A0A7I2V4F2 · A0A7I2V4F2_HUMAN

  • Protein
    Peptidylprolyl isomerase G
  • Gene
    PPIG
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentnuclear speck
Molecular Functioncyclosporin A binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Biological Processprotein peptidyl-prolyl isomerization

Names & Taxonomy

Protein names

  • Submitted names
    • Peptidylprolyl isomerase G

Gene names

    • Name
      PPIG

Organism names

Accessions

  • Primary accession
    A0A7I2V4F2

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 563 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)101PRIDEPhosphoserine
Modified residue (large scale data)215PRIDEPhosphoserine
Modified residue (large scale data)244PRIDEPhosphoserine
Modified residue (large scale data)281PRIDEPhosphoserine
Modified residue (large scale data)283PRIDEPhosphothreonine
Modified residue (large scale data)300PRIDEPhosphoserine
Modified residue (large scale data)301PRIDEPhosphoserine
Modified residue (large scale data)311PRIDEPhosphoserine
Modified residue (large scale data)322PRIDEPhosphoserine
Modified residue (large scale data)338PRIDEPhosphoserine
Modified residue (large scale data)340PRIDEPhosphoserine
Modified residue (large scale data)431PRIDEPhosphoserine
Modified residue (large scale data)458PRIDEPhosphoserine
Modified residue (large scale data)469PRIDEPhosphoserine
Modified residue (large scale data)471PRIDEPhosphoserine
Modified residue (large scale data)602PRIDEPhosphoserine
Modified residue (large scale data)612PRIDEPhosphoserine
Modified residue (large scale data)615PRIDEPhosphoserine
Modified residue (large scale data)620PRIDEPhosphoserine
Modified residue (large scale data)621PRIDEPhosphoserine
Modified residue (large scale data)641PRIDEPhosphoserine
Modified residue (large scale data)642PRIDEPhosphoserine
Modified residue (large scale data)669PRIDEPhosphoserine
Modified residue (large scale data)670PRIDEPhosphoserine
Modified residue (large scale data)673PRIDEPhosphothreonine
Modified residue (large scale data)678PRIDEPhosphoserine

Proteomic databases

Expression

Gene expression databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-104PPIase cyclophilin-type
Region105-679Disordered
Compositional bias123-146Polar residues
Compositional bias156-178Basic residues
Compositional bias213-236Basic and acidic residues
Compositional bias252-274Basic residues
Compositional bias275-293Basic and acidic residues
Compositional bias300-375Basic and acidic residues
Compositional bias390-491Basic and acidic residues
Compositional bias492-506Basic residues
Compositional bias507-527Basic and acidic residues
Compositional bias550-613Basic and acidic residues
Compositional bias628-679Basic and acidic residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    679
  • Mass (Da)
    80,148
  • Last updated
    2021-04-07 v1
  • Checksum
    65DC052946200D65
MVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPKSKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRKHKKEKKKRKKSKKSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERKNRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKNEKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRNEEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDRRAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRRRGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSESEKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVEKENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q13427PPIG_HUMANPPIG754
C9J679C9J679_HUMANPPIG104
C9JM79C9JM79_HUMANPPIG487
C9JN15C9JN15_HUMANPPIG246
E9PG73E9PG73_HUMANPPIG739
A0A7I2V2U3A0A7I2V2U3_HUMANPPIG65
A0A7I2V4W3A0A7I2V4W3_HUMANPPIG133
A0A7I2V5Q5A0A7I2V5Q5_HUMANPPIG751
A0A7I2V629A0A7I2V629_HUMANPPIG732

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias123-146Polar residues
Compositional bias156-178Basic residues
Compositional bias213-236Basic and acidic residues
Compositional bias252-274Basic residues
Compositional bias275-293Basic and acidic residues
Compositional bias300-375Basic and acidic residues
Compositional bias390-491Basic and acidic residues
Compositional bias492-506Basic residues
Compositional bias507-527Basic and acidic residues
Compositional bias550-613Basic and acidic residues
Compositional bias628-679Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC016772
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC093899
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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