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Q8CGA0

- PPM1F_MOUSE

UniProt

Q8CGA0 - PPM1F_MOUSE

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Protein

Protein phosphatase 1F

Gene
Ppm1f
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Binds 2 magnesium or manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi195 – 1951Manganese 1 By similarity
Metal bindingi195 – 1951Manganese 2 By similarity
Metal bindingi196 – 1961Manganese 1; via carbonyl oxygen By similarity
Metal bindingi357 – 3571Manganese 2 By similarity
Metal bindingi401 – 4011Manganese 2 By similarity

GO - Molecular functioni

  1. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. 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: Ensembl
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.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the PP2C family.

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

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MASGAAQNSS QMACDSEIPG FLDAFLQDFP APLSLESPLP WKVPGTVLSQ    50
EEVEAELIEL ALGFLGSRNA PPSFAVAVTH EAISQLLQTD LSEFKRLPEQ 100
EEEEEEEEEE KALVTLLDAK GLARSFFNCL WKVCSQWQKQ VPLTAQAPQW 150
QWLVSIHAIR NTRRKMEDRH VSLPAFNHLF GLSDSVHRAY FAVFDGHGGV 200
DAARYASVHV HTNASHQPEL RTNPAAALKE AFRLTDEMFL QKAKRERLQS 250
GTTGVCALIA GAALHVAWLG DSQVILVQQG RVVKLMEPHK PERQDEKARI 300
EALGGFVSLM DCWRVNGTLA VSRAIGDVFQ KPYVSGEADA ASRELTGSED 350
YLLLACDGFF DVVPHHEVTG LVHGHLLRHK GNGMRIAEEL VAVARDRGSH 400
DNITVMVVFL REPLELLEGG VQGTGDAQAD VGSQDLSTGL SELEISNTSQ 450
RS 452
Length:452
Mass (Da):49,611
Last modified:March 1, 2003 - v1
Checksum:i7C8ED2E597F9D1B8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK154192 mRNA. Translation: BAE32429.1 .
AK164964 mRNA. Translation: BAE37981.1 .
BC042570 mRNA. Translation: AAH42570.1 .
CCDSi CCDS27991.1.
RefSeqi NP_789803.1. NM_176833.4.
XP_006522570.1. XM_006522507.1.
UniGenei Mm.230296.

3D structure databases

ProteinModelPortali Q8CGA0.
SMRi Q8CGA0. Positions 114-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212948. 1 interaction.
IntActi Q8CGA0. 3 interactions.
MINTi MINT-4115705.
STRINGi 10090.ENSMUSP00000027373.

PTM databases

PhosphoSitei Q8CGA0.

Proteomic databases

MaxQBi Q8CGA0.
PaxDbi Q8CGA0.
PRIDEi Q8CGA0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027373 ; ENSMUSP00000027373 ; ENSMUSG00000026181 .
GeneIDi 68606.
KEGGi mmu:68606.
UCSCi uc007yjo.2. mouse.

Organism-specific databases

CTDi 9647.
MGIi MGI:1918464. Ppm1f.

Phylogenomic databases

eggNOGi COG0631.
GeneTreei ENSGT00740000114971.
HOGENOMi HOG000232094.
HOVERGENi HBG053656.
InParanoidi Q8CGA0.
KOi K17502.
OMAi GDVFQKP.
OrthoDBi EOG7D2FDH.
PhylomeDBi Q8CGA0.
TreeFami TF317617.

Miscellaneous databases

ChiTaRSi PPM1F. mouse.
NextBioi 327542.
PROi Q8CGA0.
SOURCEi Search...

Gene expression databases

Bgeei Q8CGA0.
CleanExi MM_PPM1F.
Genevestigatori Q8CGA0.

Family and domain databases

Gene3Di 3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81606. SSF81606. 1 hit.
PROSITEi PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 101 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

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