FKBP2_HUMAN
ID FKBP2_HUMAN Reviewed; 142 AA.
AC P26885; Q5BJH9; Q9BTS7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 182.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 rapamycin-
RT 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 project:
RT 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 guanine
RT 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., Buerckstuemmer T.,
RA 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of EPB41L2.
CC {ECO:0000269|PubMed:12606707}.
CC -!- INTERACTION:
CC P26885; P54253: ATXN1; NbExp=3; IntAct=EBI-719873, EBI-930964;
CC P26885; P42858: HTT; NbExp=6; IntAct=EBI-719873, EBI-466029;
CC P26885; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-719873, EBI-741480;
CC P26885; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-719873, EBI-10173939;
CC P26885; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-719873, EBI-947187;
CC P26885; Q9NRR5: UBQLN4; NbExp=2; IntAct=EBI-719873, EBI-711226;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: T-cells and thymus.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
CC {ECO:0000305}.
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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 CCDS; CCDS8063.1; -.
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_005273848.3.
DR PDB; 2PBC; X-ray; 1.80 A; A/B/C/D=43-142.
DR PDB; 4NNR; X-ray; 1.98 A; A/B=1-142.
DR PDBsum; 2PBC; -.
DR PDBsum; 4NNR; -.
DR AlphaFoldDB; P26885; -.
DR SMR; P26885; -.
DR BioGRID; 108576; 68.
DR IntAct; P26885; 14.
DR MINT; P26885; -.
DR STRING; 9606.ENSP00000378046; -.
DR BindingDB; P26885; -.
DR ChEMBL; CHEMBL4105949; -.
DR iPTMnet; P26885; -.
DR MetOSite; P26885; -.
DR PhosphoSitePlus; P26885; -.
DR BioMuta; FKBP2; -.
DR OGP; P26885; -.
DR EPD; P26885; -.
DR jPOST; P26885; -.
DR MassIVE; P26885; -.
DR PaxDb; P26885; -.
DR PeptideAtlas; P26885; -.
DR PRIDE; P26885; -.
DR ProteomicsDB; 54367; -.
DR TopDownProteomics; P26885; -.
DR Antibodypedia; 29197; 154 antibodies from 28 providers.
DR DNASU; 2286; -.
DR Ensembl; ENST00000309366.9; ENSP00000310935.4; ENSG00000173486.14.
DR Ensembl; ENST00000449942.6; ENSP00000398147.2; ENSG00000173486.14.
DR GeneID; 2286; -.
DR KEGG; hsa:2286; -.
DR MANE-Select; ENST00000309366.9; ENSP00000310935.4; NM_004470.4; NP_004461.2.
DR CTD; 2286; -.
DR DisGeNET; 2286; -.
DR GeneCards; FKBP2; -.
DR HGNC; HGNC:3718; FKBP2.
DR HPA; ENSG00000173486; Low tissue specificity.
DR MIM; 186946; gene.
DR neXtProt; NX_P26885; -.
DR OpenTargets; ENSG00000173486; -.
DR PharmGKB; PA28159; -.
DR VEuPathDB; HostDB:ENSG00000173486; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000157074; -.
DR HOGENOM; CLU_013615_8_2_1; -.
DR InParanoid; P26885; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; P26885; -.
DR TreeFam; TF105292; -.
DR PathwayCommons; P26885; -.
DR SignaLink; P26885; -.
DR BioGRID-ORCS; 2286; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; FKBP2; human.
DR EvolutionaryTrace; P26885; -.
DR GeneWiki; FKBP2; -.
DR GenomeRNAi; 2286; -.
DR Pharos; P26885; Tchem.
DR PRO; PR:P26885; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P26885; protein.
DR Bgee; ENSG00000173486; Expressed in pituitary gland and 96 other tissues.
DR ExpressionAtlas; P26885; baseline and differential.
DR Genevisible; P26885; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005528; F:FK506 binding; TAS:ProtInc.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PTHR45779; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Isomerase; Membrane;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..21
FT CHAIN 22..142
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP2"
FT /id="PRO_0000025506"
FT DOMAIN 49..137
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT MOTIF 139..142
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="R -> Q (in dbSNP:rs4672)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050623"
FT VARIANT 21..22
FT /note="TA -> S"
FT /id="VAR_006410"
FT VARIANT 25
FT /note="A -> T"
FT /id="VAR_006411"
FT VARIANT 97
FT /note="C -> Y"
FT /id="VAR_006412"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2PBC"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2PBC"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:2PBC"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2PBC"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2PBC"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2PBC"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:2PBC"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2PBC"
FT TURN 111..115
FT /evidence="ECO:0007829|PDB:2PBC"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2PBC"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:2PBC"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2PBC"
SQ SEQUENCE 142 AA; 15649 MW; 01024F869BA7B5DA CRC64;
MRLSWFRVLT VLSICLSAVA TATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL
EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK
IPGGATLVFE VELLKIERRT EL
