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Reviewed, UniProtKB/Swiss-Prot Q02790 (FKBP4_HUMAN)

Last modified November 25, 2008. Version 102. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    FK506-binding protein 4
    EC=5.2.1.8
Alternative name(s):
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    HSP-binding immunophilin
      Short name=HBI
    FKBP52 protein
    52 kDa FK506-binding protein
    FKBP59
    p59 protein
Gene names
Name: FKBP4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of unactivated mammalian steroid receptor complexes that sediment at 8-10 S. May have a rotamase activity. May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors.

Catalytic activity

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

Subunit structure

Interacts with NR3C1 and dynein By similarity. Associates with HSP90 and HSP70 in unactivated steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH).

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Widely expressed.

Post-translational modification

Phosphorylation by CK2 results in loss of HSP90 binding activity By similarity. Phosphorylated upon DNA damage, probably by ATM or ATR.

Sequence similarities

Contains 2 PPIase FKBP-type domains.

Contains 3 TPR repeats.

Sequence caution

The sequence AAH02887.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords

   Cellular componentCytoplasm
Nucleus
   DomainRepeat
TPR repeat
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processprotein folding Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm Ref.4

Traceable author statement. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFK506 binding Ref.3

Traceable author statement. Source: UniProtKB

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding, bridging Ref.4

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 459458FK506-binding protein 4
PRO_0000075318

Regions

Domain50 – 13889PPIase FKBP-type 1
Domain167 – 25387PPIase FKBP-type 2
Repeat270 – 30334TPR 1
Repeat319 – 35234TPR 2
Repeat353 – 38634TPR 3

Amino acid modifications

Modified residue1431Phosphothreonine; by CK2 By similarity
Modified residue2741N6-acetyllysine
Modified residue4511Phosphoserine
Modified residue4531Phosphoserine

Secondary structure

......................................................... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02790-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6A498105418D9435

FASTA45951,805
        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 

« Hide

References

« Hide 'large scale' references
[1]"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."
Peattie D.A., Harding M.W., Fleming M.A., Decenzo M.T., Lippke J.A., Livingston D.J., Benasutti M.
Proc. Natl. Acad. Sci. U.S.A. 89:10974-10978(1992) [PubMed: 1279700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Placenta.
[2]"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: Lung, Lymph and Uterus.
[3]"Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex."
Tai P.-K.K., Albers M.W., Chang H., Faber L.E., Schreiber S.L.
Science 256:1315-1318(1992) [PubMed: 1376003] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25, SUBUNIT, FUNCTION.
Tissue: Thymus.
[4]"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."
Sanchez E.R., Faber L.E., Henzel W.J., Pratt W.B.
Biochemistry 29:5145-5152(1990) [PubMed: 2378870] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
Tissue: Lymphocyte.
[5]"The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13."
Yem A.W., Tomasselli A.G., Heinrikson R.L., Zurcher-Neely H., Ruff V.A., Johnson R.A., Deibel M.R. Jr.
J. Biol. Chem. 267:2868-2871(1992) [PubMed: 1371107] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18.
Tissue: T-cell.
[6]"Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex."
Wiederrecht G., Hung S., Chan H.K., Marcy A., Martin M., Calaycay J., Boulton D., Sigal N., Kincaid R.L., Siekierka J.J.
J. Biol. Chem. 267:21753-21760(1992) [PubMed: 1383226] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-32.
[7]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
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.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-274, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, MASS SPECTROMETRY.
[10]"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-453, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

M88279 mRNA. Translation: AAA36111.1.
BC001786 mRNA. Translation: AAH01786.1.
BC002887 mRNA. Translation: AAH02887.2. Sequence problems.
BC007924 mRNA. Translation: AAH07924.1.
PIRA46372.
RefSeqNP_002005.1.
UniGeneHs.524183

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1N1AX-ray2.40A/B1-140[»]
1P5QX-ray2.80A/B/C145-459[»]
1Q1CX-ray1.90A1-260[»]
1QZ2X-ray3.00A/B/C145-459[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ02790.

PTM databases

PhosphoSiteQ02790.

2-D gel databases

REPRODUCTION-2DPAGEIPI00219005.

Proteomic databases

PeptideAtlasQ02790.

Genome annotation databases

EnsemblENSG00000004478. Homo sapiens. [Contig view]
GeneID2288.
KEGGhsa:2288.

Organism-specific databases

H-InvDBHIX0010330.
HGNCHGNC:3720. FKBP4.
HPACAB017441.
HPA006148.
MIM600611. gene.
PharmGKBPA28161.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ02790.
HOVERGENQ02790.

Gene expression databases

ArrayExpressQ02790.
CleanExHS_FKBP4.
GermOnlineENSG00000004478. Homo sapiens.

Family and domain databases

InterProIPR001179. PPIase_FKBP.
IPR001440. TPR-1.
IPR011990. TPR-like_helical.
IPR013026. TPR_region.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 3 hits.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01093. Dimethyl sulfoxide.
NextBio9299.
SOURCESearch...

Entry information

Entry nameFKBP4_HUMAN
AccessionPrimary (citable) accession number: Q02790
Secondary accession number(s): Q9UCP1, Q9UCV7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 12

Human chromosome 12: 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents