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P0C865

- MK07_RAT

UniProt

P0C865 - MK07_RAT

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Protein
Mitogen-activated protein kinase 7
Gene
Mapk7, Bmk1, Erk5
Organism
Rattus norvegicus (Rat)
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.1 Publication

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841ATP By similarity
Active sitei182 – 1821Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 699ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. MAP kinase activity Source: RGD
  3. protein binding Source: Alzheimers_University_of_Toronto

GO - Biological processi

  1. ERK5 cascade Source: RGD
  2. MAPK cascade Source: RGD
  3. cell cycle Source: UniProtKB-KW
  4. cell differentiation Source: UniProtKB-KW
  5. protein autophosphorylation Source: RGD
  6. protein phosphorylation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621505. Mapk7.

Subcellular locationi

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

GO - Cellular componenti

  1. PML body Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 806805Mitogen-activated protein kinase 7
PRO_0000349105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei710 – 7101Phosphoserine By similarity
Modified residuei723 – 7231Phosphothreonine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0C865.
PRIDEiP0C865.

PTM databases

PhosphoSiteiP0C865.

Expressioni

Gene expression databases

GenevestigatoriP0C865.

Interactioni

Subunit structurei

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.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP0C865.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 347293Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7776Required for cytoplasmic targeting By similarity
Add
BLAST
Regioni78 – 13962Required for binding to MAP2K5 By similarity
Add
BLAST
Regioni140 – 406267Necessary for oligomerization By similarity
Add
BLAST
Regioni407 – 806400May not be required for kinase activity; required to stimulate MEF2C activity By similarity
Add
BLAST
Regioni505 – 53935Nuclear localization signal By similarity
Add
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi403 – 46563Pro-rich
Add
BLAST
Compositional biasi513 – 54331Arg-rich
Add
BLAST
Compositional biasi578 – 692115Pro-rich
Add
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

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000113595.
HOVERGENiHBG108137.
PhylomeDBiP0C865.

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_dom.
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]

Sequencei

Sequence statusi: Complete.

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

P0C865-1 [UniParc]FASTAAdd to Basket

« Hide

MAEPLKEEDG EDGSGEPPGR VKAEPVHTAA SVVAKNLALL KARSFDVTFD    50
VGDEYEIIET IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL 100
RELKILKHFK HDNIIAIKDI LRPTVPYGEF RSVYVVLDLM ESDLHQIIHS 150
SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH RDLKPSNLLV NENCELKIGD 200
FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT QAIDLWSVGC 250
IFGEMLARRQ LFPGKNYVHQ LQLIMMVLGT PSPAVIQAVG AERVRAYIQS 300
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARISAAA ALRHPFLAKY 350
HDPDDEPDCA PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR 400
FQPSLQPVAS EPVCPDVEMP SPWAPSGDCA MESPPPALPP CSGPAPDTVD 450
LTLQPAPPAS ELAPPKREGA ISDNTKAALK AALLKSLRSR LRDGPSAPLE 500
APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER KERGAGTLGG 550
PSTDPLAGLV LSDNDRSLLE RWTRMARPPV PAPAPAPAPT PKPSSAQPTS 600
PPNGPVSQST APLQPAGSIP GPASQPVCPP PGPVPQPAGP VPAPLQTAPS 650
TSLLASQSLV PPSGLPGSGA PEVLPYFPSG PPPPDPGLTP QPSTSESPDV 700
NLVTQQLSKS QVEDPLPPVF SGTPKGSGAG YGVGFDLEEF LNQSFDMGVA 750
DGPQDGQADS ASLSASLLAD WLEGHGMNPA DIESLQREIQ MDSPMLLSDL 800
PDLQEP 806
Length:806
Mass (Da):87,827
Last modified:September 2, 2008 - v1
Checksum:i3CF236450A348C82
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03073216 Genomic DNA. No translation available.
UniGeneiRn.144629.

Genome annotation databases

UCSCiRGD:621505. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03073216 Genomic DNA. No translation available.
UniGenei Rn.144629.

3D structure databases

ProteinModelPortali P0C865.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei P0C865.

Proteomic databases

PaxDbi P0C865.
PRIDEi P0C865.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:621505. rat.

Organism-specific databases

RGDi 621505. Mapk7.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000113595.
HOVERGENi HBG108137.
PhylomeDBi P0C865.

Gene expression databases

Genevestigatori P0C865.

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_dom.
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. "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.
    , 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.

Entry informationi

Entry nameiMK07_RAT
AccessioniPrimary (citable) accession number: P0C865
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: June 11, 2014
This is version 39 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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