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Protein

Protein phosphatase 1F

Gene

Ppm1f

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Manganese 1By similarity
Metal bindingi194 – 1941Manganese 2By similarity
Metal bindingi195 – 1951Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi356 – 3561Manganese 2By similarity
Metal bindingi400 – 4001Manganese 2By similarity

GO - Molecular functioni

  1. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoprotein phosphatase activity Source: RGD
  4. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to drug Source: UniProtKB
  2. histone dephosphorylation Source: RGD
  3. intrinsic apoptotic signaling pathway Source: UniProtKB
  4. negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
  5. negative regulation of protein kinase activity Source: UniProtKB
  6. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. peptidyl-threonine dephosphorylation Source: UniProtKB
  9. positive regulation of cell-substrate adhesion Source: UniProtKB
  10. positive regulation of chemotaxis Source: UniProtKB
  11. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  12. positive regulation of epithelial cell migration Source: UniProtKB
  13. positive regulation of focal adhesion assembly Source: UniProtKB
  14. positive regulation of gene expression Source: UniProtKB
  15. positive regulation of growth Source: UniProtKB
  16. positive regulation of stress fiber assembly Source: Ensembl
  17. protein dephosphorylation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ppm1f
Synonyms:Popx2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi631363. Ppm1f.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. perinuclear region of cytoplasm Source: UniProtKB
  3. protein complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Protein phosphatase 1FPRO_0000057760Add
BLAST

Proteomic databases

PaxDbiQ9WVR7.
PRIDEiQ9WVR7.

PTM databases

PhosphoSiteiQ9WVR7.

Expressioni

Gene expression databases

ExpressionAtlasiQ9WVR7. baseline.
GenevestigatoriQ9WVR7.

Interactioni

Subunit structurei

Associates with FEM1B.By similarity

Protein-protein interaction databases

BioGridi252383. 1 interaction.
IntActiQ9WVR7. 1 interaction.
MINTiMINT-4621280.

Structurei

3D structure databases

ProteinModelPortaliQ9WVR7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 409258PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi99 – 10911Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000232094.
HOVERGENiHBG053656.
InParanoidiQ9WVR7.
KOiK17502.
OMAiGDVFQKP.
OrthoDBiEOG7D2FDH.
PhylomeDBiQ9WVR7.
TreeFamiTF317617.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WVR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGAPQNSS QMACDGEIPG FLDTLLQDFP APLSLESPLP WKVPGTVLGQ
60 70 80 90 100
EEVEAELTEL AMGFLGSRNA PPAVAAAVTH EAISQLLQTD LSEFKRLPEQ
110 120 130 140 150
EEEEEEEEER VLTTLLDAKG LSRSFFNCLW EVCSQWQKRV PLTAQAPQRK
160 170 180 190 200
WLVSIHAIRN TRRKMEDRHV SLPAFNHLFG LSDSVHRAYF AVFDGHGGVD
210 220 230 240 250
AARYASVHVH TNASHQPELL TDPAAALKEA FRHTDQMFLQ KAKRERLQSG
260 270 280 290 300
TTGVCALITG AALHVAWLGD SQVILVQQGQ VVKLMEPHKP ERQDEKSRIE
310 320 330 340 350
ALGGFVSLMD CWRVNGTLAV SRAIGDVFQK PYVSGEADAA SRELTGLEDY
360 370 380 390 400
LLLACDGFFD VVPHHEIPGL VHGHLLRQKG SGMHVAEELV AVARDRGSHD
410 420 430 440 450
NITVMVVFLR DPLELLEGGG QGAGGAQADV GSQDLSTGLS ELEINTSQRS
Length:450
Mass (Da):49,165
Last modified:November 1, 1999 - v1
Checksum:i67626542F32B2FD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023634 mRNA. Translation: BAA82477.1.
RefSeqiNP_786931.1. NM_175755.2.
XP_006248736.1. XM_006248674.1.
UniGeneiRn.91922.

Genome annotation databases

EnsembliENSRNOT00000002530; ENSRNOP00000002530; ENSRNOG00000037909.
GeneIDi287931.
KEGGirno:287931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023634 mRNA. Translation: BAA82477.1.
RefSeqiNP_786931.1. NM_175755.2.
XP_006248736.1. XM_006248674.1.
UniGeneiRn.91922.

3D structure databases

ProteinModelPortaliQ9WVR7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi252383. 1 interaction.
IntActiQ9WVR7. 1 interaction.
MINTiMINT-4621280.

PTM databases

PhosphoSiteiQ9WVR7.

Proteomic databases

PaxDbiQ9WVR7.
PRIDEiQ9WVR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002530; ENSRNOP00000002530; ENSRNOG00000037909.
GeneIDi287931.
KEGGirno:287931.

Organism-specific databases

CTDi9647.
RGDi631363. Ppm1f.

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000232094.
HOVERGENiHBG053656.
InParanoidiQ9WVR7.
KOiK17502.
OMAiGDVFQKP.
OrthoDBiEOG7D2FDH.
PhylomeDBiQ9WVR7.
TreeFamiTF317617.

Miscellaneous databases

NextBioi627246.
PROiQ9WVR7.

Gene expression databases

ExpressionAtlasiQ9WVR7. baseline.
GenevestigatoriQ9WVR7.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiPPM1F_RAT
AccessioniPrimary (citable) accession number: Q9WVR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1999
Last modified: April 1, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.