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Q02790

- FKBP4_HUMAN

UniProt

Q02790 - FKBP4_HUMAN

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Protein

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene
FKBP4, FKBP52
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by FK506.1 Publication

GO - Molecular functioni

  1. ATP binding Source: Ensembl
  2. FK506 binding Source: UniProtKB
  3. GTP binding Source: Ensembl
  4. heat shock protein binding Source: UniProtKB
  5. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  6. poly(A) RNA binding Source: UniProtKB
  7. protein binding Source: UniProtKB
  8. protein binding, bridging Source: ProtInc

GO - Biological processi

  1. androgen receptor signaling pathway Source: Ensembl
  2. chaperone-mediated protein folding Source: UniProtKB
  3. copper ion transport Source: Ensembl
  4. embryo implantation Source: Ensembl
  5. male sex differentiation Source: Ensembl
  6. negative regulation of microtubule polymerization Source: Ensembl
  7. negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
  8. negative regulation of neuron projection development Source: UniProtKB
  9. prostate gland development Source: Ensembl
  10. protein complex localization Source: Ensembl
  11. protein folding Source: ProtInc
  12. protein peptidyl-prolyl isomerization Source: GOC
  13. steroid hormone receptor complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiREACT_200624. Attenuation phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP4 (EC:5.2.1.8)
Short name:
PPIase FKBP4
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
Cleaved into the following chain:
Gene namesi
Name:FKBP4
Synonyms:FKBP52
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:3720. FKBP4.

Subcellular locationi

Cytoplasmcytosol By similarity. Mitochondrion. Nucleus. Cytoplasmcytoskeleton By similarity
Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor.2 Publications

GO - Cellular componenti

  1. axonal growth cone Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytosol Source: UniProtKB
  4. endoplasmic reticulum membrane Source: RefGenome
  5. extracellular vesicular exosome Source: UniProt
  6. microtubule Source: UniProtKB-KW
  7. mitochondrion Source: UniProtKB-SubCell
  8. neuronal cell body Source: Ensembl
  9. nucleus Source: HPA
  10. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 682FD → DV: Decreased catalytic activity toward TRPC1. 1 Publication

Organism-specific databases

PharmGKBiPA28161.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Peptidyl-prolyl cis-trans isomerase FKBP4PRO_0000391468Add
BLAST
Initiator methioninei1 – 11Removed; alternate4 Publications
Chaini2 – 459458Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processedPRO_0000075318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate1 Publication
Modified residuei2 – 21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial1 Publication
Modified residuei143 – 1431Phosphothreonine; by CK2 By similarity
Modified residuei282 – 2821N6-acetyllysine1 Publication
Modified residuei451 – 4511Phosphoserine3 Publications
Modified residuei453 – 4531Phosphoserine3 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ02790.
PaxDbiQ02790.
PeptideAtlasiQ02790.
PRIDEiQ02790.

2D gel databases

REPRODUCTION-2DPAGEIPI00219005.

PTM databases

PhosphoSiteiQ02790.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ArrayExpressiQ02790.
BgeeiQ02790.
CleanExiHS_FKBP4.
GenevestigatoriQ02790.

Organism-specific databases

HPAiCAB017441.
HPA006148.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO2Q9UKV82EBI-1047444,EBI-528269
HSP90AA1P079008EBI-1047444,EBI-296047
S100a1P354677EBI-1047444,EBI-6477109From a different organism.
S100A2P290343EBI-1047444,EBI-752230
S100A6P067033EBI-1047444,EBI-352877

Protein-protein interaction databases

BioGridi108578. 49 interactions.
DIPiDIP-50866N.
IntActiQ02790. 24 interactions.
MINTiMINT-3024864.
STRINGi9606.ENSP00000001008.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243
Beta strandi30 – 3910
Beta strandi42 – 443
Beta strandi52 – 6110
Beta strandi66 – 694
Helixi70 – 723
Beta strandi73 – 753
Beta strandi77 – 804
Beta strandi83 – 864
Helixi88 – 947
Beta strandi102 – 1076
Helixi109 – 1113
Turni112 – 1165
Turni119 – 1213
Beta strandi128 – 13811
Beta strandi147 – 15610
Beta strandi159 – 1613
Beta strandi169 – 17810
Beta strandi181 – 19111
Turni192 – 1943
Helixi195 – 1984
Helixi202 – 2087
Beta strandi216 – 2216
Helixi223 – 2253
Turni226 – 2305
Helixi233 – 2353
Beta strandi243 – 25311
Helixi258 – 2603
Helixi263 – 28321
Helixi286 – 29914
Turni300 – 3023
Helixi309 – 33123
Helixi335 – 34814
Helixi353 – 36513
Helixi369 – 38214
Helixi387 – 42438

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ02790.
SMRiQ02790. Positions 22-427.

Miscellaneous databases

EvolutionaryTraceiQ02790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 13889PPIase FKBP-type 1Add
BLAST
Domaini167 – 25387PPIase FKBP-type 2Add
BLAST
Repeati270 – 30334TPR 1Add
BLAST
Repeati319 – 35234TPR 2Add
BLAST
Repeati353 – 38634TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 400134Interaction with tubulin By similarityAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 3 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000256916.
HOVERGENiHBG051624.
InParanoidiQ02790.
KOiK09571.
OMAiNAELKYE.
PhylomeDBiQ02790.
TreeFamiTF354214.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 3 hits.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02790-1 [UniParc]FASTAAdd to Basket

« Hide

MTAEEMKATE SGAQSAPLPM EGVDISPKQD EGVLKVIKRE GTGTEMPMIG    50
DRVFVHYTGW LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAIATMKVG 100
EVCHITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI 150
IRRIQTRGEG YAKPNEGAIV EVALEGYYKD KLFDQRELRF EIGEGENLDL 200
PYGLERAIQR MEKGEHSIVY LKPSYAFGSV GKEKFQIPPN AELKYELHLK 250
SFEKAKESWE MNSEEKLEQS TIVKERGTVY FKEGKYKQAL LQYKKIVSWL 300
EYESSFSNEE AQKAQALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS 350
NNEKGLFRRG EAHLAVNDFE LARADFQKVL QLYPNNKAAK TQLAVCQQRI 400
RRQLAREKKL YANMFERLAE EENKAKAEAS SGDHPTDTEM KEEQKSNTAG 450
SQSQVETEA 459
Length:459
Mass (Da):51,805
Last modified:January 23, 2007 - v3
Checksum:i6A498105418D9435
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti436 – 4361T → P.
Corresponds to variant rs1042228 [ dbSNP | Ensembl ].
VAR_050624

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS8512.1.
PIRiA46372.
RefSeqiNP_002005.1. NM_002014.3.
UniGeneiHs.524183.
Hs.713721.

Genome annotation databases

EnsembliENST00000001008; ENSP00000001008; ENSG00000004478.
GeneIDi2288.
KEGGihsa:2288.
UCSCiuc001qkz.3. human.

Polymorphism databases

DMDMi399866.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

A mind astray - Issue 118 of June 2010

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS8512.1.
PIRi A46372.
RefSeqi NP_002005.1. NM_002014.3.
UniGenei Hs.524183.
Hs.713721.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N1A X-ray 2.40 A/B 1-140 [» ]
1P5Q X-ray 2.80 A/B/C 146-459 [» ]
1Q1C X-ray 1.90 A 2-260 [» ]
1QZ2 X-ray 3.00 A/B/C 145-459 [» ]
4DRJ X-ray 1.80 A 1-140 [» ]
4LAV X-ray 1.80 A/B 16-260 [» ]
4LAW X-ray 2.40 A/B 16-260 [» ]
4LAX X-ray 2.01 A 16-260 [» ]
4LAY X-ray 1.70 A 1-260 [» ]
ProteinModelPortali Q02790.
SMRi Q02790. Positions 22-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108578. 49 interactions.
DIPi DIP-50866N.
IntActi Q02790. 24 interactions.
MINTi MINT-3024864.
STRINGi 9606.ENSP00000001008.

Chemistry

BindingDBi Q02790.
ChEMBLi CHEMBL4050.
DrugBanki DB01093. Dimethyl sulfoxide.

PTM databases

PhosphoSitei Q02790.

Polymorphism databases

DMDMi 399866.

2D gel databases

REPRODUCTION-2DPAGE IPI00219005.

Proteomic databases

MaxQBi Q02790.
PaxDbi Q02790.
PeptideAtlasi Q02790.
PRIDEi Q02790.

Protocols and materials databases

DNASUi 2288.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000001008 ; ENSP00000001008 ; ENSG00000004478 .
GeneIDi 2288.
KEGGi hsa:2288.
UCSCi uc001qkz.3. human.

Organism-specific databases

CTDi 2288.
GeneCardsi GC12P002904.
H-InvDB HIX0010330.
HGNCi HGNC:3720. FKBP4.
HPAi CAB017441.
HPA006148.
MIMi 600611. gene.
neXtProti NX_Q02790.
PharmGKBi PA28161.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0545.
HOGENOMi HOG000256916.
HOVERGENi HBG051624.
InParanoidi Q02790.
KOi K09571.
OMAi NAELKYE.
PhylomeDBi Q02790.
TreeFami TF354214.

Enzyme and pathway databases

Reactomei REACT_200624. Attenuation phase.

Miscellaneous databases

ChiTaRSi FKBP4. human.
EvolutionaryTracei Q02790.
GeneWikii FKBP52.
GenomeRNAii 2288.
NextBioi 9299.
PROi Q02790.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q02790.
Bgeei Q02790.
CleanExi HS_FKBP4.
Genevestigatori Q02790.

Family and domain databases

Gene3Di 1.25.40.10. 1 hit.
InterProi IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 3 hits.
[Graphical view ]
SMARTi SM00028. TPR. 3 hits.
[Graphical view ]
PROSITEi PS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. 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. 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.

Entry informationi

Entry nameiFKBP4_HUMAN
AccessioniPrimary (citable) accession number: Q02790
Secondary accession number(s): D3DUQ1, Q9UCP1, Q9UCV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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