Full text data of FKBP3
FKBP3
(FKBP25)
[Confidence: high (present in two of the MS resources)]
Peptidyl-prolyl cis-trans isomerase FKBP3; PPIase FKBP3; 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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Peptidyl-prolyl cis-trans isomerase FKBP3; PPIase FKBP3; 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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q00688
ID FKBP3_HUMAN Reviewed; 224 AA.
AC Q00688; B2R4Q9; Q14317;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 1.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
DE Short=PPIase FKBP3;
DE EC=5.2.1.8;
DE AltName: Full=25 kDa FK506-binding protein;
DE Short=25 kDa FKBP;
DE Short=FKBP-25;
DE AltName: Full=FK506-binding protein 3;
DE Short=FKBP-3;
DE AltName: Full=Immunophilin FKBP25;
DE AltName: Full=Rapamycin-selective 25 kDa immunophilin;
DE AltName: Full=Rotamase;
GN Name=FKBP3; Synonyms=FKBP25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1376117; DOI=10.1016/S0006-291X(05)80990-8;
RA Wiederrecht G., Martin M., Sigal N., Siekierka J.J.;
RT "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin
RT binding protein.";
RL Biochem. Biophys. Res. Commun. 185:298-303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1374240; DOI=10.1016/0006-291X(92)90651-Z;
RA Hung D.T., Schreiber S.L.;
RT "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.";
RL Biochem. Biophys. Res. Commun. 184:733-738(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=1375932;
RA Jin Y.-J., Burakoff S.J., Bierer B.E.;
RT "Molecular cloning of a 25-kDa high affinity rapamycin binding
RT protein, FKBP25.";
RL J. Biol. Chem. 267:10942-10945(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.
RA Liang J., Hung D.T., Schreiber S.L., Clardy J.;
RT "Structure of the human 25 kDa FK506 binding protein complexed with
RT rapamycin.";
RL J. Am. Chem. Soc. 118:1231-1232(1996).
CC -!- FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute
CC a family of receptors for the two immunosuppressants which inhibit
CC T-cell proliferation by arresting two distinct cytoplasmic signal
CC transmission pathways. PPIases accelerate the folding of proteins.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Inhibited preferentially by rapamycin over
CC FK506.
CC -!- INTERACTION:
CC Q00987:MDM2; NbExp=2; IntAct=EBI-1044081, EBI-389668;
CC Q9UGN5:PARP2; NbExp=2; IntAct=EBI-1044081, EBI-2795348;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58474.1; Type=Frameshift; Positions=197;
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DR EMBL; M96256; AAA58471.1; -; mRNA.
DR EMBL; M90309; AAA58475.1; -; mRNA.
DR EMBL; M90820; AAA58474.1; ALT_FRAME; mRNA.
DR EMBL; BT006904; AAP35550.1; -; mRNA.
DR EMBL; AK311915; BAG34856.1; -; mRNA.
DR EMBL; CH471078; EAW65785.1; -; Genomic_DNA.
DR EMBL; BC016288; AAH16288.1; -; mRNA.
DR EMBL; BC020809; AAH20809.1; -; mRNA.
DR PIR; JQ1522; JQ1522.
DR RefSeq; NP_002004.1; NM_002013.3.
DR UniGene; Hs.509226; -.
DR PDB; 1PBK; X-ray; 2.50 A; A=109-224.
DR PDB; 2KFV; NMR; -; A=1-73.
DR PDBsum; 1PBK; -.
DR PDBsum; 2KFV; -.
DR ProteinModelPortal; Q00688; -.
DR SMR; Q00688; 1-73, 109-224.
DR IntAct; Q00688; 3.
DR STRING; 9606.ENSP00000216330; -.
DR BindingDB; Q00688; -.
DR ChEMBL; CHEMBL4746; -.
DR PhosphoSite; Q00688; -.
DR DMDM; 232096; -.
DR PaxDb; Q00688; -.
DR PeptideAtlas; Q00688; -.
DR PRIDE; Q00688; -.
DR DNASU; 2287; -.
DR Ensembl; ENST00000216330; ENSP00000216330; ENSG00000100442.
DR Ensembl; ENST00000396062; ENSP00000379374; ENSG00000100442.
DR GeneID; 2287; -.
DR KEGG; hsa:2287; -.
DR UCSC; uc010tqf.2; human.
DR CTD; 2287; -.
DR GeneCards; GC14M045584; -.
DR HGNC; HGNC:3719; FKBP3.
DR HPA; CAB012232; -.
DR HPA; CAB012520; -.
DR HPA; HPA000864; -.
DR MIM; 186947; gene.
DR neXtProt; NX_Q00688; -.
DR PharmGKB; PA28160; -.
DR eggNOG; COG0545; -.
DR HOGENOM; HOG000007963; -.
DR HOVERGEN; HBG105391; -.
DR InParanoid; Q00688; -.
DR KO; K09570; -.
DR OMA; TMSKGET; -.
DR OrthoDB; EOG7BZVT6; -.
DR PhylomeDB; Q00688; -.
DR ChiTaRS; FKBP3; human.
DR EvolutionaryTrace; Q00688; -.
DR GeneWiki; FKBP3; -.
DR GenomeRNAi; 2287; -.
DR NextBio; 9295; -.
DR PRO; PR:Q00688; -.
DR ArrayExpress; Q00688; -.
DR Bgee; Q00688; -.
DR CleanEx; HS_FKBP3; -.
DR Genevestigator; Q00688; -.
DR GO; GO:0016020; C:membrane; IBA:RefGenome.
DR GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR GO; GO:0005528; F:FK506 binding; IBA:RefGenome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:RefGenome.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR InterPro; IPR023566; PPIase_FKBP.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR10516; PTHR10516; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Isomerase; Nucleus;
KW Phosphoprotein; Reference proteome; Rotamase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 224 Peptidyl-prolyl cis-trans isomerase
FT FKBP3.
FT /FTId=PRO_0000075307.
FT DOMAIN 128 224 PPIase FKBP-type.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 36 36 Phosphoserine.
FT MOD_RES 152 152 Phosphoserine.
FT MOD_RES 170 170 N6-acetyllysine.
FT CONFLICT 181 181 T -> A (in Ref. 3; AAA58474).
FT HELIX 12 16
FT HELIX 23 32
FT HELIX 35 40
FT HELIX 47 51
FT HELIX 56 69
FT STRAND 111 117
FT STRAND 130 138
FT STRAND 144 147
FT TURN 155 157
FT STRAND 162 165
FT TURN 166 169
FT HELIX 173 179
FT STRAND 187 192
FT HELIX 194 196
FT TURN 197 201
FT HELIX 204 206
FT STRAND 214 224
SQ 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
//
ID FKBP3_HUMAN Reviewed; 224 AA.
AC Q00688; B2R4Q9; Q14317;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 1.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
DE Short=PPIase FKBP3;
DE EC=5.2.1.8;
DE AltName: Full=25 kDa FK506-binding protein;
DE Short=25 kDa FKBP;
DE Short=FKBP-25;
DE AltName: Full=FK506-binding protein 3;
DE Short=FKBP-3;
DE AltName: Full=Immunophilin FKBP25;
DE AltName: Full=Rapamycin-selective 25 kDa immunophilin;
DE AltName: Full=Rotamase;
GN Name=FKBP3; Synonyms=FKBP25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1376117; DOI=10.1016/S0006-291X(05)80990-8;
RA Wiederrecht G., Martin M., Sigal N., Siekierka J.J.;
RT "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin
RT binding protein.";
RL Biochem. Biophys. Res. Commun. 185:298-303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1374240; DOI=10.1016/0006-291X(92)90651-Z;
RA Hung D.T., Schreiber S.L.;
RT "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.";
RL Biochem. Biophys. Res. Commun. 184:733-738(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=1375932;
RA Jin Y.-J., Burakoff S.J., Bierer B.E.;
RT "Molecular cloning of a 25-kDa high affinity rapamycin binding
RT protein, FKBP25.";
RL J. Biol. Chem. 267:10942-10945(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.
RA Liang J., Hung D.T., Schreiber S.L., Clardy J.;
RT "Structure of the human 25 kDa FK506 binding protein complexed with
RT rapamycin.";
RL J. Am. Chem. Soc. 118:1231-1232(1996).
CC -!- FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute
CC a family of receptors for the two immunosuppressants which inhibit
CC T-cell proliferation by arresting two distinct cytoplasmic signal
CC transmission pathways. PPIases accelerate the folding of proteins.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Inhibited preferentially by rapamycin over
CC FK506.
CC -!- INTERACTION:
CC Q00987:MDM2; NbExp=2; IntAct=EBI-1044081, EBI-389668;
CC Q9UGN5:PARP2; NbExp=2; IntAct=EBI-1044081, EBI-2795348;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58474.1; Type=Frameshift; Positions=197;
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DR EMBL; M96256; AAA58471.1; -; mRNA.
DR EMBL; M90309; AAA58475.1; -; mRNA.
DR EMBL; M90820; AAA58474.1; ALT_FRAME; mRNA.
DR EMBL; BT006904; AAP35550.1; -; mRNA.
DR EMBL; AK311915; BAG34856.1; -; mRNA.
DR EMBL; CH471078; EAW65785.1; -; Genomic_DNA.
DR EMBL; BC016288; AAH16288.1; -; mRNA.
DR EMBL; BC020809; AAH20809.1; -; mRNA.
DR PIR; JQ1522; JQ1522.
DR RefSeq; NP_002004.1; NM_002013.3.
DR UniGene; Hs.509226; -.
DR PDB; 1PBK; X-ray; 2.50 A; A=109-224.
DR PDB; 2KFV; NMR; -; A=1-73.
DR PDBsum; 1PBK; -.
DR PDBsum; 2KFV; -.
DR ProteinModelPortal; Q00688; -.
DR SMR; Q00688; 1-73, 109-224.
DR IntAct; Q00688; 3.
DR STRING; 9606.ENSP00000216330; -.
DR BindingDB; Q00688; -.
DR ChEMBL; CHEMBL4746; -.
DR PhosphoSite; Q00688; -.
DR DMDM; 232096; -.
DR PaxDb; Q00688; -.
DR PeptideAtlas; Q00688; -.
DR PRIDE; Q00688; -.
DR DNASU; 2287; -.
DR Ensembl; ENST00000216330; ENSP00000216330; ENSG00000100442.
DR Ensembl; ENST00000396062; ENSP00000379374; ENSG00000100442.
DR GeneID; 2287; -.
DR KEGG; hsa:2287; -.
DR UCSC; uc010tqf.2; human.
DR CTD; 2287; -.
DR GeneCards; GC14M045584; -.
DR HGNC; HGNC:3719; FKBP3.
DR HPA; CAB012232; -.
DR HPA; CAB012520; -.
DR HPA; HPA000864; -.
DR MIM; 186947; gene.
DR neXtProt; NX_Q00688; -.
DR PharmGKB; PA28160; -.
DR eggNOG; COG0545; -.
DR HOGENOM; HOG000007963; -.
DR HOVERGEN; HBG105391; -.
DR InParanoid; Q00688; -.
DR KO; K09570; -.
DR OMA; TMSKGET; -.
DR OrthoDB; EOG7BZVT6; -.
DR PhylomeDB; Q00688; -.
DR ChiTaRS; FKBP3; human.
DR EvolutionaryTrace; Q00688; -.
DR GeneWiki; FKBP3; -.
DR GenomeRNAi; 2287; -.
DR NextBio; 9295; -.
DR PRO; PR:Q00688; -.
DR ArrayExpress; Q00688; -.
DR Bgee; Q00688; -.
DR CleanEx; HS_FKBP3; -.
DR Genevestigator; Q00688; -.
DR GO; GO:0016020; C:membrane; IBA:RefGenome.
DR GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR GO; GO:0005528; F:FK506 binding; IBA:RefGenome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:RefGenome.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR InterPro; IPR023566; PPIase_FKBP.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR10516; PTHR10516; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Isomerase; Nucleus;
KW Phosphoprotein; Reference proteome; Rotamase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 224 Peptidyl-prolyl cis-trans isomerase
FT FKBP3.
FT /FTId=PRO_0000075307.
FT DOMAIN 128 224 PPIase FKBP-type.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 36 36 Phosphoserine.
FT MOD_RES 152 152 Phosphoserine.
FT MOD_RES 170 170 N6-acetyllysine.
FT CONFLICT 181 181 T -> A (in Ref. 3; AAA58474).
FT HELIX 12 16
FT HELIX 23 32
FT HELIX 35 40
FT HELIX 47 51
FT HELIX 56 69
FT STRAND 111 117
FT STRAND 130 138
FT STRAND 144 147
FT TURN 155 157
FT STRAND 162 165
FT TURN 166 169
FT HELIX 173 179
FT STRAND 187 192
FT HELIX 194 196
FT TURN 197 201
FT HELIX 204 206
FT STRAND 214 224
SQ 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
//
MIM
186947
*RECORD*
*FIELD* NO
186947
*FIELD* TI
*186947 FK506-BINDING PROTEIN 3; FKBP3
;;FK506-BINDING PROTEIN, T-CELL, 25-KD; FKBP25
read more*FIELD* TX
For background information on FK506-binding proteins (FKBPs), see FKBP1A
(186945).
CLONING
Hung and Schreiber (1992) isolated a cDNA for FKBP25 from a human
hippocampus cDNA library by oligonucleotide screening. The deduced
protein contains 224 amino acids. Human FKBP25 shares 97% amino acid
identity with the bovine protein and 62% homology with human FKBP12
(186945). Wiederrecht et al. (1992) independently cloned cDNA for human
FKBP25.
MAPPING
Gross (2011) mapped the FKBP3 gene to chromosome 14q21.2 based on an
alignment of the FKBP3 sequence (GenBank GENBANK BT006904) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 3/3/2011.
2. 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. Wiederrecht, G.; Martin, M. M.; Sigal, N. H.; 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.
*FIELD* CN
Matthew B. Gross - updated: 3/3/2011
*FIELD* CD
Victor A. McKusick: 6/17/1992
*FIELD* ED
mgross: 03/03/2011
mgross: 3/3/2011
carol: 7/24/1998
alopez: 6/3/1997
carol: 2/23/1995
carol: 8/10/1992
carol: 7/23/1992
carol: 7/7/1992
carol: 6/17/1992
*RECORD*
*FIELD* NO
186947
*FIELD* TI
*186947 FK506-BINDING PROTEIN 3; FKBP3
;;FK506-BINDING PROTEIN, T-CELL, 25-KD; FKBP25
read more*FIELD* TX
For background information on FK506-binding proteins (FKBPs), see FKBP1A
(186945).
CLONING
Hung and Schreiber (1992) isolated a cDNA for FKBP25 from a human
hippocampus cDNA library by oligonucleotide screening. The deduced
protein contains 224 amino acids. Human FKBP25 shares 97% amino acid
identity with the bovine protein and 62% homology with human FKBP12
(186945). Wiederrecht et al. (1992) independently cloned cDNA for human
FKBP25.
MAPPING
Gross (2011) mapped the FKBP3 gene to chromosome 14q21.2 based on an
alignment of the FKBP3 sequence (GenBank GENBANK BT006904) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 3/3/2011.
2. 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. Wiederrecht, G.; Martin, M. M.; Sigal, N. H.; 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.
*FIELD* CN
Matthew B. Gross - updated: 3/3/2011
*FIELD* CD
Victor A. McKusick: 6/17/1992
*FIELD* ED
mgross: 03/03/2011
mgross: 3/3/2011
carol: 7/24/1998
alopez: 6/3/1997
carol: 2/23/1995
carol: 8/10/1992
carol: 7/23/1992
carol: 7/7/1992
carol: 6/17/1992