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Q8CGA0 (PPM1F_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Ppm1f
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length452 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 By similarity.

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 electronic annotation. Source: Ensembl

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 sequence or structural similarity. 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

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

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

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 – 452452Protein phosphatase 1F
PRO_0000057759

Regions

Compositional bias99 – 11012Poly-Glu

Sites

Metal binding1951Manganese 1 By similarity
Metal binding1951Manganese 2 By similarity
Metal binding1961Manganese 1; via carbonyl oxygen By similarity
Metal binding3571Manganese 2 By similarity
Metal binding4011Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CGA0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 7C8ED2E597F9D1B8

FASTA45249,611
        10         20         30         40         50         60 
MASGAAQNSS QMACDSEIPG FLDAFLQDFP APLSLESPLP WKVPGTVLSQ EEVEAELIEL 

        70         80         90        100        110        120 
ALGFLGSRNA PPSFAVAVTH EAISQLLQTD LSEFKRLPEQ EEEEEEEEEE KALVTLLDAK 

       130        140        150        160        170        180 
GLARSFFNCL WKVCSQWQKQ VPLTAQAPQW QWLVSIHAIR NTRRKMEDRH VSLPAFNHLF 

       190        200        210        220        230        240 
GLSDSVHRAY FAVFDGHGGV DAARYASVHV HTNASHQPEL RTNPAAALKE AFRLTDEMFL 

       250        260        270        280        290        300 
QKAKRERLQS GTTGVCALIA GAALHVAWLG DSQVILVQQG RVVKLMEPHK PERQDEKARI 

       310        320        330        340        350        360 
EALGGFVSLM DCWRVNGTLA VSRAIGDVFQ KPYVSGEADA ASRELTGSED YLLLACDGFF 

       370        380        390        400        410        420 
DVVPHHEVTG LVHGHLLRHK GNGMRIAEEL VAVARDRGSH DNITVMVVFL REPLELLEGG 

       430        440        450 
VQGTGDAQAD VGSQDLSTGL SELEISNTSQ RS 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK154192 mRNA. Translation: BAE32429.1.
AK164964 mRNA. Translation: BAE37981.1.
BC042570 mRNA. Translation: AAH42570.1.
RefSeqNP_789803.1. NM_176833.4.
XP_006522570.1. XM_006522507.1.
UniGeneMm.230296.

3D structure databases

ProteinModelPortalQ8CGA0.
SMRQ8CGA0. Positions 114-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CGA0. 3 interactions.
MINTMINT-4115705.
STRING10090.ENSMUSP00000027373.

PTM databases

PhosphoSiteQ8CGA0.

Proteomic databases

PaxDbQ8CGA0.
PRIDEQ8CGA0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027373; ENSMUSP00000027373; ENSMUSG00000026181.
GeneID68606.
KEGGmmu:68606.
UCSCuc007yjo.2. mouse.

Organism-specific databases

CTD9647.
MGIMGI:1918464. Ppm1f.

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00740000114971.
HOGENOMHOG000232094.
HOVERGENHBG053656.
InParanoidQ8CGA0.
KOK17502.
OMAGDVFQKP.
OrthoDBEOG7D2FDH.
PhylomeDBQ8CGA0.
TreeFamTF317617.

Gene expression databases

BgeeQ8CGA0.
CleanExMM_PPM1F.
GenevestigatorQ8CGA0.

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

ChiTaRSPPM1F. mouse.
NextBio327542.
PROQ8CGA0.
SOURCESearch...

Entry information

Entry namePPM1F_MOUSE
AccessionPrimary (citable) accession number: Q8CGA0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 98 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot