Q9WVS8 (MK07_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 7
Short name=MAP kinase 7
Short name=MAPK 7
EC=2.7.11.24

Alternative name(s):
Big MAP kinase 1
Short name=BMK-1
Extracellular signal-regulated kinase 5
Short name=ERK-5

Gene names

Name:	Mapk7
Synonyms:	Bmk1, Erk5

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	806 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression By similarity. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction By similarity. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by tyrosine and threonine phosphorylation. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF) By similarity.
Subunit structure	Interacts with MAP2K5 By similarity. Forms oligomers. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D By similarity. Interacts with SGK1 By similarity. Interacts with PML By similarity. Ref.2
Subcellular location	Cytoplasm. Nucleus. Nucleus › PML body By similarity. Note: Translocates to the nucleus upon activation By similarity. Ref.2 Isoform 1: Cytoplasm By similarity. Nucleus By similarity. Note: Isoform 1 is detected in cytoplasm and nucleus By similarity. Ref.2 Isoform 2: Nucleus By similarity. Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation By similarity. Ref.2 Isoform 3: Nucleus By similarity. Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation By similarity. Ref.2
Tissue specificity	Detected in testis, brain, kidney, lung and heart. Detected in total embryo (at protein level). Ref.2
Domain	The second proline-rich region may interact with actin targeting the kinase to a specific location in the cell. The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Differentiation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from electronic annotation. Source: GOC apoptotic process Inferred from mutant phenotype PubMed 14675480. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara negative regulation of NFAT protein import into nucleus Inferred from mutant phenotype PubMed 18347059. Source: MGI negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of heterotypic cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of response to cytokine stimulus Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from direct assay PubMed 18347059. Source: MGI positive regulation of protein metabolic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara regulation of angiogenesis Inferred from mutant phenotype PubMed 12221099. Source: MGI
Cellular_component	PML body Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from direct assay PubMed 18347059. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from direct assay PubMed 18347059. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9WVS8-1)

Also known as: Big MAP kinase 1a; mERK5a;

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.

Isoform 2 (identifier: Q9WVS8-2)

Also known as: Big MAP kinase 1b; mERK5b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: MAEPLKEEDG...VVSSARRRLT → MCGLLSRG

Note: May not have a kinase activity. May not stimulate MEF2C activity. May function as dominant negative inhibitor of the ERK5 signaling pathway.

Isoform 3 (identifier: Q9WVS8-3)

Also known as: Big MAP kinase 1c; mERK5c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Note: May not have a kinase activity. May not stimulate MEF2C activity. May function as dominant negative inhibitor of the ERK5 signaling pathway.

Isoform 4 (identifier: Q9WVS8-4)

Also known as: Big MAP kinase 1d; mERK5-T;

The sequence of this isoform differs from the canonical sequence as follows:
     493-806: DGPSAPLEAP...LSDLPDLQEP → GGVWAQQLSG

Note: Unable to translocate from the cytoplasm to the nucleus.

Isoform 5 (identifier: Q9WVS8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     757-806: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 806	805	Mitogen-activated protein kinase 7		PRO_0000186261
Regions
	Domain	55 – 347	293	Protein kinase
	Nucleotide binding	61 – 69	9	ATP By similarity
	Region	2 – 77	76	Required for cytoplasmic targeting
	Region	78 – 139	62	Required for binding to MAP2K5
	Region	140 – 406	267	Necessary for oligomerization
	Region	407 – 806	400	May not be required for kinase activity; required to stimulate MEF2C activity
	Region	505 – 539	35	Nuclear localization signal
	Motif	219 – 221	3	TXY
	Compositional bias	434 – 465	32	Pro-rich
	Compositional bias	521 – 524	4	Poly-Arg
	Compositional bias	578 – 700	123	Pro-rich
Sites
	Active site	182	1	Proton acceptor By similarity
	Binding site	84	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	710	1	Phosphoserine By similarity
	Modified residue	723	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	1 – 139	139	Missing in isoform 3.		VSP_035201
	Alternative sequence	1 – 77	77	MAEPL…RRRLT → MCGLLSRG in isoform 2.		VSP_035202
	Alternative sequence	493 – 806	314	DGPSA…DLQEP → GGVWAQQLSG in isoform 4.		VSP_035203
	Alternative sequence	757 – 806	50	Missing in isoform 5.		VSP_035204
Experimental info
	Sequence conflict	191	1	N → D in BAE28357. Ref.4
	Sequence conflict	308	1	P → H in BAE28357. Ref.4
	Sequence conflict	331	1	E → K in AAI00399. Ref.5
	Sequence conflict	409	1	A → V in AAD39394. Ref.2
	Sequence conflict	409	1	A → V in AAD39395. Ref.2
	Sequence conflict	409	1	A → V in AAD39396. Ref.2
	Sequence conflict	424	1	A → R in AAD39394. Ref.2
	Sequence conflict	424	1	A → R in AAD39395. Ref.2
	Sequence conflict	424	1	A → R in AAD39396. Ref.2
	Sequence conflict	578	1	P → PPAPA in BAE28357. Ref.4
	Sequence conflict	578	1	P → PPAPA in BAE33103. Ref.4
	Sequence conflict	588	1	A → R in AAD39394. Ref.2
	Sequence conflict	588	1	A → R in AAD39395. Ref.2
	Sequence conflict	588	1	A → R in AAD39396. Ref.2
	Sequence conflict	592	1	A → Q in AAD39394. Ref.2
	Sequence conflict	592	1	A → Q in AAD39395. Ref.2
	Sequence conflict	592	1	A → Q in AAD39396. Ref.2
	Sequence conflict	618	1	S → C in AAD39394. Ref.2
	Sequence conflict	618	1	S → C in AAD39395. Ref.2
	Sequence conflict	618	1	S → C in AAD39396. Ref.2
	Sequence conflict	642	1	P → A in AAD39394. Ref.2
	Sequence conflict	642	1	P → A in AAD39395. Ref.2
	Sequence conflict	642	1	P → A in AAD39396. Ref.2
	Sequence conflict	803	1	L → V in BAE28357. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Big MAP kinase 1a) (mERK5a) [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E7CC41C4BBDE0633	FASTA	806	87,733
	10 20 30 40 50 60 MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD VGDEYEIIET 70 80 90 100 110 120 IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 130 140 150 160 170 180 LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH 190 200 210 220 230 240 RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT 250 260 270 280 290 300 QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 310 320 330 340 350 360 LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA 370 380 390 400 410 420 PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPVCPDVEMP 430 440 450 460 470 480 SPWAPSGDCA MESPPPALPP CSDPAPDTVD LTLQPAPPAS ELAPPKREGA ISDNTKAALK 490 500 510 520 530 540 AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER 550 560 570 580 590 600 KERGAGTLGG PSTDPLAGLV LSDNDRSLLE RWTRMARPPA PAPAPAPAPA PAPSSAQPTS 610 620 630 640 650 660 TPTGPVSQST GPLQPAGSIP GPASQPVCPP PGPVPQPAGP IPAPLQTAPS TSLLASQSLV 670 680 690 700 710 720 PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV NLVTQQLSKS QVEDPLPPVF 730 740 750 760 770 780 SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDGQADS ASLSASLLAD WLEGHGMNPA 790 800 DIESLQREIQ MDSPMLLSDL PDLQEP
	Isoform 2 (Big MAP kinase 1b) (mERK5b) [UniParc]. Checksum: 29CEDCA390068527	FASTA	737	80,380
	10 20 30 40 50 60 MCGLLSRGGQ QVAIKKIPNA FDVVTNAKRT LRELKILKHF KHDNIIAIKD ILKPTVPYGE 70 80 90 100 110 120 FRSVYVVLDL MESDLHQIIH SSQPLTLEHV RYFLYQLLRG LKYMHSAQVI HRDLKPSNLL 130 140 150 160 170 180 VNENCELKIG DFGMARGLCT SPAEHQYFMT EYVATRWYRA PELMLSLHEY TQAIDLWSVG 190 200 210 220 230 240 CIFGEMLARR QLFPGKNYVH QLQLIMMVLG TPSPAVIQAV GAERVRAYIQ SLPPRQPVPW 250 260 270 280 290 300 ETVYPGADRQ ALSLLGRMLR FEPSARISAA AALRHPFLAK YHDPDDEPDC APPFDFAFDR 310 320 330 340 350 360 EALTRERIKE AIVAEIEDFH ARREGIRQQI RFQPSLQPVA SEPVCPDVEM PSPWAPSGDC 370 380 390 400 410 420 AMESPPPALP PCSDPAPDTV DLTLQPAPPA SELAPPKREG AISDNTKAAL KAALLKSLRS 430 440 450 460 470 480 RLRDGPSAPL EAPEPRKPVT AQERQREREE KRRRRQERAK EREKRRQERE RKERGAGTLG 490 500 510 520 530 540 GPSTDPLAGL VLSDNDRSLL ERWTRMARPP APAPAPAPAP APAPSSAQPT STPTGPVSQS 550 560 570 580 590 600 TGPLQPAGSI PGPASQPVCP PPGPVPQPAG PIPAPLQTAP STSLLASQSL VPPSGLPGSG 610 620 630 640 650 660 APEVLPYFPS GPPPPDPGLT PQPSTSESPD VNLVTQQLSK SQVEDPLPPV FSGTPKGSGA 670 680 690 700 710 720 GYGVGFDLEE FLNQSFDMGV ADGPQDGQAD SASLSASLLA DWLEGHGMNP ADIESLQREI 730 QMDSPMLLSD LPDLQEP
	Isoform 3 (Big MAP kinase 1c) (mERK5c) [UniParc]. Checksum: 00C42D9700759F7E	FASTA	667	72,463
	10 20 30 40 50 60 MESDLHQIIH SSQPLTLEHV RYFLYQLLRG LKYMHSAQVI HRDLKPSNLL VNENCELKIG 70 80 90 100 110 120 DFGMARGLCT SPAEHQYFMT EYVATRWYRA PELMLSLHEY TQAIDLWSVG CIFGEMLARR 130 140 150 160 170 180 QLFPGKNYVH QLQLIMMVLG TPSPAVIQAV GAERVRAYIQ SLPPRQPVPW ETVYPGADRQ 190 200 210 220 230 240 ALSLLGRMLR FEPSARISAA AALRHPFLAK YHDPDDEPDC APPFDFAFDR EALTRERIKE 250 260 270 280 290 300 AIVAEIEDFH ARREGIRQQI RFQPSLQPVA SEPVCPDVEM PSPWAPSGDC AMESPPPALP 310 320 330 340 350 360 PCSDPAPDTV DLTLQPAPPA SELAPPKREG AISDNTKAAL KAALLKSLRS RLRDGPSAPL 370 380 390 400 410 420 EAPEPRKPVT AQERQREREE KRRRRQERAK EREKRRQERE RKERGAGTLG GPSTDPLAGL 430 440 450 460 470 480 VLSDNDRSLL ERWTRMARPP APAPAPAPAP APAPSSAQPT STPTGPVSQS TGPLQPAGSI 490 500 510 520 530 540 PGPASQPVCP PPGPVPQPAG PIPAPLQTAP STSLLASQSL VPPSGLPGSG APEVLPYFPS 550 560 570 580 590 600 GPPPPDPGLT PQPSTSESPD VNLVTQQLSK SQVEDPLPPV FSGTPKGSGA GYGVGFDLEE 610 620 630 640 650 660 FLNQSFDMGV ADGPQDGQAD SASLSASLLA DWLEGHGMNP ADIESLQREI QMDSPMLLSD LPDLQEP
	Isoform 4 (Big MAP kinase 1d) (mERK5-T) [UniParc]. Checksum: 905BD56BC58913D8	FASTA	502	55,914
	10 20 30 40 50 60 MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD VGDEYEIIET 70 80 90 100 110 120 IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 130 140 150 160 170 180 LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH 190 200 210 220 230 240 RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT 250 260 270 280 290 300 QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 310 320 330 340 350 360 LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA 370 380 390 400 410 420 PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPVCPDVEMP 430 440 450 460 470 480 SPWAPSGDCA MESPPPALPP CSDPAPDTVD LTLQPAPPAS ELAPPKREGA ISDNTKAALK 490 500 AALLKSLRSR LRGGVWAQQL SG
	Isoform 5 [UniParc]. Checksum: C0CCFA5D2F8C84F5	FASTA	756	82,314
	10 20 30 40 50 60 MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD VGDEYEIIET 70 80 90 100 110 120 IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI 130 140 150 160 170 180 LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH 190 200 210 220 230 240 RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT 250 260 270 280 290 300 QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 310 320 330 340 350 360 LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY HDPDDEPDCA 370 380 390 400 410 420 PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPVCPDVEMP 430 440 450 460 470 480 SPWAPSGDCA MESPPPALPP CSDPAPDTVD LTLQPAPPAS ELAPPKREGA ISDNTKAALK 490 500 510 520 530 540 AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER 550 560 570 580 590 600 KERGAGTLGG PSTDPLAGLV LSDNDRSLLE RWTRMARPPA PAPAPAPAPA PAPSSAQPTS 610 620 630 640 650 660 TPTGPVSQST GPLQPAGSIP GPASQPVCPP PGPVPQPAGP IPAPLQTAPS TSLLASQSLV 670 680 690 700 710 720 PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV NLVTQQLSKS QVEDPLPPVF 730 740 750 SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA DGPQDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus." Kamakura S., Moriguchi T., Nishida E. J. Biol. Chem. 274:26563-26571(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains." Yan C., Luo H., Lee J.-D., Abe J.-I., Berk B.C. J. Biol. Chem. 276:10870-10878(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: C57BL/6.
[3]	"Identification and characterization of mErk5-T, a novel Erk5/Bmk1 splice variant." McCaw B.J., Chow S.Y., Wong E.S.M., Tan K.L., Guo H., Guy G.R. Gene 345:183-190(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION. Strain: C57BL/6. Tissue: Bone marrow.
[4]	"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: NOD.
[5]	"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 5). Strain: C57BL/6J. Tissue: Kidney.
[6]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[7]	"Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells." Dinev D., Jordan B.W.M., Neufeld B., Lee J.-D., Lindemann D., Rapp U.R., Ludwig S. EMBO Rep. 2:829-834(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival." Dong F., Gutkind J.S., Larner A.C. J. Biol. Chem. 276:10811-10816(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure." Hayashi M., Kim S.W., Imanaka-Yoshida K., Yoshida T., Abel E.D., Eliceiri B., Yang Y., Ulevitch R.J., Lee J.D. J. Clin. Invest. 113:1138-1148(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB019373 mRNA. Translation: BAA82039.1. AF126159 mRNA. Translation: AAD39394.1. AF126160 mRNA. Translation: AAD39395.1. AF126161 mRNA. Translation: AAD39396.1. AK148119 mRNA. Translation: BAE28357.1. AK155187 mRNA. Translation: BAE33103.1. AY534740 mRNA. Translation: AAS38576.1. BC100398 mRNA. Translation: AAI00399.1. AL604029 Genomic DNA. Translation: CAI24182.1. AL604029 Genomic DNA. Translation: CAI24184.1. AL604029 Genomic DNA. Translation: CAI24185.1.
IPI	IPI00126449. IPI00648610. IPI00903353. IPI00903360. IPI00903387.
RefSeq	NP_035971.1. NM_011841.1.
UniGene	Mm.38172.
3D structure databases
ProteinModelPortal	Q9WVS8.
SMR	Q9WVS8. Positions 11-393.
ModBase	Search...
PTM databases
PhosphoSite	Q9WVS8.
Proteomic databases
PRIDE	Q9WVS8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000079080; ENSMUSP00000078087; ENSMUSG00000001034. ENSMUST00000108714; ENSMUSP00000104354; ENSMUSG00000001034. ENSMUST00000153441; ENSMUSP00000116084; ENSMUSG00000001034.
GeneID	23939.
KEGG	mmu:23939.
UCSC	uc007jho.1. mouse. uc007jhp.1. mouse. uc007jhq.1. mouse. uc007jht.1. mouse.
Organism-specific databases
CTD	5598.
MGI	MGI:1346347. Mapk7.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074298.
HOVERGEN	HBG108137.
InParanoid	Q9WVS8.
KO	K04464.
OMA	IIETIGT.
OrthoDB	EOG4H463D.
Gene expression databases
ArrayExpress	Q9WVS8.
Bgee	Q9WVS8.
CleanEx	MM_MAPK7.
Genevestigator	Q9WVS8.
GermOnline	ENSMUSG00000001034. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. 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	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	303745.
SOURCE	Search...

Entry information

Entry name

MK07_MOUSE

Accession

Primary (citable) accession number: Q9WVS8
Secondary accession number(s): Q3U2N7 , Q3UG52, Q497T0, Q5NCN6, Q5NCN7, Q5NCN9, Q6QLU8, Q9R1D9, Q9WVF3, Q9WVF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program