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Q63932 (MP2K2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity mitogen-activated protein kinase kinase 2

Short name=MAP kinase kinase 2
Short name=MAPKK 2
EC=2.7.12.2
Alternative name(s):
ERK activator kinase 2
MAPK/ERK kinase 2
Short name=MEK 2
Gene names
Name:Map2k2
Synonyms:Mek2, Mkk2, Prkmk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases. Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Inhibited by serine/threonine phosphatase 2A.

Subunit structure

Interacts with MORG1. Interacts with SGK1 By similarity. Ref.5 Ref.6

Tissue specificity

Expressed in adult intestine, kidney, liver, lung, pancreas, spleen, thymus, and at high levels in the neonatal brain. Lower expression is found in adult brain and heart.

Post-translational modification

Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF or MEKK1) regulates positively the kinase activity. Phosphorylated by MAP2K1/MEK1. Low levels of autophosphorylation have been observed. Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Traceable author statement PubMed 19565474. Source: UniProtKB

peptidyl-serine autophosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell motility

Inferred from direct assay PubMed 20179103. Source: BHF-UCL

regulation of Golgi inheritance

Traceable author statement PubMed 19565474. Source: UniProtKB

regulation of early endosome to late endosome transport

Traceable author statement PubMed 19565474. Source: UniProtKB

regulation of stress-activated MAPK cascade

Traceable author statement PubMed 19565474. Source: UniProtKB

   Cellular_componentGolgi apparatus

Traceable author statement PubMed 19565474. Source: UniProtKB

cell cortex

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement PubMed 19565474. Source: UniProtKB

early endosome

Traceable author statement PubMed 19565474. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Traceable author statement PubMed 19565474. Source: UniProtKB

late endosome

Traceable author statement PubMed 19565474. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Traceable author statement PubMed 19565474. Source: UniProtKB

nucleus

Traceable author statement PubMed 19565474. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

peroxisomal membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from electronic annotation. Source: Ensembl

protein complex scaffold

Inferred from direct assay PubMed 20179103. Source: BHF-UCL

protein serine/threonine kinase activator activity

Inferred from electronic annotation. Source: Ensembl

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine/tyrosine kinase activity

Traceable author statement PubMed 19565474. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rgs12Q8CGE93EBI-397724,EBI-7340552

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Dual specificity mitogen-activated protein kinase kinase 2
PRO_0000086373

Regions

Domain72 – 370299Protein kinase
Nucleotide binding78 – 869ATP By similarity
Compositional bias266 – 31651Pro-rich

Sites

Active site1941Proton acceptor By similarity
Binding site1011ATP
Site10 – 112Cleavage; by anthrax lethal factor By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2221Phosphoserine; by RAF By similarity
Modified residue2261Phosphoserine; by RAF By similarity
Modified residue2931Phosphoserine By similarity
Modified residue2951Phosphoserine By similarity
Modified residue3951Phosphothreonine By similarity
Modified residue3971Phosphothreonine By similarity

Experimental info

Mutagenesis1011K → M: Inactivation.
Sequence conflict961L → F in AAC60678. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q63932 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F00CD807E86F5B26

FASTA40144,402
        10         20         30         40         50         60 
MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELDLDEQQ RKRLEAFLTQ 

        70         80         90        100        110        120 
KAKVGELKDD DFERISELGA GNGGVVTKAR HRPSGLIMAR KLIHLEIKPA VRNQIIRELQ 

       130        140        150        160        170        180 
VLHECNSPYI VGFYGAFYSD GEISICMEHM DGGSLDQVLK EAKRIPEDIL GKVSIAVLRG 

       190        200        210        220        230        240 
LAYLREKHQI MHRDVKPSNI LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMSPERLQ 

       250        260        270        280        290        300 
GTHYSVQSDI WSMGLSLVEL AIGRYPIPPP DAKELEASFG RPVVDGADGE PHSVSPRPRP 

       310        320        330        340        350        360 
PGRPISVGHG MDSRPAMAIF ELLDYIVNEP PPKLPSGVFS SDFQEFVNKC LIKNPAERAD 

       370        380        390        400 
LKLLMNHAFI KRSEGEEVDF AGWLCRTLRL KQPSTPTRTA V 

« Hide

References

« Hide 'large scale' references
[1]"MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues."
Brott B.K., Alessandrini A., Largaespada D.A., Copeland N.G., Jenkins N.A., Crews C.M., Erikson R.L.
Cell Growth Differ. 4:921-929(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
Strain: BALB/c.
Tissue: Neonatal brain.
[2]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Cerebellum and Tongue.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product."
Crews C.M., Erikson R.L.
Proc. Natl. Acad. Sci. U.S.A. 89:8205-8209(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 118-140 AND 210-238.
Tissue: T-cell.
[5]"Modular construction of a signaling scaffold: MORG1 interacts with components of the ERK cascade and links ERK signaling to specific agonists."
Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E., Bissonette E.A., Weber M.J.
Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MORG1.
[6]"A Mek1-Mek2 heterodimer determines the strength and duration of the Erk signal."
Catalanotti F., Reyes G., Jesenberger V., Galabova-Kovacs G., de Matos Simoes R., Carugo O., Baccarini M.
Nat. Struct. Mol. Biol. 16:294-303(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP2K1/MEK1, PHOSPHORYLATION BY MAP2K1/MEK1, FUNCTION IN ERK SIGNALING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S68267 mRNA. Translation: AAC60678.1.
AK009392 mRNA. Translation: BAB26261.1.
AK080574 mRNA. Translation: BAC37945.1.
CH466553 Genomic DNA. Translation: EDL31456.1.
RefSeqNP_075627.2. NM_023138.4.
UniGeneMm.275436.

3D structure databases

ProteinModelPortalQ63932.
SMRQ63932. Positions 60-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204950. 5 interactions.
DIPDIP-454N.
IntActQ63932. 7 interactions.
MINTMINT-1518275.
STRING10090.ENSMUSP00000121111.

PTM databases

PhosphoSiteQ63932.

Proteomic databases

PaxDbQ63932.
PRIDEQ63932.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000143517; ENSMUSP00000121111; ENSMUSG00000035027.
GeneID26396.
KEGGmmu:26396.
UCSCuc007gfx.2. mouse.

Organism-specific databases

CTD5605.
MGIMGI:1346867. Map2k2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00690000101918.
HOGENOMHOG000234206.
HOVERGENHBG108518.
InParanoidQ9D7B0.
KOK04369.
OMARLKQPST.
OrthoDBEOG7HF1KZ.
TreeFamTF105137.

Enzyme and pathway databases

BRENDA2.7.12.2. 3474.

Gene expression databases

ArrayExpressQ63932.
BgeeQ63932.
CleanExMM_MAP2K2.
GenevestigatorQ63932.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
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.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP2K2. mouse.
NextBio304343.
PROQ63932.
SOURCESearch...

Entry information

Entry nameMP2K2_MOUSE
AccessionPrimary (citable) accession number: Q63932
Secondary accession number(s): Q9D7B0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 120 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot