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O42781 (MAPK2_PNECA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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 2

EC=2.7.11.24
Alternative name(s):
PCM
Gene names
Name:MKP2
Synonyms:MAPK
OrganismPneumocystis carinii
Taxonomic identifier4754 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine-threonine protein kinase which may be involved in pheromone signaling. Functionally complements the MAPK pheromone signaling pathway in S.cerevisiae. Ref.1 Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1

Cofactor

Divalent cations including magnesium and manganese. Ref.3

Enzyme regulation

Activated by tyrosine and threonine phosphorylation By similarity. Inhibited by the MEK inhibitor U0126 but not by the p38 inhibitor SB203580. Cobalt abolishes kinase activity, while calcium, copper and nickel have little effect on kinase activity. Ref.3 UniProtKB P16892

Subcellular location

Nucleus By similarity UniProtKB P27638.

Developmental stage

Activity is significantly higher in trophic forms than in cysts. Ref.3

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-176 and Tyr-178, 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.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5. Ref.3

Temperature dependence:

Optimum temperature is 30-35 degrees Celsius. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Mitogen-activated protein kinase 2
PRO_0000247744

Regions

Domain16 – 304289Protein kinase
Nucleotide binding22 – 309ATP By similarity
Motif176 – 1783TXY

Sites

Active site1401Proton acceptor By similarity
Binding site451ATP By similarity

Amino acid modifications

Modified residue1761Phosphothreonine By similarity UniProtKB P16892
Modified residue1781Phosphotyrosine By similarity UniProtKB P16892

Sequences

Sequence LengthMass (Da)Tools
O42781 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 53766B1A95F050AB

FASTA35140,574
        10         20         30         40         50         60 
MTASSRNVRF NVSDDYEILD VIGEGAYGIV CSAIHKPSGQ KVAIKKISPF DHSMFCLRTL 

        70         80         90        100        110        120 
REMKLLRYFN HENIISILDI QQPQDFESFS EVYLIQELME TDMHRVIRTQ DLSDDHCQYF 

       130        140        150        160        170        180 
IYQILRALKA MHSADILHRD LKPSNLLLNA NCDLKVCDFG LARSAVSTED SSSFMTEYVA 

       190        200        210        220        230        240 
TRWYRAPEIM LTFKEYTKAI DIWSVGCILA EMLSGRPLFP GKDYHHQLML ILDVLGTPTM 

       250        260        270        280        290        300 
EDYYGIKSRR AREYIRSLPF KKRVSFASIF PRANPLALDL LEKLLAFNPA KRVTAEEALQ 

       310        320        330        340        350 
HNYLEPYHDP DDEPTAPPIS PSFFDFDRIK DSLTKNDLKI LIYKEIMSMN N 

« Hide

References

[1]"Characterization of a mitogen-activated protein kinase from Pneumocystis carinii."
Thomas C.F. Jr., Kottom T.J., Leof E.B., Limper A.H.
Am. J. Physiol. 275:L193-L199(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[2]Smulian A.G.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complementation and characterization of the Pneumocystis carinii MAPK, PCM."
Vohra P.K., Puri V., Thomas C.F. Jr.
FEBS Lett. 551:139-146(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF043941 mRNA. Translation: AAC98088.1.
AF077548 Genomic DNA. Translation: AAC27327.1.

3D structure databases

ProteinModelPortalO42781.
SMRO42781. Positions 10-348.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO42781.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
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]
PRINTSPR01773. P38MAPKINASE.
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 nameMAPK2_PNECA
AccessionPrimary (citable) accession number: O42781
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families