Full text data of FKBP2
FKBP2
(FKBP13)
[Confidence: high (present in two of the MS resources)]
Peptidyl-prolyl cis-trans isomerase FKBP2; PPIase FKBP2; 5.2.1.8 (13 kDa FK506-binding protein; 13 kDa FKBP; FKBP-13; FK506-binding protein 2; FKBP-2; Immunophilin FKBP13; Rotamase; Flags: Precursor)
Peptidyl-prolyl cis-trans isomerase FKBP2; PPIase FKBP2; 5.2.1.8 (13 kDa FK506-binding protein; 13 kDa FKBP; FKBP-13; FK506-binding protein 2; FKBP-2; Immunophilin FKBP13; Rotamase; Flags: Precursor)
hRBCD
IPI00002535
IPI00002535 FK506-binding protein 2 precursor FK506-binding protein 2 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a ER, membrane associated n/a found at its expected molecular weight found at molecular weight
IPI00002535 FK506-binding protein 2 precursor FK506-binding protein 2 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a ER, membrane associated n/a found at its expected molecular weight found at molecular weight
UniProt
P26885
ID FKBP2_HUMAN Reviewed; 142 AA.
AC P26885; Q5BJH9; Q9BTS7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP2;
DE Short=PPIase FKBP2;
DE EC=5.2.1.8;
DE AltName: Full=13 kDa FK506-binding protein;
DE Short=13 kDa FKBP;
DE Short=FKBP-13;
DE AltName: Full=FK506-binding protein 2;
DE Short=FKBP-2;
DE AltName: Full=Immunophilin FKBP13;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP2; Synonyms=FKBP13;
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].
RC TISSUE=Colon carcinoma;
RX PubMed=1713687; DOI=10.1073/pnas.88.15.6677;
RA Jin Y.-J., Albers M.W., Lane W.S., Bierer B.E., Schreiber S.L.,
RA Burakoff S.J.;
RT "Molecular cloning of a membrane-associated human FK506- and
RT rapamycin-binding protein, FKBP-13.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6677-6681(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1281998; DOI=10.1016/0006-291X(92)92276-4;
RA Dilella A.G., Hawkins A., Craig R.J., Schreiber S.L., Griffin C.A.;
RT "Chromosomal band assignments of the genes encoding human FKBP12 and
RT FKBP13.";
RL Biochem. Biophys. Res. Commun. 189:819-823(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-7.
RC TISSUE=Placenta;
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 [4]
RP INTERACTION WITH ARFGEF1.
RX PubMed=12606707; DOI=10.1073/pnas.2628047100;
RA Padilla P.I., Chang M.J., Pacheco-Rodriguez G., Adamik R., Moss J.,
RA Vaughan M.;
RT "Interaction of FK506-binding protein 13 with brefeldin A-inhibited
RT guanine nucleotide-exchange protein 1 (BIG1): effects of FK506.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2322-2327(2003).
RN [5]
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of
CC EPB41L2.
CC -!- INTERACTION:
CC Q9NRR5:UBQLN4; NbExp=2; IntAct=EBI-719873, EBI-711226;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein (Probable).
CC -!- TISSUE SPECIFICITY: T-cells and thymus.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2
CC subfamily.
CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M65128; AAA58473.1; -; mRNA.
DR EMBL; M75099; AAA36563.1; -; mRNA.
DR EMBL; BC003384; AAH03384.1; -; mRNA.
DR EMBL; BC091475; AAH91475.1; -; mRNA.
DR PIR; JC1365; JC1365.
DR RefSeq; NP_001128680.1; NM_001135208.1.
DR RefSeq; NP_004461.2; NM_004470.3.
DR RefSeq; NP_476433.1; NM_057092.2.
DR RefSeq; XP_005273905.1; XM_005273848.1.
DR UniGene; Hs.227729; -.
DR PDB; 2PBC; X-ray; 1.80 A; A/B/C/D=43-142.
DR PDBsum; 2PBC; -.
DR ProteinModelPortal; P26885; -.
DR SMR; P26885; 43-140.
DR IntAct; P26885; 5.
DR MINT; MINT-1421370; -.
DR STRING; 9606.ENSP00000310935; -.
DR PhosphoSite; P26885; -.
DR DMDM; 23503054; -.
DR OGP; P26885; -.
DR PaxDb; P26885; -.
DR PeptideAtlas; P26885; -.
DR PRIDE; P26885; -.
DR DNASU; 2286; -.
DR Ensembl; ENST00000309366; ENSP00000310935; ENSG00000173486.
DR Ensembl; ENST00000394540; ENSP00000378046; ENSG00000173486.
DR Ensembl; ENST00000449942; ENSP00000398147; ENSG00000173486.
DR GeneID; 2286; -.
DR KEGG; hsa:2286; -.
DR UCSC; uc001nyy.3; human.
DR CTD; 2286; -.
DR GeneCards; GC11P064008; -.
DR HGNC; HGNC:3718; FKBP2.
DR HPA; CAB025561; -.
DR MIM; 186946; gene.
DR neXtProt; NX_P26885; -.
DR PharmGKB; PA28159; -.
DR eggNOG; COG0545; -.
DR HOGENOM; HOG000154887; -.
DR HOVERGEN; HBG051623; -.
DR InParanoid; P26885; -.
DR KO; K09569; -.
DR OMA; KRVENCT; -.
DR OrthoDB; EOG7T1R9S; -.
DR PhylomeDB; P26885; -.
DR ChiTaRS; FKBP2; human.
DR EvolutionaryTrace; P26885; -.
DR GeneWiki; FKBP2; -.
DR GenomeRNAi; 2286; -.
DR NextBio; 9289; -.
DR PRO; PR:P26885; -.
DR ArrayExpress; P26885; -.
DR Bgee; P26885; -.
DR CleanEx; HS_FKBP2; -.
DR Genevestigator; P26885; -.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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: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; Complete proteome; Endoplasmic reticulum; Isomerase;
KW Membrane; Polymorphism; Reference proteome; Rotamase; Signal.
FT SIGNAL 1 21
FT CHAIN 22 142 Peptidyl-prolyl cis-trans isomerase
FT FKBP2.
FT /FTId=PRO_0000025506.
FT DOMAIN 49 137 PPIase FKBP-type.
FT MOTIF 139 142 Prevents secretion from ER (Potential).
FT VARIANT 7 7 R -> Q (in dbSNP:rs4672).
FT /FTId=VAR_050623.
FT VARIANT 21 22 TA -> S.
FT /FTId=VAR_006410.
FT VARIANT 25 25 A -> T.
FT /FTId=VAR_006411.
FT VARIANT 97 97 C -> Y.
FT /FTId=VAR_006412.
FT STRAND 51 59
FT STRAND 65 69
FT TURN 70 73
FT STRAND 76 79
FT STRAND 82 85
FT HELIX 87 90
FT STRAND 101 106
FT HELIX 108 110
FT TURN 111 115
FT TURN 118 120
FT STRAND 127 136
FT HELIX 137 139
SQ SEQUENCE 142 AA; 15649 MW; 01024F869BA7B5DA CRC64;
MRLSWFRVLT VLSICLSAVA TATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL
EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK
IPGGATLVFE VELLKIERRT EL
//
ID FKBP2_HUMAN Reviewed; 142 AA.
AC P26885; Q5BJH9; Q9BTS7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP2;
DE Short=PPIase FKBP2;
DE EC=5.2.1.8;
DE AltName: Full=13 kDa FK506-binding protein;
DE Short=13 kDa FKBP;
DE Short=FKBP-13;
DE AltName: Full=FK506-binding protein 2;
DE Short=FKBP-2;
DE AltName: Full=Immunophilin FKBP13;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP2; Synonyms=FKBP13;
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].
RC TISSUE=Colon carcinoma;
RX PubMed=1713687; DOI=10.1073/pnas.88.15.6677;
RA Jin Y.-J., Albers M.W., Lane W.S., Bierer B.E., Schreiber S.L.,
RA Burakoff S.J.;
RT "Molecular cloning of a membrane-associated human FK506- and
RT rapamycin-binding protein, FKBP-13.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6677-6681(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1281998; DOI=10.1016/0006-291X(92)92276-4;
RA Dilella A.G., Hawkins A., Craig R.J., Schreiber S.L., Griffin C.A.;
RT "Chromosomal band assignments of the genes encoding human FKBP12 and
RT FKBP13.";
RL Biochem. Biophys. Res. Commun. 189:819-823(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-7.
RC TISSUE=Placenta;
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 [4]
RP INTERACTION WITH ARFGEF1.
RX PubMed=12606707; DOI=10.1073/pnas.2628047100;
RA Padilla P.I., Chang M.J., Pacheco-Rodriguez G., Adamik R., Moss J.,
RA Vaughan M.;
RT "Interaction of FK506-binding protein 13 with brefeldin A-inhibited
RT guanine nucleotide-exchange protein 1 (BIG1): effects of FK506.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2322-2327(2003).
RN [5]
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of
CC EPB41L2.
CC -!- INTERACTION:
CC Q9NRR5:UBQLN4; NbExp=2; IntAct=EBI-719873, EBI-711226;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein (Probable).
CC -!- TISSUE SPECIFICITY: T-cells and thymus.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2
CC subfamily.
CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M65128; AAA58473.1; -; mRNA.
DR EMBL; M75099; AAA36563.1; -; mRNA.
DR EMBL; BC003384; AAH03384.1; -; mRNA.
DR EMBL; BC091475; AAH91475.1; -; mRNA.
DR PIR; JC1365; JC1365.
DR RefSeq; NP_001128680.1; NM_001135208.1.
DR RefSeq; NP_004461.2; NM_004470.3.
DR RefSeq; NP_476433.1; NM_057092.2.
DR RefSeq; XP_005273905.1; XM_005273848.1.
DR UniGene; Hs.227729; -.
DR PDB; 2PBC; X-ray; 1.80 A; A/B/C/D=43-142.
DR PDBsum; 2PBC; -.
DR ProteinModelPortal; P26885; -.
DR SMR; P26885; 43-140.
DR IntAct; P26885; 5.
DR MINT; MINT-1421370; -.
DR STRING; 9606.ENSP00000310935; -.
DR PhosphoSite; P26885; -.
DR DMDM; 23503054; -.
DR OGP; P26885; -.
DR PaxDb; P26885; -.
DR PeptideAtlas; P26885; -.
DR PRIDE; P26885; -.
DR DNASU; 2286; -.
DR Ensembl; ENST00000309366; ENSP00000310935; ENSG00000173486.
DR Ensembl; ENST00000394540; ENSP00000378046; ENSG00000173486.
DR Ensembl; ENST00000449942; ENSP00000398147; ENSG00000173486.
DR GeneID; 2286; -.
DR KEGG; hsa:2286; -.
DR UCSC; uc001nyy.3; human.
DR CTD; 2286; -.
DR GeneCards; GC11P064008; -.
DR HGNC; HGNC:3718; FKBP2.
DR HPA; CAB025561; -.
DR MIM; 186946; gene.
DR neXtProt; NX_P26885; -.
DR PharmGKB; PA28159; -.
DR eggNOG; COG0545; -.
DR HOGENOM; HOG000154887; -.
DR HOVERGEN; HBG051623; -.
DR InParanoid; P26885; -.
DR KO; K09569; -.
DR OMA; KRVENCT; -.
DR OrthoDB; EOG7T1R9S; -.
DR PhylomeDB; P26885; -.
DR ChiTaRS; FKBP2; human.
DR EvolutionaryTrace; P26885; -.
DR GeneWiki; FKBP2; -.
DR GenomeRNAi; 2286; -.
DR NextBio; 9289; -.
DR PRO; PR:P26885; -.
DR ArrayExpress; P26885; -.
DR Bgee; P26885; -.
DR CleanEx; HS_FKBP2; -.
DR Genevestigator; P26885; -.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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: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; Complete proteome; Endoplasmic reticulum; Isomerase;
KW Membrane; Polymorphism; Reference proteome; Rotamase; Signal.
FT SIGNAL 1 21
FT CHAIN 22 142 Peptidyl-prolyl cis-trans isomerase
FT FKBP2.
FT /FTId=PRO_0000025506.
FT DOMAIN 49 137 PPIase FKBP-type.
FT MOTIF 139 142 Prevents secretion from ER (Potential).
FT VARIANT 7 7 R -> Q (in dbSNP:rs4672).
FT /FTId=VAR_050623.
FT VARIANT 21 22 TA -> S.
FT /FTId=VAR_006410.
FT VARIANT 25 25 A -> T.
FT /FTId=VAR_006411.
FT VARIANT 97 97 C -> Y.
FT /FTId=VAR_006412.
FT STRAND 51 59
FT STRAND 65 69
FT TURN 70 73
FT STRAND 76 79
FT STRAND 82 85
FT HELIX 87 90
FT STRAND 101 106
FT HELIX 108 110
FT TURN 111 115
FT TURN 118 120
FT STRAND 127 136
FT HELIX 137 139
SQ SEQUENCE 142 AA; 15649 MW; 01024F869BA7B5DA CRC64;
MRLSWFRVLT VLSICLSAVA TATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL
EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK
IPGGATLVFE VELLKIERRT EL
//
MIM
186946
*RECORD*
*FIELD* NO
186946
*FIELD* TI
*186946 FK506-BINDING PROTEIN 2; FKBP2
;;FK506-BINDING PROTEIN, T-CELL, 13-KD; FKBP13
read more*FIELD* TX
For background information on FK506-binding proteins (FKBPs), see FKBP1A
(186945).
CLONING
Jin et al. (1991) reported the cloning and subcellular localization of a
13-kD FK506-binding protein (FKBP13), which has a 21-amino acid signal
peptide and appears to be membrane-associated. The 120-amino acid mature
protein appears to lack a transmembrane domain but a potential
endoplasmic reticulum retention sequence (arg-thr-glu-leu) is found at
its C terminus. FKBP13 shares 51% nucleotide sequence identity and 43%
amino acid sequence identity with FKBP12 (FKBP1; 186945), the
predominant FK506- and rapamycin-binding protein in human T cells. Jin
et al. (1991) noted that conserved residues that comprise the drug
binding site and rotamase active site of FKBP12 are completely conserved
in FKBP13.
GENE STRUCTURE
DiLella et al. (1992) found that the FKBP2 gene is 3 kb long and
contains 6 exons.
MAPPING
By fluorescence in situ hybridization, DiLella et al. (1992) mapped the
FKBP2 gene to 11q13.1-q13.3.
Courseaux et al. (1996) used a combination of methods to refine maps of
the approximately 5-Mb region of 11q13 that includes MEN1 (131100). They
proposed the following gene order:
cen--PGA--FTH1--UGB--AHNAK--ROM1--MDU1--CHRM1--COX8--EMK1--FKBP2--PLCB3--[PYGM,
ZFM1]--FAU--CAPN1--[MLK3, RELA]--FOSL1--SEA--CFL1--tel.
*FIELD* RF
1. Courseaux, A.; Grosgeorge, J.; Gaudray, P.; Pannett, A. A. J.;
Forbes, S. A.; Williamson, C.; Bassett, D.; Thakker, R. V.; Teh, B.
T.; Farnebo, F.; Shepherd, J.; Skogseid, B.; Larsson, C.; Giraud,
S.; Zhang, C. X.; Salandre, J.; Calender, A.: Definition of the minimal
MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. Genomics 37:
354-365, 1996.
2. DiLella, A. G.; Hawkins, A.; Craig, R. J.; Schreiber, S. L.; Griffin,
C. A.: Chromosomal band assignments of the genes encoding human FKBP12
and FKBP13. Biochem. Biophys. Res. Commun. 189: 819-823, 1992.
3. Jin, Y.-J.; Albers, M. W.; Lane, W. S.; Bierer, B. E.; Schreiber,
S. L.; Burakoff, S. J.: Molecular cloning of a membrane-associated
human FK506- and rapamycin-binding protein, FKBP-13. Proc. Nat. Acad.
Sci. 88: 6677-6681, 1991.
*FIELD* CN
Alan F. Scott - updated: 8/5/1997
*FIELD* CD
Victor A. McKusick: 9/19/1991
*FIELD* ED
mgross: 03/03/2011
terry: 2/23/2011
carol: 2/22/2011
alopez: 9/3/1998
terry: 8/5/1997
alopez: 6/3/1997
carol: 2/23/1995
carol: 2/4/1993
supermim: 3/16/1992
carol: 9/19/1991
*RECORD*
*FIELD* NO
186946
*FIELD* TI
*186946 FK506-BINDING PROTEIN 2; FKBP2
;;FK506-BINDING PROTEIN, T-CELL, 13-KD; FKBP13
read more*FIELD* TX
For background information on FK506-binding proteins (FKBPs), see FKBP1A
(186945).
CLONING
Jin et al. (1991) reported the cloning and subcellular localization of a
13-kD FK506-binding protein (FKBP13), which has a 21-amino acid signal
peptide and appears to be membrane-associated. The 120-amino acid mature
protein appears to lack a transmembrane domain but a potential
endoplasmic reticulum retention sequence (arg-thr-glu-leu) is found at
its C terminus. FKBP13 shares 51% nucleotide sequence identity and 43%
amino acid sequence identity with FKBP12 (FKBP1; 186945), the
predominant FK506- and rapamycin-binding protein in human T cells. Jin
et al. (1991) noted that conserved residues that comprise the drug
binding site and rotamase active site of FKBP12 are completely conserved
in FKBP13.
GENE STRUCTURE
DiLella et al. (1992) found that the FKBP2 gene is 3 kb long and
contains 6 exons.
MAPPING
By fluorescence in situ hybridization, DiLella et al. (1992) mapped the
FKBP2 gene to 11q13.1-q13.3.
Courseaux et al. (1996) used a combination of methods to refine maps of
the approximately 5-Mb region of 11q13 that includes MEN1 (131100). They
proposed the following gene order:
cen--PGA--FTH1--UGB--AHNAK--ROM1--MDU1--CHRM1--COX8--EMK1--FKBP2--PLCB3--[PYGM,
ZFM1]--FAU--CAPN1--[MLK3, RELA]--FOSL1--SEA--CFL1--tel.
*FIELD* RF
1. Courseaux, A.; Grosgeorge, J.; Gaudray, P.; Pannett, A. A. J.;
Forbes, S. A.; Williamson, C.; Bassett, D.; Thakker, R. V.; Teh, B.
T.; Farnebo, F.; Shepherd, J.; Skogseid, B.; Larsson, C.; Giraud,
S.; Zhang, C. X.; Salandre, J.; Calender, A.: Definition of the minimal
MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. Genomics 37:
354-365, 1996.
2. DiLella, A. G.; Hawkins, A.; Craig, R. J.; Schreiber, S. L.; Griffin,
C. A.: Chromosomal band assignments of the genes encoding human FKBP12
and FKBP13. Biochem. Biophys. Res. Commun. 189: 819-823, 1992.
3. Jin, Y.-J.; Albers, M. W.; Lane, W. S.; Bierer, B. E.; Schreiber,
S. L.; Burakoff, S. J.: Molecular cloning of a membrane-associated
human FK506- and rapamycin-binding protein, FKBP-13. Proc. Nat. Acad.
Sci. 88: 6677-6681, 1991.
*FIELD* CN
Alan F. Scott - updated: 8/5/1997
*FIELD* CD
Victor A. McKusick: 9/19/1991
*FIELD* ED
mgross: 03/03/2011
terry: 2/23/2011
carol: 2/22/2011
alopez: 9/3/1998
terry: 8/5/1997
alopez: 6/3/1997
carol: 2/23/1995
carol: 2/4/1993
supermim: 3/16/1992
carol: 9/19/1991