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O00170 (AIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AH receptor-interacting protein

Short name=AIP
Alternative name(s):
Aryl-hydrocarbon receptor-interacting protein
HBV X-associated protein 2
Short name=XAP-2
Immunophilin homolog ARA9
Gene names
Name:AIP
Synonyms:XAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.

Cellular negative regulator of the hepatitis B virus (HBV) X protein.

Subunit structure

Interacts with RET in the pituitary gland; this interaction prevents the formation of the AIP-survivin complex. Ref.9

Subcellular location

Cytoplasm.

Tissue specificity

Widely expressed. Higher levels seen in the heart, placenta and skeletal muscle. Not expressed in the liver.

Involvement in disease

Growth hormone-secreting pituitary adenoma (GHSPA) [MIM:102200]: Pituitary adenomas include somatotropinoma and prolactinoma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.8 Ref.10 Ref.11

ACTH-secreting pituitary adenoma (ASPA) [MIM:219090]: A pituitary adenoma resulting in excessive production of adrenocorticotropic hormone. This leads to hypersecretion of cortisol by the adrenal glands and ACTH-dependent Cushing syndrome. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Prolactin-secreting pituitary adenoma (PSPA) [MIM:600634]: Most common type of hormonally active pituitary adenoma.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Contains 1 PPIase FKBP-type domain.

Contains 2 TPR repeats.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330AH receptor-interacting protein
PRO_0000075339

Regions

Domain31 – 12191PPIase FKBP-type
Repeat179 – 21234TPR 1
Repeat265 – 29834TPR 2

Natural variations

Natural variant161R → H. Ref.4 Ref.10
Corresponds to variant rs145047094 [ dbSNP | Ensembl ].
VAR_043908
Natural variant47 – 548Missing in patients with pituitary adenoma; unknown pathological significance.
VAR_058407
Natural variant2281Q → K. Ref.2 Ref.3 Ref.5 Ref.8 Ref.12
Corresponds to variant rs641081 [ dbSNP | Ensembl ].
VAR_043909
Natural variant2411K → E in patients with pituitary adenoma; unknown pathological significance. Ref.4
VAR_043910
Natural variant2481Missing in a ACTH-secreting pituitary adenoma patient; unknown pathological significance. Ref.11
VAR_043911
Natural variant2711R → W in patients with pituitary adenoma; unknown pathological significance. Ref.4
VAR_043912
Natural variant3041R → Q in a ACTH-secreting pituitary adenoma patient. Ref.10
VAR_043913
Natural variant3071Q → R. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs4930199 [ dbSNP | Ensembl ].
VAR_061545

Secondary structure

.................................................... 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00170 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 9302AA6D0F8D8F51

FASTA33037,636
        10         20         30         40         50         60 
MADIIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHYRT LHSDDEGTVL DDSRARGKPM 

        70         80         90        100        110        120 
ELIIGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL VAKSLRNIAV GKDPLEGQRH 

       130        140        150        160        170        180 
CCGVAQMREH SSLGHADLDA LQQNPQPLIF HMEMLKVESP GTYQQDPWAM TDEEKAKAVP 

       190        200        210        220        230        240 
LIHQEGNRLY REGHVKEAAA KYYDAIACLK NLQMKEQPGS PEWIQLDQQI TPLLLNYCQC 

       250        260        270        280        290        300 
KLVVEEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP 

       310        320        330 
VVSRELQALE ARIRQKDEED KARFRGIFSH 

« Hide

References

« Hide 'large scale' references
[1]"XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation."
Kuzhandaivelu N., Cong Y.-S., Inouye C., Yang W.-M., Seto E.
Nucleic Acids Res. 24:4741-4750(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-307.
Tissue: Lymphoma.
[2]"Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo."
Carver L.A., Bradfield C.A.
J. Biol. Chem. 272:11452-11456(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-228 AND ARG-307.
Tissue: B-cell.
[3]"Pituitary adenoma predisposition caused by germline mutations in the AIP gene."
Vierimaa O., Georgitsi M., Lehtonen R., Vahteristo P., Kokko A., Raitila A., Tuppurainen K., Ebeling T.M.L., Salmela P.I., Paschke R., Gundogdu S., de Menis E., Jaervinen M.J., Launonen V., Karhu A., Aaltonen L.A.
Science 312:1228-1230(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-228 AND ARG-307, INVOLVEMENT IN PITUITARY ADENOMAS.
[4]"Aryl hydrocarbon receptor-interacting protein gene mutations in familial isolated pituitary adenomas: analysis in 73 families."
Daly A.F., Vanbellinghen J.-F., Khoo S.K., Jaffrain-Rea M.-L., Naves L.A., Guitelman M.A., Murat A., Emy P., Gimenez-Roqueplo A.-P., Tamburrano G., Raverot G., Barlier A., De Herder W., Penfornis A., Ciccarelli E., Estour B., Lecomte P., Gatta B. expand/collapse author list , Chabre O., Sabate M.I., Bertagna X., Garcia Basavilbaso N., Stalldecker G., Colao A., Ferolla P., Wemeau J.-L., Caron P., Sadoul J.-L., Oneto A., Archambeaud F., Calender A., Sinilnikova O., Montanana C.F., Cavagnini F., Hana V., Solano A., Delettieres D., Luccio-Camelo D.C., Basso A., Rohmer V., Brue T., Bours V., Teh B.T., Beckers A.
J. Clin. Endocrinol. Metab. 92:1891-1896(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 47-GLY--ARG-54 DEL; HIS-16; GLU-241 AND TRP-271, INVOLVEMENT IN GHSPA.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LYS-228 AND ARG-307.
Tissue: Brain.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Germline mutation in the aryl hydrocarbon receptor interacting protein gene in familial somatotropinoma."
Toledo R.A., Lourenco D.M. Jr., Liberman B., Cunha-Neto M.B.C., Cavalcanti M.G., Moyses C.B., Toledo S.P.A., Dahia P.L.M.
J. Clin. Endocrinol. Metab. 92:1934-1937(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PAP.
[8]"Mutations in the aryl hydrocarbon receptor interacting protein gene are not highly prevalent among subjects with sporadic pituitary adenomas."
Barlier A., Vanbellinghen J.-F., Daly A.F., Silvy M., Jaffrain-Rea M.-L., Trouillas J., Tamagno G., Cazabat L., Bours V., Brue T., Enjalbert A., Beckers A.
J. Clin. Endocrinol. Metab. 92:1952-1955(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GHSPA, VARIANT LYS-228.
[9]"The tyrosine kinase receptor RET interacts in vivo with aryl hydrocarbon receptor-interacting protein to alter survivin availability."
Vargiolu M., Fusco D., Kurelac I., Dirnberger D., Baumeister R., Morra I., Melcarne A., Rimondini R., Romeo G., Bonora E.
J. Clin. Endocrinol. Metab. 94:2571-2578(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RET.
[10]"Molecular diagnosis of pituitary adenoma predisposition caused by aryl hydrocarbon receptor-interacting protein gene mutations."
Georgitsi M., Raitila A., Karhu A., Tuppurainen K., Maekinen M.J., Vierimaa O., Paschke R., Saeger W., van der Luijt R.B., Sane T., Robledo M., De Menis E., Weil R.J., Wasik A., Zielinski G., Lucewicz O., Lubinski J., Launonen V., Vahteristo P., Aaltonen L.A.
Proc. Natl. Acad. Sci. U.S.A. 104:4101-4105(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-16 AND GLN-304, INVOLVEMENT IN ACTH-SECRETING PITUITARY ADENOMA, INVOLVEMENT IN GHSPA.
[11]"Aryl hydrocarbon receptor interacting protein (AIP) gene mutation analysis in children and adolescents with sporadic pituitary adenomas."
Georgitsi M., De Menis E., Cannavo S., Maekinen M.J., Tuppurainen K., Pauletto P., Curto L., Weil R.J., Paschke R., Zielinski G., Wasik A., Lubinski J., Vahteristo P., Karhu A., Aaltonen L.A.
Clin. Endocrinol. (Oxf.) 69:621-627(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-248 DEL, INVOLVEMENT IN GHSPA.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31913 mRNA. Translation: AAB39923.1.
U78521 mRNA. Translation: AAB59004.1.
AM236341 Genomic DNA. Translation: CAJ85657.1.
EF066502 Genomic DNA. Translation: ABK60081.1.
EF066504 Genomic DNA. Translation: ABK60082.1.
EF066505 Genomic DNA. Translation: ABK60083.1.
EF066510 Genomic DNA. Translation: ABK60084.1.
BC104827 mRNA. Translation: AAI04828.1.
BC104797 mRNA. Translation: AAI04798.1.
RefSeqNP_003968.2. NM_003977.2.
UniGeneHs.412433.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LKNNMR-A2-166[»]
4AIFX-ray2.01A/B173-315[»]
4APOX-ray1.90A/B166-330[»]
ProteinModelPortalO00170.
SMRO00170. Positions 2-166, 173-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114511. 23 interactions.
DIPDIP-34068N.
IntActO00170. 12 interactions.
MINTMINT-5000425.
STRING9606.ENSP00000279146.

PTM databases

PhosphoSiteO00170.

Proteomic databases

PaxDbO00170.
PRIDEO00170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279146; ENSP00000279146; ENSG00000110711.
GeneID9049.
KEGGhsa:9049.
UCSCuc001olv.3. human.

Organism-specific databases

CTD9049.
GeneCardsGC11P067251.
HGNCHGNC:358. AIP.
HPAHPA004063.
HPA050217.
MIM102200. phenotype.
219090. phenotype.
600634. phenotype.
605555. gene.
neXtProtNX_O00170.
Orphanet963. Acromegaly.
314777. Familial isolated pituitary adenoma.
PharmGKBPA24652.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250378.
HOVERGENHBG004198.
InParanoidO00170.
KOK17767.
OMAHSDKEGT.
PhylomeDBO00170.
TreeFamTF314507.

Gene expression databases

ArrayExpressO00170.
BgeeO00170.
CleanExHS_AIP.
GenevestigatorO00170.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAH_receptor-interacting_protein.
GenomeRNAi9049.
NextBio33903.
PROO00170.
SOURCESearch...

Entry information

Entry nameAIP_HUMAN
AccessionPrimary (citable) accession number: O00170
Secondary accession number(s): A0SZW3 expand/collapse secondary AC list , A0SZW4, A0SZW5, A0SZW6, Q2M3Q2, Q99606
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 28, 2009
Last modified: March 19, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM