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Protein

Peptidyl-prolyl cis-trans isomerase FKBP3

Gene

FKBP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.

Catalytic activityi

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

Enzyme regulationi

Inhibited preferentially by rapamycin over FK506.

GO - Molecular functioni

  • FK506 binding Source: ProtInc
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central
  • receptor activity Source: ProtInc
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP3 (EC:5.2.1.8)
Short name:
PPIase FKBP3
Alternative name(s):
25 kDa FK506-binding protein
Short name:
25 kDa FKBP
Short name:
FKBP-25
FK506-binding protein 3
Short name:
FKBP-3
Immunophilin FKBP25
Rapamycin-selective 25 kDa immunophilin
Rotamase
Gene namesi
Name:FKBP3
Synonyms:FKBP25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:3719. FKBP3.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000100442.
PharmGKBiPA28160.

Chemistry databases

ChEMBLiCHEMBL4746.

Polymorphism and mutation databases

BioMutaiFKBP3.
DMDMi232096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000753072 – 224Peptidyl-prolyl cis-trans isomerase FKBP3Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei36PhosphoserineCombined sources1
Modified residuei99N6-acetyllysineBy similarity1
Modified residuei152PhosphoserineCombined sources1
Modified residuei170N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ00688.
MaxQBiQ00688.
PaxDbiQ00688.
PeptideAtlasiQ00688.
PRIDEiQ00688.
TopDownProteomicsiQ00688.

PTM databases

iPTMnetiQ00688.
PhosphoSitePlusiQ00688.
SwissPalmiQ00688.

Expressioni

Gene expression databases

BgeeiENSG00000100442.
CleanExiHS_FKBP3.
ExpressionAtlasiQ00688. baseline and differential.
GenevisibleiQ00688. HS.

Organism-specific databases

HPAiCAB012232.
CAB012520.
HPA000864.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi108577. 47 interactors.
IntActiQ00688. 5 interactors.
STRINGi9606.ENSP00000216330.

Chemistry databases

BindingDBiQ00688.

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 16Combined sources5
Helixi23 – 32Combined sources10
Helixi35 – 40Combined sources6
Helixi47 – 51Combined sources5
Helixi56 – 69Combined sources14
Beta strandi110 – 117Combined sources8
Beta strandi130 – 138Combined sources9
Beta strandi144 – 147Combined sources4
Turni153 – 155Combined sources3
Turni156 – 158Combined sources3
Beta strandi162 – 165Combined sources4
Beta strandi168 – 171Combined sources4
Helixi173 – 178Combined sources6
Helixi179 – 181Combined sources3
Beta strandi187 – 192Combined sources6
Helixi194 – 196Combined sources3
Turni197 – 201Combined sources5
Helixi204 – 206Combined sources3
Beta strandi214 – 223Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PBKX-ray2.50A109-224[»]
2KFVNMR-A1-73[»]
2MPHNMR-A1-224[»]
5D75X-ray1.83A109-224[»]
5GPGX-ray1.67A109-224[»]
ProteinModelPortaliQ00688.
SMRiQ00688.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini128 – 224PPIase FKBP-typePROSITE-ProRule annotationAdd BLAST97

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated

Phylogenomic databases

eggNOGiKOG0544. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000007963.
HOVERGENiHBG105391.
InParanoidiQ00688.
KOiK09570.
OMAiCWYTGSL.
OrthoDBiEOG091G02W1.
PhylomeDBiQ00688.
TreeFamiTF105293.

Family and domain databases

InterProiView protein in InterPro
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiView protein in Pfam
PF00254. FKBP_C. 1 hit.
PROSITEiView protein in PROSITE
PS50059. FKBP_PPIASE. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q00688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV
60 70 80 90 100
AKTANKDHLV TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS
110 120 130 140 150
EETLDEGPPK YTKSVLKKGD KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ
160 170 180 190 200
TSAKKKKNAK PLSFKVGVGK VIRGWDEALL TMSKGEKARL EIEPEWAYGK
210 220
KGQPDAKIPP NAKLTFEVEL VDID
Length:224
Mass (Da):25,177
Last modified:April 1, 1993 - v1
Checksum:iC144C5AAB7EA9522
GO

Sequence cautioni

The sequence AAA58474 differs from that shown. Reason: Frameshift at position 197.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti181T → A in AAA58474 (PubMed:1375932).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96256 mRNA. Translation: AAA58471.1.
M90309 mRNA. Translation: AAA58475.1.
M90820 mRNA. Translation: AAA58474.1. Frameshift.
BT006904 mRNA. Translation: AAP35550.1.
AK311915 mRNA. Translation: BAG34856.1.
CH471078 Genomic DNA. Translation: EAW65785.1.
BC016288 mRNA. Translation: AAH16288.1.
BC020809 mRNA. Translation: AAH20809.1.
CCDSiCCDS9683.1.
PIRiJQ1522.
RefSeqiNP_002004.1. NM_002013.3.
UniGeneiHs.509226.

Genome annotation databases

EnsembliENST00000216330; ENSP00000216330; ENSG00000100442.
ENST00000396062; ENSP00000379374; ENSG00000100442.
GeneIDi2287.
KEGGihsa:2287.
UCSCiuc010tqf.3. human.

Similar proteinsi

Entry informationi

Entry nameiFKBP3_HUMAN
AccessioniPrimary (citable) accession number: Q00688
Secondary accession number(s): B2R4Q9, Q14317
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: August 30, 2017
This is version 170 of the entry and version 1 of the sequence. See 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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