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{{Infobox_gene}}
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'''Peptidyl-prolyl cis-trans isomerase FKBP1B''' is an [[enzyme]] that in humans is encoded by the ''FKBP1B'' [[gene]].<ref name="pmid7513996">{{cite journal |vauthors=Arakawa H, Nagase H, Hayashi N, Fujiwara T, Ogawa M, Shin S, Nakamura Y | title = Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts | journal = Biochem Biophys Res Commun | volume = 200 | issue = 2 | pages = 836–43 |date=Jun 1994 | pmid = 7513996 | pmc =  | doi =10.1006/bbrc.1994.1527 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2281| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FKBP1B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c9h.
| PDB = {{PDB2|1c9h}}
| Name = FK506 binding protein 1B, 12.6 kDa
| HGNCid = 3712
| Symbol = FKBP1B
| AltSymbols =; FKBP12.6; FKBP1L; FKBP9; OTK4; PKBP1L; PPIase
| OMIM = 600620
| ECnumber =
| Homologene = 68380
| MGIid = 1336205
  | GeneAtlas_image1 = PBB_GE_FKBP1B_206857_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FKBP1B_209931_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0003755 |text = peptidyl-prolyl cis-trans isomerase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2281
    | Hs_Ensembl = ENSG00000119782
    | Hs_RefseqProtein = NP_004107
    | Hs_RefseqmRNA = NM_004116
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 24126075
    | Hs_GenLoc_end = 24140055
    | Hs_Uniprot = P68106
    | Mm_EntrezGene = 14226
    | Mm_Ensembl = ENSMUSG00000020635
    | Mm_RefseqmRNA = NM_016863
    | Mm_RefseqProtein = NP_058559
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 4855525
    | Mm_GenLoc_end = 4863945
    | Mm_Uniprot = Q810R7
  }}
}}
'''FK506 binding protein 1B, 12.6 kDa''', also known as '''FKBP1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2281| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2281| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 ([[tacrolimus]]) and rapamycin ([[sirolimus]]). It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Schiene-Fischer C, Yu C |title=Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. |journal=FEBS Lett. |volume=495 |issue= 1-2 |pages= 1-6 |year= 2001 |pmid= 11322937 |doi=  }}
*{{cite journal  |vauthors=Schiene-Fischer C, Yu C |title=Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. |journal=FEBS Lett. |volume=495 |issue= 1-2 |pages= 1–6 |year= 2001 |pmid= 11322937 |doi=10.1016/S0014-5793(01)02326-2 }}
*{{cite journal  | author=Arakawa H, Nagase H, Hayashi N, ''et al.'' |title=Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts. |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 2 |pages= 836-43 |year= 1994 |pmid= 7513996 |doi= }}
*{{cite journal  |vauthors=Lam E, Martin MM, Timerman AP |title=A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26511–22 |year= 1995 |pmid= 7592869 |doi=10.1074/jbc.270.44.26511  |display-authors=etal}}
*{{cite journal  | author=Lam E, Martin MM, Timerman AP, ''et al.'' |title=A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26511-22 |year= 1995 |pmid= 7592869 |doi= }}
*{{cite journal  |vauthors=Noguchi N, Takasawa S, Nata K |title=Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3133–6 |year= 1997 |pmid= 9013543 |doi=10.1074/jbc.272.6.3133  |display-authors=etal}}
*{{cite journal  | author=Noguchi N, Takasawa S, Nata K, ''et al.'' |title=Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3133-6 |year= 1997 |pmid= 9013543 |doi=  }}
*{{cite journal  |vauthors=Deivanayagam CC, Carson M, Thotakura A |title=Structure of FKBP12.6 in complex with rapamycin. |journal=Acta Crystallogr. D |volume=56 |issue= Pt 3 |pages= 266–71 |year= 2000 |pmid= 10713512 |doi=10.1107/S0907444999016571 |display-authors=etal}}
*{{cite journal  | author=Deivanayagam CC, Carson M, Thotakura A, ''et al.'' |title=Structure of FKBP12.6 in complex with rapamycin. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=56 |issue= Pt 3 |pages= 266-71 |year= 2000 |pmid= 10713512 |doi=  }}
*{{cite journal  |vauthors=Marx SO, Reiken S, Hisamatsu Y |title=PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. |journal=Cell |volume=101 |issue= 4 |pages= 365–76 |year= 2000 |pmid= 10830164 |doi=10.1016/S0092-8674(00)80847-8 |display-authors=etal}}
*{{cite journal  | author=Marx SO, Reiken S, Hisamatsu Y, ''et al.'' |title=PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. |journal=Cell |volume=101 |issue= 4 |pages= 365-76 |year= 2000 |pmid= 10830164 |doi= }}
*{{cite journal  |vauthors=Jeyakumar LH, Ballester L, Cheng DS |title=FKBP binding characteristics of cardiac microsomes from diverse vertebrates. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 4 |pages= 979–86 |year= 2001 |pmid= 11237759 |doi= 10.1006/bbrc.2001.4444 |display-authors=etal}}
*{{cite journal  | author=Jeyakumar LH, Ballester L, Cheng DS, ''et al.'' |title=FKBP binding characteristics of cardiac microsomes from diverse vertebrates. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 4 |pages= 979-86 |year= 2001 |pmid= 11237759 |doi= 10.1006/bbrc.2001.4444 }}
*{{cite journal  |vauthors=George CH, Sorathia R, Bertrand BM, Lai FA |title=In situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6. |journal=Biochem. J. |volume=370 |issue= Pt 2 |pages= 579–89 |year= 2003 |pmid= 12443530 |doi= 10.1042/BJ20021433  | pmc=1223191 }}
*{{cite journal  | author=George CH, Sorathia R, Bertrand BM, Lai FA |title=In situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6. |journal=Biochem. J. |volume=370 |issue= Pt 2 |pages= 579-89 |year= 2003 |pmid= 12443530 |doi= 10.1042/BJ20021433 }}
*{{cite journal  |vauthors=Masumiya H, Wang R, Zhang J |title=Localization of the 12.6-kDa FK506-binding protein (FKBP12.6) binding site to the NH2-terminal domain of the cardiac Ca2+ release channel (ryanodine receptor). |journal=J. Biol. Chem. |volume=278 |issue= 6 |pages= 3786–92 |year= 2003 |pmid= 12446682 |doi= 10.1074/jbc.M210962200 |display-authors=etal}}
*{{cite journal  | author=Masumiya H, Wang R, Zhang J, ''et al.'' |title=Localization of the 12.6-kDa FK506-binding protein (FKBP12.6) binding site to the NH2-terminal domain of the cardiac Ca2+ release channel (ryanodine receptor). |journal=J. Biol. Chem. |volume=278 |issue= 6 |pages= 3786-92 |year= 2003 |pmid= 12446682 |doi= 10.1074/jbc.M210962200 }}
*{{cite journal  |vauthors=Tiso N, Salamon M, Bagattin A |title=The binding of the RyR2 calcium channel to its gating protein FKBP12.6 is oppositely affected by ARVD2 and VTSIP mutations. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 4 |pages= 594–8 |year= 2003 |pmid= 12459180 |doi=10.1016/S0006-291X(02)02689-X  |display-authors=etal}}
*{{cite journal  | author=Tiso N, Salamon M, Bagattin A, ''et al.'' |title=The binding of the RyR2 calcium channel to its gating protein FKBP12.6 is oppositely affected by ARVD2 and VTSIP mutations. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 4 |pages= 594-8 |year= 2003 |pmid= 12459180 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=George CH, Higgs GV, Mackrill JJ, Lai FA |title=Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28856–64 |year= 2003 |pmid= 12754204 |doi= 10.1074/jbc.M212440200 }}
*{{cite journal  | author=George CH, Higgs GV, Mackrill JJ, Lai FA |title=Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28856-64 |year= 2003 |pmid= 12754204 |doi= 10.1074/jbc.M212440200 }}
*{{cite journal  |vauthors=Nishanian TG, Waldman T |title=Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor. |journal=Biochem. Biophys. Res. Commun. |volume=323 |issue= 1 |pages= 91–7 |year= 2004 |pmid= 15351706 |doi= 10.1016/j.bbrc.2004.08.060 }}
*{{cite journal  | author=Nishanian TG, Waldman T |title=Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor. |journal=Biochem. Biophys. Res. Commun. |volume=323 |issue= 1 |pages= 91-7 |year= 2004 |pmid= 15351706 |doi= 10.1016/j.bbrc.2004.08.060 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Maalej A, Mbarki F, Rebai A |title=Evidence of association between FKBP1B and thyroid autoimmune disorders in a large Tunisian family. |journal=Autoimmunity |volume=37 |issue= 3 |pages= 237–9 |year= 2005 |pmid= 15497458 |doi=10.1080/08916930410001702478  |display-authors=etal}}
*{{cite journal  | author=Maalej A, Mbarki F, Rebai A, ''et al.'' |title=Evidence of association between FKBP1B and thyroid autoimmune disorders in a large Tunisian family. |journal=Autoimmunity |volume=37 |issue= 3 |pages= 237-9 |year= 2005 |pmid= 15497458 |doi= }}
*{{cite journal  |vauthors=Zissimopoulos S, Lai FA |title=Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain. |journal=J. Biol. Chem. |volume=280 |issue= 7 |pages= 5475–85 |year= 2005 |pmid= 15591045 |doi= 10.1074/jbc.M412954200 }}
*{{cite journal  | author=Zissimopoulos S, Lai FA |title=Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain. |journal=J. Biol. Chem. |volume=280 |issue= 7 |pages= 5475-85 |year= 2005 |pmid= 15591045 |doi= 10.1074/jbc.M412954200 }}
*{{cite journal  |vauthors=Aizawa Y, Ueda K, Komura S |title=A novel mutation in FKBP12.6 binding region of the human cardiac ryanodine receptor gene (R2401H) in a Japanese patient with catecholaminergic polymorphic ventricular tachycardia. |journal=Int. J. Cardiol. |volume=99 |issue= 2 |pages= 343–5 |year= 2005 |pmid= 15749201 |doi= 10.1016/j.ijcard.2003.11.050 |display-authors=etal}}
*{{cite journal  | author=Aizawa Y, Ueda K, Komura S, ''et al.'' |title=A novel mutation in FKBP12.6 binding region of the human cardiac ryanodine receptor gene (R2401H) in a Japanese patient with catecholaminergic polymorphic ventricular tachycardia. |journal=Int. J. Cardiol. |volume=99 |issue= 2 |pages= 343-5 |year= 2005 |pmid= 15749201 |doi= 10.1016/j.ijcard.2003.11.050 }}
*{{cite journal  |vauthors=Wehrens XH, Lehnart SE, Reiken S |title=Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 27 |pages= 9607–12 |year= 2005 |pmid= 15972811 |doi= 10.1073/pnas.0500353102  | pmc=1172237 |display-authors=etal}}
*{{cite journal  | author=Wehrens XH, Lehnart SE, Reiken S, ''et al.'' |title=Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 27 |pages= 9607-12 |year= 2005 |pmid= 15972811 |doi= 10.1073/pnas.0500353102 }}
*{{cite journal  |vauthors=Won J, Kim M, Yi YW |title=A magnetic nanoprobe technology for detecting molecular interactions in live cells. |journal=Science |volume=309 |issue= 5731 |pages= 121–5 |year= 2005 |pmid= 15994554 |doi= 10.1126/science.1112869 |display-authors=etal}}{{Retracted paper}}
*{{cite journal  | author=Won J, Kim M, Yi YW, ''et al.'' |title=A magnetic nanoprobe technology for detecting molecular interactions in live cells. |journal=Science |volume=309 |issue= 5731 |pages= 121-5 |year= 2005 |pmid= 15994554 |doi= 10.1126/science.1112869 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 04:49, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene.[1][2]

The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin (sirolimus). It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.[2]

References

  1. ↑ Arakawa H, Nagase H, Hayashi N, Fujiwara T, Ogawa M, Shin S, Nakamura Y (Jun 1994). "Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts". Biochem Biophys Res Commun. 200 (2): 836–43. doi:10.1006/bbrc.1994.1527. PMID 7513996.
  2. ↑ 2.0 2.1 "Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa".

Further reading


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