Q9DCL8 (IPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase inhibitor 2
Short name=IPP-2

Gene names

Name:

Ppp1r2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibitor of protein-phosphatase 1 By similarity.
Subunit structure	Heterodimer with PP1 By similarity.
Post-translational modification	Phosphorylation on Ser-45 by ATM activates PP1 by dissociating the PP1-PPP1R2 complex By similarity. Phosphorylation on Thr-74 by GSK3 activates PP1 by dissociating the PP1-PPP1R2 complex By similarity.
Sequence similarities	Belongs to the protein phosphatase inhibitor 2 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Molecular function	Protein phosphatase inhibitor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of phosphoprotein phosphatase activity Inferred from electronic annotation. Source: InterPro regulation of signal transduction Inferred from electronic annotation. Source: InterPro
Molecular function	protein phosphatase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 206

205

Protein phosphatase inhibitor 2

PRO_0000071482

Regions

Region

12 – 17

6

Required for binding PPP1CC

Region

44 – 56

13

Required for binding the 'RVXF' binding groove of PPP1CC

Region

148 – 151

4

Required for binding PPP1CC catalytic center, displacing metal ions and inhibition of PPP1CC catyltic activity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

20

1

Phosphoserine By similarity

Modified residue

45

1

Phosphoserine; by ATM By similarity

Modified residue

74

1

Phosphothreonine; by GSK3 By similarity

Modified residue

88

1

Phosphoserine By similarity

Modified residue

122

1

Phosphoserine Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Modified residue

123

1

Phosphoserine Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Experimental info

Sequence conflict

193

1

S → C in BAC26028. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

206

Helix Strand Turn

Details...

Helix

50 – 55

6

Helix

134 – 148

15

Helix

151 – 154

4

Helix

155 – 166

12

Sequences

	Sequence		Length	Mass (Da)
	Q9DCL8 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0AE35744A51A523D	FASTA	206	23,119
	10 20 30 40 50 60 MAASTASHRP IKGILKNKTS AASPPVVPSA EQPRPIVEEE LSKKSQKWDE MNILATYHPA 70 80 90 100 110 120 DKDYGLMKID EPNTPYHNMI GDDEDAYSDS EGNEVMTPDI LAKKLAAAEG SEPKYRTREQ 130 140 150 160 170 180 ESSGEEDNDL SPEEREKKRQ FEMKRKLHYN EGLNIKLARQ LISKDLHDDD EDEEMAETAD 190 200 GDSMNVEESS QGSTTSDHLQ HKSQSS

References

	« Hide 'large scale' referencesShow 'large scale' 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. , 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor and Olfactory epithelium.
[3]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, MASS SPECTROMETRY. 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: 17622165] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
[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: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, MASS SPECTROMETRY. Tissue: Melanoma.
[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: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[8]	"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: 17636256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH R.NORVEGICUS PPP1CC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00322095.

RefSeq

NP_080076.1. NM_025800.3.

UniGene

Mm.291593.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O8A	X-ray	2.61	I/J	1-206	[»]
2O8G	X-ray	2.50	I/J	1-206	[»]

ProteinModelPortal

Q9DCL8.

SMR

Q9DCL8. Positions 130-169.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9DCL8. 1 interaction.

STRING

Q9DCL8.

PTM databases

PhosphoSite

Q9DCL8.

Proteomic databases

PRIDE

Q9DCL8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000060188; ENSMUSP00000060118; ENSMUSG00000047714.

GeneID

66849.

KEGG

mmu:66849.

UCSC

uc007yxd.1. mouse.

Organism-specific databases

CTD

5504.

MGI

MGI:1914099. Ppp1r2.

Phylogenomic databases

eggNOG

roNOG15540.

GeneTree

ENSGT00390000004757.

HOVERGEN

HBG006170.

InParanoid

Q9DCL8.

OMA

SEPKYRV.

OrthoDB

EOG4PNXJC.

PhylomeDB

Q9DCL8.

Gene expression databases

ArrayExpress

Q9DCL8.

Bgee

Q9DCL8.

Genevestigator

Q9DCL8.

GermOnline

ENSMUSG00000047714. Mus musculus.

Family and domain databases

InterPro

IPR007062. PPI-2.
[Graphical view]

Pfam

PF04979. IPP-2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

322815.

SOURCE

Search...

Entry information

Entry name

IPP2_MOUSE

Accession

Primary (citable) accession number: Q9DCL8
Secondary accession number(s): Q3UD25, Q8C1A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	September 21, 2011
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program