Q8CE90 (MP2K7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity mitogen-activated protein kinase kinase 7
Short name=MAP kinase kinase 7
Short name=MAPKK 7
EC=2.7.12.2

Alternative name(s):
JNK-activating kinase 2
MAPK/ERK kinase 7
Short name=MEK 7
c-Jun N-terminal kinase kinase 2
Short name=JNK kinase 2
Short name=JNKK 2

Gene names

Name:	Map2k7
Synonyms:	Mkk7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.10 Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.4 Ref.5
Cofactor	Magnesium. Ref.4 Ref.5
Enzyme regulation	Activated by phosphorylation by specific MAP kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3, MAP3K11/MLK3 and MAP3K12/DLK. Isoforms 3 and 4 have lower basal activity but a higher level of inducible activation, than isoforms 2, 6, 7 and 8. Ref.5
Subunit structure	Interacts with RASSF7, the interaction promotes phosphorylation. Interacts with VRK2 By similarity. Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 By similarity. Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1 and MAP3K1/MEKK1 By similarity. Interacts with MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold proteins. Ref.8 Ref.9
Subcellular location	Nucleus. Cytoplasm Ref.5.
Tissue specificity	Expressed at high levels in brain, lung, liver, skeletal muscle, kidney, and testis and at lower levels in the heart and spleen. Ref.1 Ref.2 Ref.4
Developmental stage	Expressed at high levels in the brain, spinal cord, eyes, muscle, lungs, vertebrae, and intestine and at lower levels in the heart and livers at E12.5. At later stages of embryogenesis (E14.5, E16.5, and E18.5) high levels were found in the brain, retina, bone marrow, skin, intestine, lung epithelium and the epithelial layers lining the olfactory cavity and developing teeth and whiskers. Ref.1
Domain	The DVD domain (residues 393-413) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation. The D domain (residues 37-73) contains a conserved docking site and is required for the binding to MAPK substrates.
Post-translational modification	Activated by phosphorylation on Ser-287 and Thr-291 by MAP kinase kinase kinases (MAP3Ks).
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis Stress response
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of JUN kinase activity Inferred from direct assay PubMed 11959862. Source: BHF-UCL apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW JUN kinase kinase activity Inferred from electronic annotation. Source: Compara MAP kinase kinase activity Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.1. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.6 (identifier: Q8CE90-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 Ref.2 Ref.5 Ref.6 (identifier: Q8CE90-2)

Also known as: a; beta 1;

The sequence of this isoform differs from the canonical sequence as follows:
     42-58: IIVITLSPAPAPSQRAA → T
     435-435: S → R
     436-535: Missing.

Isoform 3 Ref.3 Ref.5 (identifier: Q8CE90-3)

Also known as: alpha 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
     436-519: TSVTWGAWPL...CPGASTWGLP → GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
     520-535: Missing.

Isoform 4 Ref.5 (identifier: Q8CE90-4)

Also known as: alpha 1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
     435-435: S → R
     436-535: Missing.

Isoform 5 Ref.2 (identifier: Q8CE90-5)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
     46-57: TLSPAPAPSQRA → MLTPFMPLVFNSP
     435-435: S → R
     436-535: Missing.

Note: No experimental confirmation available.

Isoform 6 Ref.1 Ref.5 Ref.7 (identifier: Q8CE90-6)

Also known as: b; gamma 1;

The sequence of this isoform differs from the canonical sequence as follows:
     435-435: S → R
     436-535: Missing.

Isoform 7 Ref.5 (identifier: Q8CE90-7)

Also known as: gamma 2;

The sequence of this isoform differs from the canonical sequence as follows:
     436-519: TSVTWGAWPL...CPGASTWGLP → GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
     520-535: Missing.

Isoform 8 Ref.5 (identifier: Q8CE90-8)

Also known as: beta 2;

The sequence of this isoform differs from the canonical sequence as follows:
     42-58: IIVITLSPAPAPSQRAA → T
     436-519: TSVTWGAWPL...CPGASTWGLP → GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
     520-535: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 535	535	Dual specificity mitogen-activated protein kinase kinase 7		PRO_0000271406
Regions
	Domain	136 – 396	261	Protein kinase
	Nucleotide binding	142 – 150	9	ATP By similarity UniProtKB Q13131
	Region	37 – 73	37	D domain By similarity
	Region	393 – 416	24	DVD domain By similarity
	Coiled coil	2 – 30	29	Potential
Sites
	Active site	259	1	Proton acceptor By similarity UniProtKB Q13131
	Binding site	165	1	ATP By similarity UniProtKB Q13131
	Site	60 – 61	2	Cleavage; by anthrax lethal factor By similarity UniProtKB O14733
	Site	92 – 93	2	Cleavage; by anthrax lethal factor By similarity UniProtKB O14733
Amino acid modifications
	Modified residue	287	1	Phosphoserine; by MAP3K By similarity
	Modified residue	291	1	Phosphothreonine; by MAP3K By similarity
Natural variations
	Alternative sequence	1 – 89	89	Missing in isoform 3 and isoform 4. Ref.3 Ref.5		VSP_052265
	Alternative sequence	1 – 45	45	Missing in isoform 5. Ref.2		VSP_052264
	Alternative sequence	42 – 58	17	IIVIT…SQRAA → T in isoform 2 and isoform 8. Ref.2 Ref.5 Ref.6		VSP_052266
	Alternative sequence	46 – 57	12	TLSPA…PSQRA → MLTPFMPLVFNSP in isoform 5. Ref.2		VSP_052267
	Alternative sequence	435	1	S → R in isoform 2, isoform 4, isoform 5 and isoform 6. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7		VSP_052268
	Alternative sequence	436 – 535	100	Missing in isoform 2, isoform 4, isoform 5 and isoform 6. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7		VSP_052269
	Alternative sequence	436 – 519	84	TSVTW…TWGLP → GSLEESPTSPPSPKSFPLSP AIPQAQAEWVSGR in isoform 3, isoform 7 and isoform 8. Ref.3 Ref.5		VSP_052270
	Alternative sequence	520 – 535	16	Missing in isoform 3, isoform 7 and isoform 8. Ref.3 Ref.5		VSP_052271
Experimental info
	Sequence conflict	47	1	L → T in AAB63448. Ref.5
	Sequence conflict	166	1	Q → K in BAC27272. Ref.6
	Sequence conflict	211	1	A → V in AAC16274. Ref.4
	Sequence conflict	217	1	T → I in AAB81848. Ref.1
	Sequence conflict	396	1	I → II in AAD15819. Ref.5
	Sequence conflict	396	1	I → II in AAD15821. Ref.5
	Sequence conflict	396	1	I → II in AAD15823. Ref.5
	Sequence conflict	418	1	E → D in AAB81848. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A96DA75565E3CD0F	FASTA	535	59,312
	10 20 30 40 50 60 MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PIIVITLSPA PAPSQRAALQ 70 80 90 100 110 120 LPLANDGGSR SPSSESSPQH PTPPTRPRHM LGLPSTLFTP RSMESIEIDQ KLQEIMKQTG 130 140 150 160 170 180 YLTIGGQRYQ AEINDLENLG EMGSGTCGQV WKMRFRKTGH IIAVKQMRRS GNKEENKRIL 190 200 210 220 230 240 MDLDVVLKSH DCPYIVQCFG TFITNTDVFI AMELMGTCAE KLKKRMQGPI PERILGKMTV 250 260 270 280 290 300 AIVKALYYLK EKHGVIHRDV KPSNILLDER GQIKLCDFGI SGRLVDSKAK TRSAGCAAYM 310 320 330 340 350 360 APERIDPPDP TKPDYDIRAD VWSLGISLVE LATGQFPYKN CKTDFEVLTK VLQEEPPLLP 370 380 390 400 410 420 GHMGFSGDFQ SFVKDCLTKD HRKRPKYNKL LEHSFIKHYE ILEVDVASWF KDVMAKTESP 430 440 450 460 470 480 RTSGVLSQHH LPFFSTSVTW GAWPLAAQTP FQSGVIRCRG RVPSPRRATG GSGGQPCVCA 490 500 510 520 530 GGPGPSFTEM GPSPSPMLSN TFFTPDPGAC PGASTWGLPR RRLCQLLTTS TPGCC
	Isoform 2 (a) (beta 1) [UniParc]. Checksum: B12F5CE8364CE6F5	FASTA	419	47,562
	10 20 30 40 50 60 MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND GGSRSPSSES 70 80 90 100 110 120 SPQHPTPPTR PRHMLGLPST LFTPRSMESI EIDQKLQEIM KQTGYLTIGG QRYQAEINDL 130 140 150 160 170 180 ENLGEMGSGT CGQVWKMRFR KTGHIIAVKQ MRRSGNKEEN KRILMDLDVV LKSHDCPYIV 190 200 210 220 230 240 QCFGTFITNT DVFIAMELMG TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI 250 260 270 280 290 300 HRDVKPSNIL LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD 310 320 330 340 350 360 IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS GDFQSFVKDC 370 380 390 400 410 LTKDHRKRPK YNKLLEHSFI KHYEILEVDV ASWFKDVMAK TESPRTSGVL SQHHLPFFR
	Isoform 3 (alpha 2) [UniParc]. Checksum: D7CFD1B827C90015	FASTA	379	42,725
	10 20 30 40 50 60 MLGLPSTLFT PRSMESIEID QKLQEIMKQT GYLTIGGQRY QAEINDLENL GEMGSGTCGQ 70 80 90 100 110 120 VWKMRFRKTG HIIAVKQMRR SGNKEENKRI LMDLDVVLKS HDCPYIVQCF GTFITNTDVF 130 140 150 160 170 180 IAMELMGTCA EKLKKRMQGP IPERILGKMT VAIVKALYYL KEKHGVIHRD VKPSNILLDE 190 200 210 220 230 240 RGQIKLCDFG ISGRLVDSKA KTRSAGCAAY MAPERIDPPD PTKPDYDIRA DVWSLGISLV 250 260 270 280 290 300 ELATGQFPYK NCKTDFEVLT KVLQEEPPLL PGHMGFSGDF QSFVKDCLTK DHRKRPKYNK 310 320 330 340 350 360 LLEHSFIKHY EILEVDVASW FKDVMAKTES PRTSGVLSQH HLPFFSGSLE ESPTSPPSPK 370 SFPLSPAIPQ AQAEWVSGR
	Isoform 4 (alpha 1) [UniParc]. Checksum: 15A41F9077C40EAB	FASTA	346	39,377
	10 20 30 40 50 60 MLGLPSTLFT PRSMESIEID QKLQEIMKQT GYLTIGGQRY QAEINDLENL GEMGSGTCGQ 70 80 90 100 110 120 VWKMRFRKTG HIIAVKQMRR SGNKEENKRI LMDLDVVLKS HDCPYIVQCF GTFITNTDVF 130 140 150 160 170 180 IAMELMGTCA EKLKKRMQGP IPERILGKMT VAIVKALYYL KEKHGVIHRD VKPSNILLDE 190 200 210 220 230 240 RGQIKLCDFG ISGRLVDSKA KTRSAGCAAY MAPERIDPPD PTKPDYDIRA DVWSLGISLV 250 260 270 280 290 300 ELATGQFPYK NCKTDFEVLT KVLQEEPPLL PGHMGFSGDF QSFVKDCLTK DHRKRPKYNK 310 320 330 340 LLEHSFIKHY EILEVDVASW FKDVMAKTES PRTSGVLSQH HLPFFR
	Isoform 5 (b) [UniParc]. Checksum: 0ABA468DBB8255F7	FASTA	391	44,210
	10 20 30 40 50 60 MLTPFMPLVF NSPALQLPLA NDGGSRSPSS ESSPQHPTPP TRPRHMLGLP STLFTPRSME 70 80 90 100 110 120 SIEIDQKLQE IMKQTGYLTI GGQRYQAEIN DLENLGEMGS GTCGQVWKMR FRKTGHIIAV 130 140 150 160 170 180 KQMRRSGNKE ENKRILMDLD VVLKSHDCPY IVQCFGTFIT NTDVFIAMEL MGTCAEKLKK 190 200 210 220 230 240 RMQGPIPERI LGKMTVAIVK ALYYLKEKHG VIHRDVKPSN ILLDERGQIK LCDFGISGRL 250 260 270 280 290 300 VDSKAKTRSA GCAAYMAPER IDPPDPTKPD YDIRADVWSL GISLVELATG QFPYKNCKTD 310 320 330 340 350 360 FEVLTKVLQE EPPLLPGHMG FSGDFQSFVK DCLTKDHRKR PKYNKLLEHS FIKHYEILEV 370 380 390 DVASWFKDVM AKTESPRTSG VLSQHHLPFF R
	Isoform 6 (b) (gamma 1) [UniParc]. Checksum: C88FDA908B97E34D	FASTA	435	49,148
	10 20 30 40 50 60 MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PIIVITLSPA PAPSQRAALQ 70 80 90 100 110 120 LPLANDGGSR SPSSESSPQH PTPPTRPRHM LGLPSTLFTP RSMESIEIDQ KLQEIMKQTG 130 140 150 160 170 180 YLTIGGQRYQ AEINDLENLG EMGSGTCGQV WKMRFRKTGH IIAVKQMRRS GNKEENKRIL 190 200 210 220 230 240 MDLDVVLKSH DCPYIVQCFG TFITNTDVFI AMELMGTCAE KLKKRMQGPI PERILGKMTV 250 260 270 280 290 300 AIVKALYYLK EKHGVIHRDV KPSNILLDER GQIKLCDFGI SGRLVDSKAK TRSAGCAAYM 310 320 330 340 350 360 APERIDPPDP TKPDYDIRAD VWSLGISLVE LATGQFPYKN CKTDFEVLTK VLQEEPPLLP 370 380 390 400 410 420 GHMGFSGDFQ SFVKDCLTKD HRKRPKYNKL LEHSFIKHYE ILEVDVASWF KDVMAKTESP 430 RTSGVLSQHH LPFFR
	Isoform 7 (gamma 2) [UniParc]. Checksum: A71A286EE0AF99FF	FASTA	468	52,497
	10 20 30 40 50 60 MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PIIVITLSPA PAPSQRAALQ 70 80 90 100 110 120 LPLANDGGSR SPSSESSPQH PTPPTRPRHM LGLPSTLFTP RSMESIEIDQ KLQEIMKQTG 130 140 150 160 170 180 YLTIGGQRYQ AEINDLENLG EMGSGTCGQV WKMRFRKTGH IIAVKQMRRS GNKEENKRIL 190 200 210 220 230 240 MDLDVVLKSH DCPYIVQCFG TFITNTDVFI AMELMGTCAE KLKKRMQGPI PERILGKMTV 250 260 270 280 290 300 AIVKALYYLK EKHGVIHRDV KPSNILLDER GQIKLCDFGI SGRLVDSKAK TRSAGCAAYM 310 320 330 340 350 360 APERIDPPDP TKPDYDIRAD VWSLGISLVE LATGQFPYKN CKTDFEVLTK VLQEEPPLLP 370 380 390 400 410 420 GHMGFSGDFQ SFVKDCLTKD HRKRPKYNKL LEHSFIKHYE ILEVDVASWF KDVMAKTESP 430 440 450 460 RTSGVLSQHH LPFFSGSLEE SPTSPPSPKS FPLSPAIPQA QAEWVSGR
	Isoform 8 (beta 2) [UniParc]. Checksum: 7243158357786C2A	FASTA	452	50,911
	10 20 30 40 50 60 MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND GGSRSPSSES 70 80 90 100 110 120 SPQHPTPPTR PRHMLGLPST LFTPRSMESI EIDQKLQEIM KQTGYLTIGG QRYQAEINDL 130 140 150 160 170 180 ENLGEMGSGT CGQVWKMRFR KTGHIIAVKQ MRRSGNKEEN KRILMDLDVV LKSHDCPYIV 190 200 210 220 230 240 QCFGTFITNT DVFIAMELMG TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI 250 260 270 280 290 300 HRDVKPSNIL LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD 310 320 330 340 350 360 IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS GDFQSFVKDC 370 380 390 400 410 420 LTKDHRKRPK YNKLLEHSFI KHYEILEVDV ASWFKDVMAK TESPRTSGVL SQHHLPFFSG 430 440 450 SLEESPTSPP SPKSFPLSPA IPQAQAEWVS GR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Activation of stress-activated protein kinases/c-Jun N-terminal protein kinases (SAPKs/JNKs) by a novel mitogen-activated protein kinase kinase (MKK7)." Yao Z., Diener K., Wang X.S., Zukowski M., Matsumoto G., Zhou G., Mo R., Sasaki T., Nishina H., Hui C.C., Tan T.-H., Woodgett J.P., Penninger J.M. J. Biol. Chem. 272:32378-32383(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"MKK7 is a stress-activated mitogen-activated protein kinase kinase functionally related to hemipterous." Holland P.M., Magali S., Campbell J.S., Noselli S., Cooper J.A. J. Biol. Chem. 272:24994-24998(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, TISSUE SPECIFICITY.
[3]	"A novel SAPK/JNK kinase, MKK7, stimulated by TNFalpha and cellular stresses." Moriguchi T., Toyoshima F., Masuyama N., Hanafusa H., Gotoh Y., Nishida E. EMBO J. 16:7045-7053(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION.
[4]	"Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli." Foltz I.N., Gerl R.E., Wieler J.S., Luckach M., Salmon R.A., Schrader J.W. J. Biol. Chem. 273:9344-9351(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-311 (ISOFORMS 2/6), FUNCTION, TISSUE SPECIFICITY. Tissue: B-cell and Thymus.
[5]	"The MKK7 gene encodes a group of c-Jun NH2-terminal kinase kinases." Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J. Mol. Cell. Biol. 19:1569-1581(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 6; 7 AND 8), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-535 (ISOFORM 6), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, SUBCELLULAR LOCATION. Strain: CD-1. Tissue: Testis.
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Fetal forelimb, Fetus and Skin.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Strain: C57BL/6. Tissue: Eye.
[8]	"A mammalian scaffold complex that selectively mediates MAP kinase activation." Whitmarsh A.J., Cavanagh J., Tournier C., Yasuda J., Davis R.J. Science 281:1671-1674(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK8IP1/JIP1.
[9]	"Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3." Kelkar N., Gupta S., Dickens M., Davis R.J. Mol. Cell. Biol. 20:1030-1043(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK8IP3/JIP3.
[10]	"MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines." Tournier C., Dong C., Turner T.K., Jones S.N., Flavell R.A., Davis R.J. Genes Dev. 15:1419-1426(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Different properties of SEK1 and MKK7 in dual phosphorylation of stress-induced activated protein kinase SAPK/JNK in embryonic stem cells." Kishimoto H., Nakagawa K., Watanabe T., Kitagawa D., Momose H., Seo J., Nishitai G., Shimizu N., Ohata S., Tanemura S., Asaka S., Goto T., Fukushi H., Yoshida H., Suzuki A., Sasaki T., Wada T., Penninger J.M., Nishina H., Katada T. J. Biol. Chem. 278:16595-16601(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Differential regulation and properties of MAPKs." Raman M., Chen W., Cobb M.H. Oncogene 26:3100-3112(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ENZYME REGULATION.
[13]	"Diverse physiological functions of MKK4 and MKK7 during early embryogenesis." Asaoka Y., Nishina H. J. Biochem. 148:393-401(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[14]	"The bottleneck of JNK signaling: molecular and functional characteristics of MKK4 and MKK7." Haeusgen W., Herdegen T., Waetzig V. Eur. J. Cell Biol. 90:536-544(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON REGULATION, REVIEW ON FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF026216 mRNA. Translation: AAB81848.1. U74463 mRNA. Translation: AAC53364.1. U74464 mRNA. Translation: AAC53365.1. AB005654 mRNA. Translation: BAA24383.1. AF022112 mRNA. Translation: AAC16274.1. AF022113 mRNA. Translation: AAC16275.1. U93030 mRNA. Translation: AAB63447.1. U93031 Genomic DNA. Translation: AAB63448.1. AF060943 mRNA. Translation: AAD15819.1. AF060944 mRNA. Translation: AAD15820.1. AF060945 mRNA. Translation: AAD15821.1. AF060946 mRNA. Translation: AAD15822.1. AF060947 mRNA. Translation: AAD15823.1. AK028772 mRNA. Translation: BAC26111.1. AK031137 mRNA. Translation: BAC27272.1. AK165184 mRNA. Translation: BAE38066.1. BC070467 mRNA. Translation: AAH70467.1.
IPI	IPI00117840. IPI00228989. IPI00280475. IPI00749972. IPI00816840. IPI00816864. IPI00816890. IPI00816911.
RefSeq	NP_001036022.1. NM_001042557.2. NP_001157644.1. NM_001164172.1. NP_036074.2. NM_011944.3.
UniGene	Mm.3906.
3D structure databases
HSSP	HSSP built from PDB template 1S9I based on UniProtKB P36507.
ProteinModelPortal	Q8CE90.
SMR	Q8CE90. Positions 80-418.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CE90. 2 interactions.
PTM databases
PhosphoSite	Q8CE90.
Proteomic databases
PaxDb	Q8CE90.
PRIDE	Q8CE90.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000003027; ENSMUSP00000003027; ENSMUSG00000002948. ENSMUST00000062686; ENSMUSP00000054512; ENSMUSG00000002948. ENSMUST00000110994; ENSMUSP00000106622; ENSMUSG00000002948. ENSMUST00000110995; ENSMUSP00000106623; ENSMUSG00000002948. ENSMUST00000110996; ENSMUSP00000106624; ENSMUSG00000002948. ENSMUST00000110998; ENSMUSP00000106626; ENSMUSG00000002948. ENSMUST00000110999; ENSMUSP00000106627; ENSMUSG00000002948. ENSMUST00000145165; ENSMUSP00000117418; ENSMUSG00000002948.
GeneID	26400.
KEGG	mmu:26400.
UCSC	uc009kti.2. mouse. uc009ktj.2. mouse. uc009ktk.2. mouse. uc009ktm.2. mouse. uc009ktn.2. mouse.
Organism-specific databases
CTD	5609.
MGI	MGI:1346871. Map2k7.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00690000101918.
HOVERGEN	HBG108518.
InParanoid	Q8CE90.
KO	K04431.
OMA	FKMSSLE.
Gene expression databases
Bgee	Q8CE90.
CleanEx	MM_MAP2K7.
Genevestigator	Q8CE90.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MAP2K7. mouse.
NextBio	304359.
SOURCE	Search...

Entry information

Entry name

MP2K7_MOUSE

Accession

Primary (citable) accession number: Q8CE90
Secondary accession number(s): O35406 , O35720, O35871, O35872, O54780, O70242, O70243, Q8BSP1, Q9QWG6, Q9R1Z3, Q9R1Z4, Q9R1Z5, Q9R1Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program