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Reviewed, UniProtKB/Swiss-Prot Q00688 (FKBP3_HUMAN)

Last modified March 2, 2010. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP3

Short name=PPIase FKBP3
EC=5.2.1.8
Alternative name(s):
FK506-binding protein 3
Short name=FKBP-3
Rotamase
Immunophilin FKBP25
25 kDa FK506-binding protein
Short name=25 kDa FKBP
Short name=FKBP-25
Rapamycin-selective 25 kDa immunophilin
Gene names
Name:FKBP3
Synonyms:FKBP25
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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 activity

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

Enzyme regulation

Inhibited preferentially by rapamycin over FK506.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Sequence caution

The sequence AAA58474.1 differs from that shown. Reason: Frameshift at position 197.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFK506 binding Ref.2

Traceable author statement. Source: ProtInc

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

receptor activity Ref.2

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 224223Peptidyl-prolyl cis-trans isomerase FKBP3
PRO_0000075307

Regions

Domain128 – 22497PPIase FKBP-type

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue1521Phosphoserine Ref.8
Modified residue1601N6-acetyllysine Ref.11
Modified residue1701N6-acetyllysine Ref.11

Experimental info

Sequence conflict1811T → A in AAA58474. Ref.3

Secondary structure

..................... 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00688-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: C144C5AAB7EA9522

FASTA22425,177
        10         20         30         40         50         60 
MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV 

        70         80         90        100        110        120 
TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD 

       130        140        150        160        170        180 
KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL 

       190        200        210        220 
TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID 

« Hide

References

« Hide 'large scale' references
[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: 1376117] [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: 1374240] [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: 1375932] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle and Skin.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, MASS SPECTROMETRY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-160 AND LYS-170, MASS SPECTROMETRY.
[12]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00024157.
PIRJQ1522.
RefSeqNP_002004.1.
UniGeneHs.509226

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PBKX-ray2.50A109-224[»]
2KFVNMR-A1-73[»]
SMRQ00688. Positions 78-224.
ModBaseSearch...

Protein-protein interaction databases

IntActQ00688. 3 interactions.
STRINGQ00688.

PTM databases

PhosphoSiteQ00688.

Proteomic databases

PeptideAtlasQ00688.
PRIDEQ00688.

Genome annotation databases

EnsemblENST00000216330; ENSP00000216330; ENSG00000100442; Homo sapiens. [Genome view]
ENST00000396062; ENSP00000379374; ENSG00000100442; Homo sapiens. [Genome view]
GeneID2287.
KEGGhsa:2287.
UCSCuc001wwb.1. human.

Organism-specific databases

CTD2287.
GeneCardsGC14M044654.
H-InvDBHIX0011622.
HGNCHGNC:3719. FKBP3.
HPACAB012232.
CAB012520.
HPA000864.
MIM186947. gene.
PharmGKBPA28160.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13468.
HOGENOMHBG731200.
HOVERGENHBG105391.
InParanoidQ00688.
OMASKIPPNA.
OrthoDBEOG95HVHJ.
PhylomeDBQ00688.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.
Pathway_Interaction_DBhdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpressQ00688.
BgeeQ00688.
CleanExHS_FKBP3.
GenevestigatorQ00688.
GermOnlineENSG00000100442. Homo sapiens.

Family and domain databases

InterProIPR001179. PPIase_FKBP.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio9295.
SOURCESearch...

Entry information

Entry nameFKBP3_HUMAN
AccessionPrimary (citable) accession number: Q00688
Secondary accession number(s): B2R4Q9, Q14317
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: March 2, 2010
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents