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Q9WVR7 (PPM1F_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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:
Protein phosphatase 1F

EC=3.1.3.16
Alternative name(s):
Ca(2+)/calmodulin-dependent protein kinase phosphatase
Short name=CaM-kinase phosphatase
Short name=CaMKPase
Partner of PIX 2
Gene names
Name:Ppm1f
Synonyms:Popx2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subunit structure

Associates with FEM1B By similarity.

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Biological processApoptosis
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

histone dephosphorylation

Inferred from direct assay PubMed 16844074. Source: RGD

intrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-threonine dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 11559703. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 10456318PubMed 16844074. Source: RGD

   Cellular_componentcytosol

Inferred from direct assay Ref.1. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalmodulin-dependent protein phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Traceable author statement Ref.1. Source: RGD

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Protein phosphatase 1F
PRO_0000057760

Regions

Compositional bias99 – 10911Poly-Glu

Sites

Metal binding1941Manganese 1 By similarity
Metal binding1941Manganese 2 By similarity
Metal binding1951Manganese 1; via carbonyl oxygen By similarity
Metal binding3561Manganese 2 By similarity
Metal binding4001Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVR7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 67626542F32B2FD0

FASTA45049,165
        10         20         30         40         50         60 
MASGAPQNSS QMACDGEIPG FLDTLLQDFP APLSLESPLP WKVPGTVLGQ EEVEAELTEL 

        70         80         90        100        110        120 
AMGFLGSRNA PPAVAAAVTH EAISQLLQTD LSEFKRLPEQ EEEEEEEEER VLTTLLDAKG 

       130        140        150        160        170        180 
LSRSFFNCLW EVCSQWQKRV PLTAQAPQRK WLVSIHAIRN TRRKMEDRHV SLPAFNHLFG 

       190        200        210        220        230        240 
LSDSVHRAYF AVFDGHGGVD AARYASVHVH TNASHQPELL TDPAAALKEA FRHTDQMFLQ 

       250        260        270        280        290        300 
KAKRERLQSG TTGVCALITG AALHVAWLGD SQVILVQQGQ VVKLMEPHKP ERQDEKSRIE 

       310        320        330        340        350        360 
ALGGFVSLMD CWRVNGTLAV SRAIGDVFQK PYVSGEADAA SRELTGLEDY LLLACDGFFD 

       370        380        390        400        410        420 
VVPHHEIPGL VHGHLLRQKG SGMHVAEELV AVARDRGSHD NITVMVVFLR DPLELLEGGG 

       430        440        450 
QGAGGAQADV GSQDLSTGLS ELEINTSQRS 

« Hide

References

[1]"Molecular cloning of Ca2+/Calmodulin-dependent protein kinase phosphatase."
Kitani T., Ishida A., Okuno S., Takeuchi M., Kameshita I., Fujisawa H.
J. Biochem. 125:1022-1028(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023634 mRNA. Translation: BAA82477.1.
RefSeqNP_786931.1. NM_175755.2.
XP_006248736.1. XM_006248674.1.
XP_006248737.1. XM_006248675.1.
UniGeneRn.91922.

3D structure databases

ProteinModelPortalQ9WVR7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid252383. 1 interaction.
IntActQ9WVR7. 1 interaction.
MINTMINT-4621280.

PTM databases

PhosphoSiteQ9WVR7.

Proteomic databases

PaxDbQ9WVR7.
PRIDEQ9WVR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002530; ENSRNOP00000002530; ENSRNOG00000037909.
GeneID287931.
KEGGrno:287931.

Organism-specific databases

CTD9647.
RGD631363. Ppm1f.

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00740000114971.
HOGENOMHOG000232094.
HOVERGENHBG053656.
InParanoidQ9WVR7.
KOK17502.
OMAGDVFQKP.
OrthoDBEOG7D2FDH.
PhylomeDBQ9WVR7.
TreeFamTF317617.

Gene expression databases

GenevestigatorQ9WVR7.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio627246.
PROQ9WVR7.

Entry information

Entry namePPM1F_RAT
AccessionPrimary (citable) accession number: Q9WVR7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families