Skip Header

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

Protein phosphatase 1F

Gene

Ppm1f

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

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 bindingi195 – 1951Manganese 1By similarity
Metal bindingi195 – 1951Manganese 2By similarity
Metal bindingi196 – 1961Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi357 – 3571Manganese 2By similarity
Metal bindingi401 – 4011Manganese 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to drug Source: UniProtKB
  2. histone dephosphorylation Source: Ensembl
  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: MGI
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
Gene namesi
Name:Ppm1f
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1918464. Ppm1f.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Protein phosphatase 1FPRO_0000057759Add
BLAST

Proteomic databases

MaxQBiQ8CGA0.
PaxDbiQ8CGA0.
PRIDEiQ8CGA0.

PTM databases

PhosphoSiteiQ8CGA0.

Expressioni

Gene expression databases

BgeeiQ8CGA0.
CleanExiMM_PPM1F.
GenevestigatoriQ8CGA0.

Interactioni

Subunit structurei

Associates with FEM1B.By similarity

Protein-protein interaction databases

BioGridi212948. 1 interaction.
IntActiQ8CGA0. 3 interactions.
MINTiMINT-4115705.
STRINGi10090.ENSMUSP00000027373.

Structurei

3D structure databases

ProteinModelPortaliQ8CGA0.
SMRiQ8CGA0. Positions 114-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi99 – 11012Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000232094.
HOVERGENiHBG053656.
InParanoidiQ8CGA0.
KOiK17502.
OMAiGDVFQKP.
OrthoDBiEOG7D2FDH.
PhylomeDBiQ8CGA0.
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. PP2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CGA0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASGAAQNSS QMACDSEIPG FLDAFLQDFP APLSLESPLP WKVPGTVLSQ
60 70 80 90 100
EEVEAELIEL ALGFLGSRNA PPSFAVAVTH EAISQLLQTD LSEFKRLPEQ
110 120 130 140 150
EEEEEEEEEE KALVTLLDAK GLARSFFNCL WKVCSQWQKQ VPLTAQAPQW
160 170 180 190 200
QWLVSIHAIR NTRRKMEDRH VSLPAFNHLF GLSDSVHRAY FAVFDGHGGV
210 220 230 240 250
DAARYASVHV HTNASHQPEL RTNPAAALKE AFRLTDEMFL QKAKRERLQS
260 270 280 290 300
GTTGVCALIA GAALHVAWLG DSQVILVQQG RVVKLMEPHK PERQDEKARI
310 320 330 340 350
EALGGFVSLM DCWRVNGTLA VSRAIGDVFQ KPYVSGEADA ASRELTGSED
360 370 380 390 400
YLLLACDGFF DVVPHHEVTG LVHGHLLRHK GNGMRIAEEL VAVARDRGSH
410 420 430 440 450
DNITVMVVFL REPLELLEGG VQGTGDAQAD VGSQDLSTGL SELEISNTSQ

RS
Length:452
Mass (Da):49,611
Last modified:March 1, 2003 - v1
Checksum:i7C8ED2E597F9D1B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154192 mRNA. Translation: BAE32429.1.
AK164964 mRNA. Translation: BAE37981.1.
BC042570 mRNA. Translation: AAH42570.1.
CCDSiCCDS27991.1.
RefSeqiNP_789803.1. NM_176833.4.
XP_006522570.1. XM_006522507.1.
UniGeneiMm.230296.

Genome annotation databases

EnsembliENSMUST00000027373; ENSMUSP00000027373; ENSMUSG00000026181.
GeneIDi68606.
KEGGimmu:68606.
UCSCiuc007yjo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154192 mRNA. Translation: BAE32429.1.
AK164964 mRNA. Translation: BAE37981.1.
BC042570 mRNA. Translation: AAH42570.1.
CCDSiCCDS27991.1.
RefSeqiNP_789803.1. NM_176833.4.
XP_006522570.1. XM_006522507.1.
UniGeneiMm.230296.

3D structure databases

ProteinModelPortaliQ8CGA0.
SMRiQ8CGA0. Positions 114-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212948. 1 interaction.
IntActiQ8CGA0. 3 interactions.
MINTiMINT-4115705.
STRINGi10090.ENSMUSP00000027373.

PTM databases

PhosphoSiteiQ8CGA0.

Proteomic databases

MaxQBiQ8CGA0.
PaxDbiQ8CGA0.
PRIDEiQ8CGA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027373; ENSMUSP00000027373; ENSMUSG00000026181.
GeneIDi68606.
KEGGimmu:68606.
UCSCiuc007yjo.2. mouse.

Organism-specific databases

CTDi9647.
MGIiMGI:1918464. Ppm1f.

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000232094.
HOVERGENiHBG053656.
InParanoidiQ8CGA0.
KOiK17502.
OMAiGDVFQKP.
OrthoDBiEOG7D2FDH.
PhylomeDBiQ8CGA0.
TreeFamiTF317617.

Miscellaneous databases

ChiTaRSiPpm1f. mouse.
NextBioi327542.
PROiQ8CGA0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CGA0.
CleanExiMM_PPM1F.
GenevestigatoriQ8CGA0.

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. PP2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.

Entry informationi

Entry nameiPPM1F_MOUSE
AccessioniPrimary (citable) accession number: Q8CGA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2003
Last modified: February 4, 2015
This is version 105 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.