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UniProtKB/Swiss-Prot entry O00170


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AIP_HUMAN
Primary accession number O00170
Secondary accession numbers Q2M3Q2 Q99606
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 73)
Name and origin of the protein
Protein name AH receptor-interacting protein
Synonyms AIP
Aryl-hydrocarbon receptor-interacting protein
Immunophilin homolog ARA9
HBV X-associated protein 2
XAP-2
Gene name
Name: AIP
Synonyms: XAP2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=B-cell;
DOI=10.1074/jbc.272.17.11452; PubMed=9111057 [NCBI, ExPASy, EBI, Israel, Japan]
Carver L.A., Bradfield C.A.;
"Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo.";
J. Biol. Chem. 272:11452-11456(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-228.
TISSUE=Lymphoma;
DOI=10.1093/nar/24.23.4741; PubMed=8972861 [NCBI, ExPASy, EBI, Israel, Japan]
Kuzhandaivelu N., Cong Y.-S., Inouye C., Yang W.-M., Seto E.;
"XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation.";
Nucleic Acids Res. 24:4741-4750(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN PAP, AND INVOLVEMENT IN GROWTH HORMONE-SECRETING PITUITARY ADENOMA.
DOI=10.1126/science.1126100; PubMed=16728643 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Pituitary adenoma predisposition caused by germline mutations in the AIP gene.";
Science 312:1228-1230(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
VARIANTS HIS-16; GLU-241 AND TRP-271, INVOLVEMENT IN GROWTH HORMONE-SECRETING PITUITARY ADENOMA, AND INVOLVEMENT IN FIPA.
DOI=10.1210/jc.2006-2513; PubMed=17244780 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Aryl hydrocarbon receptor-interacting protein gene mutations in familial isolated pituitary adenomas: analysis in 73 families.";
J. Clin. Endocrinol. Metab. 92:1891-1896(2007).
[7]
INVOLVEMENT IN PAP.
DOI=10.1210/jc.2006-2394; PubMed=17341560 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Germline mutation in the aryl hydrocarbon receptor interacting protein gene in familial somatotropinoma.";
J. Clin. Endocrinol. Metab. 92:1934-1937(2007).
[8]
INVOLVEMENT IN GROWTH HORMONE-SECRETING PITUITARY ADENOMA, AND VARIANT GLN-228.
DOI=10.1210/jc.2006-2702; PubMed=17299063 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Mutations in the aryl hydrocarbon receptor interacting protein gene are not highly prevalent among subjects with sporadic pituitary adenomas.";
J. Clin. Endocrinol. Metab. 92:1952-1955(2007).
[9]
VARIANTS HIS-16 AND GLN-304, INVOLVEMENT IN ACTH-SECRETING PITUITARY ADENOMA, AND INVOLVEMENT IN GROWTH HORMONE-SECRETING PITUITARY ADENOMA.
DOI=10.1073/pnas.0700004104; PubMed=17360484 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Molecular diagnosis of pituitary adenoma predisposition caused by aryl hydrocarbon receptor-interacting protein gene mutations.";
Proc. Natl. Acad. Sci. U.S.A. 104:4101-4105(2007).
[10]
VARIANT TYR-248 DEL, AND INVOLVEMENT IN GROWTH HORMONE-SECRETING PITUITARY ADENOMA.
DOI=10.1111/j.1365-2265.2008.03266.x; PubMed=18410548 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Aryl hydrocarbon receptor interacting protein (AIP) gene mutation analysis in children and adolescents with sporadic pituitary adenomas.";
Clin. Endocrinol. (Oxf.) 0:0-0(2008).
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.
  • FUNCTION: Cellular negative regulator of the hepatitis B virus (HBV) X protein.
  • INTERACTION:
    P35869:AHR; NbExp=1; IntAct=EBI-704197, EBI-80780;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • TISSUE SPECIFICITY: Widely expressed. Higher levels seen in the heart, placenta and skeletal muscle. Not expressed in the liver.
  • DISEASE: Defects in AIP are a cause of pituitary adenoma predisposition (PAP) [MIM:102200].
  • DISEASE: Defects in AIP are a cause of familial isolated pituitary adenoma (FIPA) [MIM:102200].
  • DISEASE: Defects in AIP are a cause of growth hormone-secreting pituitary adenoma [MIM:102200]; also known as familial isolated somatotropinomas (FIS) or isolated familial somatotropinoma (IFS) or familial somatotrophinoma or acromegaly due to pituitary adenoma.
  • DISEASE: Defects in AIP are a cause of ACTH-secreting pituitary adenoma [MIM:219090]; also known as pituitary Cushing disease. Cushing disease is a condition associated with increased blood cortisol resulting from adrenocorticotropic hormone (ACTH)-producing pituitary tumors that are resistant to glucocorticoid negative feedback.
  • SIMILARITY: Contains 1 PPIase FKBP-type domain.
  • SIMILARITY: Contains 2 TPR repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U78521; AAB59004.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U31913; AAB39923.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AM236341; CAJ85657.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC104827; AAI04828.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC104797; AAI04798.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003968.1; -.
UniGene Hs.412433
3D structure databases
ModBase O00170.
Protein-protein interaction databases
IntAct O00170; -.
PTM databases
PhosphoSite O00170; -.
Organism-specific databases
H-InvDB HIX0036007; -.
HGNC HGNC:358; AIP.
GenAtlas AIP.
HPA HPA004063; -.
MIM 102200; phenotype. [NCBI / EBI]
219090; phenotype. [NCBI / EBI]
605555; gene. [NCBI / EBI]
PharmGKB PA24652; -.
GeneCards O00170.
Gene expression databases
ArrayExpress O00170; -.
CleanEx HS_AIP; -.
GermOnline ENSG00000110711; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from HGNC).
GO:0004871; Molecular function: signal transducer activity (traceable author statement from ProtInc).
GO:0003713; Molecular function: transcription coactivator activity (traceable author statement from ProtInc).
GO:0051082; Molecular function: unfolded protein binding (inferred from direct assay from HGNC).
GO:0043681; Biological process: protein import into mitochondrion (inferred from direct assay from HGNC).
GO:0022417; Biological process: protein maturation via protein folding (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR001179; PPIase_FKBP.
IPR011990; TPR-like_helical.
IPR013105; TPR_2.
IPR013026; TPR_region.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF00254; FKBP_C; 1.
PF07719; TPR_2; 1.
Pfam graphical view of domain structure.
PROSITE PS50059; FKBP_PPIASE; 1.
PS50005; TPR; 1.
PS50293; TPR_REGION; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O00170.
Genome annotation databases
Ensembl ENSG00000110711; Homo sapiens. [Contig view]
GeneID 9049; -.
KEGG hsa:9049; -.
Phylogenomic databases
HOGENOM O00170; -.
HOVERGEN O00170; -.
Other
SOURCE AIP; Homo sapiens.
ProtoNet O00170.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Phosphoprotein; Polymorphism; Repeat; TPR repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   330  330     AH receptor-interacting protein. PRO_0000075339
DOMAIN   31   121  91     PPIase FKBP-type. 
REPEAT   179   212  34     TPR 1. 
REPEAT   265   298  34     TPR 2. 
MOD_RES   248   248        Phosphotyrosine. 
VARIANT   16    16  1     R -> H. VAR_043908 
VARIANT   228   228  1     K -> Q (in dbSNP:rs641081 [NCBI]). VAR_043909 
VARIANT   241   241  1     K -> E (in FIPA patients; uncertain pathogenicity). VAR_043910 
VARIANT   248   248  1     Missing (in a ACTH-secreting pituitary adenoma patient; uncertain pathogenicity). VAR_043911
VARIANT   271   271  1     R -> W (in FIPA patients; uncertain pathogenicity). VAR_043912 
VARIANT   304   304  1     R -> Q (in a ACTH-secreting pituitary adenoma patient). VAR_043913 
Sequence information
Length: 330 AA [This is the length of the unprocessed precursor] Molecular weight: 37664 Da [This is the MW of the unprocessed precursor] CRC64: 5C0D59A22E5F9BF8 [This is a checksum on the sequence]
        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 PEWIQLDKQI TPLLLNYCQC 

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

       310        320        330 
VVSRELRALE ARIRQKDEED KARFRGIFSH 

O00170 in FASTA format

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