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Q9WVS8

- MK07_MOUSE

UniProt

Q9WVS8 - MK07_MOUSE

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Protein

Mitogen-activated protein kinase 7

Gene

Mapk7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation. Activated in response to hyperosmolarity, hydrogen peroxide, and epidermal growth factor (EGF) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841ATPPROSITE-ProRule annotation
Active sitei182 – 1821Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 699ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB-EC
  3. protein kinase activity Source: UniProtKB
  4. protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. cellular response to hydrogen peroxide Source: Ensembl
  4. cellular response to transforming growth factor beta stimulus Source: Ensembl
  5. negative regulation of apoptotic process Source: MGI
  6. negative regulation of endothelial cell apoptotic process Source: Ensembl
  7. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  8. negative regulation of heterotypic cell-cell adhesion Source: Ensembl
  9. negative regulation of NFAT protein import into nucleus Source: MGI
  10. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  11. negative regulation of response to cytokine stimulus Source: Ensembl
  12. peptidyl-serine phosphorylation Source: MGI
  13. positive regulation of protein metabolic process Source: Ensembl
  14. positive regulation of transcription from RNA polymerase II promoter in response to stress Source: Ensembl
  15. protein phosphorylation Source: UniProtKB
  16. regulation of angiogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_210064. ERKs are inactivated.
REACT_215063. ERK/MAPK targets.
REACT_216232. Signalling to ERK5.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 7 (EC:2.7.11.24)
Short name:
MAP kinase 7
Short name:
MAPK 7
Alternative name(s):
Big MAP kinase 1
Short name:
BMK-1
Extracellular signal-regulated kinase 5
Short name:
ERK-5
Gene namesi
Name:Mapk7
Synonyms:Bmk1, Erk5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1346347. Mapk7.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. NucleusPML body By similarity
Note: Translocates to the nucleus upon activation.By similarity
Isoform 1 : Cytoplasm By similarity. Nucleus By similarity
Note: Isoform 1 is detected in cytoplasm and nucleus.By similarity
Isoform 2 : Nucleus By similarity
Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation (By similarity).By similarity
Isoform 3 : Nucleus By similarity
Note: Isoform 2 is detected only in the nucleus. Translocates to the nucleus upon activation (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: MGI
  3. nucleus Source: MGI
  4. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 806805Mitogen-activated protein kinase 7PRO_0000186261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei710 – 7101PhosphoserineBy similarity
Modified residuei723 – 7231PhosphothreonineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-219 and Tyr-221, which activates the enzyme.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9WVS8.
PRIDEiQ9WVS8.

PTM databases

PhosphoSiteiQ9WVS8.

Expressioni

Tissue specificityi

Detected in testis, brain, kidney, lung and heart. Detected in total embryo (at protein level).1 Publication

Gene expression databases

BgeeiQ9WVS8.
CleanExiMM_MAPK7.
ExpressionAtlasiQ9WVS8. baseline and differential.
GenevestigatoriQ9WVS8.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi204806. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9WVS8.
SMRiQ9WVS8. Positions 11-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 347293Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7776Required for cytoplasmic targetingAdd
BLAST
Regioni78 – 13962Required for binding to MAP2K5Add
BLAST
Regioni140 – 406267Necessary for oligomerizationAdd
BLAST
Regioni407 – 806400May not be required for kinase activity; required to stimulate MEF2C activityAdd
BLAST
Regioni505 – 53935Nuclear localization signalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi219 – 2213TXY

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi434 – 46532Pro-richAdd
BLAST
Compositional biasi521 – 5244Poly-Arg
Compositional biasi578 – 700123Pro-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074298.
HOVERGENiHBG108137.
InParanoidiQ9WVS8.
KOiK04464.
OMAiIIETIGT.
PhylomeDBiQ9WVS8.
TreeFamiTF105099.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9WVS8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD
60 70 80 90 100
VGDEYEIIET IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL
110 120 130 140 150
RELKILKHFK HDNIIAIKDI LKPTVPYGEF RSVYVVLDLM ESDLHQIIHS
160 170 180 190 200
SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH RDLKPSNLLV NENCELKIGD
210 220 230 240 250
FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT QAIDLWSVGC
260 270 280 290 300
IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS
310 320 330 340 350
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY
360 370 380 390 400
HDPDDEPDCA PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR
410 420 430 440 450
FQPSLQPVAS EPVCPDVEMP SPWAPSGDCA MESPPPALPP CSDPAPDTVD
460 470 480 490 500
LTLQPAPPAS ELAPPKREGA ISDNTKAALK AALLKSLRSR LRDGPSAPLE
510 520 530 540 550
APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER KERGAGTLGG
560 570 580 590 600
PSTDPLAGLV LSDNDRSLLE RWTRMARPPA PAPAPAPAPA PAPSSAQPTS
610 620 630 640 650
TPTGPVSQST GPLQPAGSIP GPASQPVCPP PGPVPQPAGP IPAPLQTAPS
660 670 680 690 700
TSLLASQSLV PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV
710 720 730 740 750
NLVTQQLSKS QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA
760 770 780 790 800
DGPQDGQADS ASLSASLLAD WLEGHGMNPA DIESLQREIQ MDSPMLLSDL

PDLQEP
Length:806
Mass (Da):87,733
Last modified:November 1, 1999 - v1
Checksum:iE7CC41C4BBDE0633
GO
Isoform 2 (identifier: Q9WVS8-2) [UniParc]FASTAAdd to Basket

Also known as: Big MAP kinase 1b, mERK5b

The sequence of this isoform differs from the canonical sequence as follows:
     2-77: AEPLKEEDGE...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.

Show »
Length:738
Mass (Da):80,511
Checksum:i7909E06820499AF5
GO
Isoform 3 (identifier: Q9WVS8-3) [UniParc]FASTAAdd to Basket

Also known as: Big MAP kinase 1c, mERK5c

The sequence of this isoform differs from the canonical sequence as follows:
     2-139: Missing.

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

Show »
Length:668
Mass (Da):72,594
Checksum:i8B0E505EA2545FFA
GO
Isoform 4 (identifier: Q9WVS8-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:502
Mass (Da):55,914
Checksum:i905BD56BC58913D8
GO
Isoform 5 (identifier: Q9WVS8-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:756
Mass (Da):82,314
Checksum:iC0CCFA5D2F8C84F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911N → D in BAE28357. (PubMed:16141072)Curated
Sequence conflicti308 – 3081P → H in BAE28357. (PubMed:16141072)Curated
Sequence conflicti331 – 3311E → K in AAI00399. (PubMed:15489334)Curated
Sequence conflicti409 – 4091A → V in AAD39394. (PubMed:11139578)Curated
Sequence conflicti409 – 4091A → V in AAD39395. (PubMed:11139578)Curated
Sequence conflicti409 – 4091A → V in AAD39396. (PubMed:11139578)Curated
Sequence conflicti424 – 4241A → R in AAD39394. (PubMed:11139578)Curated
Sequence conflicti424 – 4241A → R in AAD39395. (PubMed:11139578)Curated
Sequence conflicti424 – 4241A → R in AAD39396. (PubMed:11139578)Curated
Sequence conflicti578 – 5781P → PPAPA in BAE28357. (PubMed:16141072)Curated
Sequence conflicti578 – 5781P → PPAPA in BAE33103. (PubMed:16141072)Curated
Sequence conflicti588 – 5881A → R in AAD39394. (PubMed:11139578)Curated
Sequence conflicti588 – 5881A → R in AAD39395. (PubMed:11139578)Curated
Sequence conflicti588 – 5881A → R in AAD39396. (PubMed:11139578)Curated
Sequence conflicti592 – 5921A → Q in AAD39394. (PubMed:11139578)Curated
Sequence conflicti592 – 5921A → Q in AAD39395. (PubMed:11139578)Curated
Sequence conflicti592 – 5921A → Q in AAD39396. (PubMed:11139578)Curated
Sequence conflicti618 – 6181S → C in AAD39394. (PubMed:11139578)Curated
Sequence conflicti618 – 6181S → C in AAD39395. (PubMed:11139578)Curated
Sequence conflicti618 – 6181S → C in AAD39396. (PubMed:11139578)Curated
Sequence conflicti642 – 6421P → A in AAD39394. (PubMed:11139578)Curated
Sequence conflicti642 – 6421P → A in AAD39395. (PubMed:11139578)Curated
Sequence conflicti642 – 6421P → A in AAD39396. (PubMed:11139578)Curated
Sequence conflicti803 – 8031L → V in BAE28357. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 139138Missing in isoform 3. 1 PublicationVSP_035201Add
BLAST
Alternative sequencei2 – 7776AEPLK…RRRLT → MCGLLSRG in isoform 2. 2 PublicationsVSP_035202Add
BLAST
Alternative sequencei493 – 806314DGPSA…DLQEP → GGVWAQQLSG in isoform 4. 1 PublicationVSP_035203Add
BLAST
Alternative sequencei757 – 80650Missing in isoform 5. 1 PublicationVSP_035204Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS24814.1. [Q9WVS8-1]
RefSeqiNP_001277962.1. NM_001291033.1.
NP_001277963.1. NM_001291034.1. [Q9WVS8-1]
NP_001277964.1. NM_001291035.1.
NP_001277965.1. NM_001291036.1.
NP_001277966.1. NM_001291037.1.
NP_035971.1. NM_011841.2. [Q9WVS8-1]
XP_006533340.1. XM_006533277.1. [Q9WVS8-1]
XP_006533341.1. XM_006533278.1. [Q9WVS8-5]
UniGeneiMm.38172.

Genome annotation databases

EnsembliENSMUST00000079080; ENSMUSP00000078087; ENSMUSG00000001034. [Q9WVS8-1]
GeneIDi23939.
KEGGimmu:23939.
UCSCiuc007jho.1. mouse. [Q9WVS8-2]
uc007jhp.1. mouse. [Q9WVS8-1]
uc007jht.1. mouse. [Q9WVS8-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS24814.1. [Q9WVS8-1 ]
RefSeqi NP_001277962.1. NM_001291033.1.
NP_001277963.1. NM_001291034.1. [Q9WVS8-1 ]
NP_001277964.1. NM_001291035.1.
NP_001277965.1. NM_001291036.1.
NP_001277966.1. NM_001291037.1.
NP_035971.1. NM_011841.2. [Q9WVS8-1 ]
XP_006533340.1. XM_006533277.1. [Q9WVS8-1 ]
XP_006533341.1. XM_006533278.1. [Q9WVS8-5 ]
UniGenei Mm.38172.

3D structure databases

ProteinModelPortali Q9WVS8.
SMRi Q9WVS8. Positions 11-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204806. 3 interactions.

PTM databases

PhosphoSitei Q9WVS8.

Proteomic databases

MaxQBi Q9WVS8.
PRIDEi Q9WVS8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079080 ; ENSMUSP00000078087 ; ENSMUSG00000001034 . [Q9WVS8-1 ]
GeneIDi 23939.
KEGGi mmu:23939.
UCSCi uc007jho.1. mouse. [Q9WVS8-2 ]
uc007jhp.1. mouse. [Q9WVS8-1 ]
uc007jht.1. mouse. [Q9WVS8-4 ]

Organism-specific databases

CTDi 5598.
MGIi MGI:1346347. Mapk7.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074298.
HOVERGENi HBG108137.
InParanoidi Q9WVS8.
KOi K04464.
OMAi IIETIGT.
PhylomeDBi Q9WVS8.
TreeFami TF105099.

Enzyme and pathway databases

Reactomei REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_210064. ERKs are inactivated.
REACT_215063. ERK/MAPK targets.
REACT_216232. Signalling to ERK5.

Miscellaneous databases

NextBioi 303745.
PROi Q9WVS8.
SOURCEi Search...

Gene expression databases

Bgeei Q9WVS8.
CleanExi MM_MAPK7.
ExpressionAtlasi Q9WVS8. baseline and differential.
Genevestigatori Q9WVS8.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMK07_MOUSE
AccessioniPrimary (citable) accession number: Q9WVS8
Secondary accession number(s): Q3U2N7
, Q3UG52, Q497T0, Q5NCN6, Q5NCN7, Q5NCN9, Q6QLU8, Q9R1D9, Q9WVF3, Q9WVF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3