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Peptidyl-prolyl cis-trans isomerase FKBP3 (PPIase FKBP3) (EC 5.2.1.8) (25 kDa FK506-binding protein) (25 kDa FKBP) (FKBP-25) (FK506-binding protein 3) (FKBP-3) (Immunophilin FKBP25) (Rapamycin-selective 25 kDa immunophilin) (Rotamase)

 FKBP3_HUMAN             Reviewed;         224 AA.
Q00688; B2R4Q9; Q14317;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
05-DEC-2018, entry version 180.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
Short=PPIase FKBP3;
EC=5.2.1.8;
AltName: Full=25 kDa FK506-binding protein;
Short=25 kDa FKBP;
Short=FKBP-25;
AltName: Full=FK506-binding protein 3;
Short=FKBP-3;
AltName: Full=Immunophilin FKBP25;
AltName: Full=Rapamycin-selective 25 kDa immunophilin;
AltName: Full=Rotamase;
Name=FKBP3; Synonyms=FKBP25;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1376117; DOI=10.1016/S0006-291X(05)80990-8;
Wiederrecht G., Martin M., Sigal N., Siekierka J.J.;
"Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin
binding protein.";
Biochem. Biophys. Res. Commun. 185:298-303(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1374240; DOI=10.1016/0006-291X(92)90651-Z;
Hung D.T., Schreiber S.L.;
"cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.";
Biochem. Biophys. Res. Commun. 184:733-738(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=1375932;
Jin Y.-J., Burakoff S.J., Bierer B.E.;
"Molecular cloning of a 25-kDa high affinity rapamycin binding
protein, FKBP25.";
J. Biol. Chem. 267:10942-10945(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.
Liang J., Hung D.T., Schreiber S.L., Clardy J.;
"Structure of the human 25 kDa FK506 binding protein complexed with
rapamycin.";
J. Am. Chem. Soc. 118:1231-1232(1996).
-!- 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:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8;
-!- ACTIVITY REGULATION: Inhibited preferentially by rapamycin over
FK506.
-!- INTERACTION:
Q00987:MDM2; NbExp=2; IntAct=EBI-1044081, EBI-389668;
Q9UGN5:PARP2; NbExp=2; IntAct=EBI-1044081, EBI-2795348;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA58474.1; Type=Frameshift; Positions=197; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M96256; AAA58471.1; -; mRNA.
EMBL; M90309; AAA58475.1; -; mRNA.
EMBL; M90820; AAA58474.1; ALT_FRAME; mRNA.
EMBL; BT006904; AAP35550.1; -; mRNA.
EMBL; AK311915; BAG34856.1; -; mRNA.
EMBL; CH471078; EAW65785.1; -; Genomic_DNA.
EMBL; BC016288; AAH16288.1; -; mRNA.
EMBL; BC020809; AAH20809.1; -; mRNA.
CCDS; CCDS9683.1; -.
PIR; JQ1522; JQ1522.
RefSeq; NP_002004.1; NM_002013.3.
UniGene; Hs.509226; -.
PDB; 1PBK; X-ray; 2.50 A; A=109-224.
PDB; 2KFV; NMR; -; A=1-73.
PDB; 2MPH; NMR; -; A=1-224.
PDB; 5D75; X-ray; 1.83 A; A=109-224.
PDB; 5GPG; X-ray; 1.67 A; A=109-224.
PDBsum; 1PBK; -.
PDBsum; 2KFV; -.
PDBsum; 2MPH; -.
PDBsum; 5D75; -.
PDBsum; 5GPG; -.
ProteinModelPortal; Q00688; -.
SMR; Q00688; -.
BioGrid; 108577; 47.
IntAct; Q00688; 7.
MINT; Q00688; -.
STRING; 9606.ENSP00000216330; -.
BindingDB; Q00688; -.
ChEMBL; CHEMBL4746; -.
iPTMnet; Q00688; -.
PhosphoSitePlus; Q00688; -.
SwissPalm; Q00688; -.
BioMuta; FKBP3; -.
DMDM; 232096; -.
EPD; Q00688; -.
MaxQB; Q00688; -.
PaxDb; Q00688; -.
PeptideAtlas; Q00688; -.
PRIDE; Q00688; -.
ProteomicsDB; 57869; -.
TopDownProteomics; Q00688; -.
DNASU; 2287; -.
Ensembl; ENST00000216330; ENSP00000216330; ENSG00000100442.
Ensembl; ENST00000396062; ENSP00000379374; ENSG00000100442.
GeneID; 2287; -.
KEGG; hsa:2287; -.
UCSC; uc010tqf.3; human.
CTD; 2287; -.
EuPathDB; HostDB:ENSG00000100442.10; -.
GeneCards; FKBP3; -.
HGNC; HGNC:3719; FKBP3.
HPA; CAB012232; -.
HPA; CAB012520; -.
HPA; HPA000864; -.
MIM; 186947; gene.
neXtProt; NX_Q00688; -.
OpenTargets; ENSG00000100442; -.
PharmGKB; PA28160; -.
eggNOG; KOG0544; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00940000154514; -.
HOGENOM; HOG000007963; -.
HOVERGEN; HBG105391; -.
InParanoid; Q00688; -.
KO; K09570; -.
OMA; CWYTGSL; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; Q00688; -.
TreeFam; TF105293; -.
ChiTaRS; FKBP3; human.
EvolutionaryTrace; Q00688; -.
GeneWiki; FKBP3; -.
GenomeRNAi; 2287; -.
PRO; PR:Q00688; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100442; Expressed in 232 organ(s), highest expression level in biceps brachii.
CleanEx; HS_FKBP3; -.
ExpressionAtlas; Q00688; baseline and differential.
Genevisible; Q00688; HS.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005528; F:FK506 binding; TAS:ProtInc.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Isomerase; Nucleus;
Phosphoprotein; Reference proteome; Rotamase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
CHAIN 2 224 Peptidyl-prolyl cis-trans isomerase
FKBP3.
/FTId=PRO_0000075307.
DOMAIN 128 224 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 99 99 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q62446}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 170 170 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CONFLICT 181 181 T -> A (in Ref. 3; AAA58474).
{ECO:0000305}.
HELIX 12 16 {ECO:0000244|PDB:2KFV}.
HELIX 23 32 {ECO:0000244|PDB:2KFV}.
HELIX 35 40 {ECO:0000244|PDB:2KFV}.
HELIX 47 51 {ECO:0000244|PDB:2KFV}.
HELIX 56 69 {ECO:0000244|PDB:2KFV}.
STRAND 110 117 {ECO:0000244|PDB:5GPG}.
STRAND 130 138 {ECO:0000244|PDB:5GPG}.
STRAND 144 147 {ECO:0000244|PDB:5GPG}.
TURN 153 155 {ECO:0000244|PDB:2MPH}.
TURN 156 158 {ECO:0000244|PDB:5D75}.
STRAND 162 165 {ECO:0000244|PDB:5GPG}.
STRAND 168 171 {ECO:0000244|PDB:5GPG}.
HELIX 173 178 {ECO:0000244|PDB:5GPG}.
HELIX 179 181 {ECO:0000244|PDB:5GPG}.
STRAND 187 192 {ECO:0000244|PDB:5GPG}.
HELIX 194 196 {ECO:0000244|PDB:5GPG}.
TURN 197 201 {ECO:0000244|PDB:5GPG}.
HELIX 204 206 {ECO:0000244|PDB:5GPG}.
STRAND 214 223 {ECO:0000244|PDB:5GPG}.
SEQUENCE 224 AA; 25177 MW; C144C5AAB7EA9522 CRC64;
MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV
TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD
KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL
TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID


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