[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Colon carcinoma; DOI=10.1073/pnas.88.15.6677; PubMed=1713687 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1016/0006-291X(92)92276-4; PubMed=1281998 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.2628047100; PubMed=12606707 [NCBI, ExPASy, EBI, Israel, Japan] 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 [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of EPB41L2.
INTERACTION:
Q9NRR5:UBQLN4; NbExp=1; IntAct=EBI-719873, EBI-711226;
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein (Probable).
TISSUE SPECIFICITY: T-cells and thymus.
SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.
SIMILARITY: Contains 1 PPIase FKBP-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M65128; AAA58473.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M75099; AAA36563.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003384; AAH03384.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC091475; AAH91475.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00002535; -.

PIR

JC1365; JC1365.

RefSeq

NP_001128680.1; -.
NP_004461.2; -.
NP_476433.1; -.

UniGene

Hs.227729

3D structure databases

PDB

2PBC; X-ray; 1.80 A; A/B/C/D=43-142.

[ExPASy / RCSB / EBI]

PDBsum

2PBC; -.

ModBase

P26885.

Protein-protein interaction databases

IntAct

P26885; 4.

Enzyme and pathway databases

BRENDA

5.2.1.8; 247.

2D gel databases

OGP

P26885; -.

Organism-specific databases

GC11P063764; -.

HIX0009756; -.

HGNC:3718; FKBP2.

186946; gene. [NCBI / EBI]

PharmGKB

PA28159; -.

Gene expression databases

P26885; -.

P26885; -.

HS_FKBP2; -.

ENSG00000173486; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005528;	Molecular function: FK506 binding (traceable author statement from ProtInc).
GO:0003755;	Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006457;	Biological process: protein folding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001179; PPIase_FKBP.
Graphical view of domain structure.

PANTHER

PTHR10516; PPIase_FKBP; 1.

Pfam

PF00254; FKBP_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS50059; FKBP_PPIASE; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

P26885; -.

PRIDE

P26885; -.

Genome annotation databases

Ensembl

ENSG00000173486; Homo sapiens. [Contig view]

GeneID

2286; -.

KEGG

hsa:2286; -.

Phylogenomic databases

HOGENOM

P26885; -.

HOVERGEN

P26885; -.

OMA

P26885; KKLQIGI.

Other

9289; -.

FKBP2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Endoplasmic reticulum; Isomerase; Membrane; Polymorphism; Rotamase; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`CHAIN`	`22 142`	`121`	`FK506-binding protein 2.`	`PRO_0000025506`
`DOMAIN`	`49 137`	`89`	`PPIase FKBP-type.`
`MOTIF`	`139 142`	`4`	`Prevents secretion from ER (Potential).`
`VARIANT`	`7 7`	`1`	`R -> Q (in dbSNP:rs4672 [NCBI]).`	`VAR_050623`
`VARIANT`	`21 22`	`2`	`TA -> S.`	`VAR_006410`
`VARIANT`	`25 25`	`1`	`A -> T.`	`VAR_006411`
`VARIANT`	`97 97`	`1`	`C -> Y.`	`VAR_006412 [3D]`
`STRAND`	`51 59`	`9`
`STRAND`	`65 69`	`5`
`TURN`	`70 73`	`4`
`STRAND`	`76 79`	`4`
`STRAND`	`82 85`	`4`
`HELIX`	`87 90`	`4`
`STRAND`	`101 106`	`6`
`HELIX`	`108 110`	`3`
`TURN`	`111 115`	`5`
`TURN`	`118 120`	`3`
`STRAND`	`127 136`	`10`
`HELIX`	`137 139`	`3`

Sequence information

Length: 142 AA [This is the length of the unprocessed precursor]

Molecular weight: 15649 Da [This is the MW of the unprocessed precursor]

CRC64: 01024F869BA7B5DA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRLSWFRVLT VLSICLSAVA TATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL 

        70         80         90        100        110        120 
EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK 

       130        140 
IPGGATLVFE VELLKIERRT EL

P26885 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools