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UniProtKB/Swiss-Prot entry Q02790


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

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Entry information
Entry name FKBP4_HUMAN
Primary accession number Q02790
Secondary accession numbers Q9UCP1 Q9UCV7
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 110)
Name and origin of the protein
Protein name FK506-binding protein 4
Synonyms EC 5.2.1.8
Peptidyl-prolyl cis-trans isomerase
PPIase
Rotamase
HSP-binding immunophilin
HBI
FKBP52 protein
52 kDa FK506-binding protein
FKBP59
p59 protein
Gene name
Name: FKBP4
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], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
DOI=10.1073/pnas.89.22.10974; PubMed=1279700 [NCBI, ExPASy, EBI, Israel, Japan]
Peattie D.A., Harding M.W., Fleming M.A., Decenzo M.T., Lippke J.A., Livingston D.J., Benasutti M.;
"Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes.";
Proc. Natl. Acad. Sci. U.S.A. 89:10974-10978(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Lymph, and Uterus;
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).
[3]
PROTEIN SEQUENCE OF 2-25, SUBUNIT, AND FUNCTION.
TISSUE=Thymus;
DOI=10.1126/science.1376003; PubMed=1376003 [NCBI, ExPASy, EBI, Israel, Japan]
Tai P.-K.K., Albers M.W., Chang H., Faber L.E., Schreiber S.L.;
"Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex.";
Science 256:1315-1318(1992).
[4]
PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
TISSUE=Lymphocyte;
DOI=10.1021/bi00473a021; PubMed=2378870 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez E.R., Faber L.E., Henzel W.J., Pratt W.B.;
"The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins.";
Biochemistry 29:5145-5152(1990).
[5]
PROTEIN SEQUENCE OF 2-18.
TISSUE=T-cell;
PubMed=1371107 [NCBI, ExPASy, EBI, Israel, Japan]
Yem A.W., Tomasselli A.G., Heinrikson R.L., Zurcher-Neely H., Ruff V.A., Johnson R.A., Deibel M.R. Jr.;
"The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13.";
J. Biol. Chem. 267:2868-2871(1992).
[6]
PROTEIN SEQUENCE OF 16-32.
PubMed=1383226 [NCBI, ExPASy, EBI, Israel, Japan]
Wiederrecht G., Hung S., Chan H.K., Marcy A., Martin M., Calaycay J., Boulton D., Sigal N., Kincaid R.L., Siekierka J.J.;
"Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex.";
J. Biol. Chem. 267:21753-21760(1992).
[7]
INTERACTION WITH HSF1.
DOI=10.1074/jbc.M105931200; PubMed=11583998 [NCBI, ExPASy, EBI, Israel, Japan]
Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R.;
"Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex.";
J. Biol. Chem. 276:45791-45799(2001).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, 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).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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
M88279; AAA36111.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001786; AAH01786.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002887; AAH02887.2; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007924; AAH07924.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00219005; -.
PIR A46372; A46372.
RefSeq NP_002005.1; -.
UniGene Hs.524183
3D structure databases
PDB
1N1A; X-ray; 2.40 A; A/B=2-139.[ExPASy / RCSB / EBI]
1P5Q; X-ray; 2.80 A; A/B/C=146-458.[ExPASy / RCSB / EBI]
1Q1C; X-ray; 1.90 A; A=2-259.[ExPASy / RCSB / EBI]
1QZ2; X-ray; 3.00 A; A/B/C=145-458.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1N1A; -.
1P5Q; -.
1Q1C; -.
1QZ2; -.
ModBase Q02790.
Protein-protein interaction databases
IntAct Q02790; 2.
PTM databases
PhosphoSite Q02790; -.
Enzyme and pathway databases
BRENDA 5.2.1.8; 247.
Pathway_Interaction_DB ar_pathway; Coregulation of Androgen receptor activity.
2D gel databases
REPRODUCTION-2DPAGE IPI00219005; -.
Organism-specific databases
GeneCards GC12P002774; -.
H-InvDB HIX0010330; -.
HGNC HGNC:3720; FKBP4.
GenAtlas FKBP4.
HPA CAB017441; -.
HPA006148; -.
MIM 600611; gene. [NCBI / EBI]
PharmGKB PA28161; -.
Gene expression databases
ArrayExpress Q02790; -.
Bgee Q02790; -.
CleanEx HS_FKBP4; -.
GermOnline ENSG00000004478; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0005528; Molecular function: FK506 binding (traceable author statement from UniProtKB).
GO:0031072; Molecular function: heat shock protein binding (inferred from physical interaction from UniProtKB).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0030674; Molecular function: protein binding, bridging (traceable author statement from ProtInc).
GO:0006457; Biological process: protein folding (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001179; PPIase_FKBP.
IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
IPR019734; TPR_repeat.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
PANTHER PTHR10516; PPIase_FKBP; 1.
Pfam PF00254; FKBP_C; 2.
PF00515; TPR_1; 3.
Pfam graphical view of domain structure.
SMART SM00028; TPR; 3.
SMART graphical view of domain structure.
PROSITE PS50059; FKBP_PPIASE; 2.
PS50005; TPR; 3.
PS50293; TPR_REGION; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q02790; -.
PRIDE Q02790; -.
Genome annotation databases
Ensembl ENSG00000004478; Homo sapiens. [Contig view]
GeneID 2288; -.
KEGG hsa:2288; -.
Phylogenomic databases
HOGENOM Q02790; -.
HOVERGEN Q02790; -.
OMA Q02790; EHSIVYL.
Other
DrugBank DB01093; Dimethyl sulfoxide.
NextBio 9299; -.
SOURCE FKBP4; Homo sapiens.
ProtoNet Q02790.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Isomerase; Nucleus; Phosphoprotein; Polymorphism; Repeat; Rotamase; TPR repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   459  458     FK506-binding protein 4. PRO_0000075318
DOMAIN   50   138  89     PPIase FKBP-type 1. 
DOMAIN   167   253  87     PPIase FKBP-type 2. 
REPEAT   270   303  34     TPR 1. 
REPEAT   319   352  34     TPR 2. 
REPEAT   353   386  34     TPR 3. 
MOD_RES   143   143        Phosphothreonine; by CK2 (By similarity). 
MOD_RES   274   274        N6-acetyllysine. 
MOD_RES   451   451        Phosphoserine. 
MOD_RES   453   453        Phosphoserine. 
VARIANT   436   436  1     T -> P (in dbSNP:rs1042228 [NCBI]). VAR_050624 
STRAND   30    39  10      
STRAND   52    61  10      
STRAND   66    69  4      
STRAND   77    80  4      
TURN   81    84  4      
HELIX   88    94  7      
STRAND   102   107  6      
HELIX   109   111  3      
TURN   112   116  5      
TURN   119   121  3      
STRAND   128   138  11      
STRAND   147   156  10      
STRAND   169   178  10      
STRAND   181   191  11      
HELIX   195   198  4      
HELIX   202   208  7      
STRAND   216   221  6      
HELIX   223   225  3      
TURN   226   230  5      
HELIX   233   235  3      
STRAND   243   253  11      
HELIX   258   260  3      
HELIX   263   283  21      
HELIX   286   299  14      
TURN   300   302  3      
HELIX   309   331  23      
HELIX   335   348  14      
HELIX   353   365  13      
HELIX   369   382  14      
HELIX   387   424  38      
Sequence information
Length: 459 AA [This is the length of the unprocessed precursor] Molecular weight: 51805 Da [This is the MW of the unprocessed precursor] CRC64: 6A498105418D9435 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTAEEMKATE SGAQSAPLPM EGVDISPKQD EGVLKVIKRE GTGTEMPMIG DRVFVHYTGW 

        70         80         90        100        110        120 
LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAIATMKVG EVCHITCKPE YAYGSAGSPP 

       130        140        150        160        170        180 
KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIQTRGEG YAKPNEGAIV EVALEGYYKD 

       190        200        210        220        230        240 
KLFDQRELRF EIGEGENLDL PYGLERAIQR MEKGEHSIVY LKPSYAFGSV GKEKFQIPPN 

       250        260        270        280        290        300 
AELKYELHLK SFEKAKESWE MNSEEKLEQS TIVKERGTVY FKEGKYKQAL LQYKKIVSWL 

       310        320        330        340        350        360 
EYESSFSNEE AQKAQALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS NNEKGLFRRG 

       370        380        390        400        410        420 
EAHLAVNDFE LARADFQKVL QLYPNNKAAK TQLAVCQQRI RRQLAREKKL YANMFERLAE 

       430        440        450 
EENKAKAEAS SGDHPTDTEM KEEQKSNTAG SQSQVETEA 

Q02790 in FASTA format

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