MK07_MOUSE
ID MK07_MOUSE Reviewed; 806 AA.
AC Q9WVS8; Q3U2N7; Q3UG52; Q497T0; Q5NCN6; Q5NCN7; Q5NCN9; Q6QLU8; Q9R1D9;
AC Q9WVF3; Q9WVF4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Mitogen-activated protein kinase 7;
DE Short=MAP kinase 7;
DE Short=MAPK 7;
DE EC=2.7.11.24;
DE AltName: Full=Big MAP kinase 1;
DE Short=BMK-1;
DE AltName: Full=Extracellular signal-regulated kinase 5;
DE Short=ERK-5;
GN Name=Mapk7; Synonyms=Bmk1, Erk5;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10473620; DOI=10.1074/jbc.274.37.26563;
RA Kamakura S., Moriguchi T., Nishida E.;
RT "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases.
RT Identification and characterization of a signaling pathway to the
RT nucleus.";
RL J. Biol. Chem. 274:26563-26571(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11139578; DOI=10.1074/jbc.m009286200;
RA Yan C., Luo H., Lee J.-D., Abe J.-I., Berk B.C.;
RT "Molecular cloning of mouse ERK5/BMK1 splice variants and characterization
RT of ERK5 functional domains.";
RL J. Biol. Chem. 276:10870-10878(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=15716121; DOI=10.1016/j.gene.2004.11.011;
RA McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R.;
RT "Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice
RT variant.";
RL Gene 345:183-190(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NOD;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP FUNCTION.
RX PubMed=11520859; DOI=10.1093/embo-reports/kve177;
RA Dinev D., Jordan B.W.M., Neufeld B., Lee J.-D., Lindemann D., Rapp U.R.,
RA Ludwig S.;
RT "Extracellular signal regulated kinase 5 (ERK5) is required for the
RT differentiation of muscle cells.";
RL EMBO Rep. 2:829-834(2001).
RN [8]
RP FUNCTION.
RX PubMed=11278431; DOI=10.1074/jbc.m008748200;
RA Dong F., Gutkind J.S., Larner A.C.;
RT "Granulocyte colony-stimulating factor induces ERK5 activation, which is
RT differentially regulated by protein-tyrosine kinases and protein kinase C.
RT Regulation of cell proliferation and survival.";
RL J. Biol. Chem. 276:10811-10816(2001).
RN [9]
RP FUNCTION.
RX PubMed=15085193; DOI=10.1172/jci200419890;
RA Hayashi M., Kim S.W., Imanaka-Yoshida K., Yoshida T., Abel E.D.,
RA Eliceiri B., Yang Y., Ulevitch R.J., Lee J.D.;
RT "Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity
RT and leads to endothelial failure.";
RL J. Clin. Invest. 113:1138-1148(2004).
RN [10]
RP INTERACTION WITH HSP90AB1.
RX PubMed=23428871; DOI=10.1128/mcb.01246-12;
RA Erazo T., Moreno A., Ruiz-Babot G., Rodriguez-Asiain A., Morrice N.A.,
RA Espadamala J., Bayascas J.R., Gomez N., Lizcano J.M.;
RT "Canonical and kinase activity-independent mechanisms for extracellular
RT signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation
RT of Hsp90 from the ERK5-Cdc37 complex.";
RL Mol. Cell. Biol. 33:1671-1686(2013).
CC -!- FUNCTION: Plays a role in various cellular processes such as
CC proliferation, differentiation and cell survival. The upstream
CC activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it
CC translocates to the nucleus and phosphorylates various downstream
CC targets including MEF2C. EGF activates MAPK7 through a Ras-independent
CC and MAP2K5-dependent pathway. May have a role in muscle cell
CC differentiation. May be important for endothelial function and
CC maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact
CC specifically with one another and not with MEK1/ERK1 or MEK2/ERK2
CC pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth
CC factor-induced cell cycle progression (By similarity). Involved in the
CC regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:11139578,
CC ECO:0000269|PubMed:11278431, ECO:0000269|PubMed:11520859,
CC ECO:0000269|PubMed:15085193, ECO:0000269|PubMed:15716121}.
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: Activated by tyrosine and threonine
CC phosphorylation. Activated in response to hyperosmolarity, hydrogen
CC peroxide, and epidermal growth factor (EGF) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAP2K5 (By similarity). Forms oligomers.
CC Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates
CC the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not
CC MEF2D (By similarity). Interacts with SGK1 (By similarity). Interacts
CC with PML (By similarity). Interacts (via N-terminal half) with
CC HSP90AB1-CDC37 chaperone complex in resting cells; the interaction is
CC MAP2K5-independent and prevents MAPK7 from ubiquitination and
CC proteasomal degradation (PubMed:23428871). {ECO:0000250,
CC ECO:0000269|PubMed:23428871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139578}. Nucleus
CC {ECO:0000269|PubMed:11139578}. Nucleus, PML body {ECO:0000250}.
CC Note=Translocates to the nucleus upon activation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Isoform 1 is detected in cytoplasm and nucleus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250}. Note=Isoform
CC 2 is detected only in the nucleus. Translocates to the nucleus upon
CC activation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000250}. Note=Isoform
CC 2 is detected only in the nucleus. Translocates to the nucleus upon
CC activation (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Big MAP kinase 1a, mERK5a;
CC IsoId=Q9WVS8-1; Sequence=Displayed;
CC Name=2; Synonyms=Big MAP kinase 1b, mERK5b;
CC IsoId=Q9WVS8-2; Sequence=VSP_035202;
CC Name=3; Synonyms=Big MAP kinase 1c, mERK5c;
CC IsoId=Q9WVS8-3; Sequence=VSP_035201;
CC Name=4; Synonyms=Big MAP kinase 1d, mERK5-T;
CC IsoId=Q9WVS8-4; Sequence=VSP_035203;
CC Name=5;
CC IsoId=Q9WVS8-5; Sequence=VSP_035204;
CC -!- TISSUE SPECIFICITY: Detected in testis, brain, kidney, lung and heart.
CC Detected in total embryo (at protein level).
CC {ECO:0000269|PubMed:11139578}.
CC -!- DOMAIN: The second proline-rich region may interact with actin
CC targeting the kinase to a specific location in the cell.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates the
CC enzyme. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May not have a kinase activity. May not
CC stimulate MEF2C activity. May function as dominant negative inhibitor
CC of the ERK5 signaling pathway. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May not have a kinase activity. May not
CC stimulate MEF2C activity. May function as dominant negative inhibitor
CC of the ERK5 signaling pathway. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Unable to translocate from the cytoplasm to
CC the nucleus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AB019373; BAA82039.1; -; mRNA.
DR EMBL; AF126159; AAD39394.1; -; mRNA.
DR EMBL; AF126160; AAD39395.1; -; mRNA.
DR EMBL; AF126161; AAD39396.1; -; mRNA.
DR EMBL; AK148119; BAE28357.1; -; mRNA.
DR EMBL; AK155187; BAE33103.1; -; mRNA.
DR EMBL; AY534740; AAS38576.1; -; mRNA.
DR EMBL; BC100398; AAI00399.1; -; mRNA.
DR EMBL; AL604029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24814.1; -. [Q9WVS8-1]
DR CCDS; CCDS70205.1; -. [Q9WVS8-2]
DR RefSeq; NP_001277962.1; NM_001291033.1. [Q9WVS8-2]
DR RefSeq; NP_001277963.1; NM_001291034.1. [Q9WVS8-1]
DR RefSeq; NP_001277964.1; NM_001291035.1. [Q9WVS8-3]
DR RefSeq; NP_001277965.1; NM_001291036.1. [Q9WVS8-3]
DR RefSeq; NP_001277966.1; NM_001291037.1.
DR RefSeq; NP_035971.1; NM_011841.2. [Q9WVS8-1]
DR RefSeq; XP_006533340.1; XM_006533277.3. [Q9WVS8-1]
DR RefSeq; XP_006533343.1; XM_006533280.3. [Q9WVS8-3]
DR RefSeq; XP_006533344.1; XM_006533281.3.
DR RefSeq; XP_006533347.1; XM_006533284.3. [Q9WVS8-3]
DR RefSeq; XP_006533348.1; XM_006533285.3. [Q9WVS8-3]
DR RefSeq; XP_006533349.1; XM_006533286.3. [Q9WVS8-3]
DR AlphaFoldDB; Q9WVS8; -.
DR SMR; Q9WVS8; -.
DR BioGRID; 204806; 5.
DR CORUM; Q9WVS8; -.
DR STRING; 10090.ENSMUSP00000078087; -.
DR iPTMnet; Q9WVS8; -.
DR PhosphoSitePlus; Q9WVS8; -.
DR EPD; Q9WVS8; -.
DR MaxQB; Q9WVS8; -.
DR PaxDb; Q9WVS8; -.
DR PeptideAtlas; Q9WVS8; -.
DR PRIDE; Q9WVS8; -.
DR ProteomicsDB; 295670; -. [Q9WVS8-1]
DR ProteomicsDB; 295671; -. [Q9WVS8-2]
DR ProteomicsDB; 295672; -. [Q9WVS8-3]
DR ProteomicsDB; 295673; -. [Q9WVS8-4]
DR ProteomicsDB; 295674; -. [Q9WVS8-5]
DR Antibodypedia; 4345; 675 antibodies from 41 providers.
DR DNASU; 23939; -.
DR Ensembl; ENSMUST00000079080; ENSMUSP00000078087; ENSMUSG00000001034. [Q9WVS8-1]
DR Ensembl; ENSMUST00000108714; ENSMUSP00000104354; ENSMUSG00000001034. [Q9WVS8-2]
DR GeneID; 23939; -.
DR KEGG; mmu:23939; -.
DR UCSC; uc007jho.2; mouse. [Q9WVS8-2]
DR UCSC; uc007jhp.2; mouse. [Q9WVS8-1]
DR UCSC; uc007jht.1; mouse. [Q9WVS8-4]
DR CTD; 5598; -.
DR MGI; MGI:1346347; Mapk7.
DR VEuPathDB; HostDB:ENSMUSG00000001034; -.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000160215; -.
DR HOGENOM; CLU_008789_1_0_1; -.
DR InParanoid; Q9WVS8; -.
DR OMA; NWSGQQL; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9WVS8; -.
DR TreeFam; TF105099; -.
DR Reactome; R-MMU-198753; ERK/MAPK targets.
DR Reactome; R-MMU-198765; Signalling to ERK5.
DR Reactome; R-MMU-202670; ERKs are inactivated.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 23939; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Mapk7; mouse.
DR PRO; PR:Q9WVS8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WVS8; protein.
DR Bgee; ENSMUSG00000001034; Expressed in embryonic brain and 190 other tissues.
DR ExpressionAtlas; Q9WVS8; baseline and differential.
DR Genevisible; Q9WVS8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004707; F:MAP kinase activity; ISO:MGI.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
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:0033173; P:calcineurin-NFAT signaling cascade; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0071499; P:cellular response to laminar fluid shear stress; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0070375; P:ERK5 cascade; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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; 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 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cytoplasm;
KW Differentiation; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT CHAIN 2..806
FT /note="Mitogen-activated protein kinase 7"
FT /id="PRO_0000186261"
FT DOMAIN 55..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..77
FT /note="Required for cytoplasmic targeting"
FT REGION 78..139
FT /note="Required for binding to MAP2K5"
FT REGION 140..406
FT /note="Necessary for oligomerization"
FT REGION 407..806
FT /note="May not be required for kinase activity; required to
FT stimulate MEF2C activity"
FT REGION 424..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..221
FT /note="TXY"
FT MOTIF 505..539
FT /note="Nuclear localization signal"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..644
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 61..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT MOD_RES 723
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT VAR_SEQ 1..139
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11139578"
FT /id="VSP_035201"
FT VAR_SEQ 1..77
FT /note="MAEPLKEEDGEDGSGEPPGRVKAEPVHTAASVVAKNLALLKARSFDVTFDVG
FT DEYEIIETIGNGAYGVVSSARRRLT -> MCGLLSRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11139578,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035202"
FT VAR_SEQ 493..806
FT /note="DGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERG
FT AGTLGGPSTDPLAGLVLSDNDRSLLERWTRMARPPAPAPAPAPAPAPAPSSAQPTSTPT
FT GPVSQSTGPLQPAGSIPGPASQPVCPPPGPVPQPAGPIPAPLQTAPSTSLLASQSLVPP
FT SGLPGSGAPEVLPYFPSGPPPPDPGLTPQPSTSESPDVNLVTQQLSKSQVEDPLPPVFS
FT GTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPA
FT DIESLQREIQMDSPMLLSDLPDLQEP -> GGVWAQQLSG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15716121"
FT /id="VSP_035203"
FT VAR_SEQ 757..806
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035204"
FT CONFLICT 191
FT /note="N -> D (in Ref. 4; BAE28357)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="P -> H (in Ref. 4; BAE28357)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> K (in Ref. 5; AAI00399)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="A -> V (in Ref. 2; AAD39394/AAD39395/AAD39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="A -> R (in Ref. 2; AAD39394/AAD39395/AAD39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="P -> PPAPA (in Ref. 4; BAE28357/BAE33103)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="A -> R (in Ref. 2; AAD39394/AAD39395/AAD39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="A -> Q (in Ref. 2; AAD39394/AAD39395/AAD39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="S -> C (in Ref. 2; AAD39394/AAD39395/AAD39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="P -> A (in Ref. 2; AAD39394/AAD39395/AAD39396)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="L -> V (in Ref. 4; BAE28357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 87733 MW; E7CC41C4BBDE0633 CRC64;
MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD VGDEYEIIET
IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI
LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH
RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT
QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA
PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPVCPDVEMP
SPWAPSGDCA MESPPPALPP CSDPAPDTVD LTLQPAPPAS ELAPPKREGA ISDNTKAALK
AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER
KERGAGTLGG PSTDPLAGLV LSDNDRSLLE RWTRMARPPA PAPAPAPAPA PAPSSAQPTS
TPTGPVSQST GPLQPAGSIP GPASQPVCPP PGPVPQPAGP IPAPLQTAPS TSLLASQSLV
PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV NLVTQQLSKS QVEDPLPPVF
SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDGQADS ASLSASLLAD WLEGHGMNPA
DIESLQREIQ MDSPMLLSDL PDLQEP
