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Q02790 (FKBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP4

Short name=PPIase FKBP4
EC=5.2.1.8
Alternative name(s):
51 kDa FK506-binding protein
Short name=FKBP51
52 kDa FK506-binding protein
Short name=52 kDa FKBP
Short name=FKBP-52
59 kDa immunophilin
Short name=p59
FK506-binding protein 4
Short name=FKBP-4
FKBP59
HSP-binding immunophilin
Short name=HBI
Immunophilin FKBP52
Rotamase
Gene names
Name:FKBP4
Synonyms:FKBP52
OrganismHomo sapiens (Human) [Reference proteome]
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

Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. Ref.1 Ref.6 Ref.7 Ref.16 Ref.21

Catalytic activity

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

Enzyme regulation

Inhibited by FK506. Ref.1

Subunit structure

Homodimer By similarity. Associates with HSP90AA1 and HSP70 in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU. Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the interaction is Ca2+ dependent. Interaction with S100A1 and S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90 interaction. Interacts with dynein; causes partially NR3C1 transport to the nucleus. Ref.6 Ref.7 Ref.9 Ref.11 Ref.16 Ref.18 Ref.21 Ref.24

Subcellular location

Cytoplasmcytosol By similarity. Mitochondrion. Nucleus. Cytoplasmcytoskeleton By similarity. Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor. Ref.7 Ref.21

Tissue specificity

Widely expressed. Ref.1

Domain

The PPIase activity is mainly due to the fisrt PPIase FKBP-type domain (1-138 AA) By similarity.

The C-terminal region (AA 375-458) is required to prevent tubulin polymerization By similarity.

The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400 By similarity.

The TPR repeats mediate mitochondrial localization.

Post-translational modification

Phosphorylation by CK2 results in loss of HSP90 binding activity By similarity.

Sequence similarities

Contains 2 PPIase FKBP-type domains.

Contains 3 TPR repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
TPR repeat
   Molecular functionChaperone
Isomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

chaperone-mediated protein folding

Inferred from direct assay PubMed 11350175. Source: UniProtKB

copper ion transport

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

male sex differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

negative regulation of microtubule polymerization or depolymerization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

prostate gland development

Inferred from electronic annotation. Source: Ensembl

protein complex localization

Inferred from electronic annotation. Source: Ensembl

protein folding

Traceable author statement Ref.1. Source: ProtInc

protein peptidyl-prolyl isomerization

Inferred from direct assay PubMed 11350175. Source: GOC

steroid hormone receptor complex assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxonal growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: Ensembl

FK506 binding

Traceable author statement Ref.6. Source: UniProtKB

GTP binding

Inferred from electronic annotation. Source: Ensembl

heat shock protein binding

Inferred from physical interaction PubMed 9660753. Source: UniProtKB

peptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay PubMed 11350175. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12604780. Source: UniProtKB

protein binding, bridging

Traceable author statement Ref.7. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Peptidyl-prolyl cis-trans isomerase FKBP4
PRO_0000391468
Initiator methionine11Removed; alternate Ref.5 Ref.6 Ref.7 Ref.8
Chain2 – 459458Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed
PRO_0000075318

Regions

Domain50 – 13889PPIase FKBP-type 1
Domain167 – 25387PPIase FKBP-type 2
Repeat270 – 30334TPR 1
Repeat319 – 35234TPR 2
Repeat353 – 38634TPR 3
Region267 – 400134Interaction with tubulin By similarity

Amino acid modifications

Modified residue11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate Ref.5
Modified residue21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial Ref.5
Modified residue1431Phosphothreonine; by CK2 By similarity
Modified residue2821N6-acetyllysine Ref.17
Modified residue4511Phosphoserine Ref.12 Ref.13 Ref.22
Modified residue4531Phosphoserine Ref.13 Ref.14 Ref.22

Natural variations

Natural variant4361T → P.
Corresponds to variant rs1042228 [ dbSNP | Ensembl ].
VAR_050624

Experimental info

Mutagenesis67 – 682FD → DV: Decreased catalytic activity toward TRPC1. Ref.16

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02790 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Placenta.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"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: Lymph and Uterus.
[5]Bienvenut W.V., Lourenco F., Olson M.F.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-28; 40-73; 75-121; 139-152; 158-179; 187-206; 211-250; 257-274; 277-313; 319-354; 359-399; 409-426 AND 446-459, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Mammary carcinoma and Ovarian carcinoma.
[6]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25, SUBUNIT, FUNCTION.
Tissue: Thymus.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
Tissue: Lymphocyte.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18.
Tissue: T-cell.
[9]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-32, SUBUNIT.
[10]"The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52."
Bruner K.L., Derfoul A., Robertson N.M., Guerriero G., Fernandes-Alnemri T., Alnemri E.S., Litwack G.
Recept. Signal Transduct. 7:85-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TERNARY COMPLEX WITH HSP90; HSP70 AND NR3C2, DISSOCIATION UPON ALDOSTERONE BINDING.
[11]"Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex."
Guo Y., Guettouche T., Fenna M., Boellmann F., Pratt W.B., Toft D.O., Smith D.F., Voellmy R.
J. Biol. Chem. 276:45791-45799(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSF1.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening."
Shim S., Yuan J.P., Kim J.Y., Zeng W., Huang G., Milshteyn A., Kern D., Muallem S., Ming G.L., Worley P.F.
Neuron 64:471-483(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRPC1, FUNCTION, MUTAGENESIS OF 67-PHE-ASP-68.
[17]"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-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and FKBP52 through their tetratricopeptide repeats."
Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.
FEBS Lett. 584:1119-1125(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100A1; S100A2 AND S100A6.
[19]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress."
Gallo L.I., Lagadari M., Piwien-Pilipuk G., Galigniana M.D.
J. Biol. Chem. 286:30152-30160(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH GLUCOCORTICOID RECEPTOR.
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structure of the N-terminal domain of human FKBP52."
Li P., Ding Y., Wu B., Shu C., Shen B., Rao Z.
Acta Crystallogr. D 59:16-22(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-139.
[24]"3D structure of human FK506-binding protein 52: implications for the assembly of the glucocorticoid receptor/Hsp90/immunophilin heterocomplex."
Wu B., Li P., Liu Y., Lou Z., Ding Y., Shu C., Ye S., Bartlam M., Shen B., Rao Z.
Proc. Natl. Acad. Sci. U.S.A. 101:8348-8353(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-458 IN COMPLEX WITH HSP90, SUBUNIT.
+Additional computationally mapped references.

Web resources

Protein Spotlight

A mind astray - Issue 118 of June 2010

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88279 mRNA. Translation: AAA36111.1.
AC005841 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88889.1.
CH471116 Genomic DNA. Translation: EAW88890.1.
BC001786 mRNA. Translation: AAH01786.1.
BC007924 mRNA. Translation: AAH07924.1.
CCDSCCDS8512.1.
PIRA46372.
RefSeqNP_002005.1. NM_002014.3.
UniGeneHs.524183.
Hs.713721.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N1AX-ray2.40A/B1-140[»]
1P5QX-ray2.80A/B/C146-459[»]
1Q1CX-ray1.90A2-260[»]
1QZ2X-ray3.00A/B/C145-459[»]
4DRJX-ray1.80A1-140[»]
4LAVX-ray1.80A/B16-260[»]
4LAWX-ray2.40A/B16-260[»]
4LAXX-ray2.01A16-260[»]
4LAYX-ray1.70A1-260[»]
ProteinModelPortalQ02790.
SMRQ02790. Positions 22-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108578. 48 interactions.
DIPDIP-50866N.
IntActQ02790. 24 interactions.
MINTMINT-3024864.
STRING9606.ENSP00000001008.

Chemistry

BindingDBQ02790.
ChEMBLCHEMBL4050.
DrugBankDB01093. Dimethyl sulfoxide.

PTM databases

PhosphoSiteQ02790.

Polymorphism databases

DMDM399866.

2D gel databases

REPRODUCTION-2DPAGEIPI00219005.

Proteomic databases

MaxQBQ02790.
PaxDbQ02790.
PeptideAtlasQ02790.
PRIDEQ02790.

Protocols and materials databases

DNASU2288.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000001008; ENSP00000001008; ENSG00000004478.
GeneID2288.
KEGGhsa:2288.
UCSCuc001qkz.3. human.

Organism-specific databases

CTD2288.
GeneCardsGC12P002904.
H-InvDBHIX0010330.
HGNCHGNC:3720. FKBP4.
HPACAB017441.
HPA006148.
MIM600611. gene.
neXtProtNX_Q02790.
PharmGKBPA28161.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000256916.
HOVERGENHBG051624.
InParanoidQ02790.
KOK09571.
OMANAELKYE.
PhylomeDBQ02790.
TreeFamTF354214.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ02790.
BgeeQ02790.
CleanExHS_FKBP4.
GenevestigatorQ02790.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 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

ChiTaRSFKBP4. human.
EvolutionaryTraceQ02790.
GeneWikiFKBP52.
GenomeRNAi2288.
NextBio9299.
PROQ02790.
SOURCESearch...

Entry information

Entry nameFKBP4_HUMAN
AccessionPrimary (citable) accession number: Q02790
Secondary accession number(s): D3DUQ1, Q9UCP1, Q9UCV7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM