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Protein

Protein phosphatase inhibitor 2

Gene

PPP1R2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor of protein-phosphatase 1.

GO - Molecular functioni

  1. protein serine/threonine phosphatase inhibitor activity Source: ProtInc

GO - Biological processi

  1. generation of precursor metabolites and energy Source: ProtInc
  2. glycogen metabolic process Source: UniProtKB-KW
  3. negative regulation of catalytic activity Source: GOC
  4. regulation of phosphoprotein phosphatase activity Source: InterPro
  5. regulation of signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Enzyme and pathway databases

SignaLinkiP41236.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase inhibitor 2
Short name:
IPP-2
Gene namesi
Name:PPP1R2
Synonyms:IPP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9288. PPP1R2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33641.

Polymorphism and mutation databases

BioMutaiPPP1R2.
DMDMi729856.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity1 Publication
Chaini2 – 205204Protein phosphatase inhibitor 2PRO_0000071481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei44 – 441Phosphoserine; by ATM1 Publication
Modified residuei73 – 731Phosphothreonine; by GSK3By similarity
Modified residuei87 – 871Phosphoserine2 Publications
Modified residuei89 – 891Phosphothreonine1 Publication
Modified residuei92 – 921Phosphothreonine1 Publication
Modified residuei121 – 1211Phosphoserine1 Publication
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei127 – 1271Phosphoserine1 Publication

Post-translational modificationi

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.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41236.
PRIDEiP41236.

PTM databases

PhosphoSiteiP41236.

Expressioni

Gene expression databases

BgeeiP41236.
CleanExiHS_PPP1R2.
ExpressionAtlasiP41236. baseline and differential.
GenevestigatoriP41236.

Organism-specific databases

HPAiCAB025582.
HPA043729.

Interactioni

Subunit structurei

Heterodimer with PP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
LMTK2Q8IWU23EBI-1056517,EBI-2008933
PPP1CAP621362EBI-1056517,EBI-357253
PPP1CCP368734EBI-1056517,EBI-356283

Protein-protein interaction databases

BioGridi111497. 36 interactions.
DIPiDIP-781N.
IntActiP41236. 10 interactions.
MINTiMINT-2803186.
STRINGi9606.ENSP00000328178.

Structurei

3D structure databases

ProteinModelPortaliP41236.
SMRiP41236. Positions 127-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 176Required for binding PPP1CCBy similarity
Regioni43 – 5513Required for binding PPP1CCBy similarityAdd
BLAST
Regioni147 – 1504Required for binding PPP1CC catalytic center, displacing metal ions and inhibition of PPP1CC catyltic activityBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000004757.
HOVERGENiHBG006170.
InParanoidiP41236.
KOiK16833.
OMAiEMKRKMH.
PhylomeDBiP41236.
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.

P41236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTASHRP IKGILKNKTS TTSSMVASAE QPRGNVDEEL SKKSQKWDEM
60 70 80 90 100
NILATYHPAD KDYGLMKIDE PSTPYHSMMG DDEDACSDTE ATEAMAPDIL
110 120 130 140 150
ARKLAAAEGL EPKYRIQEQE SSGEEDSDLS PEEREKKRQF EMKRKLHYNE
160 170 180 190 200
GLNIKLARQL ISKDLHDDDE DEEMLETADG ESMNTEESNQ GSTPSDQQQN

KLRSS
Length:205
Mass (Da):23,015
Last modified:January 23, 2007 - v2
Checksum:iFFC005B07CD5ABFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78873 mRNA. Translation: CAA55475.1.
Z29646 mRNA. Translation: CAA82754.1.
U68111
, 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.
CCDSiCCDS3309.1.
PIRiS42406.
RefSeqiNP_006232.1. NM_006241.7.
UniGeneiHs.535731.
Hs.706920.

Genome annotation databases

EnsembliENST00000618156; ENSP00000484580; ENSG00000184203.
GeneIDi5504.
KEGGihsa:5504.
UCSCiuc003fup.3. human.

Polymorphism and mutation databases

BioMutaiPPP1R2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78873 mRNA. Translation: CAA55475.1.
Z29646 mRNA. Translation: CAA82754.1.
U68111
, 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.
CCDSiCCDS3309.1.
PIRiS42406.
RefSeqiNP_006232.1. NM_006241.7.
UniGeneiHs.535731.
Hs.706920.

3D structure databases

ProteinModelPortaliP41236.
SMRiP41236. Positions 127-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111497. 36 interactions.
DIPiDIP-781N.
IntActiP41236. 10 interactions.
MINTiMINT-2803186.
STRINGi9606.ENSP00000328178.

PTM databases

PhosphoSiteiP41236.

Polymorphism and mutation databases

BioMutaiPPP1R2.
DMDMi729856.

Proteomic databases

MaxQBiP41236.
PRIDEiP41236.

Protocols and materials databases

DNASUi5504.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000618156; ENSP00000484580; ENSG00000184203.
GeneIDi5504.
KEGGihsa:5504.
UCSCiuc003fup.3. human.

Organism-specific databases

CTDi5504.
GeneCardsiGC03M195241.
H-InvDBHIX0032078.
HIX0166147.
HIX0166426.
HIX0166678.
HIX0167196.
HIX0200910.
HGNCiHGNC:9288. PPP1R2.
HPAiCAB025582.
HPA043729.
MIMi601792. gene.
neXtProtiNX_P41236.
PharmGKBiPA33641.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000004757.
HOVERGENiHBG006170.
InParanoidiP41236.
KOiK16833.
OMAiEMKRKMH.
PhylomeDBiP41236.
TreeFamiTF105536.

Enzyme and pathway databases

SignaLinkiP41236.

Miscellaneous databases

GeneWikiiPPP1R2.
GenomeRNAii5504.
NextBioi21294.
PROiP41236.
SOURCEiSearch...

Gene expression databases

BgeeiP41236.
CleanExiHS_PPP1R2.
ExpressionAtlasiP41236. baseline and differential.
GenevestigatoriP41236.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: PHOSPHORYLATION AT SER-121; SER-122 AND SER-127.
    Tissue: Testis.

Entry informationi

Entry nameiIPP2_HUMAN
AccessioniPrimary (citable) accession number: P41236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.