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Protein

Protein phosphatase inhibitor 2

Gene

Ppp1r2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor of protein-phosphatase 1.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase inhibitor 2
Short name:
IPP-2
Gene namesi
Name:Ppp1r2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1914099. Ppp1r2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 206205Protein phosphatase inhibitor 2PRO_0000071482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei45 – 451Phosphoserine; by ATMBy similarity
Modified residuei74 – 741PhosphothreonineCombined sources
Modified residuei88 – 881PhosphoserineCombined sources
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei97 – 971PhosphothreonineCombined sources
Modified residuei117 – 1171PhosphothreonineCombined sources
Modified residuei122 – 1221PhosphoserineCombined sources
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei131 – 1311PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation on Ser-45 by ATM activates PP1 by dissociating the PP1-PPP1R2 complex. Phosphorylation on Thr-74 by GSK3 activates PP1 by dissociating the PP1-PPP1R2 complex.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DCL8.
MaxQBiQ9DCL8.
PaxDbiQ9DCL8.
PRIDEiQ9DCL8.

PTM databases

iPTMnetiQ9DCL8.
PhosphoSiteiQ9DCL8.

Expressioni

Gene expression databases

BgeeiQ9DCL8.
ExpressionAtlasiQ9DCL8. baseline and differential.
GenevisibleiQ9DCL8. MM.

Interactioni

Subunit structurei

Heterodimer with PP1.By similarity

Protein-protein interaction databases

IntActiQ9DCL8. 1 interaction.
STRINGi10090.ENSMUSP00000060118.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 556Combined sources
Helixi132 – 14817Combined sources
Helixi151 – 1544Combined sources
Helixi155 – 16612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8AX-ray2.61I/J1-206[»]
2O8GX-ray2.50I/J1-206[»]
ProteinModelPortaliQ9DCL8.
SMRiQ9DCL8. Positions 130-169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DCL8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 176Required for binding PPP1CC
Regioni44 – 5613Required for binding the 'RVXF' binding groove of PPP1CCAdd
BLAST
Regioni148 – 1514Required for binding PPP1CC catalytic center, displacing metal ions and inhibition of PPP1CC catyltic activity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4041. Eukaryota.
ENOG4111SYV. LUCA.
GeneTreeiENSGT00390000004757.
HOVERGENiHBG006170.
InParanoidiQ9DCL8.
KOiK16833.
OMAiMHYNEGR.
OrthoDBiEOG776SR7.
PhylomeDBiQ9DCL8.
TreeFamiTF105536.

Family and domain databases

InterProiIPR007062. PPI-2.
[Graphical view]
PfamiPF04979. IPP-2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DCL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTASHRP IKGILKNKTS AASPPVVPSA EQPRPIVEEE LSKKSQKWDE
60 70 80 90 100
MNILATYHPA DKDYGLMKID EPNTPYHNMI GDDEDAYSDS EGNEVMTPDI
110 120 130 140 150
LAKKLAAAEG SEPKYRTREQ ESSGEEDNDL SPEEREKKRQ FEMKRKLHYN
160 170 180 190 200
EGLNIKLARQ LISKDLHDDD EDEEMAETAD GDSMNVEESS QGSTTSDHLQ

HKSQSS
Length:206
Mass (Da):23,119
Last modified:January 23, 2007 - v3
Checksum:i0AE35744A51A523D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931S → C in BAC26028 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002671 mRNA. Translation: BAB22274.1.
AK028603 mRNA. Translation: BAC26028.1.
AK032462 mRNA. Translation: BAC27882.1.
AK053657 mRNA. Translation: BAC35465.1.
AK150281 mRNA. Translation: BAE29437.1.
BC069885 mRNA. Translation: AAH69885.1.
BC069886 mRNA. Translation: AAH69886.1.
CCDSiCCDS28104.1.
RefSeqiNP_080076.1. NM_025800.3.
UniGeneiMm.291593.
Mm.490810.

Genome annotation databases

EnsembliENSMUST00000060188; ENSMUSP00000060118; ENSMUSG00000047714.
GeneIDi66849.
KEGGimmu:66849.
UCSCiuc007yxd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002671 mRNA. Translation: BAB22274.1.
AK028603 mRNA. Translation: BAC26028.1.
AK032462 mRNA. Translation: BAC27882.1.
AK053657 mRNA. Translation: BAC35465.1.
AK150281 mRNA. Translation: BAE29437.1.
BC069885 mRNA. Translation: AAH69885.1.
BC069886 mRNA. Translation: AAH69886.1.
CCDSiCCDS28104.1.
RefSeqiNP_080076.1. NM_025800.3.
UniGeneiMm.291593.
Mm.490810.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8AX-ray2.61I/J1-206[»]
2O8GX-ray2.50I/J1-206[»]
ProteinModelPortaliQ9DCL8.
SMRiQ9DCL8. Positions 130-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DCL8. 1 interaction.
STRINGi10090.ENSMUSP00000060118.

PTM databases

iPTMnetiQ9DCL8.
PhosphoSiteiQ9DCL8.

Proteomic databases

EPDiQ9DCL8.
MaxQBiQ9DCL8.
PaxDbiQ9DCL8.
PRIDEiQ9DCL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060188; ENSMUSP00000060118; ENSMUSG00000047714.
GeneIDi66849.
KEGGimmu:66849.
UCSCiuc007yxd.1. mouse.

Organism-specific databases

CTDi5504.
MGIiMGI:1914099. Ppp1r2.

Phylogenomic databases

eggNOGiKOG4041. Eukaryota.
ENOG4111SYV. LUCA.
GeneTreeiENSGT00390000004757.
HOVERGENiHBG006170.
InParanoidiQ9DCL8.
KOiK16833.
OMAiMHYNEGR.
OrthoDBiEOG776SR7.
PhylomeDBiQ9DCL8.
TreeFamiTF105536.

Miscellaneous databases

EvolutionaryTraceiQ9DCL8.
PROiQ9DCL8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCL8.
ExpressionAtlasiQ9DCL8. baseline and differential.
GenevisibleiQ9DCL8. MM.

Family and domain databases

InterProiIPR007062. PPI-2.
[Graphical view]
PfamiPF04979. IPP-2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Eye, Kidney, Olfactory bulb and Skin.
  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: Mammary tumor and Olfactory epithelium.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-88; SER-90; THR-97; THR-117; SER-122; SER-123 AND SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Structural basis for regulation of protein phosphatase 1 by inhibitor-2."
    Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M., Dunker A.K., DePaoli-Roach A.A.
    J. Biol. Chem. 282:28874-28883(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH R.NORVEGICUS PPP1CC.

Entry informationi

Entry nameiIPP2_MOUSE
AccessioniPrimary (citable) accession number: Q9DCL8
Secondary accession number(s): Q3UD25, Q8C1A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.