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FKBP1A

From Wikipedia, the free encyclopedia
Protein and coding gene in humans

FKBP1A
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1A7X,1B6C,1BKF,1BL4,1D6O,1D7H,1D7I,1D7J,1EYM,1F40,1FAP,1FKB,1FKD,1FKF,1FKG,1FKH,1FKI,1FKJ,1FKR,1FKS,1FKT,1J4H,1J4I,1J4R,1NSG,1QPF,1QPL,2DG3,2DG4,2DG9,2FAP,2FKE,2PPN,2PPO,2PPP,2RSE,3FAP,3H9R,3MDY,4DH0,4FAP,4IPX,4N19,4ODP,4ODQ,4ODR

Identifiers
AliasesFKBP1A, FKBP-12, FKBP-1A, FKBP1, FKBP12, PKC12, PKCI2, PPIASE, FK506 binding protein 1A, FKBP prolyl isomerase 1A
External IDsOMIM:186945;MGI:95541;HomoloGene:105139;GeneCards:FKBP1A;OMA:FKBP1A - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for FKBP1A
Genomic location for FKBP1A
Band20p13Start1,368,977bp[1]
End1,393,164bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for FKBP1A
Genomic location for FKBP1A
Band2|2 G3Start151,384,403bp[2]
End151,403,612bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lung

  • monocyte

  • upper lobe of left lung

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • nucleus accumbens

  • epithelium of colon

  • rectum

  • left uterine tube

  • smooth muscle tissue
Top expressed in
  • lateral septal nucleus

  • olfactory tubercle

  • external carotid artery

  • internal carotid artery

  • dentate gyrus of hippocampal formation granule cell

  • subiculum

  • nucleus accumbens

  • anterior amygdaloid area

  • endocardial cushion

  • Gonadal ridge
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2280

14225

Ensembl

ENSG00000088832

ENSMUSG00000032966

UniProt

P62942

P26883

RefSeq (mRNA)

NM_054014
NM_000801
NM_001199786

NM_001302077
NM_001302078
NM_001302079
NM_001302080
NM_008019

NM_001355077
NM_001355078

RefSeq (protein)

NP_000792
NP_001186715
NP_463460

NP_001289006
NP_001289007
NP_001289008
NP_001289009
NP_032045

NP_001342006
NP_001342007

Location (UCSC)Chr 20: 1.37 – 1.39 MbChr 2: 151.38 – 151.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Peptidyl-prolyl cis-trans isomerase FKBP1A is anenzyme that in humans is encoded by theFKBP1Agene.[5] It is also commonly referred to as FKBP-12 or FKBP12 and is a member of a family ofFK506-binding proteins (FKBPs).

Function

[edit]

The protein encoded by this gene is a member of theimmunophilin protein family, which play a role in immunoregulation and basic cellular processes involvingprotein folding and trafficking. This encoded protein is acis-trans prolyl isomerase that binds theimmunosuppressantsFK506 (tacrolimus) andrapamycin (sirolimus). It interacts with several intracellularsignal transduction proteins includingtype I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels including thetetramericskeletal muscle ryanodine receptor. In mouse, deletion of thishomologous gene causescongenital heart disorder known asnoncompaction of left ventricular myocardium. Multiplealternatively spliced variants, encoding the same protein, have been identified. Thehuman genome contains fivepseudogenes related to this gene, at least one of which is transcribed.[6]

Interactions

[edit]

FKBP1A has been shown tointeract with:

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000088832 –Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000032966 –Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^DiLella AG (Sep 1991). "Chromosomal assignment of the human immunophilin FKBP-12 gene".Biochemical and Biophysical Research Communications.179 (3):1427–33.Bibcode:1991BBRC..179.1427D.doi:10.1016/0006-291X(91)91732-R.PMID 1930186.
  6. ^"Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa".
  7. ^Chambraud B, Radanyi C, Camonis JH, Shazand K, Rajkowski K, Baulieu EE (Dec 1996)."FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin".The Journal of Biological Chemistry.271 (51):32923–9.doi:10.1074/jbc.271.51.32923.PMID 8955134.
  8. ^Neye H (Mar 2001). "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52".Regulatory Peptides.97 (2–3):147–52.doi:10.1016/s0167-0115(00)00206-8.PMID 11164950.S2CID 20617551.
  9. ^MacMillan D, Currie S, Bradley KN, Muir TC, McCarron JG (Dec 2005)."In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin".Journal of Cell Science.118 (Pt 23):5443–51.doi:10.1242/jcs.02657.PMID 16278292.
  10. ^Cameron AM, Nucifora FC, Fung ET, Livingston DJ, Aldape RA, Ross CA, Snyder SH (Oct 1997)."FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain".The Journal of Biological Chemistry.272 (44):27582–8.doi:10.1074/jbc.272.44.27582.PMID 9346894.
  11. ^abJacinto E, Loewith R, Schmidt A, Lin S, Rüegg MA, Hall A, Hall MN (Nov 2004). "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive".Nature Cell Biology.6 (11):1122–8.doi:10.1038/ncb1183.PMID 15467718.S2CID 13831153.
  12. ^abSarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM (Jul 2004)."Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton".Current Biology.14 (14):1296–302.Bibcode:2004CBio...14.1296D.doi:10.1016/j.cub.2004.06.054.PMID 15268862.S2CID 4658268.
  13. ^Choi J, Chen J, Schreiber SL, Clardy J (Jul 1996). "Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP".Science.273 (5272):239–42.Bibcode:1996Sci...273..239C.doi:10.1126/science.273.5272.239.PMID 8662507.S2CID 27706675.
  14. ^Luker KE, Smith MC, Luker GD, Gammon ST, Piwnica-Worms H, Piwnica-Worms D (Aug 2004)."Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals".Proceedings of the National Academy of Sciences of the United States of America.101 (33):12288–93.Bibcode:2004PNAS..10112288L.doi:10.1073/pnas.0404041101.PMC 514471.PMID 15284440.
  15. ^Banaszynski LA, Liu CW, Wandless TJ (Apr 2005). "Characterization of the FKBP.rapamycin.FRB ternary complex".Journal of the American Chemical Society.127 (13):4715–21.doi:10.1021/ja043277y.PMID 15796538.
  16. ^Sabers CJ, Martin MM, Brunn GJ, Williams JM, Dumont FJ, Wiederrecht G, Abraham RT (Jan 1995)."Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells".The Journal of Biological Chemistry.270 (2):815–22.doi:10.1074/jbc.270.2.815.PMID 7822316.
  17. ^Avila G, Lee EH, Perez CF, Allen PD, Dirksen RT (Jun 2003)."FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes".The Journal of Biological Chemistry.278 (25):22600–8.doi:10.1074/jbc.M205866200.PMID 12704193.
  18. ^Bultynck G, De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys JB (Mar 2001)."Characterization and mapping of the 12 kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor".The Biochemical Journal.354 (Pt 2):413–22.doi:10.1042/bj3540413.PMC 1221670.PMID 11171121.
  19. ^Gaburjakova M, Gaburjakova J, Reiken S, Huang F, Marx SO, Rosemblit N, Marks AR (May 2001)."FKBP12 binding modulates ryanodine receptor channel gating".The Journal of Biological Chemistry.276 (20):16931–5.doi:10.1074/jbc.M100856200.PMID 11279144.
  20. ^Wang T, Donahoe PK, Zervos AS (Jul 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12".Science.265 (5172):674–6.Bibcode:1994Sci...265..674W.doi:10.1126/science.7518616.PMID 7518616.
  21. ^Liu F, Ventura F, Doody J, Massagué J (Jul 1995)."Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs".Molecular and Cellular Biology.15 (7):3479–86.doi:10.1128/mcb.15.7.3479.PMC 230584.PMID 7791754.

Further reading

[edit]
PDB gallery
  • 1a7x: FKBP12-FK1012 COMPLEX
    1a7x: FKBP12-FK1012 COMPLEX
  • 1b6c: CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12
    1b6c: CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12
  • 1bkf: FK506 BINDING PROTEIN FKBP MUTANT R42K/H87V COMPLEX WITH IMMUNOSUPPRESSANT FK506
    1bkf: FK506 BINDING PROTEIN FKBP MUTANT R42K/H87V COMPLEX WITH IMMUNOSUPPRESSANT FK506
  • 1bl4: FKBP MUTANT F36V COMPLEXED WITH REMODELED SYNTHETIC LIGAND
    1bl4: FKBP MUTANT F36V COMPLEXED WITH REMODELED SYNTHETIC LIGAND
  • 1d6o: NATIVE FKBP
    1d6o: NATIVE FKBP
  • 1d7h: FKBP COMPLEXED WITH DMSO
    1d7h: FKBP COMPLEXED WITH DMSO
  • 1d7i: FKBP COMPLEXED WITH METHYL METHYLSULFINYLMETHYL SULFIDE (DSS)
    1d7i: FKBP COMPLEXED WITH METHYL METHYLSULFINYLMETHYL SULFIDE (DSS)
  • 1d7j: FKBP COMPLEXED WITH 4-HYDROXY-2-BUTANONE
    1d7j: FKBP COMPLEXED WITH 4-HYDROXY-2-BUTANONE
  • 1eym: FK506 BINDING PROTEIN MUTANT, HOMODIMERIC COMPLEX
    1eym: FK506 BINDING PROTEIN MUTANT, HOMODIMERIC COMPLEX
  • 1f40: SOLUTION STRUCTURE OF FKBP12 COMPLEXED WITH GPI-1046, A NEUROTROPHIC LIGAND
    1f40: SOLUTION STRUCTURE OF FKBP12 COMPLEXED WITH GPI-1046, A NEUROTROPHIC LIGAND
  • 1fap: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP
    1fap: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP
  • 1fkb: ATOMIC STRUCTURE OF THE RAPAMYCIN HUMAN IMMUNOPHILIN FKBP-12 COMPLEX
    1fkb: ATOMIC STRUCTURE OF THE RAPAMYCIN HUMAN IMMUNOPHILIN FKBP-12 COMPLEX
  • 1fkd: FK-506 BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818
    1fkd: FK-506 BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818
  • 1fkf: ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX
    1fkf: ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX
  • 1fkg: DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12
    1fkg: DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12
  • 1fkh: DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12
    1fkh: DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12
  • 1fki: DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12
    1fki: DESIGN, SYNTHESIS, AND KINETIC EVALUATION OF HIGH-AFFINITY FKBP LIGANDS, AND THE X-RAY CRYSTAL STRUCTURES OF THEIR COMPLEXES WITH FKBP12
  • 1fkj: ATOMIC STRUCTURE OF FKBP12-FK506, AN IMMUNOPHILIN IMMUNOSUPPRESSANT COMPLEX
    1fkj: ATOMIC STRUCTURE OF FKBP12-FK506, AN IMMUNOPHILIN IMMUNOSUPPRESSANT COMPLEX
  • 1fkk: ATOMIC STRUCTURE OF FKBP12, AN IMMUNOPHILIN BINDING PROTEIN
    1fkk: ATOMIC STRUCTURE OF FKBP12, AN IMMUNOPHILIN BINDING PROTEIN
  • 1fkl: ATOMIC STRUCTURE OF FKBP12-RAPAYMYCIN, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX
    1fkl: ATOMIC STRUCTURE OF FKBP12-RAPAYMYCIN, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX
  • 1fkr: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
    1fkr: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
  • 1fks: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
    1fks: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
  • 1fkt: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
    1fkt: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
  • 1j4h: crystal structure analysis of the FKBP12 complexed with 000107 small molecule
    1j4h: crystal structure analysis of the FKBP12 complexed with 000107 small molecule
  • 1j4i: crystal structure analysis of the FKBP12 complexed with 000308 small molecule
    1j4i: crystal structure analysis of the FKBP12 complexed with 000308 small molecule
  • 1j4r: FK506 BINDING PROTEIN COMPLEXED WITH FKB-001
    1j4r: FK506 BINDING PROTEIN COMPLEXED WITH FKB-001
  • 1nsg: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP
    1nsg: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP
  • 1qpf: FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-709,858
    1qpf: FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-709,858
  • 1qpl: FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587
    1qpl: FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587
  • 1tco: TERNARY COMPLEX OF A CALCINEURIN A FRAGMENT, CALCINEURIN B, FKBP12 AND THE IMMUNOSUPPRESSANT DRUG FK506 (TACROLIMUS)
    1tco: TERNARY COMPLEX OF A CALCINEURIN A FRAGMENT, CALCINEURIN B, FKBP12 AND THE IMMUNOSUPPRESSANT DRUG FK506 (TACROLIMUS)
  • 2dg3: Wildtype FK506-binding protein complexed with Rapamycin
    2dg3: Wildtype FK506-binding protein complexed with Rapamycin
  • 2dg4: FK506-binding protein mutant WF59 complexed with Rapamycin
    2dg4: FK506-binding protein mutant WF59 complexed with Rapamycin
  • 2dg9: FK506-binding protein mutant WL59 complexed with Rapamycin
    2dg9: FK506-binding protein mutant WL59 complexed with Rapamycin
  • 2fap: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA
    2fap: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA
  • 2fke: FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818
    2fke: FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818
  • 3fap: ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP
    3fap: ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP
  • 4fap: ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP
    4fap: ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP
5.2.1
Activity
Regulation
Classification
Kinetics
Types
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