Human Gene PPIG (uc002uez.3) Description and Page Index
  Description: Homo sapiens peptidylprolyl isomerase G (cyclophilin G) (PPIG), mRNA.
Transcript (Including UTRs)
   Position: hg19 chr2:170,440,850-170,494,254 Size: 53,405 Total Exon Count: 14 Strand: +
Coding Region
   Position: hg19 chr2:170,460,552-170,494,033 Size: 33,482 Coding Exon Count: 12 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsOther NamesModel InformationMethods
Data last updated: 2013-06-14

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr2:170,440,850-170,494,254)mRNA (may differ from genome)Protein (754 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
BioGPSCGAPEnsemblEntrez GeneExonPrimerGeneCards
GeneNetworkHGNCHPRDLynxMGIneXtProt
OMIMPubMedStanford SOURCETreefamUniProtKBWikipedia

-  Comments and Description Text from UniProtKB
  ID: PPIG_HUMAN
DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase G; Short=PPIase G; Short=Peptidyl-prolyl isomerase G; EC=5.2.1.8; AltName: Full=CASP10; AltName: Full=Clk-associating RS-cyclophilin; Short=CARS-Cyp; Short=CARS-cyclophilin; Short=SR-cyclophilin; Short=SR-cyp; Short=SRcyp; AltName: Full=Cyclophilin G; AltName: Full=Rotamase G;
FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.
CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
ENZYME REGULATION: Cyclosporin A (CsA)-sensitive.
SUBUNIT: Interacts with CLK1, PNN and with the phosphorylated C- terminal domain of RNA polymerase II.
SUBCELLULAR LOCATION: Nucleus matrix. Nucleus speckle. Note=Colocalizes with RNA splicing factors at nuclear speckles.
TISSUE SPECIFICITY: Ubiquitous.
DOMAIN: The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
SIMILARITY: Contains 1 PPIase cyclophilin-type domain.

-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): PPIG
CDC HuGE Published Literature: PPIG

-  MalaCards Disease Associations
  MalaCards Gene Search: PPIG
Diseases sorted by gene-association score: bietti crystalline corneoretinal dystrophy (10), chronic cystitis (8), uterine corpus endometrial carcinoma (7), hemorrhagic cystitis (7), tinea cruris (7), bladder disease (6), neurotic excoriation (6), tinea unguium (6), blackwater fever (6), clopidogrel resistance (6), gnathomiasis (6), balkan nephropathy (6), fish allergy (5), acute maxillary sinusitis (5), kleptomania (4), myocardial infarction (1), nicotine dependence, protection against (1)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
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-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 18.86 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 504.28 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
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-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -84.10220-0.382 Picture PostScript Text
3' UTR -40.40221-0.183 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR002130 - Cyclophilin-like_PPIase_dom
IPR020892 - Cyclophilin-type_PPIase_CS

Pfam Domains:
PF00160 - Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD

SCOP Domains:
50891 - Cyclophilin-like

Protein Data Bank (PDB) 3-D Structure
MuPIT help

2GW2
- X-ray MuPIT

2WFI
- X-ray MuPIT

2WFJ
- X-ray MuPIT


ModBase Predicted Comparative 3D Structure on Q13427
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
Gene SorterGene Sorter    
 RGD    
 Protein Sequence    
 Alignment    

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003723 RNA binding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0016018 cyclosporin A binding
GO:0016853 isomerase activity

Biological Process:
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0008380 RNA splicing

Cellular Component:
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005829 cytosol
GO:0016363 nuclear matrix
GO:0016607 nuclear speck


-  Descriptions from all associated GenBank mRNAs
  BC109373 - Homo sapiens peptidylprolyl isomerase G (cyclophilin G), mRNA (cDNA clone IMAGE:4774355), partial cds.
AK307552 - Homo sapiens cDNA, FLJ97500.
BC111693 - Homo sapiens peptidylprolyl isomerase G (cyclophilin G), mRNA (cDNA clone MGC:133241 IMAGE:40034815), complete cds.
BC001555 - Homo sapiens peptidylprolyl isomerase G (cyclophilin G), mRNA (cDNA clone IMAGE:3461499), complete cds.
X99717 - H.sapiens mRNA for SRcyp protein.
U40763 - Human Clk-associated RS cyclophilin CARS-Cyp mRNA, complete cds.
BC063711 - Homo sapiens peptidylprolyl isomerase G (cyclophilin G), mRNA (cDNA clone IMAGE:5123534), partial cds.
AB590647 - Synthetic construct DNA, clone: pFN21AE2081, Homo sapiens PPIG gene for peptidylprolyl isomerase G, without stop codon, in Flexi system.
KJ901967 - Synthetic construct Homo sapiens clone ccsbBroadEn_11361 PPIG gene, encodes complete protein.
KJ901966 - Synthetic construct Homo sapiens clone ccsbBroadEn_11360 PPIG gene, encodes complete protein.

-  Other Names for This Gene
  Alternate Gene Symbols: D3DPC5, D3DPC6, NM_004792, NP_004783, O00706, PPIG_HUMAN, Q13427, Q53R40, Q53SN4, Q96DG9
UCSC ID: uc002uez.3
RefSeq Accession: NM_004792
Protein: Q13427 (aka PPIG_HUMAN)
CCDS: CCDS2235.1

-  Gene Model Information
 
category: coding nonsense-mediated-decay: no RNA accession: NM_004792.2
exon count: 14CDS single in 3' UTR: no RNA size: 2717
ORF size: 2265CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 4633.50frame shift in genome: no % Coverage: 99.60
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.