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-NOV-2009, entry version 88. DE RecName: Full=FK506-binding protein 2; DE EC=5.2.1.8; DE AltName: Full=Peptidyl-prolyl cis-trans isomerase; DE Short=PPIase; DE Short=Rotamase; DE AltName: Full=13 kDa FKBP; DE AltName: Full=FKBP-13; 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 MEDLINE=91319747; 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 MEDLINE=93112052; 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. 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=1; 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 IPI; IPI00002535; -. DR PIR; JC1365; JC1365. DR RefSeq; NP_001128680.1; -. DR RefSeq; NP_004461.2; -. DR RefSeq; NP_476433.1; -. DR UniGene; Hs.227729; -. DR PDB; 2PBC; X-ray; 1.80 A; A/B/C/D=43-142. DR PDBsum; 2PBC; -. DR IntAct; P26885; 4. DR STRING; P26885; -. DR OGP; P26885; -. DR PeptideAtlas; P26885; -. DR PRIDE; P26885; -. DR Ensembl; ENST00000309366; ENSP00000310935; ENSG00000173486; Homo sapiens. DR Ensembl; ENST00000394540; ENSP00000378046; ENSG00000173486; Homo sapiens. DR Ensembl; ENST00000449942; ENSP00000398147; ENSG00000173486; Homo sapiens. DR GeneID; 2286; -. DR KEGG; hsa:2286; -. DR UCSC; uc001nyy.1; human. DR CTD; 2286; -. DR GeneCards; GC11P063764; -. DR H-InvDB; HIX0009756; -. DR HGNC; HGNC:3718; FKBP2. DR HPA; CAB025561; -. DR MIM; 186946; gene. DR PharmGKB; PA28159; -. DR HOGENOM; P26885; -. DR HOVERGEN; P26885; -. DR OMA; KKLQIGI; -. DR BRENDA; 5.2.1.8; 247. DR NextBio; 9289; -. DR ArrayExpress; P26885; -. DR Bgee; P26885; -. DR CleanEx; HS_FKBP2; -. DR Genevestigator; P26885; -. DR GermOnline; ENSG00000173486; Homo sapiens. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005528; F:FK506 binding; TAS:ProtInc. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW. DR InterPro; IPR001179; PPIase_FKBP. DR PANTHER; PTHR10516; PPIase_FKBP; 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; Rotamase; Signal. FT SIGNAL 1 21 FT CHAIN 22 142 FK506-binding protein 2. 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 //