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P0C865

- MK07_RAT

UniProt

P0C865 - MK07_RAT

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Protein

Mitogen-activated protein kinase 7

Gene

Mapk7

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).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: RGD
  2. MAP kinase activity Source: RGD

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. ERK5 cascade Source: RGD
  4. MAPK cascade Source: RGD
  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. cytoplasm Source: UniProtKB
  2. nucleus Source: RGD
  3. 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_0000349105Add
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

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliP0C865.
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 targetingBy similarityAdd
BLAST
Regioni78 – 13962Required for binding to MAP2K5By similarityAdd
BLAST
Regioni140 – 406267Necessary for oligomerizationBy similarityAdd
BLAST
Regioni407 – 806400May not be required for kinase activity; required to stimulate MEF2C activityBy similarityAdd
BLAST
Regioni505 – 53935Nuclear localization signalBy similarityAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi403 – 46563Pro-richAdd
BLAST
Compositional biasi513 – 54331Arg-richAdd
BLAST
Compositional biasi578 – 692115Pro-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.
HOGENOMiHOG000113595.
HOVERGENiHBG108137.
InParanoidiP0C865.
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.
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

        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 LRPTVPYGEF 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 CSGPAPDTVD
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 RWTRMARPPV PAPAPAPAPT PKPSSAQPTS
610 620 630 640 650
PPNGPVSQST APLQPAGSIP GPASQPVCPP PGPVPQPAGP VPAPLQTAPS
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):87,827
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.
InParanoidi P0C865.
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.
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: October 29, 2014
This is version 41 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