Q02790 (FKBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Cleaved into the following chain:

1. Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed

Gene names

Name:	FKBP4
Synonyms:	FKBP52

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Immunophilin protein with PPIase and co-chaperone activities By similarity. Component of unligated 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 By similarity. 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.15 Ref.20
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by FK506. Ref.1
Subunit structure	Homodimer. Associates with HSP90 and HSP70 in unactivated steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with HSF1 in the HSP90 complex. Associates with tubulin By similarity. Interacts with MAPT/TAU By similarity. Interacts with NR3C1 and dynein By similarity. 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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.15 Ref.17 Ref.20 Ref.23
Subcellular location	Cytoplasm › cytosol By similarity. Mitochondrion. Nucleus. Cytoplasm › cytoskeleton By similarity. Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor. Ref.7 Ref.20
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 component	Cytoplasm Cytoskeleton Microtubule Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat
Molecular function	Chaperone Isomerase Rotamase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara chaperone-mediated protein folding Inferred from direct assay PubMed 11350175. Source: UniProtKB copper ion transport Inferred from electronic annotation. Source: Compara embryo implantation Inferred from electronic annotation. Source: Compara male sex differentiation Inferred from electronic annotation. Source: Compara negative regulation of microtubule polymerization Inferred from electronic annotation. Source: Compara 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: Compara protein complex localization Inferred from electronic annotation. Source: Compara steroid hormone receptor complex assembly Inferred from electronic annotation. Source: Compara
Cellular_component	axonal growth cone Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB 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: Compara nucleus Inferred from direct assay. Source: HPA perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara FK506 binding Traceable author statement Ref.6. Source: UniProtKB GTP binding Inferred from electronic annotation. Source: Compara peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay PubMed 11350175. Source: UniProtKB protein binding, bridging Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 459

459

Peptidyl-prolyl cis-trans isomerase FKBP4

PRO_0000391468

Initiator methionine

1

1

Removed; alternate Ref.5 Ref.6 Ref.7 Ref.8

Chain

2 – 459

458

Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed

PRO_0000075318

Regions

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

Region

267 – 400

134

Interaction with tubulin By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate Ref.5

Modified residue

2

1

N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial Ref.5

Modified residue

143

1

Phosphothreonine; by CK2 By similarity

Modified residue

282

1

N6-acetyllysine Ref.16

Modified residue

451

1

Phosphoserine Ref.12 Ref.13 Ref.21

Modified residue

453

1

Phosphoserine Ref.13 Ref.14 Ref.21

Natural variations

Natural variant

436

1

T → P.
Corresponds to variant rs1042228 [ dbSNP | Ensembl ].

VAR_050624

Experimental info

Mutagenesis

67 – 68

2

FD → DV: Decreased catalytic activity toward TRPC1. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

459

Helix Strand Turn

Details...

Beta strand

22 – 24

3

Beta strand

30 – 39

10

Beta strand

42 – 44

3

Beta strand

52 – 61

10

Beta strand

66 – 70

5

Beta strand

73 – 75

3

Beta strand

77 – 80

4

Beta strand

83 – 86

4

Helix

88 – 94

7

Beta strand

102 – 107

6

Helix

109 – 111

3

Turn

112 – 116

5

Turn

119 – 121

3

Beta strand

128 – 138

11

Beta strand

147 – 156

10

Beta strand

169 – 178

10

Beta strand

181 – 191

11

Helix

195 – 198

4

Helix

202 – 208

7

Beta strand

216 – 221

6

Helix

223 – 225

3

Turn

226 – 230

5

Helix

233 – 235

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Q02790 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6A498105418D9435	FASTA	459	51,805
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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.
[16]	"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, MASS SPECTROMETRY.
[17]	"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.
[18]	"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.
[19]	"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].
[20]	"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.
[21]	"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, MASS SPECTROMETRY.
[22]	"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.
[23]	"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.

IPI

IPI00219005.

PIR

A46372.

RefSeq

NP_002005.1. NM_002014.3.

UniGene

Hs.524183.
Hs.713721.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N1A	X-ray	2.40	A/B	2-139	[»]
1P5Q	X-ray	2.80	A/B/C	146-458	[»]
1Q1C	X-ray	1.90	A	2-259	[»]
1QZ2	X-ray	3.00	A/B/C	145-458	[»]
4DRJ	X-ray	1.80	A	1-140	[»]

ProteinModelPortal

Q02790.

SMR

Q02790. Positions 21-427.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-50866N.

IntAct

Q02790. 18 interactions.

MINT

MINT-3024864.

STRING

9606.ENSP00000001008.

PTM databases

PhosphoSite

Q02790.

Polymorphism databases

DMDM

399866.

2D gel databases

REPRODUCTION-2DPAGE

IPI00219005.

Proteomic databases

PaxDb

Q02790.

PeptideAtlas

Q02790.

PRIDE

Q02790.

Protocols and materials databases

DNASU

2288.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000001008; ENSP00000001008; ENSG00000004478.

GeneID

2288.

KEGG

hsa:2288.

UCSC

uc001qkz.3. human.

Organism-specific databases

CTD

2288.

GeneCards

GC12P002904.

H-InvDB

HIX0010330.

HGNC

HGNC:3720. FKBP4.

HPA

CAB017441.
HPA006148.

MIM

600611. gene.

neXtProt

NX_Q02790.

PharmGKB

PA28161.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0545.

HOGENOM

HOG000256916.

HOVERGEN

HBG051624.

InParanoid

Q02790.

KO

K09571.

OMA

KVFVHYV.

OrthoDB

EOG49GKGJ.

PhylomeDB

Q02790.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

Q02790.

Bgee

Q02790.

CleanEx

HS_FKBP4.

Genevestigator

Q02790.

GermOnline

ENSG00000004478. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

PANTHER

PTHR10516. PTHR10516. 1 hit.

Pfam

PF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 3 hits.
[Graphical view]

SMART

SM00028. TPR. 3 hits.
[Graphical view]

PROSITE

PS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q02790.

ChEMBL

CHEMBL4050.

ChiTaRS

FKBP4. human.

DrugBank

DB01093. Dimethyl sulfoxide.

EvolutionaryTrace

Q02790.

GenomeRNAi

2288.

NextBio

9299.

SOURCE

Search...

Entry information

Entry name

FKBP4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 153 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.