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P41236 (IPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase inhibitor 2

Short name=IPP-2
Gene names
Name:PPP1R2
Synonyms:IPP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibitor of protein-phosphatase 1.

Subunit structure

Heterodimer with PP1. Ref.9

Post-translational modification

Phosphorylation on Thr-73 by GSK3 activates PP1 by dissociating the PP1-PPP1R2 complex By similarity. Phosphorylation on Ser-44 by ATM activates PP1 by dissociating the PP1-PPP1R2 complex.

Sequence similarities

Belongs to the protein phosphatase inhibitor 2 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 205204Protein phosphatase inhibitor 2
PRO_0000071481

Regions

Region12 – 176Required for binding PPP1CC By similarity
Region43 – 5513Required for binding PPP1CC By similarity
Region147 – 1504Required for binding PPP1CC catalytic center, displacing metal ions and inhibition of PPP1CC catyltic activity By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue441Phosphoserine; by ATM Ref.9
Modified residue731Phosphothreonine; by GSK3 By similarity
Modified residue871Phosphoserine Ref.10 Ref.11
Modified residue891Phosphothreonine Ref.10
Modified residue921Phosphothreonine Ref.8
Modified residue1211Phosphoserine Ref.13
Modified residue1221Phosphoserine Ref.13
Modified residue1271Phosphoserine Ref.13

Sequences

Sequence LengthMass (Da)Tools
P41236 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FFC005B07CD5ABFC

FASTA20523,015
        10         20         30         40         50         60 
MAASTASHRP IKGILKNKTS TTSSMVASAE QPRGNVDEEL SKKSQKWDEM NILATYHPAD 

        70         80         90        100        110        120 
KDYGLMKIDE PSTPYHSMMG DDEDACSDTE ATEAMAPDIL ARKLAAAEGL EPKYRIQEQE 

       130        140        150        160        170        180 
SSGEEDSDLS PEEREKKRQF EMKRKLHYNE GLNIKLARQL ISKDLHDDDE DEEMLETADG 

       190        200 
ESMNTEESNQ GSTPSDQQQN KLRSS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of human phosphatase inhibitor-2 (IPP-2) sequences."
Sanseau P., Jackson A., Alderton R.P., Beck S., Senger G., Sheer D., Kelly A., Trowsdale J.
Mamm. Genome 5:490-496(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of the complete coding region for human protein phosphatase inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E. coli."
Helps N.R., Street A.J., Elledge S.J., Cohen P.T.W.
FEBS Lett. 340:93-98(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genetic analysis of human type 1 protein phosphatase inhibitor 2 in insulin-resistant Pima Indians."
Permana P.A., Mott D.M.
Genomics 41:110-114(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Inhibitor 2 of protein phosphatase 1 is differentially expressed between the colon cancer cell lines SW480 and SW620."
Croke D.T., McWilliam P.M., Parle-McDermott A., Dunican D., Tighe O.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Cloning of inhibitor-2 of protein phosphatase type 1 from human heart."
Mishra S., Tiwari N., Sabbah H.N., Gupta R.C.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[6]"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].
Tissue: Skin.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-33.
Tissue: Platelet.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A novel ATM-dependent pathway regulates protein phosphatase 1 in response to DNA damage."
Tang X., Hui Z.G., Cui X.L., Garg R., Kastan M.B., Xu B.
Mol. Cell. Biol. 28:2559-2566(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-44, SUBUNIT.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND THR-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Identification and characterization of two distinct PPP1R2 isoforms in human spermatozoa."
Korrodi-Gregorio L., Ferreira M., Vintem A.P., Wu W., Muller T., Marcus K., Vijayaraghavan S., Brautigan D.L., da Cruz E Silva O.A., Fardilha M., da Cruz E Silva E.F.
BMC Cell Biol. 14:15-15(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-121; SER-122 AND SER-127.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78873 mRNA. Translation: CAA55475.1.
Z29646 mRNA. Translation: CAA82754.1.
U68111 expand/collapse EMBL AC list , U68106, U68107, U68108, U68109, U68110 Genomic DNA. Translation: AAC51206.1.
AJ133812 mRNA. Translation: CAB41680.1.
AY063767 mRNA. Translation: AAL48322.1.
BC007655 mRNA. Translation: AAH07655.1.
CCDSCCDS3309.1.
PIRS42406.
RefSeqNP_006232.1. NM_006241.7.
UniGeneHs.535731.
Hs.706920.

3D structure databases

ProteinModelPortalP41236.
SMRP41236. Positions 127-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111497. 36 interactions.
DIPDIP-781N.
IntActP41236. 10 interactions.
MINTMINT-2803186.
STRING9606.ENSP00000328178.

PTM databases

PhosphoSiteP41236.

Polymorphism databases

DMDM729856.

Proteomic databases

MaxQBP41236.
PRIDEP41236.

Protocols and materials databases

DNASU5504.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328432; ENSP00000328178; ENSG00000184203.
GeneID5504.
KEGGhsa:5504.
UCSCuc003fup.3. human.

Organism-specific databases

CTD5504.
GeneCardsGC03M195241.
H-InvDBHIX0032078.
HIX0166147.
HIX0166426.
HIX0166678.
HIX0167196.
HIX0200910.
HGNCHGNC:9288. PPP1R2.
HPACAB025582.
HPA043729.
MIM601792. gene.
neXtProtNX_P41236.
PharmGKBPA33641.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG006170.
InParanoidP41236.
KOK16833.
OMAAAEESMN.
PhylomeDBP41236.
TreeFamTF105536.

Enzyme and pathway databases

SignaLinkP41236.

Gene expression databases

ArrayExpressP41236.
BgeeP41236.
CleanExHS_PPP1R2.
GenevestigatorP41236.

Family and domain databases

InterProIPR007062. PPI-2.
[Graphical view]
PfamPF04979. IPP-2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPPP1R2.
GenomeRNAi5504.
NextBio21294.
PROP41236.
SOURCESearch...

Entry information

Entry nameIPP2_HUMAN
AccessionPrimary (citable) accession number: P41236
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM