AH receptor-interacting protein

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AIP
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases AIP, ARA9, FKBP16, FKBP37, SMTPHN, XAP-2, XAP2, aryl hydrocarbon receptor interacting protein
External IDs MGI: 109622 HomoloGene: 2959 GeneCards: AIP
RNA expression pattern
PBB GE AIP 201782 s at fs.png

PBB GE AIP 201781 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003977
NM_001302959
NM_001302960

NM_001276284
NM_016666

RefSeq (protein)

NP_001289888
NP_001289889
NP_003968

NP_001263213.1
NP_057875.1
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[edit]

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[edit]

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[edit]

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[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: AIP aryl hydrocarbon receptor interacting protein". 
  4. ^ 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. doi:10.1093/nar/24.23.4741. PMC 146319Freely accessible. PMID 8972861. 
  5. ^ a b c 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. doi:10.1074/jbc.272.17.11452. PMID 9111057. 
  6. ^ 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. doi:10.1530/EJE-10-0327. PMID 20530095. 
  7. ^ 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. doi:10.1074/jbc.M006873200. PMID 10986286. 
  8. ^ 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. doi:10.1074/jbc.272.14.8878. PMID 9083006. 
  9. ^ 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. doi:10.1074/jbc.M211261200. PMID 12482853. 
  10. ^ 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. doi:10.1128/MCB.21.7.2594-2607.2001. PMC 86890Freely accessible. PMID 11259606. 

Further reading[edit]