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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
  • poly(A) RNA binding Source: UniProtKB
  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciZFISH:HS02087-MONOMER.

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

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi2287.
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

WithEntry#Exp.IntActNotes
MDM2Q009872EBI-1044081,EBI-389668
PARP2Q9UGN52EBI-1044081,EBI-2795348

Protein-protein interaction databases

BioGridi108577. 41 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 strandi111 – 117Combined sources7
Beta strandi130 – 139Combined sources10
Beta strandi144 – 147Combined sources4
Turni153 – 155Combined sources3
Turni156 – 158Combined sources3
Beta strandi162 – 171Combined sources10
Helixi173 – 179Combined sources7
Beta strandi187 – 192Combined sources6
Helixi194 – 196Combined sources3
Turni197 – 201Combined sources5
Turni204 – 207Combined sources4
Beta strandi214 – 224Combined sources11

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
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

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

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.

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi108577. 41 interactors.
IntActiQ00688. 5 interactors.
STRINGi9606.ENSP00000216330.

Chemistry databases

BindingDBiQ00688.
ChEMBLiCHEMBL4746.

PTM databases

iPTMnetiQ00688.
PhosphoSitePlusiQ00688.
SwissPalmiQ00688.

Polymorphism and mutation databases

BioMutaiFKBP3.
DMDMi232096.

Proteomic databases

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

Protocols and materials databases

DNASUi2287.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2287.
DisGeNETi2287.
GeneCardsiFKBP3.
HGNCiHGNC:3719. FKBP3.
HPAiCAB012232.
CAB012520.
HPA000864.
MIMi186947. gene.
neXtProtiNX_Q00688.
OpenTargetsiENSG00000100442.
PharmGKBiPA28160.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS02087-MONOMER.

Miscellaneous databases

ChiTaRSiFKBP3. human.
EvolutionaryTraceiQ00688.
GeneWikiiFKBP3.
GenomeRNAii2287.
PROiQ00688.
SOURCEiSearch...

Gene expression databases

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

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]
ProtoNetiSearch...

Entry informationi

Entry nameiFKBP3_HUMAN
AccessioniPrimary (citable) accession number: Q00688
Secondary accession number(s): B2R4Q9, Q14317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 30, 2016
This is version 166 of the entry and version 1 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.