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O09110 (MP2K3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity mitogen-activated protein kinase kinase 3

Short name=MAP kinase kinase 3
Short name=MAPKK 3
EC=2.7.12.2
Alternative name(s):
MAPK/ERK kinase 3
Short name=MEK 3
Gene names
Name:Map2k3
Synonyms:Mkk3, Prkmk3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by dual phosphorylation on Ser-218 and Thr-222 By similarity.

Subunit structure

Binds to DYRK1B/MIRK and increases its kinase activity By similarity. Part of a complex with MAP3K3, RAC1 and CCM2. Interacts with ARRB1 By similarity. Ref.5

Post-translational modification

Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases regulates positively the kinase activity. Phosphorylated by TAOK2 By similarity. Autophosphorylated.

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
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.2. Source: MGI

activation of MAPK activity

Inferred from direct assay PubMed 15767678. Source: MGI

cardiac muscle contraction

Inferred from mutant phenotype PubMed 11593045. Source: MGI

inflammatory response

Inferred from mutant phenotype PubMed 10097111PubMed 10202148. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of cytokine biosynthetic process

Inferred from mutant phenotype PubMed 10097111. Source: MGI

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from direct assay PubMed 10202148Ref.2. Source: MGI

protein binding

Inferred from physical interaction PubMed 17438131. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 18948261. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: O09110-1)

Also known as: 3b;

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.
Isoform 1 (identifier: O09110-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSN → MSKP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Dual specificity mitogen-activated protein kinase kinase 3
PRO_0000086379

Regions

Domain64 – 325262Protein kinase
Nucleotide binding70 – 789ATP By similarity

Sites

Active site1901Proton acceptor By similarity
Binding site931ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue31Phosphoserine By similarity
Modified residue2181Phosphoserine By similarity
Modified residue2221Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 3737MESPA…PPVSN → MSKP in isoform 1.
VSP_004879

Experimental info

Sequence conflict391T → A Ref.1
Sequence conflict601E → K in CAA63649. Ref.1
Sequence conflict173 – 347175IVRAL…LGEDS → M Ref.4
Sequence conflict2161V → E in CAA63649. Ref.1
Sequence conflict2921D → Y in CAA63649. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (3b) [UniParc].

Last modified November 1, 2002. Version 2.
Checksum: 4A2A420EDCA8A2BC

FASTA34739,296
        10         20         30         40         50         60 
MESPAASPPA SLPQTKGKSK RKKDLRISCV SKPPVSNPTP PRNLDSRTFI TIGDRNFEVE 

        70         80         90        100        110        120 
ADDLVTISEL GRGAYGVVEK VRHAQSGTIM AVKRIRATVN TQEQKRLLMD LDINMRTVDC 

       130        140        150        160        170        180 
FYTVTFYGAL FREGDVWICM ELMDTSLDKF YRKVLEKNMK IPEDILGEIA VSIVRALEHL 

       190        200        210        220        230        240 
HSKLSVIHRD VKPSNVLINK EGHVKMCDFG ISGYLVDSVA KTMDAGCKPY MAPERINPEL 

       250        260        270        280        290        300 
NQKGYNVKSD VWSLGITMIE MAILRFPYES WGTPFQQLKQ VVEEPSPQLP ADQFSPEFVD 

       310        320        330        340 
FTSQCLRKNP AERMSYLELM EHPFFTLHKT KKTDIAAFVK EILGEDS 

« Hide

Isoform 1 [UniParc].

Checksum: 3F85122E7F272D5B
Show »

FASTA31435,836

References

« Hide 'large scale' references
[1]Neininger A., Gaestel M.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Purification and identification of a major activator for p38 from osmotically shocked cells: activation of mitogen-activated protein kinase kinase 6 by osmotic shock, tumor necrosis factor-alpha, and H2O2."
Moriguchi T., Toyoshima F., Gotoh Y., Iwamatsu A., Irie K., Mori E., Kuroyanagi N., Hagiwara M., Matsumoto K., Nishida E.
J. Biol. Chem. 271:26981-26988(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Embryonic liver and Small intestine.
[4]"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 1).
Tissue: Mammary gland.
[5]"Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock."
Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D., Lobel-Rice K.E., Horne E.A., Dell'Acqua M.L., Johnson G.L.
Nat. Cell Biol. 5:1104-1110(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K3; RAC1 AND CCM2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X93150 mRNA. Translation: CAA63649.1.
D87115 mRNA. Translation: BAA13247.1.
AK011002 mRNA. Translation: BAB27321.1.
AK008141 mRNA. Translation: BAB25489.1.
BC007467 mRNA. Translation: AAH07467.1.
CCDSCCDS24804.1. [O09110-1]
RefSeqNP_032954.1. NM_008928.4. [O09110-1]
UniGeneMm.18494.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LEZX-ray2.30B16-32[»]
ProteinModelPortalO09110.
SMRO09110. Positions 16-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204951. 8 interactions.
IntActO09110. 3 interactions.
MINTMINT-4102274.

PTM databases

PhosphoSiteO09110.

Proteomic databases

MaxQBO09110.
PaxDbO09110.
PRIDEO09110.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019076; ENSMUSP00000019076; ENSMUSG00000018932. [O09110-1]
ENSMUST00000130269; ENSMUSP00000114430; ENSMUSG00000018932.
GeneID26397.
KEGGmmu:26397.
UCSCuc007jgw.1. mouse. [O09110-1]

Organism-specific databases

CTD5606.
MGIMGI:1346868. Map2k3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00690000102058.
HOGENOMHOG000234206.
HOVERGENHBG108518.
InParanoidO09110.
KOK04432.
OMANYLELME.
OrthoDBEOG7J9VPW.
PhylomeDBO09110.
TreeFamTF350701.

Enzyme and pathway databases

BRENDA2.7.12.2. 3474.

Gene expression databases

ArrayExpressO09110.
BgeeO09110.
CleanExMM_MAP2K3.
GenevestigatorO09110.

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

NextBio304347.
PROO09110.
SOURCESearch...

Entry information

Entry nameMP2K3_MOUSE
AccessionPrimary (citable) accession number: O09110
Secondary accession number(s): P97293, Q91VX1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 2002
Last modified: July 9, 2014
This is version 134 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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