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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

  1. FK506 binding Source: GO_Central
  2. peptidyl-prolyl cis-trans isomerase activity Source: GO_Central
  3. poly(A) RNA binding Source: UniProtKB
  4. receptor activity Source: ProtInc

GO - Biological processi

  1. chaperone-mediated protein folding Source: GO_Central
  2. protein peptidyl-prolyl isomerization Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, 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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:3719. FKBP3.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: GO_Central
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 224223Peptidyl-prolyl cis-trans isomerase FKBP3PRO_0000075307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei170 – 1701N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ00688.
PaxDbiQ00688.
PeptideAtlasiQ00688.
PRIDEiQ00688.

PTM databases

PhosphoSiteiQ00688.

Expressioni

Gene expression databases

BgeeiQ00688.
CleanExiHS_FKBP3.
ExpressionAtlasiQ00688. baseline and differential.
GenevestigatoriQ00688.

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. 38 interactions.
IntActiQ00688. 3 interactions.
STRINGi9606.ENSP00000216330.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 165Combined sources
Helixi23 – 3210Combined sources
Helixi35 – 406Combined sources
Helixi47 – 515Combined sources
Helixi56 – 6914Combined sources
Beta strandi111 – 1177Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi144 – 1474Combined sources
Turni155 – 1573Combined sources
Beta strandi162 – 1654Combined sources
Turni166 – 1694Combined sources
Helixi173 – 1797Combined sources
Beta strandi187 – 1926Combined sources
Helixi194 – 1963Combined sources
Turni197 – 2015Combined sources
Helixi204 – 2063Combined sources
Beta strandi214 – 22411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBKX-ray2.50A109-224[»]
2KFVNMR-A1-73[»]
ProteinModelPortaliQ00688.
SMRiQ00688. Positions 1-73, 109-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini128 – 22497PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000007963.
HOVERGENiHBG105391.
InParanoidiQ00688.
KOiK09570.
OMAiTMSKGET.
OrthoDBiEOG7BZVT6.
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 AAA58474.1 differs from that shown. Reason: Frameshift at position 197. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811T → A in AAA58474. (PubMed:1375932)Curated

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.2. human.

Polymorphism databases

DMDMi232096.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBKX-ray2.50A109-224[»]
2KFVNMR-A1-73[»]
ProteinModelPortaliQ00688.
SMRiQ00688. Positions 1-73, 109-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108577. 38 interactions.
IntActiQ00688. 3 interactions.
STRINGi9606.ENSP00000216330.

Chemistry

BindingDBiQ00688.
ChEMBLiCHEMBL4746.

PTM databases

PhosphoSiteiQ00688.

Polymorphism databases

DMDMi232096.

Proteomic databases

MaxQBiQ00688.
PaxDbiQ00688.
PeptideAtlasiQ00688.
PRIDEiQ00688.

Protocols and materials databases

DNASUi2287.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216330; ENSP00000216330; ENSG00000100442.
ENST00000396062; ENSP00000379374; ENSG00000100442.
GeneIDi2287.
KEGGihsa:2287.
UCSCiuc010tqf.2. human.

Organism-specific databases

CTDi2287.
GeneCardsiGC14M045584.
HGNCiHGNC:3719. FKBP3.
HPAiCAB012232.
CAB012520.
HPA000864.
MIMi186947. gene.
neXtProtiNX_Q00688.
PharmGKBiPA28160.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000007963.
HOVERGENiHBG105391.
InParanoidiQ00688.
KOiK09570.
OMAiTMSKGET.
OrthoDBiEOG7BZVT6.
PhylomeDBiQ00688.
TreeFamiTF105293.

Miscellaneous databases

ChiTaRSiFKBP3. human.
EvolutionaryTraceiQ00688.
GeneWikiiFKBP3.
GenomeRNAii2287.
NextBioi9295.
PROiQ00688.
SOURCEiSearch...

Gene expression databases

BgeeiQ00688.
CleanExiHS_FKBP3.
ExpressionAtlasiQ00688. baseline and differential.
GenevestigatoriQ00688.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein."
    Wiederrecht G., Martin M., Sigal N., Siekierka J.J.
    Biochem. Biophys. Res. Commun. 185:298-303(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein."
    Hung D.T., Schreiber S.L.
    Biochem. Biophys. Res. Commun. 184:733-738(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25."
    Jin Y.-J., Burakoff S.J., Bierer B.E.
    J. Biol. Chem. 267:10942-10945(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymus.
  4. "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].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Skeletal muscle and Skin.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structure of the human 25 kDa FK506 binding protein complexed with rapamycin."
    Liang J., Hung D.T., Schreiber S.L., Clardy J.
    J. Am. Chem. Soc. 118:1231-1232(1996)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.

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: February 4, 2015
This is version 148 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

External Data

Dasty 3

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 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.