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   27-MAR-2024, entry version 191.
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; 76.
DR   IntAct; P26885; 15.
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; 9606-ENSP00000378046; -.
DR   PeptideAtlas; P26885; -.
DR   ProteomicsDB; 54367; -.
DR   Pumba; P26885; -.
DR   TopDownProteomics; P26885; -.
DR   Antibodypedia; 29197; 174 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   AGR; HGNC:3718; -.
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   PhylomeDB; P26885; -.
DR   TreeFam; TF105292; -.
DR   PathwayCommons; P26885; -.
DR   SignaLink; P26885; -.
DR   BioGRID-ORCS; 2286; 17 hits in 1155 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 98 other cell types or tissues.
DR   ExpressionAtlas; P26885; baseline and differential.
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   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:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP2; 1.
DR   PANTHER; PTHR45779; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   Genevisible; P26885; HS.
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
//