MKNK2_MOUSE
ID MKNK2_MOUSE Reviewed; 459 AA.
AC Q8CDB0; O08606; Q75PY0; Q9D893;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=MAP kinase-interacting serine/threonine-protein kinase 2;
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase signal-integrating kinase 2;
DE Short=MAPK signal-integrating kinase 2;
DE Short=Mnk2;
GN Name=Mknk2; Synonyms=Mnk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:CAA71966.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15254222; DOI=10.1128/mcb.24.15.6539-6549.2004;
RA Ueda T., Watanabe-Fukunaga R., Fukuyama H., Nagata S., Fukunaga R.;
RT "Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation
RT of eukaryotic initiation factor 4E but not for cell growth or
RT development.";
RL Mol. Cell. Biol. 24:6539-6549(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Small intestine, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-459 (ISOFORM 1), FUNCTION, AND INTERACTION
RP WITH MAPK3 AND MAPK1.
RC TISSUE=Embryo;
RX PubMed=9155017; DOI=10.1093/emboj/16.8.1909;
RA Waskiewicz A.J., Flynn A., Proud C.G., Cooper J.A.;
RT "Mitogen-activated protein kinases activate the serine/threonine kinases
RT Mnk1 and Mnk2.";
RL EMBO J. 16:1909-1920(1997).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-459 (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION AS EIF4E KINASE, PHOSPHORYLATION AT SER-74; SER-431; SER-434;
RP SER-446 AND THR-450, PHOSPHORYLATION BY MAPK1/ERK2; MAPK11 AND MAPK14, AND
RP INTERACTION WITH EIF4G PROTEINS.
RX PubMed=11154262; DOI=10.1128/mcb.21.3.743-754.2001;
RA Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
RT "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a
RT eukaryotic initiation factor 4E kinase with high levels of basal activity
RT in mammalian cells.";
RL Mol. Cell. Biol. 21:743-754(2001).
RN [6]
RP INTERACTION WITH MAPK3/ERK1 AND MAPK1/ERK2, AND MUTAGENESIS OF ASP-238;
RP LEU-438; GLN-440; SER-446 AND SER-448.
RX PubMed=16162500; DOI=10.1074/jbc.m508356200;
RA Parra J.L., Buxade M., Proud C.G.;
RT "Features of the catalytic domains and C termini of the MAPK signal-
RT integrating kinases Mnk1 and Mnk2 determine their differing activities and
RT regulatory properties.";
RL J. Biol. Chem. 280:37623-37633(2005).
RN [7]
RP FUNCTION IN SERUM-WITHDRAWAL INDUCED APOPTOSIS, AND ACTIVITY REGULATION.
RX PubMed=17903173; DOI=10.1111/j.1365-2443.2007.01122.x;
RA Chrestensen C.A., Eschenroeder A., Ross W.G., Ueda T.,
RA Watanabe-Fukunaga R., Fukunaga R., Sturgill T.W.;
RT "Loss of MNK function sensitizes fibroblasts to serum-withdrawal induced
RT apoptosis.";
RL Genes Cells 12:1133-1140(2007).
RN [8]
RP FUNCTION AS EIF4E KINASE.
RX PubMed=17689282; DOI=10.1016/j.biocel.2007.05.001;
RA Shenberger J.S., Zhang L., Hughlock M.K., Ueda T., Watanabe-Fukunaga R.,
RA Fukunaga R.;
RT "Roles of mitogen-activated protein kinase signal-integrating kinases 1 and
RT 2 in oxidant-mediated eIF4E phosphorylation.";
RL Int. J. Biochem. Cell Biol. 39:1828-1842(2007).
RN [9]
RP FUNCTION IN MRNA TRANSLATION REGULATION DURING SPERMATOGENESIS.
RX PubMed=20574055; DOI=10.1095/biolreprod.110.085050;
RA Messina V., Di Sauro A., Pedrotti S., Adesso L., Latina A., Geremia R.,
RA Rossi P., Sette C.;
RT "Differential contribution of the MTOR and MNK pathways to the regulation
RT of mRNA translation in meiotic and postmeiotic mouse male germ cells.";
RL Biol. Reprod. 83:607-615(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION AS EIF4E KINASE, AND INTERACTION WITH EIF4G1.
RX PubMed=20823271; DOI=10.1128/mcb.00448-10;
RA Shveygert M., Kaiser C., Bradrick S.S., Gromeier M.;
RT "Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by
RT mitogen-activated protein kinase occurs through modulation of Mnk1-eIF4G
RT interaction.";
RL Mol. Cell. Biol. 30:5160-5167(2010).
RN [12]
RP FUNCTION IN EIF4E PHOSPHORYLATION REGULATION, DEPHOSPHORYLATION BY PP2A,
RP AND ACTIVITY REGULATION.
RX PubMed=20927323; DOI=10.1593/neo.10704;
RA Li Y., Yue P., Deng X., Ueda T., Fukunaga R., Khuri F.R., Sun S.-Y.;
RT "Protein phosphatase 2A negatively regulates eukaryotic initiation factor
RT 4E phosphorylation and eIF4F assembly through direct dephosphorylation of
RT Mnk and eIF4E.";
RL Neoplasia 12:848-855(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase that phosphorylates SFPQ/PSF,
CC HNRNPA1 and EIF4E. May play a role in the response to environmental
CC stress and cytokines. Appears to regulate translation by
CC phosphorylating EIF4E, thus increasing the affinity of this protein for
CC the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-
CC inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from
CC cytoplasm to nucleus. Enhances the formation of EIF4F complex in
CC pachytene spermatocytes, thus promoting mRNA translation during
CC spermatogenesis. Displays a high basal kinase activity. Acts as a
CC mediator of the suppressive effects of IFNgamma on hematopoiesis.
CC Negative regulator for signals that control generation of arsenic
CC trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses.
CC Involved in anti-apoptotic signaling in response to serum withdrawal.
CC {ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:17689282,
CC ECO:0000269|PubMed:17903173, ECO:0000269|PubMed:20574055,
CC ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:20927323,
CC ECO:0000269|PubMed:9155017}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:9155017};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:9155017};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9155017};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by CGP57380 and staurosporine.
CC {ECO:0000269|PubMed:17903173, ECO:0000269|PubMed:20927323}.
CC -!- SUBUNIT: Interacts with ESR2 and EIF4E in the nucleus (By similarity).
CC Monomer. Interacts with the C-terminal regions of EIF4G1 and EIF4G2;
CC this interaction is promoted when MAPK pathways are repressed but
CC repressed upon ERK proteins activation. Also binds to dephosphorylated
CC MAPK3/ERK1 and MAPK1/ERK2. Interaction with phosphorylated MAPK3/ERK1
CC and MAPK1/ERK2 protects it from dephosphorylation and inactivation.
CC {ECO:0000250, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:16162500,
CC ECO:0000269|PubMed:20823271, ECO:0000269|PubMed:9155017}.
CC -!- INTERACTION:
CC Q8CDB0; P63085: Mapk1; NbExp=23; IntAct=EBI-646209, EBI-397697;
CC Q8CDB0; P39429: Traf2; NbExp=3; IntAct=EBI-646209, EBI-520016;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, PML body
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9155017};
CC IsoId=Q8CDB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDB0-2; Sequence=VSP_007355;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined,
CC with high levels in skeletal muscle and low levels in brain.
CC {ECO:0000269|PubMed:9155017}.
CC -!- PTM: Dual phosphorylation of Thr-244 and Thr-249 activates the kinase.
CC Phosphorylation of Thr-379 activates the kinase. Phosphorylated upon
CC arsenic trioxide As(2)O(3) treatment. Phosphorylated by MAPK1/ERK2,
CC MAPK11 and MAPK14 (By similarity). Dephosphorylated by PP2A.
CC {ECO:0000250, ECO:0000269|PubMed:11154262}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10256.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB25570.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA71966.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB164081; BAD18852.1; -; mRNA.
DR EMBL; AK008277; BAB25570.2; ALT_FRAME; mRNA.
DR EMBL; AK030830; BAC27151.2; -; mRNA.
DR EMBL; AK154235; BAE32453.1; -; mRNA.
DR EMBL; Y11092; CAA71966.1; ALT_FRAME; mRNA.
DR EMBL; BC010256; AAH10256.1; ALT_INIT; mRNA.
DR CCDS; CCDS24030.2; -. [Q8CDB0-1]
DR RefSeq; NP_067437.2; NM_021462.4. [Q8CDB0-1]
DR RefSeq; XP_006513379.1; XM_006513316.1. [Q8CDB0-1]
DR RefSeq; XP_017169313.1; XM_017313824.1.
DR AlphaFoldDB; Q8CDB0; -.
DR SMR; Q8CDB0; -.
DR BioGRID; 201432; 3.
DR IntAct; Q8CDB0; 3.
DR MINT; Q8CDB0; -.
DR STRING; 10090.ENSMUSP00000003433; -.
DR ChEMBL; CHEMBL4523384; -.
DR iPTMnet; Q8CDB0; -.
DR PhosphoSitePlus; Q8CDB0; -.
DR EPD; Q8CDB0; -.
DR MaxQB; Q8CDB0; -.
DR PaxDb; Q8CDB0; -.
DR PRIDE; Q8CDB0; -.
DR ProteomicsDB; 295954; -. [Q8CDB0-1]
DR ProteomicsDB; 295955; -. [Q8CDB0-2]
DR Antibodypedia; 10678; 309 antibodies from 30 providers.
DR DNASU; 17347; -.
DR Ensembl; ENSMUST00000200082; ENSMUSP00000143508; ENSMUSG00000020190. [Q8CDB0-1]
DR GeneID; 17347; -.
DR KEGG; mmu:17347; -.
DR UCSC; uc007gef.3; mouse. [Q8CDB0-1]
DR CTD; 2872; -.
DR MGI; MGI:894279; Mknk2.
DR VEuPathDB; HostDB:ENSMUSG00000020190; -.
DR eggNOG; KOG0607; Eukaryota.
DR GeneTree; ENSGT00940000154587; -.
DR InParanoid; Q8CDB0; -.
DR OMA; NKMTEVT; -.
DR OrthoDB; 608695at2759; -.
DR PhylomeDB; Q8CDB0; -.
DR TreeFam; TF314050; -.
DR BioGRID-ORCS; 17347; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mknk2; mouse.
DR PRO; PR:Q8CDB0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8CDB0; protein.
DR Bgee; ENSMUSG00000020190; Expressed in peripheral lymph node and 263 other tissues.
DR ExpressionAtlas; Q8CDB0; baseline and differential.
DR Genevisible; Q8CDB0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISO:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Alternative splicing; Apoptosis; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Translation regulation; Zinc.
FT CHAIN 1..459
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase 2"
FT /id="PRO_0000086337"
FT DOMAIN 84..368
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 37..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 438..442
FT /note="MAP kinase binding"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 90..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 160..162
FT /ligand="staurosporine"
FT /ligand_id="ChEBI:CHEBI:57491"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="staurosporine"
FT /ligand_id="ChEBI:CHEBI:57491"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11154262,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH9"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH9"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH9"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11154262"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11154262"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11154262"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11154262"
FT VAR_SEQ 48..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007355"
FT MUTAGEN 238
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16162500"
FT MUTAGEN 438
FT /note="L->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:16162500"
FT MUTAGEN 440
FT /note="Q->R: Reduced MAPK3/ERK1 and MAPK1/ERK2-binding."
FT /evidence="ECO:0000269|PubMed:16162500"
FT MUTAGEN 446
FT /note="S->A,D: Normal MAPK3/ERK1 and MAPK1/ERK2-binding."
FT /evidence="ECO:0000269|PubMed:16162500"
FT MUTAGEN 448
FT /note="S->A: Normal MAPK3/ERK1 and MAPK1/ER2K-binding."
FT /evidence="ECO:0000269|PubMed:16162500"
FT MUTAGEN 448
FT /note="S->D: Reduced MAPK3/ERK1 and MAPK1/ER2K-binding."
FT /evidence="ECO:0000269|PubMed:16162500"
FT CONFLICT 256
FT /note="Y -> D (in Ref. 2; BAB25570)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> P (in Ref. 2; BAB25570)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="L -> I (in Ref. 2; BAB25570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 51633 MW; 5252C711AD99729A CRC64;
MVQKRTAELQ GFHRSFKGQN PFELAFSLDL AQHRDSDFSP QCEARPDMPS SQPIDIPDAK
KRGRKKKRCR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT CVNLITNQEY AVKIIEKQLG
HIRSRVFREV EMLYQCQGHR NVLELIEFFE EEDRFYLVFE KMRGGSILSH IHRRRHFNEL
EASVVVQDVA SALDFLHNKG IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS
PISTPELLTP CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGHCG
SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWSHISFA AKDLISKLLV RDAKQRLSAA
QVLQHPWVQG CAPENTLPTP LVLQRNSCAK DLTSFAAEAI AMNRQLAQCE EDAGQDQPVV
IRATSRCLQL SPPSQSKLAQ RRQRASLSAT PVVLVGDRA
