AH receptor-interacting protein (Redirected from AIP gene mutation)

AIP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAIP, ARA9, FKBP16, FKBP37, SMTPHN, XAP-2, XAP2, aryl hydrocarbon receptor interacting protein, PITA1
External IDsOMIM: 605555 MGI: 109622 HomoloGene: 2959 GeneCards: AIP
Orthologs
SpeciesHumanMouse
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
NP_057875

Location (UCSC)Chr 11: 67.47 – 67.49 MbChr 19: 4.16 – 4.18 Mb
PubMed search
Wikidata
View/Edit HumanView/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. The protein is a member of the 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. Further, it's been known to suppress antiviral signaling and the induction of type I interferon by targeting IRF7, a key player in the antiviral signal pathways. AIP consists of an N-terminal FKBP52 like domain and a C-terminal TPR domain.

Mutations and 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.

Interactions

AIP has been shown to interact with the aryl hydrocarbon receptor, peroxisome proliferator-activated receptor alpha and the aryl hydrocarbon receptor nuclear translocator. Further, it has shown that AIP can interact with IRF7 to exert its novel function of negatively regulating antiviral signal pathways.


This page was last updated at 2024-03-28 03:31 UTC. Update now. View original page.

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