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Showing Protein Peptidyl-prolyl cis-trans isomerase FKBP8 (HMDBP07687)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP07687
Secondary Accession Numbers
  • 13396
Name Peptidyl-prolyl cis-trans isomerase FKBP8
Synonyms
  1. 38 kDa FK506-binding protein
  2. 38 kDa FKBP
  3. FK506-binding protein 8
  4. FKBP-38
  5. FKBP-8
  6. FKBPR38
  7. PPIase FKBP8
  8. Rotamase
  9. hFKBP38
Gene Name FKBP8
Protein Type Unknown
Biological Properties
General Function Involved in protein folding
Specific Function Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
Process
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein folding
protein metabolic process
Cellular Location
  1. Mitochondrion membrane
  2. Cytoplasmic side
  3. Single-pass membrane protein
Gene Properties
Chromosome Location Chromosome:1
Locus 19p12
SNPs FKBP8
Gene Sequence 
>1239 bp
ATGGCATCGTGTGCTGAACCCTCTGAGCCCTCTGCCCCACTGCCCGCCGGGGTCCCACCG
CTCGAGGACTTCGAGGTACTGGATGGGGTTGAGGATGCAGAGGGTGAGGAGGAAGAGGAG
GAGGAAGAGGAGGAAGAGGATGACCTGAGTGAGCTGCCACCGCTGGAGGACATGGGACAA
CCCCCGGCGGAGGAGGCTGAGCAGCCTGGGGCCCTGGCCCGAGAGTTCCTTGCTGCCATG
GAGCCCGAGCCCGCCCCAGCCCCGGCCCCAGAAGAGTGGCTGGACATTCTGGGGAACGGG
CTGTTGAGGAAGAAGACGCTGGTCCCAGGGCCGCCAGGTTCGAGCCGCCCGGTCAAGGGC
CAGGTGGTCACCGTACATCTGCAGACGTCGCTGGAGAATGGCACACGGGTGCAGGAGGAG
CCGGAGCTGGTGTTCACTCTGGGTGACTGTGACGTCATCCAGGCCCTGGATCTCAGTGTC
CCACTCATGGACGTGGGGGAGACGGCCATGGTCACTGCTGACTCCAAGTACTGCTACGGC
CCCCAAGGCAGGAGCCCATACATCCCCCCGCACGCGGCCCTGTGCCTGGAGGTGACCCTG
AAGACGGCTGTGGACGGGCCTGACCTGGAGATGCTCACGGGGCAGGAGCGCGTGGCCCTG
GCCAACCGGAAGCGGGAGTGCGGCAACGCCCACTACCAGCGGGCGGACTTCGTCCTGGCC
GCCAACTCCTACGACCTCGCCATCAAGGCTATCACCTCCAGCGCCAAAGTGGACATGACG
TTCGAGGAGGAGGCACAGCTCCTGCAGTTGAAGGTGAAGTGTCTGAACAACCTGGCGGCC
TCGCAGCTGAAGCTCGACCACTACCGCGCAGCCCTGCGCTCCTGCAGCCTTGTGCTGGAG
CACCAGCCAGACAACATCAAGGCTCTCTTCCGCAAGGGCAAGGTGCTGGCCCAGCAGGGG
GAGTACAGTGAGGCCATCCCCATCCTGAGGGCAGCCCTGAAGCTGGAACCTTCCAACAAG
ACGATCCACGCAGAGCTCTCAAAGCTGGTGAAGAAGCATGCGGCGCAGCGGAGCACGGAG
ACCGCCTTGTACCGGAAAATGCTGGGCAACCCCAGCCGGCTGCCTGCTAAGTGCCCTGGC
AAGGGTGCCTGGTCCATCCCATGGAAGTGGCTGTTTGGGGCGACTGCTGTTGCCTTGGGG
GGTGTGGCACTCTCTGTGGTCATCGCTGCCAGGAACTGA
Protein Properties
Number of Residues 412
Molecular Weight 44561.3
Theoretical pI 4.49
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • 390-410
Protein Sequence 
>Peptidyl-prolyl cis-trans isomerase FKBP8
MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQ
PPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKG
QVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYG
PQGRSPYIPPHAALCLEVTLKTAVDGPDLEMLTGQERVALANRKRECGNAHYQRADFVLA
ANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLE
HQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTE
TALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
GenBank ID Protein 28395543
UniProtKB/Swiss-Prot ID Q14318
UniProtKB/Swiss-Prot Entry Name FKBP8_HUMAN
PDB IDs Not Available
GenBank Gene ID AY225339
GeneCard ID FKBP8
GenAtlas ID FKBP8
HGNC ID HGNC:3724
References
General References
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  2. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
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  6. Kang CB, Tai J, Chia J, Yoon HS: The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38). FEBS Lett. 2005 Feb 28;579(6):1469-76. [PubMed:15733859 ]
  7. Portier BP, Taglialatela G: Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression. J Biol Chem. 2006 Dec 29;281(52):40493-502. Epub 2006 Nov 7. [PubMed:17090549 ]
  8. Shirane M, Nakayama KI: Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat Cell Biol. 2003 Jan;5(1):28-37. [PubMed:12510191 ]
  9. Bulgakov OV, Eggenschwiler JT, Hong DH, Anderson KV, Li T: FKBP8 is a negative regulator of mouse sonic hedgehog signaling in neural tissues. Development. 2004 May;131(9):2149-59. [PubMed:15105374 ]
  10. Lam E, Martin M, Wiederrecht G: Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs. Gene. 1995 Jul 28;160(2):297-302. [PubMed:7543869 ]
  11. Kang CB, Feng L, Chia J, Yoon HS: Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2. Biochem Biophys Res Commun. 2005 Nov 11;337(1):30-8. [PubMed:16176796 ]
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