AH receptor-interacting protein

AIP

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2LKN, 4AIF, 4APO

Identifiers

Aliases

AIP, ARA9, FKBP16, FKBP37, SMTPHN, XAP-2, XAP2, aryl hydrocarbon receptor interacting protein

External IDs

MGI: 109622 HomoloGene: 2959 GeneCards: AIP

Gene ontology
Molecular function	• protein binding • signal transducer activity • transcription cofactor activity • unfolded protein binding • transcription factor binding • GAF domain binding • transcription coactivator activity • aryl hydrocarbon receptor binding
Cellular component	• aryl hydrocarbon receptor complex • membrane • plasma membrane • cytosol • nucleoplasm • cytoplasm
Biological process	• protein targeting to mitochondrion • regulation of nucleic acid-templated transcription • negative regulation of cyclic-nucleotide phosphodiesterase activity • regulation of protein kinase A signaling • protein maturation by protein folding • xenobiotic metabolic process • interleukin-12-mediated signaling pathway
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


9049


11632

Ensembl


ENSG00000110711


n/a

UniProt


O00170


O08915

RefSeq (mRNA)


NM_003977 NM_001302959 NM_001302960


NM_001276284 NM_016666

RefSeq (protein)


NP_001289888 NP_001289889 NP_003968


NP_001263213 NP_057875

Location (UCSC)

Chr 11: 67.48 – 67.49 Mb

Chr 19: 4.11 – 4.13 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

AH receptor-interacting protein (AIP) also known as aryl-hydrocarbon receptor-interacting protein, immunophilin homolog ARA9, or HBV X-associated protein 2 (XAP-2) is a protein that in humans is encoded by the AIP gene.^[3]^[4]^[5] The protein is a member of FKBP family.

Function

AIP may play a positive role in aryl hydrocarbon receptor-mediated signalling possibly by influencing its receptivity for ligand and/or its nuclear targeting. AIP is the cellular negative regulator of the hepatitis B virus (HBV) X protein.^[3]

Role in Disease

AIP mutations may be the cause of a familial form of acromegaly, familial isolated pituitary adenoma (FIPA). Somatotropinomas (i.e. GH-producing pituitary adenomas), sometimes associated with prolactinomas, are present in most AIP mutated patients.^[6]

Interactions

AIP has been shown to interact with the aryl hydrocarbon receptor,^[5]^[7]^[8] peroxisome proliferator-activated receptor alpha^[9] and the aryl hydrocarbon receptor nuclear translocator.^[5]^[10]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: AIP aryl hydrocarbon receptor interacting protein".
↑ Kuzhandaivelu N, Cong YS, Inouye C, Yang WM, Seto E (December 1996). "XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation". Nucleic Acids Res. 24 (23): 4741–50. PMC 146319 . PMID 8972861. doi:10.1093/nar/24.23.4741.
1 2 3 Carver LA, Bradfield CA (April 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. doi:10.1074/jbc.272.17.11452.
↑ Occhi G, Trivellin G, Ceccato F, et al. (2010). "Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia.". Eur. J. Endocrinol. 163 (3): 369–376. PMID 20530095. doi:10.1530/EJE-10-0327.
↑ Petrulis JR, Hord NG, Perdew GH (December 2000). "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. PMID 10986286. doi:10.1074/jbc.M006873200.
↑ Ma Q, Whitlock JP (April 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. doi:10.1074/jbc.272.14.8878.
↑ Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH (February 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. PMID 12482853. doi:10.1074/jbc.M211261200.
↑ Kazlauskas A, Sundström S, Poellinger L, Pongratz I (April 2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Mol. Cell. Biol. 21 (7): 2594–607. PMC 86890 . PMID 11259606. doi:10.1128/MCB.21.7.2594-2607.2001.

Chen HS, Perdew GH (1994). "Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex.". J. Biol. Chem. 269 (44): 27554–8. PMID 7961671.
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. doi:10.1074/jbc.272.14.8878.
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. PMC 108810 . 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. doi:10.1074/jbc.273.50.33580.
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. doi:10.1210/jc.85.2.707.
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. PMID 10986286. doi:10.1074/jbc.M006873200.
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. PMID 11013261. doi:10.1074/jbc.M007765200.
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. PMC 86890 . PMID 11259606. doi:10.1128/MCB.21.7.2594-2607.2001.
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. PMID 11805120. doi:10.1074/jbc.M200053200.
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. PMID 12036304. doi:10.1006/geno.2002.6777.
Berg P, Pongratz I (2002). "Two parallel pathways mediate cytoplasmic localization of the dioxin (aryl hydrocarbon) receptor.". J. Biol. Chem. 277 (35): 32310–9. PMID 12065584. doi:10.1074/jbc.M203351200.
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. doi:10.1016/S0003-9861(02)00444-7.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 12482853. doi:10.1074/jbc.M211261200.
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. PMID 12721663. doi:10.1007/s00109-003-0427-x.
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. PMID 12837759. doi:10.1074/jbc.M302430200.
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. PMC 2173431 . PMID 14557246. doi:10.1083/jcb.200305051.
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. PMID 14730974. doi:10.1021/bi035827v.
Occhi G, Trivellin G, Ceccato F, et al. (2010). "Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia.". Eur. J. Endocrinol. 163 (3): 369–376. PMID 20530095. doi:10.1530/EJE-10-0327.

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AH receptor-interacting protein

Function

Role in Disease

Interactions

References

Further reading