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Literature summary for 5.2.1.8 extracted from

  • Xia, H.; Lv, H.; Chen, K.; Yao, Q.; Lv, P.; Li, J.; Chen, H.; Wang, L.
    Cloning and characterization of peptidylprolyl isomerase B in the silkworm, Bombyx mori (2009), Afr. J. Biotechnol., 8, 7116-7124.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene PPIB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21 (DE3) Bombyx mori

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Bombyx mori 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21474
-
x * 21474, sequence calculation Bombyx mori

Organism

Organism UniProt Comment Textmining
Bombyx mori B2LU30 gene PPIB
-

Source Tissue

Source Tissue Comment Organism Textmining
blood-lymph
-
Bombyx mori
-
embryo
-
Bombyx mori
-
fat body
-
Bombyx mori
-
hemolymph
-
Bombyx mori
-
malpighian tubule
-
Bombyx mori
-
midgut
-
Bombyx mori
-
additional information broad tissue PPIase expression pattern Bombyx mori
-
ovary
-
Bombyx mori
-
silk gland
-
Bombyx mori
-
testis
-
Bombyx mori
-
tuba Malpighii
-
Bombyx mori
-

Subunits

Subunits Comment Organism
? x * 21474, sequence calculation Bombyx mori
More peptide mass fingerprinting and mass spectrometric analysis, homology-modeling Bombyx mori

Synonyms

Synonyms Comment Organism
More PPIB contains conserved and unique cyclophilin domain and belongs to cyclophilin superfamily Bombyx mori
peptidylprolyl isomerase
-
Bombyx mori
PPIase
-
Bombyx mori
PpiB
-
Bombyx mori

pI Value

Organism Comment pI Value Maximum pI Value
Bombyx mori sequence calculation
-
8.05

General Information

General Information Comment Organism
physiological function peptidylprolyl isomerases play essential roles in protein folding and are implicated in immune response and cell cycle control. Bombyx mori PPIases may be involved in anti-Bombyx mori nucleopolyhedrovirus response, mechanism, overview Bombyx mori