Q00688 (FKBP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP3
Short name=PPIase FKBP3
EC=5.2.1.8

Alternative name(s):
25 kDa FK506-binding protein
Short name=25 kDa FKBP
Short name=FKBP-25
FK506-binding protein 3
Short name=FKBP-3
Immunophilin FKBP25
Rapamycin-selective 25 kDa immunophilin
Rotamase

Gene names

Name:	FKBP3
Synonyms:	FKBP25

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	224 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited preferentially by rapamycin over FK506.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the FKBP-type PPIase family. Contains 1 PPIase FKBP-type domain.
Sequence caution	The sequence AAA58474.1 differs from that shown. Reason: Frameshift at position 197.

Ontologies

Keywords
Cellular component	Nucleus
Molecular function	Isomerase Rotamase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	membrane Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome peptidyl-prolyl cis-trans isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome receptor activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 224

224

Peptidyl-prolyl cis-trans isomerase FKBP3

PRO_0000075307

Regions

Domain

128 – 224

97

PPIase FKBP-type

Amino acid modifications

Modified residue

36

1

Phosphoserine Ref.11

Modified residue

152

1

Phosphoserine Ref.9

Modified residue

170

1

N6-acetyllysine Ref.10

Experimental info

Sequence conflict

181

1

T → A in AAA58474. Ref.3

Secondary structure

1

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224

Helix Strand Turn

Details...

Helix

12 – 16

5

Helix

23 – 32

10

Helix

35 – 40

6

Helix

47 – 51

5

Helix

56 – 69

14

Beta strand

111 – 117

7

Beta strand

130 – 138

9

Beta strand

144 – 147

4

Turn

155 – 157

3

Beta strand

162 – 165

4

Turn

166 – 169

4

Helix

173 – 179

7

Beta strand

187 – 192

6

Helix

194 – 196

3

Turn

197 – 201

5

Helix

204 – 206

3

Beta strand

214 – 224

11

Sequences

	Sequence		Length	Mass (Da)
	Q00688 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: C144C5AAB7EA9522	FASTA	224	25,177
	10 20 30 40 50 60 MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV 70 80 90 100 110 120 TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD 130 140 150 160 170 180 KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL 190 200 210 220 TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein." Wiederrecht G., Martin M., Sigal N., Siekierka J.J. Biochem. Biophys. Res. Commun. 185:298-303(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein." Hung D.T., Schreiber S.L. Biochem. Biophys. Res. Commun. 184:733-738(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25." Jin Y.-J., Burakoff S.J., Bierer B.E. J. Biol. Chem. 267:10942-10945(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[6]	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].
[7]	"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: Skeletal muscle and Skin.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"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-152, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-170, MASS SPECTROMETRY.
[11]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"Structure of the human 25 kDa FK506 binding protein complexed with rapamycin." Liang J., Hung D.T., Schreiber S.L., Clardy J. J. Am. Chem. Soc. 118:1231-1232(1996) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96256 mRNA. Translation: AAA58471.1.
M90309 mRNA. Translation: AAA58475.1.
M90820 mRNA. Translation: AAA58474.1. Frameshift.
BT006904 mRNA. Translation: AAP35550.1.
AK311915 mRNA. Translation: BAG34856.1.
CH471078 Genomic DNA. Translation: EAW65785.1.
BC016288 mRNA. Translation: AAH16288.1.
BC020809 mRNA. Translation: AAH20809.1.

IPI

IPI00024157.

PIR

JQ1522.

RefSeq

NP_002004.1. NM_002013.3.

UniGene

Hs.509226.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PBK	X-ray	2.50	A	109-224	[»]
2KFV	NMR	-	A	1-73	[»]

ProteinModelPortal

Q00688.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000216330.

PTM databases

PhosphoSite

Q00688.

Polymorphism databases

DMDM

232096.

Proteomic databases

PaxDb

Q00688.

PeptideAtlas

Q00688.

PRIDE

Q00688.

Protocols and materials databases

DNASU

2287.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216330; ENSP00000216330; ENSG00000100442.
ENST00000396062; ENSP00000379374; ENSG00000100442.

GeneID

2287.

KEGG

hsa:2287.

UCSC

uc010tqf.2. human.

Organism-specific databases

CTD

2287.

GeneCards

GC14M045584.

HGNC

HGNC:3719. FKBP3.

HPA

CAB012232.
CAB012520.
HPA000864.

MIM

186947. gene.

neXtProt

NX_Q00688.

PharmGKB

PA28160.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0545.

HOGENOM

HOG000007963.

HOVERGEN

HBG105391.

InParanoid

Q00688.

KO

K09570.

OMA

FKGTESV.

OrthoDB

EOG43FGXV.

PhylomeDB

Q00688.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpress

Q00688.

Bgee

Q00688.

CleanEx

HS_FKBP3.

Genevestigator

Q00688.

GermOnline

ENSG00000100442. Homo sapiens.

Family and domain databases

InterPro

IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]

PANTHER

PTHR10516. PTHR10516. 1 hit.

Pfam

PF00254. FKBP_C. 1 hit.
[Graphical view]

PROSITE

PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q00688.

ChEMBL

CHEMBL4746.

ChiTaRS

FKBP3. human.

EvolutionaryTrace

Q00688.

GenomeRNAi

2287.

NextBio

9295.

SOURCE

Search...

Entry information

Entry name

FKBP3_HUMAN

Accession

Primary (citable) accession number: Q00688
Secondary accession number(s): B2R4Q9, Q14317

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 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.