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P62942

- FKB1A_HUMAN

UniProt

P62942 - FKB1A_HUMAN

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Protein
Peptidyl-prolyl cis-trans isomerase FKBP1A
Gene
FKBP1A, FKBP1, FKBP12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.2 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by both FK506 and rapamycin.

GO - Molecular functioni

  1. FK506 binding Source: BHF-UCL
  2. SMAD binding Source: BHF-UCL
  3. activin binding Source: BHF-UCL
  4. ion channel binding Source: BHF-UCL
  5. macrolide binding Source: BHF-UCL
  6. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
  7. protein binding Source: UniProtKB
  8. signal transducer activity Source: UniProtKB
  9. transforming growth factor beta receptor binding Source: BHF-UCL
  10. type I transforming growth factor beta receptor binding Source: BHF-UCL

GO - Biological processi

  1. 'de novo' protein folding Source: BHF-UCL
  2. SMAD protein complex assembly Source: BHF-UCL
  3. T cell activation Source: BHF-UCL
  4. amyloid fibril formation Source: BHF-UCL
  5. calcium ion transmembrane transport Source: BHF-UCL
  6. chaperone-mediated protein folding Source: RefGenome
  7. extracellular fibril organization Source: BHF-UCL
  8. heart morphogenesis Source: BHF-UCL
  9. heart trabecula formation Source: BHF-UCL
  10. negative regulation of protein phosphatase type 2B activity Source: BHF-UCL
  11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  12. positive regulation of protein binding Source: BHF-UCL
  13. positive regulation of protein ubiquitination Source: BHF-UCL
  14. protein folding Source: UniProtKB
  15. protein maturation by protein folding Source: BHF-UCL
  16. protein peptidyl-prolyl isomerization Source: BHF-UCL
  17. protein refolding Source: BHF-UCL
  18. regulation of activin receptor signaling pathway Source: BHF-UCL
  19. regulation of amyloid precursor protein catabolic process Source: ParkinsonsUK-UCL
  20. regulation of immune response Source: BHF-UCL
  21. regulation of protein localization Source: ParkinsonsUK-UCL
  22. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  23. transforming growth factor beta receptor signaling pathway Source: Reactome
  24. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_169445. TGFBR1 LBD Mutants in Cancer.
SignaLinkiP62942.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
Short name:
PPIase FKBP1A
Alternative name(s):
12 kDa FK506-binding protein
Short name:
12 kDa FKBP
Short name:
FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name:
FKBP-1A
Immunophilin FKBP12
Rotamase
Gene namesi
Name:FKBP1A
Synonyms:FKBP1, FKBP12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:3711. FKBP1A.

Subcellular locationi

GO - Cellular componenti

  1. Z disc Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. cytosol Source: BHF-UCL
  4. endoplasmic reticulum membrane Source: RefGenome
  5. extracellular vesicular exosome Source: UniProt
  6. membrane Source: BHF-UCL
  7. terminal cisterna Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28153.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1A
PRO_0000075289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei9 – 91Phosphoserine2 Publications
Modified residuei53 – 531N6-acetyllysine; alternate By similarity
Modified residuei53 – 531N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62942.
PaxDbiP62942.
PRIDEiP62942.

PTM databases

PhosphoSiteiP62942.

Miscellaneous databases

PMAP-CutDBP62942.

Expressioni

Gene expression databases

ArrayExpressiP62942.
BgeeiP62942.
CleanExiHS_FKBP1A.
GenevestigatoriP62942.

Organism-specific databases

HPAiCAB004639.
HPA051798.

Interactioni

Subunit structurei

Interacts directly with RYR1, RYR2 and RYR3. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) By similarity. Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with ACVR1B and SMAD7.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACVR1BP368962EBI-1027571,EBI-1384128
MTORP423452EBI-1027571,EBI-359260
SMAD7O151053EBI-1027571,EBI-3861591

Protein-protein interaction databases

BioGridi108570. 25 interactions.
DIPiDIP-29710N.
IntActiP62942. 8 interactions.
MINTiMINT-87893.
STRINGi9606.ENSP00000371138.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97
Beta strandi22 – 3110
Beta strandi36 – 394
Helixi40 – 434
Beta strandi47 – 504
Turni51 – 544
Helixi58 – 647
Beta strandi72 – 776
Helixi79 – 813
Turni82 – 865
Turni89 – 913
Beta strandi98 – 10811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7XX-ray2.00A/B2-108[»]
1B6CX-ray2.60A/C/E/G2-108[»]
1BKFX-ray1.60A2-108[»]
1BL4X-ray1.90A/B2-108[»]
1D6OX-ray1.85A/B2-108[»]
1D7HX-ray1.90A/B2-108[»]
1D7IX-ray1.90A/B2-108[»]
1D7JX-ray1.85A/B2-108[»]
1EYMX-ray2.00A/B2-108[»]
1F40NMR-A2-108[»]
1FAPX-ray2.70A2-108[»]
1FKBX-ray1.70A2-108[»]
1FKDX-ray1.72A2-108[»]
1FKFX-ray1.70A2-108[»]
1FKGX-ray2.00A2-108[»]
1FKHX-ray1.95A2-108[»]
1FKIX-ray2.20A/B2-108[»]
1FKJX-ray1.70A2-108[»]
1FKRNMR-A2-108[»]
1FKSNMR-A2-108[»]
1FKTNMR-A2-108[»]
1J4HX-ray1.80A2-108[»]
1J4IX-ray1.80A2-108[»]
1J4RX-ray1.80A/B/D2-108[»]
1NSGX-ray2.20A2-108[»]
1QPFX-ray2.50A/D2-108[»]
1QPLX-ray2.90A/C2-108[»]
2DG3X-ray1.70A2-108[»]
2DG4X-ray1.70A2-108[»]
2DG9X-ray1.70A2-108[»]
2FAPX-ray2.20A2-108[»]
2FKEX-ray1.72A2-108[»]
2PPNX-ray0.92A2-108[»]
2PPOX-ray1.29A2-108[»]
2PPPX-ray0.94A2-108[»]
2RSENMR-A2-108[»]
3FAPX-ray1.85A2-108[»]
3H9RX-ray2.35B1-108[»]
3MDYX-ray2.05B/D1-108[»]
4DH0X-ray2.10A2-108[»]
4FAPX-ray2.80A2-108[»]
4IPXX-ray1.70A2-108[»]
4N19X-ray1.20A2-108[»]
ProteinModelPortaliP62942.
SMRiP62942. Positions 2-108.

Miscellaneous databases

EvolutionaryTraceiP62942.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10889PPIase FKBP-type
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0545.
HOVERGENiHBG051623.
InParanoidiP62942.
KOiK09568.
OMAiSPQKGDT.
OrthoDBiEOG7ZGX5T.
PhylomeDBiP62942.
TreeFamiTF105291.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62942-1 [UniParc]FASTAAdd to Basket

« Hide

MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM    50
LGKQEVIRGW EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF 100
DVELLKLE 108
Length:108
Mass (Da):11,951
Last modified:January 23, 2007 - v2
Checksum:i9CC8493C802540B4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601W → R in CAG28541. 1 Publication
Sequence conflicti91 – 911I → V in CAG28541. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34539 mRNA. Translation: AAA35844.1.
M92423, M92422 Genomic DNA. Translation: AAA58476.1.
M93060 Genomic DNA. No translation available.
X55741 Genomic DNA. Translation: CAA39272.1.
M80199 Genomic DNA. Translation: AAA58472.1.
X52220 mRNA. Translation: CAA36462.1.
BT007066 mRNA. Translation: AAP35729.1.
CR407613 mRNA. Translation: CAG28541.1.
CR542168 mRNA. Translation: CAG46965.1.
AL136531, AL109658 Genomic DNA. Translation: CAH72382.1.
AL109658, AL136531 Genomic DNA. Translation: CAI22728.1.
CH471133 Genomic DNA. Translation: EAX10633.1.
CH471133 Genomic DNA. Translation: EAX10634.1.
CH471133 Genomic DNA. Translation: EAX10635.1.
BC001925 mRNA. Translation: AAH01925.3.
BC005147 mRNA. Translation: AAH05147.1.
CCDSiCCDS13014.1.
PIRiI65284. A35780.
RefSeqiNP_000792.1. NM_000801.4.
NP_463460.1. NM_054014.3.
UniGeneiHs.471933.
Hs.700839.

Genome annotation databases

EnsembliENST00000381719; ENSP00000371138; ENSG00000088832.
ENST00000400137; ENSP00000383003; ENSG00000088832.
GeneIDi2280.
KEGGihsa:2280.
UCSCiuc002wey.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34539 mRNA. Translation: AAA35844.1 .
M92423 , M92422 Genomic DNA. Translation: AAA58476.1 .
M93060 Genomic DNA. No translation available.
X55741 Genomic DNA. Translation: CAA39272.1 .
M80199 Genomic DNA. Translation: AAA58472.1 .
X52220 mRNA. Translation: CAA36462.1 .
BT007066 mRNA. Translation: AAP35729.1 .
CR407613 mRNA. Translation: CAG28541.1 .
CR542168 mRNA. Translation: CAG46965.1 .
AL136531 , AL109658 Genomic DNA. Translation: CAH72382.1 .
AL109658 , AL136531 Genomic DNA. Translation: CAI22728.1 .
CH471133 Genomic DNA. Translation: EAX10633.1 .
CH471133 Genomic DNA. Translation: EAX10634.1 .
CH471133 Genomic DNA. Translation: EAX10635.1 .
BC001925 mRNA. Translation: AAH01925.3 .
BC005147 mRNA. Translation: AAH05147.1 .
CCDSi CCDS13014.1.
PIRi I65284. A35780.
RefSeqi NP_000792.1. NM_000801.4.
NP_463460.1. NM_054014.3.
UniGenei Hs.471933.
Hs.700839.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A7X X-ray 2.00 A/B 2-108 [» ]
1B6C X-ray 2.60 A/C/E/G 2-108 [» ]
1BKF X-ray 1.60 A 2-108 [» ]
1BL4 X-ray 1.90 A/B 2-108 [» ]
1D6O X-ray 1.85 A/B 2-108 [» ]
1D7H X-ray 1.90 A/B 2-108 [» ]
1D7I X-ray 1.90 A/B 2-108 [» ]
1D7J X-ray 1.85 A/B 2-108 [» ]
1EYM X-ray 2.00 A/B 2-108 [» ]
1F40 NMR - A 2-108 [» ]
1FAP X-ray 2.70 A 2-108 [» ]
1FKB X-ray 1.70 A 2-108 [» ]
1FKD X-ray 1.72 A 2-108 [» ]
1FKF X-ray 1.70 A 2-108 [» ]
1FKG X-ray 2.00 A 2-108 [» ]
1FKH X-ray 1.95 A 2-108 [» ]
1FKI X-ray 2.20 A/B 2-108 [» ]
1FKJ X-ray 1.70 A 2-108 [» ]
1FKR NMR - A 2-108 [» ]
1FKS NMR - A 2-108 [» ]
1FKT NMR - A 2-108 [» ]
1J4H X-ray 1.80 A 2-108 [» ]
1J4I X-ray 1.80 A 2-108 [» ]
1J4R X-ray 1.80 A/B/D 2-108 [» ]
1NSG X-ray 2.20 A 2-108 [» ]
1QPF X-ray 2.50 A/D 2-108 [» ]
1QPL X-ray 2.90 A/C 2-108 [» ]
2DG3 X-ray 1.70 A 2-108 [» ]
2DG4 X-ray 1.70 A 2-108 [» ]
2DG9 X-ray 1.70 A 2-108 [» ]
2FAP X-ray 2.20 A 2-108 [» ]
2FKE X-ray 1.72 A 2-108 [» ]
2PPN X-ray 0.92 A 2-108 [» ]
2PPO X-ray 1.29 A 2-108 [» ]
2PPP X-ray 0.94 A 2-108 [» ]
2RSE NMR - A 2-108 [» ]
3FAP X-ray 1.85 A 2-108 [» ]
3H9R X-ray 2.35 B 1-108 [» ]
3MDY X-ray 2.05 B/D 1-108 [» ]
4DH0 X-ray 2.10 A 2-108 [» ]
4FAP X-ray 2.80 A 2-108 [» ]
4IPX X-ray 1.70 A 2-108 [» ]
4N19 X-ray 1.20 A 2-108 [» ]
ProteinModelPortali P62942.
SMRi P62942. Positions 2-108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108570. 25 interactions.
DIPi DIP-29710N.
IntActi P62942. 8 interactions.
MINTi MINT-87893.
STRINGi 9606.ENSP00000371138.

Chemistry

BindingDBi P62942.
ChEMBLi CHEMBL1902.
DrugBanki DB00337. Pimecrolimus.
DB00877. Sirolimus.
DB00864. Tacrolimus.
GuidetoPHARMACOLOGYi 2609.

PTM databases

PhosphoSitei P62942.

Proteomic databases

MaxQBi P62942.
PaxDbi P62942.
PRIDEi P62942.

Protocols and materials databases

DNASUi 2280.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381719 ; ENSP00000371138 ; ENSG00000088832 .
ENST00000400137 ; ENSP00000383003 ; ENSG00000088832 .
GeneIDi 2280.
KEGGi hsa:2280.
UCSCi uc002wey.3. human.

Organism-specific databases

CTDi 2280.
GeneCardsi GC20M001349.
HGNCi HGNC:3711. FKBP1A.
HPAi CAB004639.
HPA051798.
MIMi 186945. gene.
neXtProti NX_P62942.
PharmGKBi PA28153.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0545.
HOVERGENi HBG051623.
InParanoidi P62942.
KOi K09568.
OMAi SPQKGDT.
OrthoDBi EOG7ZGX5T.
PhylomeDBi P62942.
TreeFami TF105291.

Enzyme and pathway databases

Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_169263. TGFBR1 KD Mutants in Cancer.
REACT_169440. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_169445. TGFBR1 LBD Mutants in Cancer.
SignaLinki P62942.

Miscellaneous databases

EvolutionaryTracei P62942.
GeneWikii FKBP1A.
GenomeRNAii 2280.
NextBioi 9269.
PMAP-CutDB P62942.
PROi P62942.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62942.
Bgeei P62942.
CleanExi HS_FKBP1A.
Genevestigatori P62942.

Family and domain databases

InterProi IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF00254. FKBP_C. 1 hit.
[Graphical view ]
PROSITEi PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin."
    Maki N., Sekiguchi F., Nishimaki J., Miwa K., Hayano T., Takahashi N., Suzuki M.
    Proc. Natl. Acad. Sci. U.S.A. 87:5440-5443(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and overexpression of the human FK506-binding protein FKBP."
    Standaert R.F., Galat A., Verdine G.L., Schreiber S.L.
    Nature 346:671-674(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains."
    Dilella A.G., Craig R.J.
    Biochemistry 30:8512-8517(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12."
    Peattie D.A., Hsiao K., Benasutti M., Lippke J.A.
    Gene 150:251-257(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Placenta.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Placenta.
  10. "The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase."
    Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y., Cryan J., Hodges P.J., Sigal N.H.
    J. Biol. Chem. 265:21011-21015(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-52.
  11. "A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase."
    Harding M.W., Galat A., Uehling D.E., Schreiber S.L.
    Nature 341:758-760(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17.
  12. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14.
    Tissue: Platelet.
  13. "Mechanism of TGFbeta receptor inhibition by FKBP12."
    Chen Y.G., Liu F., Massague J.
    EMBO J. 16:3866-3876(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TGFBR1 INHIBITION, INTERACTION WITH TGFBR1.
  14. "Further characterization of the type 3 ryanodine receptor (RyR3) purified from rabbit diaphragm."
    Murayama T., Oba T., Katayama E., Oyamada H., Oguchi K., Kobayashi M., Otsuka K., Ogawa Y.
    J. Biol. Chem. 274:17297-17308(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RYR3.
  15. "FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."
    Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.
    J. Mol. Endocrinol. 36:569-579(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACVR1B AND SMAD7, FUNCTION.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Characterization of the binding sites for the interactions between FKBP12 and intracellular calcium release channels."
    Wen H., Kang S., Song Y., Song Y., Yang H.J., Kim M.H., Park S.
    Arch. Biochem. Biophys. 517:37-42(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RYR3.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein."
    Rosen M.K., Michnick S.W., Karplus M., Schreiber S.L.
    Biochemistry 30:4774-4789(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  23. "Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin."
    Michnick S.W., Rosen M.K., Wandless T.J., Karplus M., Schreiber S.L.
    Science 252:836-839(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  24. "Solution structure of FK506 bound to FKBP-12."
    Lepre C.A., Thomson J.A., Moore J.M.
    FEBS Lett. 302:89-96(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  25. "1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin."
    Xu R.X., Nettesheim D., Olejniczak E.T., Meadows R., Gemmecker G., Fesik S.W.
    Biopolymers 33:535-550(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN.
  26. "Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex."
    van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.
    Science 252:839-842(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  27. "Atomic structure of the rapamycin human immunophilin FKBP-12 complex."
    van Duyne G.D., Standaert R.F., Schreiber S.L., Clardy J.
    J. Am. Chem. Soc. 113:7433-7434(1991)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  28. "Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin."
    van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.
    J. Mol. Biol. 229:105-124(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
  29. "Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12."
    Huse M., Chen Y.-G., Massague J., Kuriyan J.
    Cell 96:425-436(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-107 IN COMPLEX WITH TGFBR1.
  30. "X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies."
    Burkhard P., Taylor P., Walkinshaw M.D.
    J. Mol. Biol. 295:953-962(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

Entry informationi

Entry nameiFKB1A_HUMAN
AccessioniPrimary (citable) accession number: P62942
Secondary accession number(s): D3DVW6
, P20071, Q4VC47, Q6FGD9, Q6LEU3, Q9H103, Q9H566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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