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P0C865 (MK07_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

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. Forms oligomers By similarity. Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D. Interacts with SGK1 By similarity. Interacts with PML By similarity. Ref.2

Subcellular location

Cytoplasm. Nucleus. NucleusPML body By similarity. Note: Translocates to the nucleus upon activation By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 806805Mitogen-activated protein kinase 7
PRO_0000349105

Regions

Domain55 – 347293Protein kinase
Nucleotide binding61 – 699ATP By similarity
Region2 – 7776Required for cytoplasmic targeting By similarity
Region78 – 13962Required for binding to MAP2K5 By similarity
Region140 – 406267Necessary for oligomerization By similarity
Region407 – 806400May not be required for kinase activity; required to stimulate MEF2C activity By similarity
Region505 – 53935Nuclear localization signal By similarity
Motif219 – 2213TXY By similarity
Compositional bias403 – 46563Pro-rich
Compositional bias513 – 54331Arg-rich
Compositional bias578 – 692115Pro-rich

Sites

Active site1821Proton acceptor By similarity
Binding site841ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue7101Phosphoserine By similarity
Modified residue7231Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C865 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 3CF236450A348C82

FASTA80687,827
        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 
LRPTVPYGEF 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 CSGPAPDTVD LTLQPAPPAS ELAPPKREGA ISDNTKAALK 

       490        500        510        520        530        540 
AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER 

       550        560        570        580        590        600 
KERGAGTLGG PSTDPLAGLV LSDNDRSLLE RWTRMARPPV PAPAPAPAPT PKPSSAQPTS 

       610        620        630        640        650        660 
PPNGPVSQST APLQPAGSIP GPASQPVCPP PGPVPQPAGP VPAPLQTAPS 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 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1."
Yang C.-C., Ornatsky O.I., McDermott J.C., Cruz T.F., Prody C.A.
Nucleic Acids Res. 26:4771-4777(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEF2A; MEF2C AND MEF2D.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03073216 Genomic DNA. No translation available.
UniGeneRn.144629.

3D structure databases

ProteinModelPortalP0C865.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP0C865.

Proteomic databases

PaxDbP0C865.
PRIDEP0C865.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:621505. rat.

Organism-specific databases

RGD621505. Mapk7.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000113595.
HOVERGENHBG108137.
PhylomeDBP0C865.

Gene expression databases

GenevestigatorP0C865.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMK07_RAT
AccessionPrimary (citable) accession number: P0C865
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families