Antibody-points Bulletin: PPIA
Sep-12-2017 0 comments Cube Biosystems

Antibody-points Bulletin:
Peptidyl-prolyl cis-trans isomerase A

BOLO:

Name: Peptidyl-prolyl cis-trans isomerase A

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. PPIA is believed to inhibit HIV-1 infection by blocking nuclear import of the HIV-1 preintegration complex.
Artist Rendering of Peptidyl-prolyl cis-trans isomerase A (AA:1-165)
Source: Swiss-Model  
CC License

PID: P62937

GID: 5478

Nicknames: PPIA

AKA: CYPA, CYPH, HEL-S-69p, PPIase A, Cyclophilin A, Rotamase A

Vitals:

   Origins: 17p13.1
   DNA: NC_000007.14 6488 bp, (44796636..44803123)
   RNA: NM_001300981.1 2455 bp
   Exons: 6
   Protein: 165 aa, 18 kDa

Description:

This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

PPIA is believed to inhibit HIV-1 infection by blocking nuclear import of the HIV-1 preintegration complex.

Protein of Interest in the Following Cases:

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. PPIA is believed to inhibit HIV-1 infection by blocking nuclear import of the HIV-1 preintegration complex.

Source: Open Targets Platform

Last Known Addresses:

  •  Cytoplasm
  •  Secreted

Known Hangouts:

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. PPIA is believed to inhibit HIV-1 infection by blocking nuclear import of the HIV-1 preintegration complex.

Source: NCBI

Known Associates:

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. PPIA is believed to inhibit HIV-1 infection by blocking nuclear import of the HIV-1 preintegration complex.

Source: BioGrid

Gang Associations:

  •  
  •  Establishment Of Integrated Proviral Latency
  •  Fusion Of Virus Membrane With Host Plasma Membrane
  •  Leukocyte Migration
  •  Lipid Particle Organization
  •  Neuron Differentiation
  •  Neutrophil Degranulation
  •  Positive Regulation Of Protein Secretion
  •  Positive Regulation Of Viral Genome Replication
  •  Protein Folding
  •  Protein Peptidyl-Prolyl Isomerization
  •  Regulation Of Viral Genome Replication
  •  Rna-Dependent Dna Biosynthetic Process
  •  Uncoating Of Virus
  •  Viral Life Cycle
  •  Viral Release From Host Cell
  •  Virion Assembly

Known Weaknesses:
Cyclosporine for

  •  Chronic Obstructive Pulmonary Disease
  •  Acute Graft vs. Host Disease
  •  Acute Kidney Injury
  •  Allergic Conjunctivitis
  •  Atopic Eczema
  •  Bronchiolitis Obliterans
  •  Chronic Interstitial Cystitis
  •  Chronic Kidney Disease
  •  Focal Segmental Glomerulosclerosis
  •  Glaucoma
  •  Leprosy
  •  Psoriasis
  •  Abdominal Aortic Aneurysm
  •  Acute Myeloid Leukemia
  •  Autoimmune Hepatitis
  •  Dry Eye Syndrome
  •  Chronic
  •  Diabetes Mellitus
  •  Lymphoid Leukemia
  •  Lymphoma
  •  Autoimmune Thrombocytopenic Purpura

Reported Sightings:

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. PPIA is believed to inhibit HIV-1 infection by blocking nuclear import of the HIV-1 preintegration complex.

Source: Pubmed

Means of Capture:

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