MP2K7_MOUSE
ID MP2K7_MOUSE Reviewed; 535 AA.
AC Q8CE90; O35406; O35720; O35871; O35872; O54780; O70242; O70243; Q8BSP1;
AC Q9QWG6; Q9R1Z3; Q9R1Z4; Q9R1Z5; Q9R1Z6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 7;
DE Short=MAP kinase kinase 7;
DE Short=MAPKK 7;
DE EC=2.7.12.2 {ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090};
DE AltName: Full=JNK-activating kinase 2;
DE AltName: Full=MAPK/ERK kinase 7;
DE Short=MEK 7;
DE AltName: Full=c-Jun N-terminal kinase kinase 2;
DE Short=JNK kinase 2;
DE Short=JNKK 2;
GN Name=Map2k7 {ECO:0000312|MGI:MGI:1346871};
GN Synonyms=Mkk7 {ECO:0000312|EMBL:AAC16274.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAB81848.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9405446; DOI=10.1074/jbc.272.51.32378;
RA Yao Z., Diener K., Wang X.S., Zukowski M., Matsumoto G., Zhou G., Mo R.,
RA Sasaki T., Nishina H., Hui C.C., Tan T.-H., Woodgett J.P., Penninger J.M.;
RT "Activation of stress-activated protein kinases/c-Jun N-terminal protein
RT kinases (SAPKs/JNKs) by a novel mitogen-activated protein kinase kinase
RT (MKK7).";
RL J. Biol. Chem. 272:32378-32383(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC53365.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9312105; DOI=10.1074/jbc.272.40.24994;
RA Holland P.M., Magali S., Campbell J.S., Noselli S., Cooper J.A.;
RT "MKK7 is a stress-activated mitogen-activated protein kinase kinase
RT functionally related to hemipterous.";
RL J. Biol. Chem. 272:24994-24998(1997).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA24383.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND FUNCTION.
RX PubMed=9384583; DOI=10.1093/emboj/16.23.7045;
RA Moriguchi T., Toyoshima F., Masuyama N., Hanafusa H., Gotoh Y., Nishida E.;
RT "A novel SAPK/JNK kinase, MKK7, stimulated by TNFalpha and cellular
RT stresses.";
RL EMBO J. 16:7045-7053(1997).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAC16274.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-311 (ISOFORMS 2/6), FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=B-cell {ECO:0000312|EMBL:AAC16274.1}, and
RC Thymus {ECO:0000312|EMBL:AAC16275.1};
RX PubMed=9535930; DOI=10.1074/jbc.273.15.9344;
RA Foltz I.N., Gerl R.E., Wieler J.S., Luckach M., Salmon R.A., Schrader J.W.;
RT "Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly
RT conserved c-Jun N-terminal kinase/stress-activated protein kinase
RT (JNK/SAPK) activated by environmental stresses and physiological stimuli.";
RL J. Biol. Chem. 273:9344-9351(1998).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAD15819.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 6; 7 AND 8), NUCLEOTIDE
RP SEQUENCE [GENOMIC DNA] OF 47-535 (ISOFORM 6), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=CD-1 {ECO:0000312|EMBL:AAB63447.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAB63447.1};
RX PubMed=9891090; DOI=10.1128/mcb.19.2.1569;
RA Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
RT "The MKK7 gene encodes a group of c-Jun NH2-terminal kinase kinases.";
RL Mol. Cell. Biol. 19:1569-1581(1999).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAC26111.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26111.1};
RC TISSUE=Fetal forelimb {ECO:0000312|EMBL:BAC27272.1},
RC Fetus {ECO:0000312|EMBL:BAE38066.1}, and
RC Skin {ECO:0000312|EMBL:BAC26111.1};
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAH70467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH70467.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH70467.1};
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 [8]
RP INTERACTION WITH MAPK8IP1/JIP1.
RX PubMed=9733513; DOI=10.1126/science.281.5383.1671;
RA Whitmarsh A.J., Cavanagh J., Tournier C., Yasuda J., Davis R.J.;
RT "A mammalian scaffold complex that selectively mediates MAP kinase
RT activation.";
RL Science 281:1671-1674(1998).
RN [9]
RP INTERACTION WITH MAPK8IP3/JIP3.
RX PubMed=10629060; DOI=10.1128/mcb.20.3.1030-1043.2000;
RA Kelkar N., Gupta S., Dickens M., Davis R.J.;
RT "Interaction of a mitogen-activated protein kinase signaling module with
RT the neuronal protein JIP3.";
RL Mol. Cell. Biol. 20:1030-1043(2000).
RN [10]
RP FUNCTION.
RX PubMed=11390361; DOI=10.1101/gad.888501;
RA Tournier C., Dong C., Turner T.K., Jones S.N., Flavell R.A., Davis R.J.;
RT "MKK7 is an essential component of the JNK signal transduction pathway
RT activated by proinflammatory cytokines.";
RL Genes Dev. 15:1419-1426(2001).
RN [11]
RP FUNCTION.
RX PubMed=12624093; DOI=10.1074/jbc.m213182200;
RA Kishimoto H., Nakagawa K., Watanabe T., Kitagawa D., Momose H., Seo J.,
RA Nishitai G., Shimizu N., Ohata S., Tanemura S., Asaka S., Goto T.,
RA Fukushi H., Yoshida H., Suzuki A., Sasaki T., Wada T., Penninger J.M.,
RA Nishina H., Katada T.;
RT "Different properties of SEK1 and MKK7 in dual phosphorylation of stress-
RT induced activated protein kinase SAPK/JNK in embryonic stem cells.";
RL J. Biol. Chem. 278:16595-16601(2003).
RN [12]
RP REVIEW ON ACTIVITY REGULATION.
RX PubMed=17496909; DOI=10.1038/sj.onc.1210392;
RA Raman M., Chen W., Cobb M.H.;
RT "Differential regulation and properties of MAPKs.";
RL Oncogene 26:3100-3112(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=20801953; DOI=10.1093/jb/mvq098;
RA Asaoka Y., Nishina H.;
RT "Diverse physiological functions of MKK4 and MKK7 during early
RT embryogenesis.";
RL J. Biochem. 148:393-401(2010).
RN [15]
RP REVIEW ON REGULATION, AND REVIEW ON FUNCTION.
RX PubMed=21333379; DOI=10.1016/j.ejcb.2010.11.008;
RA Haeusgen W., Herdegen T., Waetzig V.;
RT "The bottleneck of JNK signaling: molecular and functional characteristics
RT of MKK4 and MKK7.";
RL Eur. J. Cell Biol. 90:536-544(2011).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC1; MAP3K11; MAPK8IP1 AND MAPK8.
RX PubMed=23963642; DOI=10.1002/eji.201343635;
RA Cunningham C.A., Knudson K.M., Peng B.J., Teixeiro E., Daniels M.A.;
RT "The POSH/JIP-1 scaffold network regulates TCR-mediated JNK1 signals and
RT effector function in CD8(+) T cells.";
RL Eur. J. Immunol. 43:3361-3371(2013).
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH SH3RF1; RAC2; MAP3K7; MAPK8IP1; MAPK8 AND
RP MAPK9.
RX PubMed=27084103; DOI=10.4049/jimmunol.1501728;
RA Cunningham C.A., Cardwell L.N., Guan Y., Teixeiro E., Daniels M.A.;
RT "POSH regulates CD4+ T cell differentiation and survival.";
RL J. Immunol. 196:4003-4013(2016).
RN [18]
RP FUNCTION.
RX PubMed=28111074; DOI=10.1016/j.cell.2016.12.044;
RA Huang Y.A., Zhou B., Wernig M., Suedhof T.C.;
RT "ApoE2, ApoE3, and ApoE4 Differentially Stimulate APP Transcription and
RT Abeta Secretion.";
RL Cell 168:427-441(2017).
CC -!- FUNCTION: Dual specificity protein kinase which acts as an essential
CC component of the MAP kinase signal transduction pathway. Essential
CC component of the stress-activated protein kinase/c-Jun N-terminal
CC kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the
CC only known kinase to directly activate the stress-activated protein
CC kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3.
CC MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation,
CC but they differ in their preference for the phosphorylation site in the
CC Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of
CC the Tyr residue and MAP2K7/MKK7 for the Thr residue. The
CC monophosphorylation of JNKs on the Thr residue is sufficient to
CC increase JNK activity indicating that MAP2K7/MKK7 is important to
CC trigger JNK activity, while the additional phosphorylation of the Tyr
CC residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific
CC role in JNK signal transduction pathway activated by pro-inflammatory
CC cytokines. The MKK/JNK signaling pathway is also involved in
CC mitochondrial death signaling pathway, including the release cytochrome
CC c, leading to apoptosis. Part of a non-canonical MAPK signaling
CC pathway, composed of the upstream MAP3K12 kinase and downstream MAP
CC kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated
CC transcription of APP in response to APOE (PubMed:28111074).
CC {ECO:0000269|PubMed:11390361, ECO:0000269|PubMed:12624093,
CC ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:9312105,
CC ECO:0000269|PubMed:9384583, ECO:0000269|PubMed:9405446,
CC ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090}.
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=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090};
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=2.7.12.2; Evidence={ECO:0000269|PubMed:9535930,
CC ECO:0000269|PubMed:9891090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation by specific MAP
CC kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3, MAP3K11/MLK3
CC and MAP3K12/DLK. Isoforms 3 and 4 have lower basal activity but a
CC higher level of inducible activation, than isoforms 2, 6, 7 and 8.
CC {ECO:0000269|PubMed:9891090}.
CC -!- SUBUNIT: Interacts with RASSF7, the interaction promotes
CC phosphorylation. Interacts with VRK2 (By similarity). Interacts (via
CC its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and
CC MAPK10/JNK3 (By similarity). Interacts (via its DVD domain) with MAP3Ks
CC activators like MAP3K5/ASK1 and MAP3K1/MEKK1 (By similarity). Interacts
CC with SH3RF1, MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold
CC proteins. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3,
CC MAPK8IP1/JIP1 and MAPK8/JNK1 (PubMed:23963642). Found in a complex with
CC SH3RF1, RAC2, MAP3K7/TAK1, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2
CC (PubMed:27084103). {ECO:0000250|UniProtKB:O14733,
CC ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:23963642,
CC ECO:0000269|PubMed:27084103, ECO:0000269|PubMed:9733513}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9891090}. Cytoplasm
CC {ECO:0000269|PubMed:9891090}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8CE90-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:9312105,
CC ECO:0000269|PubMed:9891090}; Synonyms=a {ECO:0000269|PubMed:9312105},
CC beta 1 {ECO:0000269|PubMed:9891090};
CC IsoId=Q8CE90-2; Sequence=VSP_052266, VSP_052268, VSP_052269;
CC Name=3 {ECO:0000269|PubMed:9384583, ECO:0000269|PubMed:9891090};
CC Synonyms=alpha 2 {ECO:0000269|PubMed:9891090};
CC IsoId=Q8CE90-3; Sequence=VSP_052265, VSP_052270, VSP_052271;
CC Name=4 {ECO:0000269|PubMed:9891090}; Synonyms=alpha 1
CC {ECO:0000269|PubMed:9891090};
CC IsoId=Q8CE90-4; Sequence=VSP_052265, VSP_052268, VSP_052269;
CC Name=5 {ECO:0000269|PubMed:9312105}; Synonyms=b
CC {ECO:0000269|PubMed:9312105};
CC IsoId=Q8CE90-5; Sequence=VSP_052264, VSP_052267, VSP_052268,
CC VSP_052269;
CC Name=6 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9405446,
CC ECO:0000269|PubMed:9891090}; Synonyms=b {ECO:0000269|PubMed:15489334},
CC gamma 1 {ECO:0000269|PubMed:9891090};
CC IsoId=Q8CE90-6; Sequence=VSP_052268, VSP_052269;
CC Name=7 {ECO:0000269|PubMed:9891090}; Synonyms=gamma 2
CC {ECO:0000269|PubMed:9891090};
CC IsoId=Q8CE90-7; Sequence=VSP_052270, VSP_052271;
CC Name=8 {ECO:0000269|PubMed:9891090}; Synonyms=beta 2
CC {ECO:0000269|PubMed:9891090};
CC IsoId=Q8CE90-8; Sequence=VSP_052266, VSP_052270, VSP_052271;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, lung, liver,
CC skeletal muscle, kidney, and testis and at lower levels in the heart
CC and spleen. {ECO:0000269|PubMed:9312105, ECO:0000269|PubMed:9405446,
CC ECO:0000269|PubMed:9535930}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in the brain, spinal
CC cord, eyes, muscle, lungs, vertebrae, and intestine and at lower levels
CC in the heart and livers at 12.5 dpc. At later stages of embryogenesis
CC (14.5 dpc, 16.5 dpc, and 18.5 dpc) high levels were found in the brain,
CC retina, bone marrow, skin, intestine, lung epithelium and the
CC epithelial layers lining the olfactory cavity and developing teeth and
CC whiskers. {ECO:0000269|PubMed:9405446}.
CC -!- DOMAIN: The DVD domain (residues 393-413) contains a conserved docking
CC site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD
CC sites bind to their specific upstream MAP kinase kinase kinases
CC (MAP3Ks) and are essential for activation.
CC -!- DOMAIN: The D domain (residues 37-73) contains a conserved docking site
CC and is required for the binding to MAPK substrates.
CC -!- PTM: Activated by phosphorylation on Ser-287 and Thr-291 by MAP kinase
CC kinase kinases (MAP3Ks). {ECO:0000269|PubMed:9891090}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AF026216; AAB81848.1; -; mRNA.
DR EMBL; U74463; AAC53364.1; -; mRNA.
DR EMBL; U74464; AAC53365.1; -; mRNA.
DR EMBL; AB005654; BAA24383.1; -; mRNA.
DR EMBL; AF022112; AAC16274.1; -; mRNA.
DR EMBL; AF022113; AAC16275.1; -; mRNA.
DR EMBL; U93030; AAB63447.1; -; mRNA.
DR EMBL; U93031; AAB63448.1; -; Genomic_DNA.
DR EMBL; AF060943; AAD15819.1; -; mRNA.
DR EMBL; AF060944; AAD15820.1; -; mRNA.
DR EMBL; AF060945; AAD15821.1; -; mRNA.
DR EMBL; AF060946; AAD15822.1; -; mRNA.
DR EMBL; AF060947; AAD15823.1; -; mRNA.
DR EMBL; AK028772; BAC26111.1; -; mRNA.
DR EMBL; AK031137; BAC27272.1; -; mRNA.
DR EMBL; AK165184; BAE38066.1; -; mRNA.
DR EMBL; BC070467; AAH70467.1; -; mRNA.
DR CCDS; CCDS40208.1; -. [Q8CE90-7]
DR CCDS; CCDS40209.1; -. [Q8CE90-2]
DR CCDS; CCDS52474.1; -. [Q8CE90-6]
DR CCDS; CCDS80852.1; -. [Q8CE90-8]
DR CCDS; CCDS80853.1; -. [Q8CE90-3]
DR CCDS; CCDS80854.1; -. [Q8CE90-4]
DR RefSeq; NP_001036022.1; NM_001042557.2. [Q8CE90-7]
DR RefSeq; NP_001157644.1; NM_001164172.1. [Q8CE90-6]
DR RefSeq; NP_001278706.1; NM_001291777.1. [Q8CE90-8]
DR RefSeq; NP_001278707.1; NM_001291778.1. [Q8CE90-3]
DR RefSeq; NP_001278712.1; NM_001291783.1. [Q8CE90-4]
DR RefSeq; NP_036074.2; NM_011944.3. [Q8CE90-2]
DR AlphaFoldDB; Q8CE90; -.
DR SMR; Q8CE90; -.
DR BioGRID; 204954; 10.
DR CORUM; Q8CE90; -.
DR IntAct; Q8CE90; 1.
DR MINT; Q8CE90; -.
DR STRING; 10090.ENSMUSP00000003027; -.
DR ChEMBL; CHEMBL4523385; -.
DR iPTMnet; Q8CE90; -.
DR PhosphoSitePlus; Q8CE90; -.
DR EPD; Q8CE90; -.
DR MaxQB; Q8CE90; -.
DR PaxDb; Q8CE90; -.
DR PeptideAtlas; Q8CE90; -.
DR PRIDE; Q8CE90; -.
DR ProteomicsDB; 290295; -. [Q8CE90-1]
DR ProteomicsDB; 290296; -. [Q8CE90-2]
DR ProteomicsDB; 290297; -. [Q8CE90-3]
DR ProteomicsDB; 290298; -. [Q8CE90-4]
DR ProteomicsDB; 290299; -. [Q8CE90-5]
DR ProteomicsDB; 290300; -. [Q8CE90-6]
DR ProteomicsDB; 290301; -. [Q8CE90-7]
DR ProteomicsDB; 290302; -. [Q8CE90-8]
DR DNASU; 26400; -.
DR Ensembl; ENSMUST00000003027; ENSMUSP00000003027; ENSMUSG00000002948. [Q8CE90-7]
DR Ensembl; ENSMUST00000062686; ENSMUSP00000054512; ENSMUSG00000002948. [Q8CE90-6]
DR Ensembl; ENSMUST00000110994; ENSMUSP00000106622; ENSMUSG00000002948. [Q8CE90-4]
DR Ensembl; ENSMUST00000110995; ENSMUSP00000106623; ENSMUSG00000002948. [Q8CE90-3]
DR Ensembl; ENSMUST00000110996; ENSMUSP00000106624; ENSMUSG00000002948. [Q8CE90-5]
DR Ensembl; ENSMUST00000110998; ENSMUSP00000106626; ENSMUSG00000002948. [Q8CE90-2]
DR Ensembl; ENSMUST00000110999; ENSMUSP00000106627; ENSMUSG00000002948. [Q8CE90-8]
DR Ensembl; ENSMUST00000145165; ENSMUSP00000117418; ENSMUSG00000109061. [Q8CE90-1]
DR GeneID; 26400; -.
DR KEGG; mmu:26400; -.
DR UCSC; uc009kti.2; mouse. [Q8CE90-2]
DR UCSC; uc009ktj.2; mouse. [Q8CE90-6]
DR UCSC; uc009ktk.2; mouse. [Q8CE90-7]
DR UCSC; uc009ktm.2; mouse. [Q8CE90-4]
DR UCSC; uc009ktn.2; mouse. [Q8CE90-5]
DR UCSC; uc057ake.1; mouse. [Q8CE90-8]
DR UCSC; uc057akf.1; mouse. [Q8CE90-3]
DR CTD; 5609; -.
DR MGI; MGI:1346871; Map2k7.
DR VEuPathDB; HostDB:ENSMUSG00000002948; -.
DR VEuPathDB; HostDB:ENSMUSG00000109061; -.
DR eggNOG; KOG0983; Eukaryota.
DR GeneTree; ENSGT00940000158914; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q8CE90; -.
DR OMA; CFGYFIT; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q8CE90; -.
DR TreeFam; TF350701; -.
DR BRENDA; 2.7.12.2; 3474.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR BioGRID-ORCS; 26400; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Map2k7; mouse.
DR PRO; PR:Q8CE90; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CE90; protein.
DR Bgee; ENSMUSG00000002948; Expressed in external carotid artery and 255 other tissues.
DR ExpressionAtlas; Q8CE90; baseline and differential.
DR Genevisible; Q8CE90; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008545; F:JUN kinase kinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071347; P:cellular response to interleukin-1; IMP:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0072709; P:cellular response to sorbitol; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IDA:BHF-UCL.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:2000671; P:regulation of motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0009411; P:response to UV; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Coiled coil;
KW Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14733"
FT CHAIN 2..535
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 7"
FT /id="PRO_0000271406"
FT DOMAIN 136..396
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 37..73
FT /note="D domain"
FT /evidence="ECO:0000250"
FT REGION 63..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..416
FT /note="DVD domain"
FT /evidence="ECO:0000250"
FT COILED 2..30
FT /evidence="ECO:0000255"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 142..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13131,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 60..61
FT /note="Cleavage; by anthrax lethal factor"
FT /evidence="ECO:0000250"
FT SITE 92..93
FT /note="Cleavage; by anthrax lethal factor"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O14733"
FT MOD_RES 287
FT /note="Phosphoserine; by MAP3K"
FT /evidence="ECO:0000250"
FT MOD_RES 291
FT /note="Phosphothreonine; by MAP3K"
FT /evidence="ECO:0000250"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14733"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9891090"
FT /id="VSP_052265"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9312105"
FT /id="VSP_052264"
FT VAR_SEQ 42..58
FT /note="IIVITLSPAPAPSQRAA -> T (in isoform 2 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9312105, ECO:0000303|PubMed:9891090"
FT /id="VSP_052266"
FT VAR_SEQ 46..57
FT /note="TLSPAPAPSQRA -> MLTPFMPLVFNSP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9312105"
FT /id="VSP_052267"
FT VAR_SEQ 435
FT /note="S -> R (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9312105,
FT ECO:0000303|PubMed:9405446, ECO:0000303|PubMed:9891090"
FT /id="VSP_052268"
FT VAR_SEQ 436..535
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9312105,
FT ECO:0000303|PubMed:9405446, ECO:0000303|PubMed:9891090"
FT /id="VSP_052269"
FT VAR_SEQ 436..519
FT /note="TSVTWGAWPLAAQTPFQSGVIRCRGRVPSPRRATGGSGGQPCVCAGGPGPSF
FT TEMGPSPSPMLSNTFFTPDPGACPGASTWGLP -> GSLEESPTSPPSPKSFPLSPAIP
FT QAQAEWVSGR (in isoform 3, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:9384583,
FT ECO:0000303|PubMed:9891090"
FT /id="VSP_052270"
FT VAR_SEQ 520..535
FT /note="Missing (in isoform 3, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:9384583,
FT ECO:0000303|PubMed:9891090"
FT /id="VSP_052271"
FT CONFLICT 47
FT /note="L -> T (in Ref. 5; AAB63448)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="Q -> K (in Ref. 6; BAC27272)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="A -> V (in Ref. 4; AAC16274)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="T -> I (in Ref. 1; AAB81848)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> II (in Ref. 5; AAD15819/AAD15821/AAD15823)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="E -> D (in Ref. 1; AAB81848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59312 MW; A96DA75565E3CD0F CRC64;
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PIIVITLSPA PAPSQRAALQ
LPLANDGGSR SPSSESSPQH PTPPTRPRHM LGLPSTLFTP RSMESIEIDQ KLQEIMKQTG
YLTIGGQRYQ AEINDLENLG EMGSGTCGQV WKMRFRKTGH IIAVKQMRRS GNKEENKRIL
MDLDVVLKSH DCPYIVQCFG TFITNTDVFI AMELMGTCAE KLKKRMQGPI PERILGKMTV
AIVKALYYLK EKHGVIHRDV KPSNILLDER GQIKLCDFGI SGRLVDSKAK TRSAGCAAYM
APERIDPPDP TKPDYDIRAD VWSLGISLVE LATGQFPYKN CKTDFEVLTK VLQEEPPLLP
GHMGFSGDFQ SFVKDCLTKD HRKRPKYNKL LEHSFIKHYE ILEVDVASWF KDVMAKTESP
RTSGVLSQHH LPFFSTSVTW GAWPLAAQTP FQSGVIRCRG RVPSPRRATG GSGGQPCVCA
GGPGPSFTEM GPSPSPMLSN TFFTPDPGAC PGASTWGLPR RRLCQLLTTS TPGCC
