FKBP1A

FKBP1A
Strwythurau
PDB	Human UniProt search: PDBe RCSB
Rhestr o ddynodwyr PDB
	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
Dynodwyr
Cyfenwau	FKBP1A, FKBP-12, FKBP-1A, FKBP1, FKBP12, PKC12, PKCI2, PPIASE, FK506 binding protein 1A, FKBP prolyl isomerase 1A
Dynodwyr allanol	OMIM: 186945 HomoloGene: 105139 GeneCards: FKBP1A
Patrwm RNA pattern
	; ; ; ;
	Rhagor o gyfeiriadau
Ontoleg y genyn
Gweithrediad moleciwlaidd	• calcium channel inhibitor activity; • activin binding; • isomerase activity; • macrolide binding; • peptidyl-prolyl cis-trans isomerase activity; • signal transducer activity; • GO:0001948, GO:0016582 protein binding; • SMAD binding; • transforming growth factor beta receptor binding; • FK506 binding; • enzyme binding; • Hsp70 protein binding; • type I transforming growth factor beta receptor binding; • protein homodimerization activity; • transmembrane transporter binding;
Cydrannau o'r gell	• cytoplasm; • terminal cisterna; • Z discdkac; • extracellular exosome; • extrinsic component of organelle membrane; • cytoplasmic side of membrane; • ryanodine receptor complex; • cytosol; • bilen; • sarcoplasmic reticulum; • sarcoplasmic reticulum membrane; • intracellular membrane-bounded organelle; • axon terminus;
Prosesau biolegol	• SMAD protein complex assembly; • amyloid fibril formation; • regulation of activin receptor signaling pathway; • protein maturation by protein folding; • regulation of amyloid precursor protein catabolic process; • protein peptidyl-prolyl isomerization; • negative regulation of ryanodine-sensitive calcium-release channel activity; • regulation of protein localization; • calcium ion transmembrane transport; • protein refolding; • regulation of immune response; • positive regulation of I-kappaB kinase/NF-kappaB signaling; • negative regulation of release of sequestered calcium ion into cytosol; • positive regulation of protein binding; • positive regulation of protein ubiquitination; • 'de novo' protein folding; • transforming growth factor beta receptor signaling pathway; • T cell activation; • chaperone-mediated protein folding; • supramolecular fiber organization; • negative regulation of phosphoprotein phosphatase activity; • protein folding; • GO:0033128 negative regulation of protein phosphorylation; • heart morphogenesis; • muscle contraction; • response to iron ion; • cytokine-mediated signaling pathway; • response to caffeine; • T cell proliferation; • release of sequestered calcium ion into cytosol; • ventricular cardiac muscle tissue morphogenesis; • regulation of ryanodine-sensitive calcium-release channel activity; • heart trabecula formation;
	Sources:Amigo / QuickGO
Orthologau
	2280
	n/a
	ENSG00000088832
	n/a
	P62942
	n/a
	NM_054014; NM_000801; NM_001199786
	n/a
	NP_000792; NP_001186715; NP_463460
	n/a
	Wicidata
Gweld/Golygu Bod dynol

Protein sy'n cael ei godio yn y corff dynol gan y genyn FKBP1A yw FKBP1A a elwir hefyd yn FK506 binding protein 1A (Saesneg). Segment o DNA yw'r genyn, sy'n amgodio ffwythiant arbennig. Mae'r genyn yma wedi ei leoli ar yr edefyn ôl o gromosom dynol 20, band 20p13.^[2]

Cyfystyron

Yn aml mae gan enynnau lawer o gyfystyron. Mae hyn oherwydd eu bod yn aml yn cael eu darganfod gan nifer o bobl mewn cyd-destunau gwahanol heb wybod mai'r un genynnau oeddyn nhw. Hefyd mae gan wahanol gymunedau gwyddonol safonau gwahanol ar gyfer enwi genynnau. Dyma restr o gyfystyron ar gyfer y genyn FKBP1A.

FKBP1
PKC12
PKCI2
FKBP12
PPIASE
FKBP-12
FKBP-1A

Llyfryddiaeth

"Dynamics of Aromatic Side Chains in the Active Site of FKBP12. ". Biochemistry. 2017. PMID 27936610.
"Electrostatic effects on the folding stability of FKBP12. ". Protein Eng Des Sel. 2016. PMID 27381026.
"Role of FK506 binding protein 12 in morphine-induced Î¼-opioid receptor internalization and desensitization. ". Neurosci Lett. 2014. PMID 24607931.
"Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6. ". Acta Crystallogr D Biol Crystallogr. 2014. PMID 24598733.
"FKBP12.6 activates RyR1: investigating the amino acid residues critical for channel modulation.". Biophys J. 2014. PMID 24559985.

Cyfeiriadau

[1] "Human PubMed Reference:".

[2] FKBP1A - Cronfa NCBI

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[2]