
RN   [9]
RP   AUTOPHOSPHORYLATION.
RX   MEDLINE=91296777; PubMed=1712480; DOI=10.1073/pnas.88.14.6142;
RA   Seger R., Ahn N.G., Boulton T.G., Yancopoulos G.D., Panayotatos N.,
RA   Radziejewska E., Ericsson L., Bratlien R.L., Cobb M.H., Krebs E.G.;
RT   "Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo
RT   autophosphorylation on both tyrosine and threonine residues:
RT   implications for their mechanism of activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6142-6146(1991).
RN   [10]
RP   PHOSPHORYLATION OF EIF4EBP1.
RX   MEDLINE=95025978; PubMed=7939721; DOI=10.1126/science.7939721;
RA   Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J.,
RA   Sonenberg N., Lawrence J.C. Jr.;
RT   "PHAS-I as a link between mitogen-activated protein kinase and
RT   translation initiation.";
RL   Science 266:653-656(1994).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Kidney;
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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). Phosphorylates SPZ1. Phosphorylates heat shock factor
CC       protein 4 (HSF4) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated and tyrosine phosphorylated in
CC       response to insulin and NGF.
CC   -!- SUBUNIT: Interacts with NISCH, MORG1 and HSF4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=A;
CC         IsoId=P21708-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=P21708-2; Sequence=VSP_004830;
CC   -!- TISSUE SPECIFICITY: Highest levels within the nervous system,
CC       expressed in different tissues, mostly in intestine, placenta and
CC       lung.
CC   -!- DEVELOPMENTAL STAGE: Increased expression during development.
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.
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; S46779; AAA11604.1; -; mRNA.
DR   EMBL; X65198; CAA46318.1; -; mRNA.
DR   EMBL; AF155236; AAF71666.1; -; mRNA.
DR   EMBL; M61177; AAA63486.1; -; mRNA.
DR   EMBL; M38194; AAA41123.1; -; mRNA.
DR   EMBL; U12008; AAA20009.1; -; mRNA.
DR   IPI; IPI00206172; -.
DR   IPI; IPI00231081; -.
DR   PIR; JC1451; JC1451.
DR   RefSeq; NP_059043.1; -.
DR   UniGene; Rn.2592; -.
DR   HSSP; P28482; 1PME.
DR   SMR; P21708; 30-374.
DR   DIP; DIP:487N; -.
DR   STRING; P21708; -.
DR   PhosphoSite; P21708; -.
DR   Ensembl; ENSRNOT00000026627; ENSRNOP00000026627; ENSRNOG00000019601; Rattus norvegicus.
DR   GeneID; 50689; -.
DR   KEGG; rno:50689; -.
DR   NMPDR; fig|10116.3.peg.2990; -.
DR   UCSC; NM_017347; rat.
DR   CTD; 50689; -.
DR   RGD; 3046; Mapk3.
DR   HOVERGEN; P21708; -.
DR   OMA; EALETEP; -.
DR   BRENDA; 2.7.11.24; 248.
DR   NextBio; 610550; -.
DR   ArrayExpress; P21708; -.
DR   Genevestigator; P21708; -.
DR   GermOnline; ENSRNOG00000019601; Rattus norvegicus.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005626; C:insoluble fraction; IDA:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IDA:RGD.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IDA:RGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000189; P:nuclear translocation of MAPK; IDA:RGD.
DR   GO; GO:0045941; P:positive regulation of transcription; IEP:RGD.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IDA:RGD.
DR   GO; GO:0006461; P:protein complex assembly; 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; P21708.
DR   SWISS-2DPAGE; P21708.
KW   Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW   Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; 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_0000186253.
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   VAR_SEQ     340    340       E -> EVSRPPAAGRGISVPSVRPVPYCLCPQ (in
FT                                isoform 2).
FT                                /FTId=VSP_004830.
FT   CONFLICT     95     95       R -> G (in Ref. 1, 4 and 7).
SQ   SEQUENCE   380 AA;  43081 MW;  49C4EA95B627237F 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 RFQPGAPEAP
//

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