SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O42781

- MAPK2_PNECA

UniProt

O42781 - MAPK2_PNECA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Mitogen-activated protein kinase 2

Gene
MKP2, MAPK
Organism
Pneumocystis carinii
Status
Reviewed - 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

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 similarity1 Publication

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 – 451ATP By similarity
Active sitei140 – 1401Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATP By similarity

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
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:MKP2
Synonyms:MAPK
OrganismiPneumocystis carinii
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Subcellular locationi

Nucleus By similarity 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 – 1761Phosphothreonine By similarityBy similarity
Modified residuei178 – 1781Phosphotyrosine By similarityBy 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 304289Protein kinaseAdd
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

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: April 16, 2014
This is version 65 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