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P41236

- IPP2_HUMAN

UniProt

P41236 - IPP2_HUMAN

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Protein
Protein phosphatase inhibitor 2
Gene
PPP1R2, IPP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Inhibitor of protein-phosphatase 1.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. 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: Chromosome 3

Organism-specific databases

HGNCiHGNC:9288. PPP1R2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 205204Protein phosphatase inhibitor 2
PRO_0000071481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei44 – 441Phosphoserine; by ATM1 Publication
Modified residuei73 – 731Phosphothreonine; by GSK3 By 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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41236.
PRIDEiP41236.

PTM databases

PhosphoSiteiP41236.

Expressioni

Gene expression databases

ArrayExpressiP41236.
BgeeiP41236.
CleanExiHS_PPP1R2.
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.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG006170.
InParanoidiP41236.
KOiK16833.
OMAiAAEESMN.
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

MAASTASHRP IKGILKNKTS TTSSMVASAE QPRGNVDEEL SKKSQKWDEM    50
NILATYHPAD KDYGLMKIDE PSTPYHSMMG DDEDACSDTE ATEAMAPDIL 100
ARKLAAAEGL EPKYRIQEQE SSGEEDSDLS PEEREKKRQF EMKRKLHYNE 150
GLNIKLARQL ISKDLHDDDE DEEMLETADG ESMNTEESNQ GSTPSDQQQN 200
KLRSS 205
Length:205
Mass (Da):23,015
Last modified:January 23, 2007 - v2
Checksum:iFFC005B07CD5ABFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000328432; ENSP00000328178; ENSG00000184203.
GeneIDi5504.
KEGGihsa:5504.
UCSCiuc003fup.3. human.

Polymorphism databases

DMDMi729856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3309.1.
PIRi S42406.
RefSeqi NP_006232.1. NM_006241.7.
UniGenei Hs.535731.
Hs.706920.

3D structure databases

ProteinModelPortali P41236.
SMRi P41236. Positions 127-168.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111497. 36 interactions.
DIPi DIP-781N.
IntActi P41236. 10 interactions.
MINTi MINT-2803186.
STRINGi 9606.ENSP00000328178.

PTM databases

PhosphoSitei P41236.

Polymorphism databases

DMDMi 729856.

Proteomic databases

MaxQBi P41236.
PRIDEi P41236.

Protocols and materials databases

DNASUi 5504.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328432 ; ENSP00000328178 ; ENSG00000184203 .
GeneIDi 5504.
KEGGi hsa:5504.
UCSCi uc003fup.3. human.

Organism-specific databases

CTDi 5504.
GeneCardsi GC03M195241.
H-InvDB HIX0032078.
HIX0166147.
HIX0166426.
HIX0166678.
HIX0167196.
HIX0200910.
HGNCi HGNC:9288. PPP1R2.
HPAi CAB025582.
HPA043729.
MIMi 601792. gene.
neXtProti NX_P41236.
PharmGKBi PA33641.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG006170.
InParanoidi P41236.
KOi K16833.
OMAi AAEESMN.
PhylomeDBi P41236.
TreeFami TF105536.

Enzyme and pathway databases

SignaLinki P41236.

Miscellaneous databases

GeneWikii PPP1R2.
GenomeRNAii 5504.
NextBioi 21294.
PROi P41236.
SOURCEi Search...

Gene expression databases

ArrayExpressi P41236.
Bgeei P41236.
CleanExi HS_PPP1R2.
Genevestigatori P41236.

Family and domain databases

InterProi IPR007062. PPI-2.
[Graphical view ]
Pfami PF04979. IPP-2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 135 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

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