ID MK01_RAT Reviewed; 358 AA. AC P63086; P27703; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 203. DE RecName: Full=Mitogen-activated protein kinase 1 {ECO:0000305}; DE Short=MAP kinase 1; DE Short=MAPK 1; DE EC=2.7.11.24; DE AltName: Full=ERT1; DE AltName: Full=Extracellular signal-regulated kinase 2; DE Short=ERK-2; DE AltName: Full=MAP kinase isoform p42; DE Short=p42-MAPK; DE AltName: Full=Mitogen-activated protein kinase 2; DE Short=MAP kinase 2; DE Short=MAPK 2; GN Name=Mapk1 {ECO:0000312|RGD:70500}; Synonyms=Erk2, Mapk, Prkm1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=2032290; DOI=10.1016/0092-8674(91)90098-j; RA Boulton T.G., Nye S.H., Robbins D.J., Ip N.Y., Radziejewska E., RA Morgenbesser S.D., DePinho R.A., Panayotatos N., Cobb M.H., RA Yancopoulos G.D.; RT "ERKs: a family of protein-serine/threonine kinases that are activated and RT tyrosine phosphorylated in response to insulin and NGF."; RL Cell 65:663-675(1991). RN [2] RP PROTEIN SEQUENCE OF 2-13; 69-75; 137-170; 193-201 AND 341-351, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Pheochromocytoma; RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.; RL Submitted (AUG-2006) to UniProtKB. RN [3] RP PROTEIN SEQUENCE OF 163-170, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (JUL-2007) to UniProtKB. RN [4] RP AUTOPHOSPHORYLATION. RX 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: implications RT for their mechanism of activation."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6142-6146(1991). RN [5] RP PHOSPHORYLATION OF EIF4EBP1. RX PubMed=7939721; DOI=10.1126/science.7939721; RA Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J., Sonenberg N., RA Lawrence J.C. Jr.; RT "PHAS-I as a link between mitogen-activated protein kinase and translation RT initiation."; RL Science 266:653-656(1994). RN [6] RP INTERACTION WITH ARRB2. RX PubMed=11226259; DOI=10.1073/pnas.041604898; RA Luttrell L.M., Roudabush F.L., Choy E.W., Miller W.E., Field M.E., RA Pierce K.L., Lefkowitz R.J.; RT "Activation and targeting of extracellular signal-regulated kinases by RT beta-arrestin scaffolds."; RL Proc. Natl. Acad. Sci. U.S.A. 98:2449-2454(2001). RN [7] RP FUNCTION, AND INTERACTION WITH CDK2AP2. RX PubMed=12944431; DOI=10.1242/dev.00731; RA Terret M.E., Lefebvre C., Djiane A., Rassinier P., Moreau J., Maro B., RA Verlhac M.H.; RT "DOC1R: a MAP kinase substrate that control microtubule organization of RT metaphase II mouse oocytes."; RL Development 130:5169-5177(2003). RN [8] RP INTERACTION WITH GIT1. RX PubMed=15923189; DOI=10.1074/jbc.m502271200; RA Yin G., Zheng Q., Yan C., Berk B.C.; RT "GIT1 is a scaffold for ERK1/2 activation in focal adhesions."; RL J. Biol. Chem. 280:27705-27712(2005). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [10] RP INTERACTION WITH CAV2. RX PubMed=19778377; DOI=10.1111/j.1582-4934.2009.00391.x; RA Kwon H., Jeong K., Pak Y.; RT "Identification of pY19-caveolin-2 as a positive regulator of insulin- RT stimulated actin cytoskeleton-dependent mitogenesis."; RL J. Cell. Mol. Med. 13:1549-1564(2009). RN [11] RP INTERACTION WITH CAV2. RX PubMed=19427337; DOI=10.1016/j.bbamcr.2009.04.015; RA Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S., Pak Y.; RT "Caveolin-2 regulation of STAT3 transcriptional activation in response to RT insulin."; RL Biochim. Biophys. Acta 1793:1325-1333(2009). RN [12] RP REVIEW ON FUNCTION. RX PubMed=16393692; DOI=10.1080/02699050500284218; RA Yoon S., Seger R.; RT "The extracellular signal-regulated kinase: multiple substrates regulate RT diverse cellular functions."; RL Growth Factors 24:21-44(2006). RN [13] RP REVIEW ON FUNCTION, AND REVIEW ON SUBCELLULAR LOCATION. RX PubMed=19565474; DOI=10.1002/biof.52; RA Yao Z., Seger R.; RT "The ERK signaling cascade--views from different subcellular RT compartments."; RL BioFactors 35:407-416(2009). RN [14] RP REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION. RX PubMed=21779493; DOI=10.1177/1947601911407328; RA Wortzel I., Seger R.; RT "The ERK cascade: distinct functions within various subcellular RT organelles."; RL Genes Cancer 2:195-209(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [16] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CAVIN4. RX PubMed=24567387; DOI=10.1073/pnas.1315359111; RA Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K., RA Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.; RT "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric RT cardiac hypertrophy induced by alpha1-adrenergic receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014). RN [17] RP INTERACTION WITH DUSP7. RX PubMed=27783954; DOI=10.1016/j.celrep.2016.10.007; RA Tischer T., Schuh M.; RT "The phosphatase Dusp7 drives meiotic resumption and chromosome alignment RT in mouse oocytes."; RL Cell Rep. 17:1426-1437(2016). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=8107865; DOI=10.1038/367704a0; RA Zhang F., Strand A., Robbins D., Cobb M.H., Goldsmith E.J.; RT "Atomic structure of the MAP kinase ERK2 at 2.3-A resolution."; RL Nature 367:704-710(1994). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP. RX PubMed=8639522; DOI=10.1021/bi952723e; RA Robinson M.J., Harkins P.C., Zhang J., Baer R., Haycock J.W., Cobb M.H., RA Goldsmith E.J.; RT "Mutation of position 52 in ERK2 creates a nonproductive binding mode for RT adenosine 5'-triphosphate."; RL Biochemistry 35:5641-5646(1996). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=9298898; DOI=10.1016/s0092-8674(00)80351-7; RA Canagarajah B.J., Khokhlatchev A., Cobb M.H., Goldsmith E.J.; RT "Activation mechanism of the MAP kinase ERK2 by dual phosphorylation."; RL Cell 90:859-869(1997). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR. RX PubMed=9753691; DOI=10.1016/s0969-2126(98)00113-0; RA Wang Z., Canagarajah B.J., Boehm J.C., Kassisa S., Cobb M.H., Young P.R., RA Abdel-Meguid S., Adams J.L., Goldsmith E.J.; RT "Structural basis of inhibitor selectivity in MAP kinases."; RL Structure 6:1117-1128(1998). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-357, AND INTERACTION WITH RP DUSP6. RX PubMed=16567630; DOI=10.1073/pnas.0510506103; RA Liu S., Sun J.P., Zhou B., Zhang Z.Y.; RT "Structural basis of docking interactions between ERK2 and MAP kinase RT phosphatase 3."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5326-5331(2006). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-357. RX PubMed=16765894; DOI=10.1016/j.str.2006.04.006; RA Zhou T., Sun L., Humphreys J., Goldsmith E.J.; RT "Docking interactions induce exposure of activation loop in the MAP kinase RT ERK2."; RL Structure 14:1011-1019(2006). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-358 IN COMPLEX WITH INHIBITOR. RX PubMed=18571434; DOI=10.1016/j.jsb.2008.05.002; RA Rastelli G., Rosenfeld R., Reid R., Santi D.V.; RT "Molecular modeling and crystal structure of ERK2-hypothemycin complexes."; RL J. Struct. Biol. 164:18-23(2008). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR. RX PubMed=18767165; DOI=10.1002/prot.22207; RA Katayama N., Orita M., Yamaguchi T., Hisamichi H., Kuromitsu S., RA Kurihara H., Sakashita H., Matsumoto Y., Fujita S., Niimi T.; RT "Identification of a key element for hydrogen-bonding patterns between RT protein kinases and their inhibitors."; RL Proteins 73:795-801(2008). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH DCC, FUNCTION IN RP PHOSPHORYLATION OF DCC, INTERACTION WITH DCC, AND MUTAGENESIS OF GLN-117; RP HIS-123 AND LEU-155. RX PubMed=21070949; DOI=10.1016/j.str.2010.08.011; RA Ma W., Shang Y., Wei Z., Wen W., Wang W., Zhang M.; RT "Phosphorylation of DCC by ERK2 is facilitated by direct docking of the RT receptor P1 domain to the kinase."; RL Structure 18:1502-1511(2010). CC -!- FUNCTION: Serine/threonine kinase which acts as an essential component CC of the MAP kinase signal transduction pathway. MAPK1/ERK2 and CC MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK CC cascade. They participate also in a signaling cascade initiated by CC activated KIT and KITLG/SCF. Depending on the cellular context, the CC MAPK/ERK cascade mediates diverse biological functions such as cell CC growth, adhesion, survival and differentiation through the regulation CC of transcription, translation, cytoskeletal rearrangements. The CC MAPK/ERK cascade also plays a role in initiation and regulation of CC meiosis, mitosis, and postmitotic functions in differentiated cells by CC phosphorylating a number of transcription factors. About 160 substrates CC have already been discovered for ERKs. Many of these substrates are CC localized in the nucleus, and seem to participate in the regulation of CC transcription upon stimulation. However, other substrates are found in CC the cytosol as well as in other cellular organelles, and those are CC responsible for processes such as translation, mitosis and apoptosis. CC Moreover, the MAPK/ERK cascade is also involved in the regulation of CC the endosomal dynamics, including lysosome processing and endosome CC cycling through the perinuclear recycling compartment (PNRC); as well CC as in the fragmentation of the Golgi apparatus during mitosis. The CC substrates include transcription factors (such as ATF2, BCL6, ELK1, CC ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, CC GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such CC as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of CC translation (such as EIF4EBP1 and FXR1) and a variety of other CC signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein CC kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, CC RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, CC MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or CC DUSP16) are other substrates which enable the propagation the MAPK/ERK CC signal to additional cytosolic and nuclear targets, thereby extending CC the specificity of the cascade. Mediates phosphorylation of TPR in CC response to EGF stimulation. May play a role in the spindle assembly CC checkpoint. Phosphorylates PML and promotes its interaction with PIN1, CC leading to PML degradation (By similarity). Phosphorylates CDK2AP2 CC (PubMed:12944431). {ECO:0000250|UniProtKB:P28482, CC ECO:0000269|PubMed:12944431, ECO:0000269|PubMed:21070949, CC ECO:0000303|PubMed:16393692, ECO:0000303|PubMed:19565474, CC ECO:0000303|PubMed:21779493}. CC -!- FUNCTION: Acts as a transcriptional repressor. Binds to a [GC]AAA[GC] CC consensus sequence. Repress the expression of interferon gamma-induced CC genes. Seems to bind to the promoter of CCL5, DMP1, IFIH1, IFITM1, CC IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and STAT1. Transcriptional activity CC is independent of kinase activity. {ECO:0000250|UniProtKB:P28482}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.24; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2 on CC Thr-183 and Tyr-185 in response to external stimuli like insulin or CC NGF. Both phosphorylations are required for activity. This CC phosphorylation causes dramatic conformational changes, which enable CC full activation and interaction of MAPK1/ERK2 with its substrates. CC Phosphorylation on Ser-27 by SGK1 results in its activation by CC enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. CC Dephosphorylated and inactivated by DUSP1, DUSP3, DUSP6 and DUSP9. CC Inactivated by pyrimidylpyrrole inhibitors. CC -!- SUBUNIT: Binds both upstream activators and downstream substrates in CC multimolecular complexes. Interacts with ADAM15, ARHGEF2, DAPK1 (via CC death domain), HSF4, IER3, IPO7, MKNK2, MORG1, NISCH, PEA15, SGK1, and CC isoform 1 of NEK2 (By similarity). Interacts (via phosphorylated form) CC with TPR (via C-terminal region and phosphorylated form); the CC interaction requires dimerization of MAPK1/ERK2 and increases following CC EGF stimulation (By similarity). Interacts with MAP2K1 (By similarity). CC Interacts with DUSP6 (PubMed:16567630). Interacts with ARRB2 CC (PubMed:11226259). Interacts (phosphorylated form) with CAV2 ('Tyr-19'- CC phosphorylated form); the interaction, promoted by insulin, leads to CC nuclear location and MAPK1 activation (PubMed:19778377, CC PubMed:19427337). MKNK2 isoform 1 binding prevents from CC dephosphorylation and inactivation (By similarity). Interacts with DCC CC (PubMed:21070949). The phosphorylated form interacts with PML (By CC similarity). Interacts with STYX (By similarity). Interacts with CC CDK2AP2 (PubMed:12944431). Interacts with CAVIN4 (PubMed:24567387). CC Interacts with DUSP7; the interaction enhances DUSP7 phosphatase CC activity (PubMed:27783954). Interacts with GIT1; this interaction is CC necessary for MAPK1 localization to focal adhesions (PubMed:15923189). CC Interacts with ZNF263 (By similarity). {ECO:0000250|UniProtKB:P28482, CC ECO:0000250|UniProtKB:P63085, ECO:0000269|PubMed:11226259, CC ECO:0000269|PubMed:12944431, ECO:0000269|PubMed:15923189, CC ECO:0000269|PubMed:16567630, ECO:0000269|PubMed:19427337, CC ECO:0000269|PubMed:19778377, ECO:0000269|PubMed:21070949, CC ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:27783954}. CC -!- INTERACTION: CC P63086; Q63155: Dcc; NbExp=10; IntAct=EBI-397710, EBI-1798965; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}. CC Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250}. Cytoplasm CC {ECO:0000269|PubMed:24567387}. Membrane, caveola CC {ECO:0000269|PubMed:24567387}. Cell junction, focal adhesion CC {ECO:0000250|UniProtKB:P63085}. Note=Associated with the spindle during CC prometaphase and metaphase. PEA15-binding and phosphorylated DAPK1 CC promote its cytoplasmic retention. Phosphorylation at Ser- 244 and Ser- CC 246 as well as autophosphorylation at Thr-188 promote nuclear CC localization. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highest levels within the nervous system, expressed CC in different tissues, mostly in muscle, thymus and heart. 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-183 and Tyr-185, which activates the CC enzyme. Phosphorylated upon FLT3 and KIT signaling. Ligand-activated CC ALK induces tyrosine phosphorylation (By similarity). Dephosphorylated CC by PTPRJ at Tyr-185 (By similarity). Autophosphorylated on threonine CC and tyrosine residues in vitro, which correlates with a slow and low CC level of activation. Phosphorylation on Ser-27 by SGK1 results in its CC activation by enhancing its interaction with MAP2K1/MEK1 and CC MAP2K2/MEK2 (By similarity). Dephosphorylated by DUSP1 and DUSP2 at CC Thr-183 and Tyr-185 (By similarity). {ECO:0000250|UniProtKB:P28482, CC ECO:0000250|UniProtKB:P63085}. CC -!- PTM: ISGylated. {ECO:0000250}. CC -!- PTM: Ubiquitinated by TRIM15 via 'Lys-63'-linked ubiquitination; CC leading to activation. Deubiquitinated by CYLD. CC {ECO:0000250|UniProtKB:P27361}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M64300; AAA41124.1; -; mRNA. DR PIR; A40033; A40033. DR RefSeq; NP_446294.1; NM_053842.2. DR RefSeq; XP_006248720.1; XM_006248658.3. DR RefSeq; XP_006248721.1; XM_006248659.3. DR RefSeq; XP_008767070.1; XM_008768848.2. DR PDB; 1GOL; X-ray; 2.80 A; A=1-358. DR PDB; 2ERK; X-ray; 2.40 A; A=1-358. DR PDB; 2FYS; X-ray; 2.50 A; A/B=2-358. DR PDB; 2GPH; X-ray; 1.90 A; A=2-358. DR PDB; 2Z7L; X-ray; 2.41 A; A=1-358. DR PDB; 3C9W; X-ray; 2.50 A; A/B=2-358. DR PDB; 3ERK; X-ray; 2.10 A; A=1-358. DR PDB; 3O71; X-ray; 1.95 A; A=1-358. DR PDB; 3QYW; X-ray; 1.50 A; A=1-358. DR PDB; 3QYZ; X-ray; 1.46 A; A=1-358. DR PDB; 3R63; X-ray; 1.70 A; A=1-358. DR PDB; 3ZU7; X-ray; 1.97 A; A=3-358. DR PDB; 3ZUV; X-ray; 2.72 A; A/C=3-358. DR PDB; 4ERK; X-ray; 2.20 A; A=1-358. DR PDB; 4GSB; X-ray; 1.80 A; A=1-358. DR PDB; 4GT3; X-ray; 1.68 A; A=1-358. DR PDB; 4GVA; X-ray; 1.83 A; A=1-358. DR PDB; 4I5H; X-ray; 1.90 A; A=2-358. DR PDB; 4N4S; X-ray; 2.20 A; A/B=2-358. DR PDB; 4QYY; X-ray; 1.65 A; A=1-358. DR PDB; 4S2Z; X-ray; 1.48 A; A=1-358. DR PDB; 4S30; X-ray; 2.00 A; A=1-358. DR PDB; 4S31; X-ray; 1.45 A; A=1-358. DR PDB; 4S32; X-ray; 1.34 A; A=1-358. DR PDB; 4S33; X-ray; 1.48 A; A=1-358. DR PDB; 4S34; X-ray; 2.50 A; A=1-358. DR PDB; 4XNE; X-ray; 1.80 A; A=9-354. DR PDB; 4XOY; X-ray; 2.10 A; A=8-358. DR PDB; 4XOZ; X-ray; 1.95 A; A=8-358. DR PDB; 4XP0; X-ray; 1.46 A; A=8-358. DR PDB; 4XP2; X-ray; 1.75 A; A=8-358. DR PDB; 4XP3; X-ray; 1.78 A; A=8-358. DR PDB; 4XRJ; X-ray; 1.69 A; A=9-354. DR PDB; 4XRL; X-ray; 2.55 A; A=9-353. DR PDB; 5HD4; X-ray; 1.45 A; A=1-358. DR PDB; 5HD7; X-ray; 1.69 A; A=1-358. DR PDB; 5KE0; X-ray; 1.68 A; A=1-358. DR PDB; 5U6I; X-ray; 1.69 A; A=1-358. DR PDB; 5UMO; X-ray; 2.26 A; A=4-354. DR PDB; 6CPW; X-ray; 1.85 A; A=1-358. DR PDB; 6DCG; X-ray; 1.45 A; A=1-358. DR PDB; 6FI3; X-ray; 1.52 A; A=1-358. DR PDB; 6FI6; X-ray; 1.65 A; A=1-358. DR PDB; 6FJ0; X-ray; 1.66 A; A=1-358. DR PDB; 6FJB; X-ray; 1.85 A; A=1-358. DR PDB; 6FJZ; X-ray; 1.86 A; A=1-358. DR PDB; 6FLE; X-ray; 1.48 A; A=1-358. DR PDB; 6FLV; X-ray; 1.91 A; A=1-358. DR PDB; 6FMA; X-ray; 1.67 A; A=1-358. DR PDB; 6FN5; X-ray; 1.93 A; A=1-358. DR PDB; 6FQ7; X-ray; 1.60 A; A=1-358. DR PDB; 6FR1; X-ray; 1.56 A; A=1-358. DR PDB; 6FRP; X-ray; 1.53 A; A=1-358. DR PDB; 6FXV; X-ray; 1.53 A; A=1-358. DR PDB; 6OPK; X-ray; 2.54 A; A=7-358. DR PDB; 6OT6; X-ray; 1.65 A; A=1-358. DR PDB; 6OTS; X-ray; 2.10 A; A=1-358. DR PDB; 6RFO; X-ray; 1.70 A; A=1-163, A=200-358. DR PDB; 6RFP; X-ray; 1.74 A; A=1-358. DR PDB; 7UGB; X-ray; 1.90 A; A=3-358. DR PDBsum; 1GOL; -. DR PDBsum; 2ERK; -. DR PDBsum; 2FYS; -. DR PDBsum; 2GPH; -. DR PDBsum; 2Z7L; -. DR PDBsum; 3C9W; -. DR PDBsum; 3ERK; -. DR PDBsum; 3O71; -. DR PDBsum; 3QYW; -. DR PDBsum; 3QYZ; -. DR PDBsum; 3R63; -. DR PDBsum; 3ZU7; -. DR PDBsum; 3ZUV; -. DR PDBsum; 4ERK; -. DR PDBsum; 4GSB; -. DR PDBsum; 4GT3; -. DR PDBsum; 4GVA; -. DR PDBsum; 4I5H; -. DR PDBsum; 4N4S; -. DR PDBsum; 4QYY; -. DR PDBsum; 4S2Z; -. DR PDBsum; 4S30; -. DR PDBsum; 4S31; -. DR PDBsum; 4S32; -. DR PDBsum; 4S33; -. DR PDBsum; 4S34; -. DR PDBsum; 4XNE; -. DR PDBsum; 4XOY; -. DR PDBsum; 4XOZ; -. DR PDBsum; 4XP0; -. DR PDBsum; 4XP2; -. DR PDBsum; 4XP3; -. DR PDBsum; 4XRJ; -. DR PDBsum; 4XRL; -. DR PDBsum; 5HD4; -. DR PDBsum; 5HD7; -. DR PDBsum; 5KE0; -. DR PDBsum; 5U6I; -. DR PDBsum; 5UMO; -. DR PDBsum; 6CPW; -. DR PDBsum; 6DCG; -. DR PDBsum; 6FI3; -. DR PDBsum; 6FI6; -. DR PDBsum; 6FJ0; -. DR PDBsum; 6FJB; -. DR PDBsum; 6FJZ; -. DR PDBsum; 6FLE; -. DR PDBsum; 6FLV; -. DR PDBsum; 6FMA; -. DR PDBsum; 6FN5; -. DR PDBsum; 6FQ7; -. DR PDBsum; 6FR1; -. DR PDBsum; 6FRP; -. DR PDBsum; 6FXV; -. DR PDBsum; 6OPK; -. DR PDBsum; 6OT6; -. DR PDBsum; 6OTS; -. DR PDBsum; 6RFO; -. DR PDBsum; 6RFP; -. DR PDBsum; 7UGB; -. DR AlphaFoldDB; P63086; -. DR BMRB; P63086; -. DR SMR; P63086; -. DR BioGRID; 250505; 176. DR DIP; DIP-29117N; -. DR ELM; P63086; -. DR IntAct; P63086; 15. DR MINT; P63086; -. DR STRING; 10116.ENSRNOP00000002533; -. DR BindingDB; P63086; -. DR ChEMBL; CHEMBL5233; -. DR CarbonylDB; P63086; -. DR GlyGen; P63086; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63086; -. DR PhosphoSitePlus; P63086; -. DR jPOST; P63086; -. DR PaxDb; 10116-ENSRNOP00000002533; -. DR Ensembl; ENSRNOT00000002533.8; ENSRNOP00000002533.6; ENSRNOG00000001849.8. DR Ensembl; ENSRNOT00055006213; ENSRNOP00055004732; ENSRNOG00055003901. DR Ensembl; ENSRNOT00060004151; ENSRNOP00060002931; ENSRNOG00060002574. DR Ensembl; ENSRNOT00065013385; ENSRNOP00065009913; ENSRNOG00065008439. DR GeneID; 116590; -. DR KEGG; rno:116590; -. DR AGR; RGD:70500; -. DR CTD; 5594; -. DR RGD; 70500; Mapk1. DR eggNOG; KOG0660; Eukaryota. DR GeneTree; ENSGT00940000156771; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; P63086; -. DR OrthoDB; 158564at2759; -. DR PhylomeDB; P63086; -. DR BRENDA; 2.7.11.24; 5301. DR Reactome; R-RNO-111995; phospho-PLA2 pathway. DR Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation. DR Reactome; R-RNO-112411; MAPK1 (ERK2) activation. DR Reactome; R-RNO-1181150; Signaling by NODAL. DR Reactome; R-RNO-1295596; Spry regulation of FGF signaling. DR Reactome; R-RNO-1502540; Signaling by Activin. DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-RNO-170968; Frs2-mediated activation. DR Reactome; R-RNO-198753; ERK/MAPK targets. DR Reactome; R-RNO-202670; ERKs are inactivated. DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-RNO-2559585; Oncogene Induced Senescence. DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation. DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth. DR Reactome; R-RNO-437239; Recycling pathway of L1. DR Reactome; R-RNO-445144; Signal transduction by L1. DR Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors. DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs). DR Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling. DR Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling. DR Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling. DR Reactome; R-RNO-5654733; Negative regulation of FGFR4 signaling. DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases. DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade. DR Reactome; R-RNO-5674135; MAP2K and MAPK activation. DR Reactome; R-RNO-5674499; Negative feedback regulation of MAPK pathway. DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-RNO-74749; Signal attenuation. DR Reactome; R-RNO-877300; Interferon gamma signaling. DR Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK. DR Reactome; R-RNO-8939211; ESR-mediated signaling. DR Reactome; R-RNO-9627069; Regulation of the apoptosome activity. DR Reactome; R-RNO-9634635; Estrogen-stimulated signaling through PRKCZ. DR Reactome; R-RNO-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling. DR Reactome; R-RNO-9732724; IFNG signaling activates MAPKs. DR Reactome; R-RNO-982772; Growth hormone receptor signaling. DR EvolutionaryTrace; P63086; -. DR PRO; PR:P63086; -. DR Proteomes; UP000002494; Chromosome 11. DR Bgee; ENSRNOG00000001849; Expressed in frontal cortex and 19 other cell types or tissues. DR GO; GO:0030424; C:axon; IDA:RGD. DR GO; GO:0005901; C:caveola; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD. DR GO; GO:0005769; C:early endosome; TAS:UniProtKB. DR GO; GO:0005925; C:focal adhesion; TAS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB. DR GO; GO:0005770; C:late endosome; TAS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0043204; C:perikaryon; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0031143; C:pseudopodium; ISO:RGD. DR GO; GO:0005524; F:ATP binding; IDA:RGD. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0016301; F:kinase activity; ISO:RGD. DR GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB. DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD. DR GO; GO:0019902; F:phosphatase binding; ISO:RGD. DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD. DR GO; GO:0004672; F:protein kinase activity; ISO:RGD. DR GO; GO:0019901; F:protein kinase binding; IPI:RGD. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI. DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISO:RGD. DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:RGD. DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD. DR GO; GO:0060020; P:Bergmann glial cell differentiation; ISO:RGD. DR GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; ISO:RGD. DR GO; GO:0072584; P:caveolin-mediated endocytosis; TAS:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central. DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD. DR GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD. DR GO; GO:0071310; P:cellular response to organic substance; IDA:RGD. DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD. DR GO; GO:0019858; P:cytosine metabolic process; ISO:RGD. DR GO; GO:0046697; P:decidualization; IDA:RGD. DR GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IMP:CAFA. DR GO; GO:0006974; P:DNA damage response; ISO:RGD. DR GO; GO:0038127; P:ERBB signaling pathway; ISO:RGD. DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; ISO:RGD. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:CAFA. DR GO; GO:0060324; P:face development; ISO:RGD. DR GO; GO:0007507; P:heart development; ISO:RGD. DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD. DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD. DR GO; GO:0060425; P:lung morphogenesis; ISO:RGD. DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISO:RGD. DR GO; GO:0000165; P:MAPK cascade; IMP:RGD. DR GO; GO:0042552; P:myelination; ISO:RGD. DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD. DR GO; GO:0014032; P:neural crest cell development; ISO:RGD. DR GO; GO:0042473; P:outer ear morphogenesis; ISO:RGD. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD. DR GO; GO:0030335; P:positive regulation of cell migration; IEP:RGD. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEP:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:CAFA. DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:RGD. DR GO; GO:0120041; P:positive regulation of macrophage proliferation; ISO:RGD. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:RGD. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB. DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD. DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD. DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:RGD. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0030641; P:regulation of cellular pH; ISO:RGD. DR GO; GO:0051493; P:regulation of cytoskeleton organization; TAS:UniProtKB. DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB. DR GO; GO:0090170; P:regulation of Golgi inheritance; TAS:UniProtKB. DR GO; GO:0030278; P:regulation of ossification; ISO:RGD. DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB. DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB. DR GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB. DR GO; GO:0043627; P:response to estrogen; IDA:RGD. DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD. DR GO; GO:0035094; P:response to nicotine; IGI:ARUK-UCL. DR GO; GO:0009636; P:response to toxic substance; IDA:RGD. DR GO; GO:0014044; P:Schwann cell development; ISO:RGD. DR GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB. DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISO:RGD. DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:RGD. DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD. DR GO; GO:0048538; P:thymus development; ISO:RGD. DR GO; GO:0030878; P:thyroid gland development; ISO:RGD. DR GO; GO:0060440; P:trachea formation; ISO:RGD. DR CDD; cd07849; STKc_ERK1_2_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID50321; -. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008349; MAPK_ERK1/2. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF599; MITOGEN-ACTIVATED PROTEIN KINASE 1; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01770; ERK1ERK2MAPK. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR World-2DPAGE; 0004:P63086; -. DR Genevisible; P63086; RN. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; ATP-binding; Cell cycle; KW Cell junction; Cytoplasm; Cytoskeleton; Direct protein sequencing; Kinase; KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.2" FT CHAIN 2..358 FT /note="Mitogen-activated protein kinase 1" FT /id="PRO_0000186249" FT DOMAIN 23..311 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 183..185 FT /note="TXY" FT ACT_SITE 147 FT /note="Proton acceptor" FT BINDING 29..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:8639522" FT BINDING 52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:8639522" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.2" FT MOD_RES 27 FT /note="Phosphoserine; by SGK1" FT /evidence="ECO:0000250|UniProtKB:P28482" FT MOD_RES 183 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 185 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 188 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P28482" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28482" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28482" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28482" FT MUTAGEN 117 FT /note="Q->A: Reduced affinity for DCC. Strongly reduced FT affinity for DCC; when associated with A-123." FT /evidence="ECO:0000269|PubMed:21070949" FT MUTAGEN 123 FT /note="H->A: Reduced affinity for DCC. Strongly reduced FT affinity for DCC; when associated with A-117." FT /evidence="ECO:0000269|PubMed:21070949" FT MUTAGEN 155 FT /note="L->A: Reduced affinity for DCC." FT /evidence="ECO:0000269|PubMed:21070949" FT STRAND 10..17 FT /evidence="ECO:0007829|PDB:5HD4" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 23..31 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 33..42 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 43..46 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 47..54 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:6FXV" FT HELIX 60..75 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 99..104 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 110..116 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 121..140 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:3O71" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:2ERK" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:3O71" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:6OPK" FT HELIX 206..221 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 231..242 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 247..251 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 256..264 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:4S32" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:2ERK" FT HELIX 282..291 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 302..306 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:4S32" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 317..319 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:4N4S" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:6OT6" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:4S32" FT HELIX 354..356 FT /evidence="ECO:0007829|PDB:1GOL" SQ SEQUENCE 358 AA; 41276 MW; 3BBCF22471EDBA0B CRC64; MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA IKKISPFEHQ TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY IVQDLMETDL YKLLKTQHLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNTTCD LKICDFGLAR VADPDHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA RFQPGYRS //