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Q8BHN0 (PPM1L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1L

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 1-like
Protein phosphatase 2C isoform epsilon
Short name=PP2C-epsilon
Gene names
Name:Ppm1l
Synonyms:Kiaa4175
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6. Ref.1

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

Interacts with MAP3K7/TAK1 and MAP3K5. Ref.1 Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Expressed in brain, heart, testis, liver, lung and skeletal muscle. Ref.1

Disruption phenotype

Mice exhibit increased fat mass and higher plasma glucose levels compared to wild type mice. Male mice also exhibit a decrease in free fatty acids and higher blood pressure. Ref.7

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Sequence caution

The sequence AAO43055.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACBD3Q9H3P73EBI-7970002,EBI-1791792From a different organism.
MARK3P274483EBI-7970002,EBI-707595From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BHN0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BHN0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-105: Missing.
     106-133: EDRFEVLTDLANKTHPSIFGIFDGHGGE → MPTEQPEVPSQSLEAVEKGSLSSEDAGL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Protein phosphatase 1L
PRO_0000057755

Regions

Topological domain1 – 2525Extracellular Potential
Transmembrane26 – 4217Helical; Potential
Topological domain43 – 360318Cytoplasmic Potential
Domain91 – 344254PP2C-like

Sites

Metal binding1281Manganese 1 By similarity
Metal binding1281Manganese 2 By similarity
Metal binding1291Manganese 1; via carbonyl oxygen By similarity
Metal binding3021Manganese 2 By similarity
Metal binding3421Manganese 2 By similarity

Natural variations

Alternative sequence1 – 105105Missing in isoform 2.
VSP_016928
Alternative sequence106 – 13328EDRFE…GHGGE → MPTEQPEVPSQSLEAVEKGS LSSEDAGL in isoform 2.
VSP_016929

Experimental info

Mutagenesis1301H → L: Abolishes phosphatase activity. Ref.1
Mutagenesis2391R → G: Slightly abolishes phosphatase activity. Ref.1
Mutagenesis2411R → G: Abolishes phosphatase activity. Ref.1
Mutagenesis2651R → A: Abolishes phosphatase activity. Ref.1
Mutagenesis3021D → A: Abolishes phosphatase activity, prevents MAP3K7/TAK1 phosphorylation in vitro, does not abolish interaction with MAP3K7/TAK1, found in a complex with MAP3K7/TAK1, MAP2K4 or MAP2K6 and enhances the association between MAP3K7/TAK1, MAP2K4 or MAP2K6. Ref.1
Sequence conflict51T → I Ref.1
Sequence conflict511S → Y in BAC27913. Ref.2
Sequence conflict891K → E in AAO43055. Ref.1
Sequence conflict1981A → P in AAD17235. Ref.5
Sequence conflict2361L → P in AAD17235. Ref.5
Sequence conflict3321V → I in BAE28196. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 026CAC7687E5EA1E

FASTA36041,049
        10         20         30         40         50         60 
MIEDTMTLLS LLGRIMRYFL LRPETLFLLC ISLALWSYFF HTDEVKTIVK SSRDAVKMVK 

        70         80         90        100        110        120 
GKVAEIMQND RLGGLDVLEA EFSKTWEFKS HNVAVYSIQG RRDHMEDRFE VLTDLANKTH 

       130        140        150        160        170        180 
PSIFGIFDGH GGETAAEYVK SRLPEALKQH LQDYEKDKEN SVLTYQTILE QQILSIDREM 

       190        200        210        220        230        240 
LEKLTVSYDE AGTTCLIALL SDKDLTVANV GDSRGVLCDK DGNAIPLSHD HKPYQLKERK 

       250        260        270        280        290        300 
RIKRAGGFIS FNGSWRVQGI LAMSRSLGDY PLKNLNVVIP DPDILTFDLD KLQPEFMILA 

       310        320        330        340        350        360 
SDGLWDAFSN EEAVRFIKER LDEPHFGAKS IVLQSFYRGC PDNITVMVVK FRNSSKTEEH 

« Hide

Isoform 2 [UniParc].

Checksum: 0D09778B248E52CC
Show »

FASTA25528,649

References

« Hide 'large scale' references
[1]"Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon)."
Li M.G., Katsura K., Nomiyama H., Komaki K., Ninomiya-Tsuji J., Matsumoto K., Kobayashi T., Tamura S.
J. Biol. Chem. 278:12013-12021(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MAP3K7, MUTAGENESIS OF HIS-130; ARG-239; ARG-241; ARG-265 AND ASP-302, 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Cerebellum, Corpora quadrigemina, Embryonic head, Melanocyte and Olfactory bulb.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[4]"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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Embryonic brain.
[5]"Isolation of PP2C sequences using degenerate-oligo PCR."
Stothard P.M., Pilgrim D.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 133-299 (ISOFORMS 1/2).
Tissue: Lung.
[6]"Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase 2Cepsilon."
Saito J., Toriumi S., Awano K., Ichijo H., Sasaki K., Kobayashi T., Tamura S.
Biochem. J. 405:591-596(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K5.
[7]"Variations in DNA elucidate molecular networks that cause disease."
Chen Y., Zhu J., Lum P.Y., Yang X., Pinto S., MacNeil D.J., Zhang C., Lamb J., Edwards S., Sieberts S.K., Leonardson A., Castellini L.W., Wang S., Champy M.-F., Zhang B., Emilsson V., Doss S., Ghazalpour A. expand/collapse author list , Horvath S., Drake T.A., Lusis A.J., Schadt E.E.
Nature 452:429-435(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY184801 mRNA. Translation: AAO43055.1. Different initiation.
AK028275 mRNA. Translation: BAC25853.1.
AK032529 mRNA. Translation: BAC27913.1.
AK035912 mRNA. Translation: BAC29241.1.
AK045724 mRNA. Translation: BAC32472.1.
AK131646 mRNA. Translation: BAE20738.1.
AK147876 mRNA. Translation: BAE28196.1.
AK220523 mRNA. Translation: BAD90308.1.
BC096031 mRNA. Translation: AAH96031.1.
AF117832 mRNA. Translation: AAD17235.1.
CCDSCCDS17405.1. [Q8BHN0-1]
RefSeqNP_848841.2. NM_178726.3. [Q8BHN0-1]
UniGeneMm.40577.

3D structure databases

ProteinModelPortalQ8BHN0.
SMRQ8BHN0. Positions 97-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BHN0. 5 interactions.

PTM databases

PhosphoSiteQ8BHN0.

Proteomic databases

PaxDbQ8BHN0.
PRIDEQ8BHN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029355; ENSMUSP00000029355; ENSMUSG00000027784. [Q8BHN0-1]
GeneID242083.
KEGGmmu:242083.
UCSCuc008pmg.1. mouse. [Q8BHN0-1]
uc008pmh.1. mouse. [Q8BHN0-2]

Organism-specific databases

CTD151742.
MGIMGI:2139740. Ppm1l.
RougeSearch...

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00740000114971.
HOGENOMHOG000233896.
HOVERGENHBG079483.
InParanoidQ8BHN0.
KOK17506.
OMATERIVAC.
OrthoDBEOG74J98W.
PhylomeDBQ8BHN0.
TreeFamTF332888.

Gene expression databases

ArrayExpressQ8BHN0.
BgeeQ8BHN0.
CleanExMM_PPM1L.
GenevestigatorQ8BHN0.

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

NextBio385221.
PROQ8BHN0.
SOURCESearch...

Entry information

Entry namePPM1L_MOUSE
AccessionPrimary (citable) accession number: Q8BHN0
Secondary accession number(s): Q3UGL2 expand/collapse secondary AC list , Q810H0, Q8C021, Q8C1D5, Q9Z0T1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
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 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