MK01_RAT
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 03-AUG-2022, entry version 194.
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 a variety of other signaling-related
CC molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as
CC RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK,
CC MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or
CC MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are
CC other substrates which enable the propagation the MAPK/ERK signal to
CC additional cytosolic and nuclear targets, thereby extending the
CC specificity of the cascade. Mediates phosphorylation of TPR in response
CC to EGF stimulation. May play a role in the spindle assembly checkpoint.
CC Phosphorylates PML and promotes its interaction with PIN1, leading to
CC 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 -!- 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 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 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 iPTMnet; P63086; -.
DR PhosphoSitePlus; P63086; -.
DR World-2DPAGE; 0004:P63086; -.
DR jPOST; P63086; -.
DR PaxDb; P63086; -.
DR PRIDE; P63086; -.
DR Ensembl; ENSRNOT00000002533; ENSRNOP00000002533; ENSRNOG00000001849.
DR GeneID; 116590; -.
DR KEGG; rno:116590; -.
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 OMA; SFFDFDY; -.
DR OrthoDB; 741207at2759; -.
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-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-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-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 tissues.
DR Genevisible; P63086; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA: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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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; IDA: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:0004708; F:MAP kinase kinase activity; ISO:RGD.
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:0007568; P:aging; IDA: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:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:1903351; P:cellular response to dopamine; ISO:RGD.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; 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:0038127; P:ERBB 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: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: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:0010628; P:positive regulation of gene expression; ISO:RGD.
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:0051973; P:positive regulation of telomerase activity; ISO:RGD.
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:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:0045727; P:positive regulation of translation; IMP: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:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA: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 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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01770; ERK1ERK2MAPK.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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;
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
