Ignet

Gene Information

Gene symbol: FKBP1B

Gene name: FK506 binding protein 1B, 12.6 kDa

HGNC ID: 3712

Synonyms: OTK4, FKBP12.6, PPIase, FKBP9

Related Genes

#	Gene Symbol	Number of hits
1	FKBP1A	1 hits
2	PIN1	1 hits
3	PPIA	1 hits
4	PPIB	1 hits
5	PPIC	1 hits
6	PPIH	1 hits
7	SH2D3A	1 hits

Related Sentences

#	PMID	Sentence
1	14976191	This folding activity is consistent with the homology of a segment of PrsA with parvulin-type peptidyl-prolyl cis/trans isomerases (PPIase).
2	14976191	PrsA exhibits PPIase activity in a manner dependent on the parvulin-like domain.
3	14976191	Surprisingly, none of the predicted active site residues of the parvulin-like domain was essential for growth and protein secretion, although several active site mutations reduced or abolished the PPIase activity or the ability of PrsA to catalyze proline-limited protein folding in vitro.
4	14976191	Our results indicate that PrsA is a PPIase, but the essential role in vivo seems to depend on some non-PPIase activity of both the parvulin-like and flanking domains.
5	14976191	This folding activity is consistent with the homology of a segment of PrsA with parvulin-type peptidyl-prolyl cis/trans isomerases (PPIase).
6	14976191	PrsA exhibits PPIase activity in a manner dependent on the parvulin-like domain.
7	14976191	Surprisingly, none of the predicted active site residues of the parvulin-like domain was essential for growth and protein secretion, although several active site mutations reduced or abolished the PPIase activity or the ability of PrsA to catalyze proline-limited protein folding in vitro.
8	14976191	Our results indicate that PrsA is a PPIase, but the essential role in vivo seems to depend on some non-PPIase activity of both the parvulin-like and flanking domains.
9	14976191	This folding activity is consistent with the homology of a segment of PrsA with parvulin-type peptidyl-prolyl cis/trans isomerases (PPIase).
10	14976191	PrsA exhibits PPIase activity in a manner dependent on the parvulin-like domain.
11	14976191	Surprisingly, none of the predicted active site residues of the parvulin-like domain was essential for growth and protein secretion, although several active site mutations reduced or abolished the PPIase activity or the ability of PrsA to catalyze proline-limited protein folding in vitro.
12	14976191	Our results indicate that PrsA is a PPIase, but the essential role in vivo seems to depend on some non-PPIase activity of both the parvulin-like and flanking domains.
13	14976191	This folding activity is consistent with the homology of a segment of PrsA with parvulin-type peptidyl-prolyl cis/trans isomerases (PPIase).
14	14976191	PrsA exhibits PPIase activity in a manner dependent on the parvulin-like domain.
15	14976191	Surprisingly, none of the predicted active site residues of the parvulin-like domain was essential for growth and protein secretion, although several active site mutations reduced or abolished the PPIase activity or the ability of PrsA to catalyze proline-limited protein folding in vitro.
16	14976191	Our results indicate that PrsA is a PPIase, but the essential role in vivo seems to depend on some non-PPIase activity of both the parvulin-like and flanking domains.
17	22046132	In this study, we used a systems biology approach employing a genome-wide yeast-two hybrid interaction screen to identify immunopilins (PPIA, PPIB, PPIH, PPIG, FKBP1A, FKBP1B) as interaction partners of the CoV non-structural protein 1 (Nsp1).
18	22046132	Overexpression of NSP1 and infection with live SARS-CoV strongly increased signalling through the Calcineurin/NFAT pathway and enhanced the induction of interleukin 2, compatible with late-stage immunopathogenicity and long-term cytokine dysregulation as observed in severe SARS cases.
19	26468663	Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolyl cis/trans isomerase (PPIase) proteins.