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O42781

- MAPK2_PNECA

UniProt

O42781 - MAPK2_PNECA

Protein

Mitogen-activated protein kinase 2

Gene

MKP2

Organism
Pneumocystis carinii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    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

    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. cell cycle arrest in response to pheromone Source: UniProtKB
    2. MAPK cascade Source: GOC
    3. response to pheromone Source: UniProtKB
    4. signal transduction Source: UniProtKB

    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

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    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

    ProteinModelPortaliO42781.
    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_dom.
    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

    MTASSRNVRF NVSDDYEILD VIGEGAYGIV CSAIHKPSGQ KVAIKKISPF    50
    DHSMFCLRTL REMKLLRYFN HENIISILDI QQPQDFESFS EVYLIQELME 100
    TDMHRVIRTQ DLSDDHCQYF IYQILRALKA MHSADILHRD LKPSNLLLNA 150
    NCDLKVCDFG LARSAVSTED SSSFMTEYVA TRWYRAPEIM LTFKEYTKAI 200
    DIWSVGCILA EMLSGRPLFP GKDYHHQLML ILDVLGTPTM EDYYGIKSRR 250
    AREYIRSLPF KKRVSFASIF PRANPLALDL LEKLLAFNPA KRVTAEEALQ 300
    HNYLEPYHDP DDEPTAPPIS PSFFDFDRIK DSLTKNDLKI LIYKEIMSMN 350
    N 351
    Length:351
    Mass (Da):40,574
    Last modified:June 1, 1998 - v1
    Checksum:i53766B1A95F050AB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043941 mRNA. Translation: AAC98088.1.
    AF077548 Genomic DNA. Translation: AAC27327.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043941 mRNA. Translation: AAC98088.1 .
    AF077548 Genomic DNA. Translation: AAC27327.1 .

    3D structure databases

    ProteinModelPortali O42781.
    SMRi O42781. Positions 10-348.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O42781.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01773. P38MAPKINASE.
    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

    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: October 1, 2014
    This is version 66 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