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Peptidyl-prolyl cis-trans isomerase FKBP2 (PPIase FKBP2) (EC 5.2.1.8) (13 kDa FK506-binding protein) (13 kDa FKBP) (FKBP-13) (FK506-binding protein 2) (FKBP-2) (Immunophilin FKBP13) (Rotamase)

 FKBP2_HUMAN             Reviewed;         142 AA.
P26885; Q5BJH9; Q9BTS7;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
05-DEC-2018, entry version 162.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP2;
Short=PPIase FKBP2;
EC=5.2.1.8;
AltName: Full=13 kDa FK506-binding protein;
Short=13 kDa FKBP;
Short=FKBP-13;
AltName: Full=FK506-binding protein 2;
Short=FKBP-2;
AltName: Full=Immunophilin FKBP13;
AltName: Full=Rotamase;
Flags: Precursor;
Name=FKBP2; Synonyms=FKBP13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Colon carcinoma;
PubMed=1713687; DOI=10.1073/pnas.88.15.6677;
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. Natl. Acad. Sci. U.S.A. 88:6677-6681(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1281998; DOI=10.1016/0006-291X(92)92276-4;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-7.
TISSUE=Placenta;
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).
[4]
INTERACTION WITH ARFGEF1.
PubMed=12606707; DOI=10.1073/pnas.2628047100;
Padilla P.I., Chang M.J., Pacheco-Rodriguez G., Adamik R., Moss J.,
Vaughan M.;
"Interaction of FK506-binding protein 13 with brefeldin A-inhibited
guanine nucleotide-exchange protein 1 (BIG1): effects of FK506.";
Proc. Natl. Acad. Sci. U.S.A. 100:2322-2327(2003).
[5]
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).
[6]
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).
[7]
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).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides.
-!- 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 by both FK506 and rapamycin.
-!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of
EPB41L2. {ECO:0000269|PubMed:12606707}.
-!- INTERACTION:
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-719873, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-719873, EBI-10173939;
Q9NRR5:UBQLN4; NbExp=2; IntAct=EBI-719873, EBI-711226;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: T-cells and thymus.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M65128; AAA58473.1; -; mRNA.
EMBL; M75099; AAA36563.1; -; mRNA.
EMBL; BC003384; AAH03384.1; -; mRNA.
EMBL; BC091475; AAH91475.1; -; mRNA.
CCDS; CCDS8063.1; -.
PIR; JC1365; JC1365.
RefSeq; NP_001128680.1; NM_001135208.1.
RefSeq; NP_004461.2; NM_004470.3.
RefSeq; NP_476433.1; NM_057092.2.
RefSeq; XP_005273905.1; XM_005273848.3.
UniGene; Hs.227729; -.
PDB; 2PBC; X-ray; 1.80 A; A/B/C/D=43-142.
PDB; 4NNR; X-ray; 1.98 A; A/B=1-142.
PDBsum; 2PBC; -.
PDBsum; 4NNR; -.
ProteinModelPortal; P26885; -.
SMR; P26885; -.
BioGrid; 108576; 47.
IntAct; P26885; 9.
STRING; 9606.ENSP00000310935; -.
iPTMnet; P26885; -.
PhosphoSitePlus; P26885; -.
BioMuta; FKBP2; -.
OGP; P26885; -.
EPD; P26885; -.
PaxDb; P26885; -.
PeptideAtlas; P26885; -.
PRIDE; P26885; -.
ProteomicsDB; 54367; -.
TopDownProteomics; P26885; -.
DNASU; 2286; -.
Ensembl; ENST00000309366; ENSP00000310935; ENSG00000173486.
Ensembl; ENST00000394540; ENSP00000378046; ENSG00000173486.
Ensembl; ENST00000449942; ENSP00000398147; ENSG00000173486.
GeneID; 2286; -.
KEGG; hsa:2286; -.
CTD; 2286; -.
DisGeNET; 2286; -.
EuPathDB; HostDB:ENSG00000173486.12; -.
GeneCards; FKBP2; -.
HGNC; HGNC:3718; FKBP2.
HPA; CAB025561; -.
HPA; HPA049405; -.
MIM; 186946; gene.
neXtProt; NX_P26885; -.
OpenTargets; ENSG00000173486; -.
PharmGKB; PA28159; -.
eggNOG; KOG0549; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00940000157074; -.
HOGENOM; HOG000154887; -.
HOVERGEN; HBG051623; -.
InParanoid; P26885; -.
KO; K09569; -.
OMA; GILGMCE; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; P26885; -.
TreeFam; TF105292; -.
ChiTaRS; FKBP2; human.
EvolutionaryTrace; P26885; -.
GeneWiki; FKBP2; -.
GenomeRNAi; 2286; -.
PRO; PR:P26885; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000173486; Expressed in 230 organ(s), highest expression level in pituitary gland.
CleanEx; HS_FKBP2; -.
ExpressionAtlas; P26885; baseline and differential.
Genevisible; P26885; HS.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005528; F:FK506 binding; TAS:ProtInc.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; Complete proteome; Endoplasmic reticulum; Isomerase;
Membrane; Polymorphism; Reference proteome; Rotamase; Signal.
SIGNAL 1 21
CHAIN 22 142 Peptidyl-prolyl cis-trans isomerase
FKBP2.
/FTId=PRO_0000025506.
DOMAIN 49 137 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
MOTIF 139 142 Prevents secretion from ER.
{ECO:0000255}.
VARIANT 7 7 R -> Q (in dbSNP:rs4672).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_050623.
VARIANT 21 22 TA -> S.
/FTId=VAR_006410.
VARIANT 25 25 A -> T.
/FTId=VAR_006411.
VARIANT 97 97 C -> Y.
/FTId=VAR_006412.
STRAND 51 59 {ECO:0000244|PDB:2PBC}.
STRAND 65 69 {ECO:0000244|PDB:2PBC}.
TURN 70 73 {ECO:0000244|PDB:2PBC}.
STRAND 76 79 {ECO:0000244|PDB:2PBC}.
STRAND 82 85 {ECO:0000244|PDB:2PBC}.
HELIX 87 90 {ECO:0000244|PDB:2PBC}.
STRAND 101 106 {ECO:0000244|PDB:2PBC}.
HELIX 108 110 {ECO:0000244|PDB:2PBC}.
TURN 111 115 {ECO:0000244|PDB:2PBC}.
TURN 118 120 {ECO:0000244|PDB:2PBC}.
STRAND 127 136 {ECO:0000244|PDB:2PBC}.
HELIX 137 139 {ECO:0000244|PDB:2PBC}.
SEQUENCE 142 AA; 15649 MW; 01024F869BA7B5DA CRC64;
MRLSWFRVLT VLSICLSAVA TATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL
EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK
IPGGATLVFE VELLKIERRT EL


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