FKBP1A

Proteína 1A de unión a FK506
	; Estructura tridimensional de la proteína FKBP1A.
Estructuras disponibles
PDB	Buscar ortólogos: PDBe, RCSB Lista de códigos PDB 1a7x
Identificadores
Símbolos	FKBP1A (HGNC: 3711) FKBP-12, FKBP1, FKBP12, FKBP12C, PKC12, PKCI2, PPIASE
Identificadores; externos	OMIM: 186945 ; EBI: FKBP1A; GeneCards: Gen FKBP1A; UniProt: FKBP1A;
Locus	Cr. 20 p13
	Referencias: AmiGO / QuickGO
Ortólogos
Humano	Ratón
2280
P62942	n/a
NP_000792	n/a
	v; t; e;
	[editar datos en Wikidata]

La proteína 1A de unión a FK506, también denominada peptidil-prolil cis-trans isomerasa y FKBP1A, es una enzima codificada en humanos por el gen fkbp1A.^[1]

La proteína FKBP1A pertenece a la familia de las inmunofilinas, las cuales juegan un importante papel en inmunorregulación y en procesos básicos de la célula, como plegamiento de proteínas y transporte. Esta proteína es una cis-trans prolil isomerasa que se une a los inmunosupresores FK506 y rapamicina. Tiene una elevada similitud estructural y funcional con la proteína FKBP52, pero por el contrario, esta sí posee actividad inmunosupresora cuando forma un complejo con FK506. También interacciona con diversos canales de liberación de calcio intracelular, incluyendo el receptor tetramérico ryanodine de músculo esquelético. En ratón, la deleción del gen ortólogo causa un desorden congénito del corazón conocido como ventrículo izquierdo no compactado. Se han descrito diversas variantes transcripcionales de este gen, pero no se ha determinado el tamaño total de todas ellas.^[2]

Interacciones[editar]

La proteína FKBP1A ha demostrado ser capaz de interaccionar con:

Véase también[editar]

Referencias[editar]

↑ DiLella AG (Nov de 1991). «Chromosomal assignment of the human immunophilin FKBP-12 gene». Biochem Biophys Res Commun 179 (3): 1427-33. PMID 1930186.
↑ «Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa».
↑ Avila, Guillermo; Lee Eun Hui, Perez Claudio F, Allen P D, Dirksen Robert T (Jun. de 2003). «FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes». J. Biol. Chem. (United States) 278 (25): 22600-8. ISSN 0021-9258. PMID 12704193. doi:10.1074/jbc.M205866200.
↑ Bultynck, G; De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys J B (Mar. de 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». Biochem. J. (England) 354 (Pt 2): 413-22. ISSN 0264-6021. PMID 11171121.
↑ Gaburjakova, M; Gaburjakova J, Reiken S, Huang F, Marx S O, Rosemblit N, Marks A R (mayo. de 2001). «FKBP12 binding modulates ryanodine receptor channel gating». J. Biol. Chem. (United States) 276 (20): 16931-5. ISSN 0021-9258. PMID 11279144. doi:10.1074/jbc.M100856200.
↑ ^a ^b Jacinto, Estela; Loewith Robbie, Schmidt Anja, Lin Shuo, Rüegg Markus A, Hall Alan, Hall Michael N (Nov. de 2004). «Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive». Nat. Cell Biol. (England) 6 (11): 1122-8. ISSN 1465-7392. PMID 15467718. doi:10.1038/ncb1183.
↑ ^a ^b Sarbassov, D D; Ali Siraj M, Kim Do-Hyung, Guertin David A, Latek Robert R, Erdjument-Bromage Hediye, Tempst Paul, Sabatini David M (Jul. de 2004). «Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton». Curr. Biol. (England) 14 (14): 1296-302. ISSN 0960-9822. PMID 15268862. doi:10.1016/j.cub.2004.06.054.
↑ Choi, J; Chen J, Schreiber S L, Clardy J (Jul. de 1996). «Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP». Science (UNITED STATES) 273 (5272): 239-42. ISSN 0036-8075. PMID 8668994.
↑ Luker, Kathryn E; Smith Matthew C P, Luker Gary D, Gammon Seth T, Piwnica-Worms Helen, Piwnica-Worms David (Aug. de 2004). «Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals». Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (33): 12288-93. ISSN 0027-8424. PMID 15284440. doi:10.1073/pnas.0404041101.
↑ Banaszynski, Laura A; Liu Corey W, Wandless Thomas J (Apr. de 2005). «Characterization of the FKBP.rapamycin.FRB ternary complex». J. Am. Chem. Soc. (United States) 127 (13): 4715-21. ISSN 0002-7863. PMID 15796538. doi:10.1021/ja043277y.
↑ Sabers, C J; Martin M M, Brunn G J, Williams J M, Dumont F J, Wiederrecht G, Abraham R T (Jan. de 1995). «Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells». J. Biol. Chem. (UNITED STATES) 270 (2): 815-22. ISSN 0021-9258. PMID 7822316.
↑ Wang, T; Donahoe P K, Zervos A S (Jul. de 1994). «Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12». Science (UNITED STATES) 265 (5172): 674-6. ISSN 0036-8075. PMID 7518616.
↑ Liu, F; Ventura F, Doody J, Massagué J (Jul. de 1995). «Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs». Mol. Cell. Biol. (UNITED STATES) 15 (7): 3479-86. ISSN 0270-7306. PMID 7791754.
↑ Chambraud, B; Radanyi C, Camonis J H, Shazand K, Rajkowski K, Baulieu E E (Dec. de 1996). «FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin». J. Biol. Chem. (UNITED STATES) 271 (51): 32923-9. ISSN 0021-9258. PMID 8955134.
↑ Neye, H (Mar. de 2001). «Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52». Regul. Pept. (Netherlands) 97 (2-3): 147-52. ISSN 0167-0115. PMID 11164950.
↑ MacMillan, Debbi; Currie Susan, Bradley Karen N, Muir Thomas C, McCarron John G (Dec. de 2005). «In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin». J. Cell. Sci. (England) 118 (Pt 23): 5443-51. ISSN 0021-9533. PMID 16278292. doi:10.1242/jcs.02657.
↑ Cameron, A M; Nucifora F C, Fung E T, Livingston D J, Aldape R A, Ross C A, Snyder S H (Oct. de 1997). «FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain». J. Biol. Chem. (UNITED STATES) 272 (44): 27582-8. ISSN 0021-9258. PMID 9346894.

Enlaces externos[editar]

MeSH: FKBP1A (en inglés)

Datos: Q17928420

[pmid1930186-1] DiLella AG (Nov de 1991). «Chromosomal assignment of the human immunophilin FKBP-12 gene». Biochem Biophys Res Commun 179 (3): 1427-33. PMID 1930186.

[2] «Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa».

[pmid12704193-3] Avila, Guillermo; Lee Eun Hui, Perez Claudio F, Allen P D, Dirksen Robert T (Jun. de 2003). «FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes». J. Biol. Chem. (United States) 278 (25): 22600-8. ISSN 0021-9258. PMID 12704193. doi:10.1074/jbc.M205866200.

[pmid11171121-4] Bultynck, G; De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys J B (Mar. de 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». Biochem. J. (England) 354 (Pt 2): 413-22. ISSN 0264-6021. PMID 11171121.

[pmid11279144-5] Gaburjakova, M; Gaburjakova J, Reiken S, Huang F, Marx S O, Rosemblit N, Marks A R (mayo. de 2001). «FKBP12 binding modulates ryanodine receptor channel gating». J. Biol. Chem. (United States) 276 (20): 16931-5. ISSN 0021-9258. PMID 11279144. doi:10.1074/jbc.M100856200.

[pmid15467718-6] Jacinto, Estela; Loewith Robbie, Schmidt Anja, Lin Shuo, Rüegg Markus A, Hall Alan, Hall Michael N (Nov. de 2004). «Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive». Nat. Cell Biol. (England) 6 (11): 1122-8. ISSN 1465-7392. PMID 15467718. doi:10.1038/ncb1183.

[pmid15268862-7] Sarbassov, D D; Ali Siraj M, Kim Do-Hyung, Guertin David A, Latek Robert R, Erdjument-Bromage Hediye, Tempst Paul, Sabatini David M (Jul. de 2004). «Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton». Curr. Biol. (England) 14 (14): 1296-302. ISSN 0960-9822. PMID 15268862. doi:10.1016/j.cub.2004.06.054.

[pmid8662507-8] Choi, J; Chen J, Schreiber S L, Clardy J (Jul. de 1996). «Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP». Science (UNITED STATES) 273 (5272): 239-42. ISSN 0036-8075. PMID 8668994.

[pmid15284440-9] Luker, Kathryn E; Smith Matthew C P, Luker Gary D, Gammon Seth T, Piwnica-Worms Helen, Piwnica-Worms David (Aug. de 2004). «Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals». Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (33): 12288-93. ISSN 0027-8424. PMID 15284440. doi:10.1073/pnas.0404041101.

[pmid15796538-10] Banaszynski, Laura A; Liu Corey W, Wandless Thomas J (Apr. de 2005). «Characterization of the FKBP.rapamycin.FRB ternary complex». J. Am. Chem. Soc. (United States) 127 (13): 4715-21. ISSN 0002-7863. PMID 15796538. doi:10.1021/ja043277y.

[pmid7822316-11] Sabers, C J; Martin M M, Brunn G J, Williams J M, Dumont F J, Wiederrecht G, Abraham R T (Jan. de 1995). «Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells». J. Biol. Chem. (UNITED STATES) 270 (2): 815-22. ISSN 0021-9258. PMID 7822316.

[pmid7518616-12] Wang, T; Donahoe P K, Zervos A S (Jul. de 1994). «Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12». Science (UNITED STATES) 265 (5172): 674-6. ISSN 0036-8075. PMID 7518616.

[pmid7791754-13] Liu, F; Ventura F, Doody J, Massagué J (Jul. de 1995). «Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs». Mol. Cell. Biol. (UNITED STATES) 15 (7): 3479-86. ISSN 0270-7306. PMID 7791754.

[pmid8955134-14] Chambraud, B; Radanyi C, Camonis J H, Shazand K, Rajkowski K, Baulieu E E (Dec. de 1996). «FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin». J. Biol. Chem. (UNITED STATES) 271 (51): 32923-9. ISSN 0021-9258. PMID 8955134.

[pmid11164950-15] Neye, H (Mar. de 2001). «Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52». Regul. Pept. (Netherlands) 97 (2-3): 147-52. ISSN 0167-0115. PMID 11164950.

[pmid16278292-16] MacMillan, Debbi; Currie Susan, Bradley Karen N, Muir Thomas C, McCarron John G (Dec. de 2005). «In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin». J. Cell. Sci. (England) 118 (Pt 23): 5443-51. ISSN 0021-9533. PMID 16278292. doi:10.1242/jcs.02657.

[pmid9346894-17] Cameron, A M; Nucifora F C, Fung E T, Livingston D J, Aldape R A, Ross C A, Snyder S H (Oct. de 1997). «FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain». J. Biol. Chem. (UNITED STATES) 272 (44): 27582-8. ISSN 0021-9258. PMID 9346894.

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