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Protein

Mitogen-activated protein kinase 1

Gene

MKP1

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 maintenance of cell integrity. Functionally complements SLT2 null mutant in S.cerevisiae.1 Publication

Catalytic activityi

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

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation. Activated by oxidative stress.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52ATPPROSITE-ProRule annotation1
Active sitei149Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi27 – 35ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent protein binding Source: UniProtKB
  • MAP kinase activity Source: UniProtKB

GO - Biological processi

  • cellular component organization Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • positive regulation of growth rate Source: UniProtKB
  • response to oxidative stress 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 1 (EC:2.7.11.24)
Alternative name(s):
MAP kinase Mkp1
Gene namesi
Name:MKP1Imported
OrganismiPneumocystis carinii
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52K → R: Loss of kinase activity. 2 Publications1
Mutagenesisi182T → A: No change in activity; when associated with F-184. 1 Publication1
Mutagenesisi184Y → F: No change in activity; when associated with A-182. 1 Publication1
Mutagenesisi186T → A: Loss of kinase activity; when associated with F-188. 2 Publications1
Mutagenesisi188Y → F: Loss of kinase activity; when associated with A-186. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002477431 – 370Mitogen-activated protein kinase 1Add BLAST370

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei186Phosphothreonine1 Publication1
Modified residuei188Phosphotyrosine1 Publication1

Post-translational modificationi

Dually phosphorylated on Thr-186 and Tyr-188, which activates the enzyme.

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiO94737.

Interactioni

GO - Molecular functioni

  • ATP-dependent protein binding Source: UniProtKB

Structurei

3D structure databases

ProteinModelPortaliO94737.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 314Protein kinasePROSITE-ProRule annotationAdd BLAST294

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi186 – 188TXY3

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.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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.

O94737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSKHSVFNV MGQEFVLQKG YEVIKGLGKG SYGVVCSAKN IEVEDNNKVA
60 70 80 90 100
IKKITNIFSK KMLAKRALRE IMLLQHFRNH KNITTLYDMD IVDPSKFNEL
110 120 130 140 150
YLYEELMQAN LNSIIRSDQP LTDAHFQSFI YQILCGLKYI HSANVLHRDL
160 170 180 190 200
KPSNLLINAD CKLKICDFGL SRGISVNQGQ GTEYMTEYVT TRWYRAPEVM
210 220 230 240 250
LSFQSYSKAI DLWSVGCILA ELLGRKPFFK GSNYVDQLNQ IFCILGTPNE
260 270 280 290 300
NIISKIKSAS AQSYIRSLPT LPKMPYSKIF PYANPDALDL LNCLLTFDPY
310 320 330 340 350
DRISCEEALE HPYLIIWHDP NKEPVCSEQF DFGFEAIDSI EEIRQMIINE
360 370
VSRFKGLTGN QKLYHSISNT
Length:370
Mass (Da):42,396
Last modified:May 1, 1999 - v1
Checksum:i7DE7E10B8A06536E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077677 mRNA. Translation: AAD10000.1.
AF084383 Genomic DNA. Translation: AAD16043.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077677 mRNA. Translation: AAD10000.1.
AF084383 Genomic DNA. Translation: AAD16043.1.

3D structure databases

ProteinModelPortaliO94737.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiO94737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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...

Entry informationi

Entry nameiMAPK1_PNECA
AccessioniPrimary (citable) accession number: O94737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 75 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

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 one 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.