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Protein Page:
AIP (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
AIP May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting. Defects in AIP are a cause of growth hormone-secreting pituitary adenoma (GHSPA); also known as familial isolated somatotropinomas (FIS) or isolated familial somatotropinoma (IFS) or familial somatotrophinoma or acromegaly due to pituitary adenoma. Defects in AIP are a cause of ACTH-secreting pituitary adenoma (ASPA); also known as pituitary Cushing disease. A pituary 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 trunkal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. Defects in AIP are a cause of prolactin-secreting pituitary adenoma (PSPA); also known as prolactinoma. Prolactin-secreting pituitary adenoma is the most common type of hormonally active pituitary adenoma. Note: This description may include information from UniProtKB.
Protein type: Transcription, coactivator/corepressor; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 11q13.3
Cellular Component: cytoplasm; cytosol; nucleoplasm; plasma membrane
Molecular Function: aryl hydrocarbon receptor binding; protein binding; signal transducer activity; transcription coactivator activity; transcription factor binding; unfolded protein binding
Biological Process: negative regulation of cyclic-nucleotide phosphodiesterase activity; protein maturation via protein folding; protein targeting to mitochondrion; signal transduction; xenobiotic metabolic process
Disease: Pituitary Adenoma, Acth-secreting; Pituitary Adenoma, Growth Hormone-secreting; Pituitary Adenoma, Prolactin-secreting
Reference #:  O00170 (UniProtKB)
Alt. Names/Synonyms: AH receptor-interacting protein; AIP; ARA9; aryl hydrocarbon receptor interacting protein; aryl hydrocarbon receptor-interacting protein; aryl-hydrocarbon receptor interacting protein; Aryl-hydrocarbon receptor-interacting protein; FKBP16; FKBP37; HBV X-associated protein 2; HBV-X associated protein; Immunophilin homolog ARA9; SMTPHN; XAP-2; XAP2
Gene Symbols: AIP
Molecular weight: 37,636 Da
Basal Isoelectric point: 5.88  Predict pI for various phosphorylation states
Select Structure to View Below

AIP

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: S53‑p
molecular association, regulation: S131‑p, S132‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K33‑ub PDFQDGTkATFHYRT
1 2 S43‑p FHYRTLHsDDEGTVL
1 0 S53‑p EGTVLDDsRARGKPM
0 1 K66‑ac PMELIIGkKFkLPVW
0 1 K69‑ub LIIGkKFkLPVWETI
0 1 T79‑p VWETIVCtMREGEIA
0 2 S104‑p LYPLVAKsLRNIAVG
0 1 K112 LRNIAVGKDPLEGQR
0 2 K112‑ub LRNIAVGkDPLEGQR
1 0 S131‑p VAQMREHssLGHADL
1 0 S132‑p AQMREHssLGHADLD
0 2 S159‑p MEMLKVEsPGTyQQD
0 1 Y163‑p KVEsPGTyQQDPWAM
0 1 K177‑ub MTDEEKAkAVPLIHQ
0 10 Y203‑p KEAAAKYyDAIACLk
0 1 K210‑ub yDAIACLkNLQMKEQ
0 55 Y247‑p CKLVVEEyyEVLDHC
0 136 Y248‑p KLVVEEyyEVLDHCS
0 2 K266‑ub NKYDDNVkAYFKRGk
0 1 K273‑ub kAYFKRGkAHAAVWN
1 0 S329‑p ARFRGIFsH______
  mouse

 
K33 PDFQDGTKATFHFRT
S43 FHFRTLHSDNEGSVI
S53 EGSVIDDSRTRGKPM
K66 PMELIVGKKFKLPVW
K69 LIVGKKFKLPVWETI
T79 VWETIVCTMREGEIA
S104 LYPLVAKSLRNIAEG
K112‑ac LRNIAEGkDPLEGQR
K112 LRNIAEGKDPLEGQR
S131 IAQMHEHSSLGHADL
S132 AQMHEHSSLGHADLD
S159 IEMLKVESPGTYQQD
Y163 KVESPGTYQQDPWAM
K177 MTDEEKAKAVPVIHQ
Y203 KEAAAKYYDAIACLK
K210 YDAIACLKNLQMKEQ
Y247 CKLVAQEYYEVLDHC
Y248 KLVAQEYYEVLDHCS
K266‑ub NKYDDNVkAYFKRGK
K273 kAYFKRGKAHAAVWN
S329 ARFRGIFSH______
  rat

 
K33 PEFQDGTKATFHFRT
S43 FHFRTLHSDPEGSVI
S53 EGSVIDDSRARGKPM
K66 PMELIIGKKFKLPVW
K69 LIIGKKFKLPVWETI
T79 VWETIVRTMREGETA
S104 LYPLVAKSLRNIAEG
K112 LRNIAEGKDPLEGQR
K112 LRNIAEGKDPLEGQR
S131 IAQMHEHSSLGHADL
S132 AQMHEHSSLGHADLD
S159 IEMLKVESPGTYQQD
Y163 KVESPGTYQQDPWAM
K177 MTDEEKAKAVPLIHQ
Y203 KEAAAKYYDAIACLK
K210 YDAIACLKNLQMKEQ
Y247 CKLVAQEYYEVLDHC
Y248 KLVAQEYYEVLDHCS
K266 NKYDDNVKAYFKRGK
K273 KAYFKRGKAHAAVWN
S329 ARFRGIFSH______
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