AIP (gene)

From Wikipedia, the free encyclopedia

Aryl hydrocarbon receptor interacting protein

Identifiers

AIP; ARA9; FKBP16; FKBP37; XAP2

External IDs

OMIM: 605555 MGI: 109622 HomoloGene: 2959

Gene ontology
Molecular Function:	• transcription coactivator activity • signal transducer activity
Cellular Component:	• membrane fraction • cytoplasm
Biological Process:	• protein folding • xenobiotic metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003977 (mRNA)
NP_003968 (protein)

NM_016666 (mRNA)
NP_057875 (protein)

Location

Chr 11: 67.01 - 67.02 Mb

Chr 19: 4.11 - 4.13 Mb

Pubmed search

[1]

[2]

Aryl hydrocarbon receptor interacting protein, also known as AIP, is a human gene.^[1]

AIP may play a positive role in AHR-mediated signalling possibly by influencing its receptivity for ligand and/or its nuclear targeting. AIP is the cellular negative regulator of the HBV X protein.^[1]

[edit] References

^ ^a ^b Entrez Gene: AIP aryl hydrocarbon receptor interacting protein.

[edit] Further reading

Chen HS, Perdew GH (1994). "Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex.". J. Biol. Chem. 269 (44): 27554–8. PMID 7961671.
Kuzhandaivelu N, Cong YS, Inouye C, et al. (1997). "XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation.". Nucleic Acids Res. 24 (23): 4741–50. PMID 8972861.
Ma Q, Whitlock JP (1997). "A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin.". J. Biol. Chem. 272 (14): 8878–84. PMID 9083006.
Carver LA, Bradfield CA (1997). "Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo.". J. Biol. Chem. 272 (17): 11452–6. PMID 9111057.
Meyer BK, Pray-Grant MG, Vanden Heuvel JP, Perdew GH (1998). "Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity.". Mol. Cell. Biol. 18 (2): 978–88. PMID 9447995.
Carver LA, LaPres JJ, Jain S, et al. (1999). "Characterization of the Ah receptor-associated protein, ARA9.". J. Biol. Chem. 273 (50): 33580–7. PMID 9837941.
Gadelha MR, Une KN, Rohde K, et al. (2000). "Isolated familial somatotropinomas: establishment of linkage to chromosome 11q13.1-11q13.3 and evidence for a potential second locus at chromosome 2p16-12.". J. Clin. Endocrinol. Metab. 85 (2): 707–14. PMID 10690880.
Petrulis JR, Hord NG, Perdew GH (2001). "Subcellular localization of the aryl hydrocarbon receptor is modulated by the immunophilin homolog hepatitis B virus X-associated protein 2.". J. Biol. Chem. 275 (48): 37448–53. doi:10.1074/jbc.M006873200. PMID 10986286.
Kazlauskas A, Poellinger L, Pongratz I (2001). "The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor.". J. Biol. Chem. 275 (52): 41317–24. doi:10.1074/jbc.M007765200. PMID 11013261.
Kazlauskas A, Sundström S, Poellinger L, Pongratz I (2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor.". Mol. Cell. Biol. 21 (7): 2594–607. doi:10.1128/MCB.21.7.2594-2607.2001. PMID 11259606.
Kazlauskas A, Poellinger L, Pongratz I (2002). "Two distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90.". J. Biol. Chem. 277 (14): 11795–801. doi:10.1074/jbc.M200053200. PMID 11805120.
Patterson CE, Gao J, Rooney AP, Davis EC (2002). "Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family.". Genomics 79 (6): 881–9. doi:10.1006/geno.2002.6777. PMID 12036304.
Berg P, Pongratz I (2002). "Two parallel pathways mediate cytoplasmic localization of the dioxin (aryl hydrocarbon) receptor.". J. Biol. Chem. 277 (35): 32310–9. doi:10.1074/jbc.M203351200. PMID 12065584.
Dull AB, Carlson DB, Petrulis JR, Perdew GH (2002). "Characterization of the phosphorylation status of the hepatitis B virus X-associated protein 2.". Arch. Biochem. Biophys. 406 (2): 209–21. PMID 12361709.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Sumanasekera WK, Tien ES, Turpey R, et al. (2003). "Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2.". J. Biol. Chem. 278 (7): 4467–73. doi:10.1074/jbc.M211261200. PMID 12482853.
Zhao Y, Meng XM, Wei YJ, et al. (2004). "Cloning and characterization of a novel cardiac-specific kinase that interacts specifically with cardiac troponin I.". J. Mol. Med. 81 (5): 297–304. doi:10.1007/s00109-003-0427-x. PMID 12721663.
Lees MJ, Peet DJ, Whitelaw ML (2003). "Defining the role for XAP2 in stabilization of the dioxin receptor.". J. Biol. Chem. 278 (38): 35878–88. doi:10.1074/jbc.M302430200. PMID 12837759.
Yano M, Terada K, Mori M (2003). "AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins.". J. Cell Biol. 163 (1): 45–56. doi:10.1083/jcb.200305051. PMID 14557246.
Ramadoss P, Petrulis JR, Hollingshead BD, et al. (2004). "Divergent roles of hepatitis B virus X-associated protein 2 (XAP2) in human versus mouse Ah receptor complexes.". Biochemistry 43 (3): 700–9. doi:10.1021/bi035827v. PMID 14730974.