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UniProtKB/Swiss-Prot entry Q00688


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FKBP3_HUMAN
Primary accession number Q00688
Secondary accession number Q14317
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 91)
Name and origin of the protein
Protein name FK506-binding protein 3
Synonyms EC 5.2.1.8
Peptidyl-prolyl cis-trans isomerase
PPIase
Rotamase
25 kDa FKBP
FKBP-25
Rapamycin-selective 25 kDa immunophilin
Gene name
Name: FKBP3
Synonyms: FKBP25
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0006-291X(05)80990-8; PubMed=1376117 [NCBI, ExPASy, EBI, Israel, Japan]
Wiederrecht G., Martin M., Sigal N., Siekierka J.J.;
"Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein.";
Biochem. Biophys. Res. Commun. 185:298-303(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0006-291X(92)90651-Z; PubMed=1374240 [NCBI, ExPASy, EBI, Israel, Japan]
Hung D.T., Schreiber S.L.;
"cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.";
Biochem. Biophys. Res. Commun. 184:733-738(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=1375932 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Y.-J., Burakoff S.J., Bierer B.E.;
"Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25.";
J. Biol. Chem. 267:10942-10945(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.
Liang J., Hung D.T., Schreiber S.L., Clardy J.;
"Structure of the human 25 kDa FK506 binding protein complexed with rapamycin.";
J. Am. Chem. Soc. 118:1231-1232(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M96256; AAA58471.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M90309; AAA58475.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M90820; AAA58474.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006904; AAP35550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016288; AAH16288.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020809; AAH20809.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00024157; -.
PIR JQ1522; JQ1522.
RefSeq NP_002004.1; -.
UniGene Hs.509226
3D structure databases
PDB
1PBK; X-ray; 2.50 A; A=109-224.[ExPASy / RCSB / EBI]
PDBsum 1PBK; -.
ModBase Q00688.
Protein-protein interaction databases
IntAct Q00688; 3.
PTM databases
PhosphoSite Q00688; -.
Enzyme and pathway databases
BRENDA 5.2.1.8; 247.
Pathway_Interaction_DB hdac_classi_pathway; Signaling events mediated by HDAC Class I.
Organism-specific databases
GeneCards GC14M044654; -.
H-InvDB HIX0011622; -.
HGNC HGNC:3719; FKBP3.
GenAtlas FKBP3.
HPA CAB012232; -.
CAB012520; -.
HPA000864; -.
MIM 186947; gene. [NCBI / EBI]
PharmGKB PA28160; -.
Gene expression databases
ArrayExpress Q00688; -.
Bgee Q00688; -.
CleanEx HS_FKBP3; -.
GermOnline ENSG00000100442; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005528; Molecular function: FK506 binding (traceable author statement from ProtInc).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0004872; Molecular function: receptor activity (traceable author statement from ProtInc).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001179; PPIase_FKBP.
Graphical view of domain structure.
PANTHER PTHR10516; PPIase_FKBP; 1.
Pfam PF00254; FKBP_C; 1.
Pfam graphical view of domain structure.
PROSITE PS50059; FKBP_PPIASE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q00688; -.
PRIDE Q00688; -.
Genome annotation databases
Ensembl ENSG00000100442; Homo sapiens. [Contig view]
GeneID 2287; -.
KEGG hsa:2287; -.
Phylogenomic databases
HOGENOM Q00688; -.
HOVERGEN Q00688; -.
OMA Q00688; SKIPPNA.
Other
NextBio 9295; -.
SOURCE FKBP3; Homo sapiens.
ProtoNet Q00688.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Isomerase; Nucleus; Phosphoprotein; Rotamase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   224  224     FK506-binding protein 3. PRO_0000075307
DOMAIN   128   224  97     PPIase FKBP-type. 
MOD_RES   152   152        Phosphoserine. 
CONFLICT   181   181        T -> A (in Ref. 3; AAA58474). 
STRAND   111   117  7      
STRAND   130   138  9      
STRAND   144   147  4      
TURN   155   157  3      
STRAND   162   165  4      
TURN   166   169  4      
HELIX   173   179  7      
STRAND   187   192  6      
HELIX   194   196  3      
TURN   197   201  5      
HELIX   204   206  3      
Sequence information
Length: 224 AA [This is the length of the unprocessed precursor] Molecular weight: 25177 Da [This is the MW of the unprocessed precursor] CRC64: C144C5AAB7EA9522 [This is a checksum on the sequence]
        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 

Q00688 in FASTA format

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