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Protein

Mitogen-activated protein kinase 2

Gene

MKP2

Organism
Pneumocystis carinii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine-threonine protein kinase which may be involved in pheromone signaling. Functionally complements the MAPK pheromone signaling pathway in S.cerevisiae.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent cations including magnesium and manganese.1 Publication

Enzyme regulationi

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.By similarity

pH dependencei

Optimum pH is 6.5.1 Publication

Temperature dependencei

Optimum temperature is 30-35 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATPPROSITE-ProRule annotation
Active sitei140 – 1401Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB

GO - Biological processi

  1. MAPK cascade Source: GOC
  2. mitotic cell cycle arrest in response to pheromone Source: UniProtKB
  3. response to pheromone Source: UniProtKB
  4. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 2 (EC:2.7.11.24)
Alternative name(s):
PCM
Gene namesi
Name:MKP2Imported
Synonyms:MAPKImported
OrganismiPneumocystis carinii
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Subcellular locationi

  1. Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Mitogen-activated protein kinase 2PRO_0000247744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761PhosphothreonineBy similarity
Modified residuei178 – 1781PhosphotyrosineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-176 and Tyr-178, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO42781.

Expressioni

Developmental stagei

Activity is significantly higher in trophic forms than in cysts.1 Publication

Structurei

3D structure databases

SMRiO42781. Positions 10-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 304289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi176 – 1783TXY

Domaini

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

Family and domain databases

InterProiIPR011009. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
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.

O42781-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASSRNVRF NVSDDYEILD VIGEGAYGIV CSAIHKPSGQ KVAIKKISPF
60 70 80 90 100
DHSMFCLRTL REMKLLRYFN HENIISILDI QQPQDFESFS EVYLIQELME
110 120 130 140 150
TDMHRVIRTQ DLSDDHCQYF IYQILRALKA MHSADILHRD LKPSNLLLNA
160 170 180 190 200
NCDLKVCDFG LARSAVSTED SSSFMTEYVA TRWYRAPEIM LTFKEYTKAI
210 220 230 240 250
DIWSVGCILA EMLSGRPLFP GKDYHHQLML ILDVLGTPTM EDYYGIKSRR
260 270 280 290 300
AREYIRSLPF KKRVSFASIF PRANPLALDL LEKLLAFNPA KRVTAEEALQ
310 320 330 340 350
HNYLEPYHDP DDEPTAPPIS PSFFDFDRIK DSLTKNDLKI LIYKEIMSMN

N
Length:351
Mass (Da):40,574
Last modified:June 1, 1998 - v1
Checksum:i53766B1A95F050AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043941 mRNA. Translation: AAC98088.1.
AF077548 Genomic DNA. Translation: AAC27327.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043941 mRNA. Translation: AAC98088.1.
AF077548 Genomic DNA. Translation: AAC27327.1.

3D structure databases

SMRiO42781. Positions 10-348.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO42781.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR011009. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiMAPK2_PNECA
AccessioniPrimary (citable) accession number: O42781
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: June 1, 1998
Last modified: April 1, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.