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Q8BXN7 (PPM1K_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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 1K, mitochondrial

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 2C isoform kappa
Short name=PP2C-kappa
Gene names
Name:Ppm1k
Synonyms:Pp2cm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development. Ref.1

Catalytic activity

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

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subcellular location

Mitochondrion matrix Ref.1.

Tissue specificity

Highly expressed in the heart, kidney, brain and liver and to a lesser extent in testis, lung, spleen and adipose tissue. Very low amount in muscle (at protein level). Also expressed in the thymus (at protein level) and the diaphragm. Significantly reduced in hypertrophied hearts. Ref.1 Ref.4

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion
Chain30 – 372343Protein phosphatase 1K, mitochondrial
PRO_0000278209

Regions

Domain93 – 346254PP2C-like

Sites

Metal binding1271Magnesium By similarity
Metal binding1281Magnesium; via carbonyl oxygen By similarity
Metal binding3371Magnesium By similarity

Amino acid modifications

Modified residue2481Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8BXN7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3749BEB94F211E7A

FASTA37240,918
        10         20         30         40         50         60 
MLSAAFITLL RSGGNQVKKR VLLSSILLQD HRQATPACYF STSEARCSRF DPDGSGQPAT 

        70         80         90        100        110        120 
WDNFGIWDNR IDEPILLPPS IKYGKPIPKI SLENVGCASL IGKRKENEDR FGFAQLTEEV 

       130        140        150        160        170        180 
LYFAVYDGHG GPAAADFCHT HMEKCVMDLL PREKDLETVL TLAFLEIDKA FASYAHLSAD 

       190        200        210        220        230        240 
ASLLTSGTTA TVALLRDGVE LVVASVGDSR ALLCRKGKPM KLTTDHTPER KDEKERIKKF 

       250        260        270        280        290        300 
GGFVAWNSLG QPHVNGRLAM TRSIGDLDLK ASGVIAEPET TRIKLYHADD SFLVLTTDGI 

       310        320        330        340        350        360 
NFMVNSQEIC DFVNQCHDPK EAAHSVTEQA IQYGTEDNST AVVVPFGAWG KYKNSEITFS 

       370 
FSRSFASSGR WA 

« Hide

References

« Hide 'large scale' references
[1]"A novel mitochondrial matrix serine/threonine protein phosphatase regulates the mitochondria permeability transition pore and is essential for cellular survival and development."
Lu G., Ren S., Korge P., Choi J., Dong Y., Weiss J., Koehler C., Chen J.-N., Wang Y.
Genes Dev. 21:784-796(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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].
Strain: C57BL/6J.
Tissue: Retina.
[3]"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: C57BL/6.
Tissue: Head.
[4]"Identification of a novel PP2C-type mitochondrial phosphatase."
Joshi M.A., Jeoung N.H., Popov K.M., Harris R.A.
Biochem. Biophys. Res. Commun. 356:38-44(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK044610 mRNA. Translation: BAC32001.1.
BC092238 mRNA. Translation: AAH92238.1.
RefSeqNP_780732.1. NM_175523.4.
UniGeneMm.396893.
Mm.491373.

3D structure databases

ProteinModelPortalQ8BXN7.
SMRQ8BXN7. Positions 90-349.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BXN7.

Proteomic databases

PaxDbQ8BXN7.
PRIDEQ8BXN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042766; ENSMUSP00000041395; ENSMUSG00000037826.
GeneID243382.
KEGGmmu:243382.
UCSCuc009cch.1. mouse.

Organism-specific databases

CTD152926.
MGIMGI:2442111. Ppm1k.

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00740000114971.
HOGENOMHOG000059620.
HOVERGENHBG096199.
InParanoidQ8BXN7.
KOK17505.
OMADTFGIWD.
OrthoDBEOG7992QN.
PhylomeDBQ8BXN7.
TreeFamTF354344.

Gene expression databases

ArrayExpressQ8BXN7.
BgeeQ8BXN7.
CleanExMM_PPM1K.
GenevestigatorQ8BXN7.

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

NextBio385765.
PROQ8BXN7.
SOURCESearch...

Entry information

Entry namePPM1K_MOUSE
AccessionPrimary (citable) accession number: Q8BXN7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 92 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