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Protein

AH receptor-interacting protein

Gene

AIP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • GAF domain binding Source: UniProtKB
  • signal transducer activity Source: ProtInc
  • transcription coactivator activity Source: ProtInc
  • transcription factor binding Source: ProtInc
  • unfolded protein binding Source: HGNC

GO - Biological processi

  • negative regulation of cyclic-nucleotide phosphodiesterase activity Source: Ensembl
  • protein maturation by protein folding Source: HGNC
  • protein targeting to mitochondrion Source: HGNC
  • regulation of nucleic acid-templated transcription Source: GOC
  • regulation of protein kinase A signaling Source: Ensembl
  • signal transduction Source: GOC
  • xenobiotic metabolic process Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:AIP
Synonyms:XAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:358. AIP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • membrane Source: Ensembl
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Pituitary adenoma, growth hormone-secreting, 1 (PAGH1)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA growth hormone-secreting, benign neoplasm of the anterior pituitary gland, also known as somatotropinoma. It clinically results in acromegaly, a condition characterized by coarse facial features, protruding jaw, and enlarged extremities. Excessive production of growth hormone in children or adolescents before the closure of epiphyses causes gigantism, a condition characterized by abnormally tall stature.

See also OMIM:102200
ACTH-secreting pituitary adenoma (ASPA)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:219090
Prolactin-secreting pituitary adenoma (PSPA)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMost common type of hormonally active pituitary adenoma.

See also OMIM:600634

Keywords - Diseasei

Cushing syndrome

Organism-specific databases

MIMi102200. phenotype.
219090. phenotype.
600634. phenotype.
Orphaneti963. Acromegaly.
314777. Familial isolated pituitary adenoma.
PharmGKBiPA24652.

Polymorphism and mutation databases

BioMutaiAIP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330AH receptor-interacting proteinPRO_0000075339Add
BLAST

Proteomic databases

MaxQBiO00170.
PaxDbiO00170.
PRIDEiO00170.

PTM databases

PhosphoSiteiO00170.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO00170.
CleanExiHS_AIP.
ExpressionAtlasiO00170. baseline and differential.
GenevestigatoriO00170.

Organism-specific databases

HPAiCAB069477.
HPA004063.
HPA050217.

Interactioni

Subunit structurei

Interacts with RET in the pituitary gland; this interaction prevents the formation of the AIP-survivin complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082383EBI-704197,EBI-352572
IRF7Q929852EBI-704197,EBI-968267
PDE2AO004086EBI-704197,EBI-1785967

Protein-protein interaction databases

BioGridi114511. 32 interactions.
DIPiDIP-34068N.
IntActiO00170. 27 interactions.
MINTiMINT-5000425.
STRINGi9606.ENSP00000279146.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Beta strandi17 – 193Combined sources
Beta strandi33 – 375Combined sources
Beta strandi39 – 413Combined sources
Beta strandi43 – 464Combined sources
Beta strandi49 – 535Combined sources
Turni54 – 574Combined sources
Beta strandi60 – 678Combined sources
Helixi72 – 776Combined sources
Beta strandi85 – 895Combined sources
Helixi92 – 954Combined sources
Helixi98 – 1058Combined sources
Helixi108 – 1103Combined sources
Turni113 – 1175Combined sources
Turni137 – 1393Combined sources
Helixi140 – 1434Combined sources
Beta strandi149 – 15810Combined sources
Turni160 – 1623Combined sources
Helixi173 – 1764Combined sources
Helixi178 – 19215Combined sources
Helixi195 – 21319Combined sources
Helixi221 – 24323Combined sources
Helixi248 – 26013Combined sources
Helixi265 – 27713Combined sources
Helixi281 – 29414Combined sources
Helixi296 – 2983Combined sources
Helixi299 – 31113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LKNNMR-A2-166[»]
4AIFX-ray2.01A/B172-315[»]
4APOX-ray1.90A/B166-330[»]
ProteinModelPortaliO00170.
SMRiO00170. Positions 2-166, 173-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 12191PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST
Repeati179 – 21234TPR 1Add
BLAST
Repeati231 – 26434TPR 2Add
BLAST
Repeati265 – 29834TPR 3Add
BLAST

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiNOG250378.
HOVERGENiHBG004198.
InParanoidiO00170.
KOiK17767.
OMAiIVCTMRE.
PhylomeDBiO00170.
TreeFamiTF314507.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHYRT LHSDDEGTVL
60 70 80 90 100
DDSRARGKPM ELIIGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL
110 120 130 140 150
VAKSLRNIAV GKDPLEGQRH CCGVAQMREH SSLGHADLDA LQQNPQPLIF
160 170 180 190 200
HMEMLKVESP GTYQQDPWAM TDEEKAKAVP LIHQEGNRLY REGHVKEAAA
210 220 230 240 250
KYYDAIACLK NLQMKEQPGS PEWIQLDQQI TPLLLNYCQC KLVVEEYYEV
260 270 280 290 300
LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP
310 320 330
VVSRELQALE ARIRQKDEED KARFRGIFSH
Length:330
Mass (Da):37,636
Last modified:July 28, 2009 - v2
Checksum:i9302AA6D0F8D8F51
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161R → H.2 Publications
Corresponds to variant rs145047094 [ dbSNP | Ensembl ].
VAR_043908
Natural varianti47 – 548Missing in patients with pituitary adenoma; unknown pathological significance. 1 Publication
VAR_058407
Natural varianti228 – 2281Q → K.5 Publications
Corresponds to variant rs641081 [ dbSNP | Ensembl ].
VAR_043909
Natural varianti241 – 2411K → E in patients with pituitary adenoma; unknown pathological significance. 1 Publication
VAR_043910
Natural varianti248 – 2481Missing in a ACTH-secreting pituitary adenoma patient; unknown pathological significance. 1 Publication
VAR_043911
Natural varianti271 – 2711R → W in patients with pituitary adenoma; unknown pathological significance. 1 Publication
VAR_043912
Natural varianti304 – 3041R → Q in a ACTH-secreting pituitary adenoma patient. 1 Publication
VAR_043913
Natural varianti307 – 3071Q → R.4 Publications
Corresponds to variant rs4930199 [ dbSNP | Ensembl ].
VAR_061545

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8168.1.
RefSeqiNP_001289888.1. NM_001302959.1.
NP_001289889.1. NM_001302960.1.
NP_003968.3. NM_003977.3.
UniGeneiHs.412433.

Genome annotation databases

EnsembliENST00000279146; ENSP00000279146; ENSG00000110711.
GeneIDi9049.
KEGGihsa:9049.
UCSCiuc001olv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8168.1.
RefSeqiNP_001289888.1. NM_001302959.1.
NP_001289889.1. NM_001302960.1.
NP_003968.3. NM_003977.3.
UniGeneiHs.412433.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LKNNMR-A2-166[»]
4AIFX-ray2.01A/B172-315[»]
4APOX-ray1.90A/B166-330[»]
ProteinModelPortaliO00170.
SMRiO00170. Positions 2-166, 173-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114511. 32 interactions.
DIPiDIP-34068N.
IntActiO00170. 27 interactions.
MINTiMINT-5000425.
STRINGi9606.ENSP00000279146.

PTM databases

PhosphoSiteiO00170.

Polymorphism and mutation databases

BioMutaiAIP.

Proteomic databases

MaxQBiO00170.
PaxDbiO00170.
PRIDEiO00170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279146; ENSP00000279146; ENSG00000110711.
GeneIDi9049.
KEGGihsa:9049.
UCSCiuc001olv.3. human.

Organism-specific databases

CTDi9049.
GeneCardsiGC11P067251.
GeneReviewsiAIP.
HGNCiHGNC:358. AIP.
HPAiCAB069477.
HPA004063.
HPA050217.
MIMi102200. phenotype.
219090. phenotype.
600634. phenotype.
605555. gene.
neXtProtiNX_O00170.
Orphaneti963. Acromegaly.
314777. Familial isolated pituitary adenoma.
PharmGKBiPA24652.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250378.
HOVERGENiHBG004198.
InParanoidiO00170.
KOiK17767.
OMAiIVCTMRE.
PhylomeDBiO00170.
TreeFamiTF314507.

Miscellaneous databases

GeneWikiiAH_receptor-interacting_protein.
GenomeRNAii9049.
NextBioi33903.
PROiO00170.
SOURCEiSearch...

Gene expression databases

BgeeiO00170.
CleanExiHS_AIP.
ExpressionAtlasiO00170. baseline and differential.
GenevestigatoriO00170.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
PS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-228 AND ARG-307, INVOLVEMENT IN PITUITARY ADENOMAS.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 47-GLY--ARG-54 DEL; HIS-16; GLU-241 AND TRP-271, INVOLVEMENT IN PAGH1.
  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 PAGH1, 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. "Structure of the TPR domain of AIP: lack of client protein interaction with the C-terminal alpha-7 helix of the TPR domain of AIP is sufficient for pituitary adenoma predisposition."
    Morgan R.M., Hernandez-Ramirez L.C., Trivellin G., Zhou L., Roe S.M., Korbonits M., Prodromou C.
    PLoS ONE 7:E53339-E53339(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 166-330 IN COMPLEX WITH HSP90 AND TOMM20 PEPTIDES, TPR REPEATS.
  11. Cited for: VARIANTS HIS-16 AND GLN-304, INVOLVEMENT IN ACTH-SECRETING PITUITARY ADENOMA, INVOLVEMENT IN PAGH1.
  12. "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 PAGH1.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAIP_HUMAN
AccessioniPrimary (citable) accession number: O00170
Secondary accession number(s): A0SZW3
, A0SZW4, A0SZW5, A0SZW6, Q2M3Q2, Q99606
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 28, 2009
Last modified: May 27, 2015
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.