ALB

gene
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Summary

ALB (albumin, HGNC:399) is a protein-coding gene on chromosome 4q13.3, encoding Albumin (P02768). Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs.

This gene encodes the most abundant protein in human blood. This protein functions in the regulation of blood plasma colloid osmotic pressure and acts as a carrier protein for a wide range of endogenous molecules including hormones, fatty acids, and metabolites, as well as exogenous drugs. Additionally, this protein exhibits an esterase-like activity with broad substrate specificity. The encoded preproprotein is proteolytically processed to generate the mature protein. A peptide derived from this protein, EPI-X4, is an endogenous inhibitor of the CXCR4 chemokine receptor.

Source: NCBI Gene 213 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): congenital analbuminemia (Definitive, ClinGen) — +1 more curated relationship
  • Clinical variants (ClinVar): 234 total — 19 pathogenic, 1 likely-pathogenic
  • Phenotypes (HPO): 31
  • Druggable target: yes — 36 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_000477

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:399
Approved symbolALB
Namealbumin
Location4q13.3
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000163631
Ensembl biotypeprotein_coding
OMIM103600
Entrez213

Gene structure

Transcript identifiers

Ensembl transcripts: 66 — 55 protein_coding, 6 retained_intron, 4 protein_coding_CDS_not_defined, 1 nonsense_mediated_decay

ENST00000295897, ENST00000401494, ENST00000415165, ENST00000441319, ENST00000476441, ENST00000484992, ENST00000486939, ENST00000495173, ENST00000503124, ENST00000504043, ENST00000505649, ENST00000507673, ENST00000508932, ENST00000509063, ENST00000510166, ENST00000511370, ENST00000514786, ENST00000515133, ENST00000876006, ENST00000876007, ENST00000876008, ENST00000876009, ENST00000876010, ENST00000876011, ENST00000876012, ENST00000876013, ENST00000876014, ENST00000876015, ENST00000876016, ENST00000876017, ENST00000876018, ENST00000876019, ENST00000876020, ENST00000876021, ENST00000876022, ENST00000876023, ENST00000876024, ENST00000876025, ENST00000876026, ENST00000876027, ENST00000876028, ENST00000876029, ENST00000876030, ENST00000876031, ENST00000876032, ENST00000876033, ENST00000876034, ENST00000876035, ENST00000876036, ENST00000876037, ENST00000876038, ENST00000876039, ENST00000876040, ENST00000876041, ENST00000876042, ENST00000876043, ENST00000876044, ENST00000876045, ENST00000876046, ENST00000876047, ENST00000876048, ENST00000876049, ENST00000876050, ENST00000876051, ENST00000876052, ENST00000944004

RefSeq mRNA: 1 — MANE Select: NM_000477 NM_000477

CCDS: CCDS3555

Canonical transcript exons

ENST00000295897 — 15 exons

ExonStartEnd
ENSE000018232307342109273421482
ENSE000034694607340428773404406
ENSE000034782567341503573415167
ENSE000034837917342025473420321
ENSE000034961687341753173417669
ENSE000035436127341950773419639
ENSE000035683587340511673405173
ENSE000035797117341808873418311
ENSE000035978627341031273410409
ENSE000036175717340935573409487
ENSE000036351567341625673416353
ENSE000036453997340859473408805
ENSE000036650287341199673412125
ENSE000036808497340662973406761
ENSE000036893837341342073413634

Expression profiles

Bgee: expression breadth ubiquitous, 178 present calls, max score 99.99.

FANTOM5 (CAGE): breadth tissue_specific, TPM avg 460.6669 / max 168941.6138, expressed in 170 samples.

FANTOM5 promoters (42 alternative TSS)

Promoter IDTPM avgSamples expressed
48080451.4215138
480941.337622
480901.153420
481210.608624
481220.588919
480860.487919
480980.471817
480870.434716
481310.433516
481280.427013

Top tissues by expression

292 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
right lobe of liverUBERON:000111499.99gold quality
liverUBERON:000210799.99gold quality
body of pancreasUBERON:000115099.55gold quality
pancreasUBERON:000126497.08gold quality
adult mammalian kidneyUBERON:000008296.05gold quality
nephron tubuleUBERON:000123195.55gold quality
islet of LangerhansUBERON:000000694.95gold quality
kidney epitheliumUBERON:000481994.71gold quality
colonic epitheliumUBERON:000039793.29gold quality
renal glomerulusUBERON:000007493.17gold quality
metanephric glomerulusUBERON:000473693.08gold quality
kidneyUBERON:000211392.22gold quality
adrenal tissueUBERON:001830390.63gold quality
male germ line stem cell (sensu Vertebrata) in testisCL:0000089 ∩ UBERON:000047387.78gold quality
metanephros cortexUBERON:001053386.75gold quality
cortex of kidneyUBERON:000122586.70gold quality
metanephrosUBERON:000008185.56gold quality
adult organismUBERON:000702384.89gold quality
primordial germ cell in gonadCL:0000670 ∩ UBERON:000099183.19gold quality
renal medullaUBERON:000036282.08gold quality
body of stomachUBERON:000116180.69gold quality
buccal mucosa cellCL:000233680.24silver quality
stomachUBERON:000094579.19gold quality
right uterine tubeUBERON:000130278.03gold quality
left uterine tubeUBERON:000130377.17gold quality
fundus of stomachUBERON:000116077.16gold quality
descending thoracic aortaUBERON:000234577.12gold quality
epithelial cell of pancreasCL:000008373.86gold quality
ectocervixUBERON:001224973.43gold quality
right coronary arteryUBERON:000162573.29gold quality

Single-cell (SCXA)

Detected in 16 experiment(s), a significant marker in 14.

ExperimentMarker?Max mean expression
E-MTAB-10553yes182542.37
E-CURD-98yes154104.78
E-GEOD-130473yes122463.03
E-MTAB-6701yes101974.44
E-MTAB-7407yes82492.32
E-HCAD-9yes31685.68
E-CURD-122yes5866.53
E-MTAB-10137yes4145.24
E-MTAB-8495yes4124.52
E-HCAD-32yes1388.53
E-ANND-5yes950.92
E-GEOD-81547yes26.65
E-MTAB-5061yes19.31
E-MTAB-8221no60215.40
E-HCAD-31no3.66

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

26 targeting ALB, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-1250-3P99.9670.044038
HSA-MIR-6809-3P99.9171.453814
HSA-MIR-3140-3P99.8868.472069
HSA-MIR-391999.8769.452489
HSA-MIR-30A-3P99.8769.742928
HSA-MIR-30D-3P99.8769.922917
HSA-MIR-30E-3P99.8769.682942
HSA-MIR-469899.8471.414303
HSA-MIR-430799.8270.453374
HSA-MIR-6505-5P99.7369.251595
HSA-MIR-1211799.5067.57868
HSA-MIR-143-3P99.4969.051457
HSA-MIR-477099.4969.091451
HSA-MIR-568399.3668.592083
HSA-MIR-608899.2968.451284
HSA-MIR-580-5P99.2870.941776
HSA-MIR-4795-5P99.1166.90876
HSA-MIR-447899.0765.162320
HSA-MIR-5197-3P98.7167.051905
HSA-MIR-49698.6669.80931
HSA-MIR-392998.3265.581026
HSA-MIR-1245B-3P98.0168.911387
HSA-MIR-4708-5P97.7767.82831
HSA-MIR-376A-5P97.7065.61863
HSA-MIR-4524B-3P95.5264.12964
HSA-MIR-6777-3P95.3564.30699

Literature-anchored findings (GeneRIF, showing 40)

  • binding study with novel antiretroviral nucleoside derivatives of AZT (PMID:11689002)
  • solvent effects on the secondary structure of two proteins (serum albumin and apomyoglobin) were examined by circular dichroism following encapsulation in the hydrated pores of a silica glass matrix by the sol-gel method (PMID:11734007)
  • first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4) (PMID:11743713)
  • Tryptophan at amino acid position 214 is the principal site for nitrosation. (PMID:11810025)
  • Results support the involvement of certain basic amino acid residues in the catabolism of HSA-bound 15-keto-PGE2. (PMID:11847277)
  • structural characterization of structure in solution and dry state (PMID:11906609)
  • Efficient identification of photolabelled amino acid residues by combining immunoaffinity purification with MS: revealing the semotiadil-binding site and its relevance to binding sites for myristates in domain III of human serum albumin. (PMID:11931649)
  • Data show that glucose interacts with multiple sites on human serum albumin, affecting its biochemical and biophysical properties. This may interfere with HSA normal function contributing to diabetic complications. (PMID:12009306)
  • chemical analysis of electrostatic interactions in human serum albumin (PMID:12118010)
  • Albumin is the major component of plasma that blocks CLL cell killing by chlorambucil or radiation. (PMID:12480711)
  • review of role of serum albumin as a transport protein (PMID:12617161)
  • albumin is a substrate of human chymase (PMID:12815038)
  • Synthesis rate of albumin and fibrinogen are coordinately up-regulated. (PMID:12969171)
  • albumin affects glucose metabolism by impairing insulin-induced insulin receptor substrate (IRS) signaling through a protein kinase C alpha-mediated mechanism (PMID:12970360)
  • A detailed chemometric analysis of ligand binding to domain-3A of human serum albumin is described. NMR & fluorescence data on a set of 889 chemically diverse compounds were used to develop a group contribution model based on 74 chemical fragments. (PMID:13677478)
  • Albumin isolated from uraemic plasma had a characteristically increased melting temperature because of bound ligands; purification of uraemic plasma at pH 5.08 completely restored the binding affinity of albumin for all the marker ligands (PMID:14520007)
  • The developed immunoassay system using fluorescence dye and lateral-flow chromatography is a simple, fast and reliable method for quantifying the albumin concentration in whole blood. (PMID:14687905)
  • Propofol-binding sites are primarily found in domain III, whereas halothane sites are more widely distributed. Greater hydrophobic contacts, van der Waals interactions & hydrogen-bond formation account for the stronger binding of propofol. (PMID:14759223)
  • serum albumin may have a role in preventing the progression of atherosclerosis to major adverse cardiac events in patients with a low risk profile (PMID:14983239)
  • human serum albumin studied by acoustic relaxation spectroscopy (PMID:15137089)
  • ALB increased at 10 min postexercise in younger men only, whereas fibrinogen was elevated in both groups through 180 min postexercise. (PMID:15149953)
  • The effective specific volume, the activation energy and entropy of viscous flow for hydrated HSA were calculated (PMID:15210122)
  • the role of this fluidity in the correlation between stability and function of the protein (PMID:15353599)
  • albumin may have a role in progression of bronchial carcinoma (PMID:15646839)
  • Based on the fluorescence responses for both hypocrellin B(JB) and human serum albumin HSA), binding of HB to HSA are more specific rather than distributed randomly on the surface of HSA. (PMID:15716124)
  • Albumin colocalized together with its transcription factor PCD/DCoH/HNF-1alpha in suprabasal keratinocytes in human full-thickness skin sections and in keratinocytes cultured in serum-free medium. (PMID:15740590)
  • The protein secondary structure showed no alterations at low PEG concentration (0.1 mM), whereas at high polymer content (1 mM), a reduction of alpha-helix from 59 ) to 53% and an increase of beta-turn from 11 to 22% occurred in the PEG-HSA complexes. (PMID:15832324)
  • glycation can influence or change local secondary structure in human serum albumin, as shown through NMR analysis of synthetic peptides (PMID:15837789)
  • A pictorial model for the unfolding of the domains has been formulated (PMID:15890566)
  • Contribution of histidine residues located in domain I into the neutral-to-basic (N-B) transition of human serum albumin was studied using site-directed mutagenesis. (PMID:15913893)
  • Cardamonin binding to albumin bindig site II alters protein secondary structure. (PMID:15942949)
  • Analbuminemia in a Swiss family is caused by a C –> T transition at nucleotide 4446 (PMID:15996651)
  • Modification of arginine residues by methylglyoxal may be particularly damaging because arginine residues have a high frequency of occurrence in ligand and substrate recognition sites in receptor and enzyme active sites. (PMID:16037246)
  • In the present study, the qualitative modification of albumin in HD patients (n = 20) was examined and their results were compared with healthy age-matched controls (n = 10). (PMID:16054887)
  • report myristate binding to the N and B conformational states of Mn(III)heme-HSA (i.e. at pH 7.0 and 10.0, respectively) as investigated by optical absorbance and NMR spectroscopy (PMID:16156788)
  • All three major serum-binding proteins, thyroxine-binding globulin, transthyretin, and albumin, were present in cytosol. May modify thyroid hormone deiodination and materno-fetal thyroid hormone transport. (PMID:16159939)
  • Data show that after the vitamin B6 was added into HSA solution the fluorescence of HSA was quenched partially. (PMID:16201370)
  • Human plasma contains four esterases: butyrylcholinesterase, paraoxonase, acetylcholinesterase, and albumin. (PMID:16213467)
  • Human granulosa cells express the carboxyl and amino terminal part of the HSA gene in levels comparable to those found in human hepatocytes. (PMID:16253963)
  • The unfolding of domain II precedes that of domain I and the unfolding of domain III follows that of domain I. (PMID:16324740)

Cross-species orthologs

2 orthologs

OrganismSymbolGene ID
mus_musculusAlbENSMUSG00000029368
rattus_norvegicusAlbENSRNOG00000002911

Paralogs (3): AFM (ENSG00000079557), AFP (ENSG00000081051), GC (ENSG00000145321)

Protein

Protein identifiers

AlbuminP02768 (reviewed: P02768)

All UniProt accessions (8): A0A0C4DGB6, B7WNR0, C9JKR2, D6RCE7, D6RHD5, P02768, H0YA55, H7C013

UniProt curated annotations — full annotation on UniProt →

Function. Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma. Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner. The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood. The rank order of affinity is zinc > calcium > magnesium. Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli. Does not prevent iron uptake by the bacterial siderophore aerobactin.

Subunit / interactions. Interacts with FCGRT; this interaction regulates ALB homeostasis. Interacts with TASOR. In plasma, occurs in a covalently-linked complex with chromophore-bound alpha-1-microglobulin with molar ratio 1:2 and 1:1; this interaction does not prevent fatty acid binding to ALB.

Subcellular location. Secreted.

Tissue specificity. Plasma.

Post-translational modifications. Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606. Glycated in diabetic patients. Phosphorylated by FAM20C in the extracellular medium. Acetylated on Lys-223 by acetylsalicylic acid.

Disease relevance. Hyperthyroxinemia, familial dysalbuminemic (FDAH) [MIM:615999] A disorder characterized by abnormally elevated levels of total serum thyroxine (T4) in euthyroid patients. It is due to abnormal serum albumin that binds T4 with enhanced affinity. The disease is caused by variants affecting the gene represented in this entry. Analbuminemia (ANALBA) [MIM:616000] A rare autosomal recessive disorder manifested by the presence of a very low amount of circulating serum albumin. Affected individuals manifest mild edema, hypotension, fatigue, and, occasionally, lower body lipodystrophy (mainly in adult females). The most common biochemical finding is hyperlipidemia, with a significant increase in the total and LDL cholesterol concentrations, but normal concentrations of HDL cholesterol and triglycerides. The disease is caused by variants affecting the gene represented in this entry.

Polymorphism. A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. The sequence shown is that of variant albumin A.

Similarity. Belongs to the ALB/AFP/VDB family.

Isoforms (3)

UniProt IDNamesCanonical?
P02768-11yes
P02768-22
P02768-33

RefSeq proteins (1): NP_000468* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR000264ALB/AFP/VDBFamily
IPR014760Serum_albumin_NDomain
IPR020857Serum_albumin_CSConserved_site
IPR020858Serum_albumin-likeHomologous_superfamily
IPR021177Serum_albumin/AFP/AfaminFamily

Pfam: PF00273

UniProt features (253 total): sequence variant 66, site 38, helix 34, glycosylation site 24, disulfide bond 17, sequence conflict 16, strand 15, modified residue 14, binding site 12, turn 8, domain 3, splice variant 2, signal peptide 1, propeptide 1, mutagenesis site 1, chain 1

Structure

Experimental structures (PDB)

189 structures, top 30 by resolution.

PDBMethodResolution (Å)
9IK6X-RAY DIFFRACTION1.69
6YG9X-RAY DIFFRACTION1.89
1N5UX-RAY DIFFRACTION1.9
8RCOX-RAY DIFFRACTION1.9
8RCPX-RAY DIFFRACTION1.9
8RGKX-RAY DIFFRACTION1.9
8RGLX-RAY DIFFRACTION1.9
9EODX-RAY DIFFRACTION1.9
9CSGX-RAY DIFFRACTION1.91
6QIOX-RAY DIFFRACTION1.95
9IK7X-RAY DIFFRACTION1.97
7VR0X-RAY DIFFRACTION1.98
7Y2DX-RAY DIFFRACTION2
8A9QX-RAY DIFFRACTION2
4L8UX-RAY DIFFRACTION2.01
9ULRX-RAY DIFFRACTION2.01
7DJNX-RAY DIFFRACTION2.04
3SQJX-RAY DIFFRACTION2.05
7FFSX-RAY DIFFRACTION2.05
8Z8VX-RAY DIFFRACTION2.05
6L4KX-RAY DIFFRACTION2.09
8YG7X-RAY DIFFRACTION2.09
7AAIX-RAY DIFFRACTION2.1
7X7XX-RAY DIFFRACTION2.1
9EOSX-RAY DIFFRACTION2.1
8K1YX-RAY DIFFRACTION2.15
5Z0BX-RAY DIFFRACTION2.17
4Z69X-RAY DIFFRACTION2.19
3A73X-RAY DIFFRACTION2.19
1E7AX-RAY DIFFRACTION2.2

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-P02768-F192.570.88

Antibody-complex structures (SAbDab): 112ESG, 4HGK, 4HGM, 5FUO, 5VNW, 6M58, 8OI2, 8Y9S, 8Y9T, 8Y9U, 8Z8V

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (38): 28 (not glycated); 44 (not glycated); 65 (not glycated); 88 (not glycated); 97 (not glycated); 117 (not glycated); 130 (not glycated); 160 (not glycated); 183 (not glycated); 198 (not glycated); 205 (not glycated); 214 (not glycated) …

Ligand- & substrate-binding residues (12): 264; 268; 271; 273; 273; 276; 279; 283; 27; 30; 37; 91

Post-translational modifications (14): 29, 82, 89, 107, 229, 297, 443, 444, 446, 460, 513, 543, 558, 588

Disulfide bonds (17): 269–277, 289–303, 302–313, 340–385, 384–393, 416–462, 461–472, 485–501, 500–511, 538–583, 582–591, 77–86, 99–115, 114–125, 148–193, 192–201, 224–270

Glycosylation sites (24): 36, 75, 161, 186, 223, 249, 257, 300, 305, 337, 341, 342, 347, 375, 402, 437, 463, 468, 518, 549 …

Mutagenesis-validated functional residues (1):

PositionPhenotype
91impairs metal binding.

Function

Pathways and Gene Ontology

Reactome pathways

31 pathways

IDPathway
R-HSA-114608Platelet degranulation
R-HSA-159418Recycling of bile acids and salts
R-HSA-189451Heme biosynthesis
R-HSA-189483Heme degradation
R-HSA-2168880Scavenging of heme from plasma
R-HSA-381426Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8957275Post-translational protein phosphorylation
R-HSA-8964058HDL remodeling
R-HSA-9707564Cytoprotection by HMOX1
R-HSA-9749641Aspirin ADME
R-HSA-9757110Prednisone ADME
R-HSA-9793528Ciprofloxacin ADME
R-HSA-109582Hemostasis
R-HSA-1430728Metabolism
R-HSA-174824Plasma lipoprotein assembly, remodeling, and clearance
R-HSA-189445Metabolism of porphyrins
R-HSA-194068Bile acid and bile salt metabolism
R-HSA-2173782Binding and Uptake of Ligands by Scavenger Receptors
R-HSA-2262752Cellular responses to stress
R-HSA-382551Transport of small molecules
R-HSA-392499Metabolism of proteins
R-HSA-556833Metabolism of lipids
R-HSA-5653656Vesicle-mediated transport
R-HSA-597592Post-translational protein modification
R-HSA-76002Platelet activation, signaling and aggregation
R-HSA-76005Response to elevated platelet cytosolic Ca2+
R-HSA-8953897Cellular responses to stimuli
R-HSA-8957322Metabolism of steroids
R-HSA-8963899Plasma lipoprotein remodeling
R-HSA-9711123Cellular response to chemical stress

MSigDB gene sets: 254 (showing top): MODULE_93, MODULE_52, GOBP_MEMBRANE_DEPOLARIZATION, YAGI_AML_WITH_INV_16_TRANSLOCATION, PID_HNF3B_PATHWAY, GOCC_SECRETORY_GRANULE, REACTOME_PLATELET_ACTIVATION_SIGNALING_AND_AGGREGATION, REACTOME_METABOLISM_OF_PORPHYRINS, HUMMERICH_BENIGN_SKIN_TUMOR_DN, HUMMERICH_MALIGNANT_SKIN_TUMOR_DN, HNF1_Q6, GOBP_REGULATION_OF_MEMBRANE_DEPOLARIZATION, CEBPB_01, GOBP_ORGANIC_ACID_TRANSPORT, chr4q13

GO Biological Process (6): cellular response to starvation (GO:0009267), bilirubin transport (GO:0015723), response to nutrient levels (GO:0031667), negative regulation of mitochondrial depolarization (GO:0051902), cellular response to calcium ion starvation (GO:0072732), cellular oxidant detoxification (GO:0098869)

GO Molecular Function (15): DNA binding (GO:0003677), fatty acid binding (GO:0005504), copper ion binding (GO:0005507), toxic substance binding (GO:0015643), antioxidant activity (GO:0016209), pyridoxal phosphate binding (GO:0030170), identical protein binding (GO:0042802), protein-folding chaperone binding (GO:0051087), molecular carrier activity (GO:0140104), exogenous protein binding (GO:0140272), enterobactin binding (GO:1903981), protein binding (GO:0005515), lipid binding (GO:0008289), oxygen binding (GO:0019825), metal ion binding (GO:0046872)

GO Cellular Component (11): extracellular region (GO:0005576), obsolete extracellular space (GO:0005615), nucleus (GO:0005634), endoplasmic reticulum (GO:0005783), endoplasmic reticulum lumen (GO:0005788), Golgi apparatus (GO:0005794), platelet alpha granule lumen (GO:0031093), protein-containing complex (GO:0032991), extracellular exosome (GO:0070062), blood microparticle (GO:0072562), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-14 pathways:

CategoryPathways
Drug ADME3
Metabolism of porphyrins2
Response to elevated platelet cytosolic Ca2+1
Bile acid and bile salt metabolism1
Binding and Uptake of Ligands by Scavenger Receptors1
Metabolism of proteins1
Post-translational protein modification1
Plasma lipoprotein remodeling1
Cellular response to chemical stress1
Transport of small molecules1
Metabolism1
Metabolism of steroids1
Vesicle-mediated transport1
Cellular responses to stimuli1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
binding4
protein binding3
cellular anatomical structure3
intracellular membrane-bounded organelle3
molecular_function2
anion binding2
cytoplasm2
endomembrane system2
cellular response to nutrient levels1
cellular response to stress1
response to starvation1
dicarboxylic acid transport1
nitrogen compound transport1
response to stimulus1
mitochondrial depolarization1
regulation of mitochondrial depolarization1
negative regulation of membrane depolarization1
cellular response to starvation1
cellular detoxification1
nucleic acid binding1
lipid binding1
monocarboxylic acid binding1
transition metal ion binding1
cellular oxidant detoxification1
vitamin B6 binding1
macrolide binding1
heterocyclic compound binding1
small molecule binding1
cation binding1
endoplasmic reticulum1
intracellular organelle lumen1
platelet alpha granule1
secretory granule lumen1
cellular_component1
extracellular vesicle1
extracellular region1
intracellular anatomical structure1

Protein interactions and networks

STRING

10898 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
ALBINSP01308999
ALBORM2P19652998
ALBORM1P02763997
ALBLALBAP00709997
ALBFN1P02751997
ALBFCGRTP55899997
ALBLTFP02788996
ALBSERPINA1P01009996
ALBSHBGP04278996
ALBAPOA1P02647994
ALBHPP00737994
ALBLRP2P98164994
ALBCUBNO60494992
ALBMBP02144992
ALBSPARCP09486991
ALBTTRP02766991

IntAct

191 interactions, top by confidence:

ABTypeScore
MED4MED19psi-mi:“MI:0914”(association)0.900
MAPK6HERC2psi-mi:“MI:0914”(association)0.840
MED20MED19psi-mi:“MI:0914”(association)0.840
CTBP1ZEB2psi-mi:“MI:0914”(association)0.800
ALBALBpsi-mi:“MI:0407”(direct interaction)0.760
HSPA8GAKpsi-mi:“MI:0914”(association)0.760
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710
CCNA2GMNNpsi-mi:“MI:0914”(association)0.640
ALBTFRCpsi-mi:“MI:0407”(direct interaction)0.560
ALBpsi-mi:“MI:0407”(direct interaction)0.540
ALBpsi-mi:“MI:0915”(physical association)0.540
FOXP3FOXP2psi-mi:“MI:0914”(association)0.530
CA8IGLL5psi-mi:“MI:0914”(association)0.530
DDX31IGLL5psi-mi:“MI:0914”(association)0.530
ADAMTS18ALBpsi-mi:“MI:0914”(association)0.530
ALBFAM20Cpsi-mi:“MI:0217”(phosphorylation reaction)0.440
FCGRTALBpsi-mi:“MI:0407”(direct interaction)0.440

BioGRID (455): ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Two-hybrid), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS), ALB (Affinity Capture-MS)

ESM2 similar proteins: A2V9Z4, A6YF56, G3MYZ3, O01454, O35090, O89020, P02768, P02769, P02770, P02771, P02772, P02773, P02774, P04276, P07724, P08759, P08835, P14639, P14872, P19121, P21614, P21847, P21848, P28050, P35747, P36953, P43652, P49064, P49065, P49066, P49822, P53789, P83632, P84407, Q03156, Q17077, Q25513, Q27388, Q28522, Q28789

Diamond homologs: A2V9Z4, A6YF56, G3MYZ3, O35090, O89020, P02768, P02769, P02770, P02771, P02772, P02773, P07724, P08759, P08835, P14639, P14872, P19121, P21847, P28050, P35747, P36953, P43652, P49064, P49065, P49066, P49822, P81188, P84407, P85295, Q28522, Q28789, Q3SZ57, Q3T478, Q5NVH5, Q5XLE4, Q8MJ76, Q8MJU5, P83517, P21848, Q03156

SIGNOR signaling

1 interactions.

AEffectBMechanism
HNF1B“up-regulates quantity by expression”ALB“transcriptional regulation”

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 209 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
Downstream signal transduction514.1×2e-03
Response to elevated platelet cytosolic Ca2+67.2×5e-03
Platelet activation, signaling and aggregation86.3×3e-03
Platelet degranulation85.2×5e-03
Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)85.1×5e-03
RAF/MAP kinase cascade94.1×8e-03
Vesicle-mediated transport143.6×3e-03
Membrane Trafficking133.6×4e-03

GO biological processes:

GO termPartnersFoldFDR
negative regulation of cytokine production514.8×7e-03
autophagosome maturation612.2×5e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

234 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic19
Likely pathogenic1
Uncertain significance96
Likely benign25
Benign16

Top pathogenic / likely-pathogenic (20)

Variant IDHGVSClassification
156314NM_000477.7(ALB):c.166C>T (p.Gln56Ter)Pathogenic
156319NM_000477.7(ALB):c.228_229del (p.Val78fs)Pathogenic
156320NM_000477.7(ALB):c.412C>T (p.Arg138Ter)Pathogenic
156323NM_000477.7(ALB):c.714G>A (p.Trp238Ter)Pathogenic
18186NM_000477.5(ALB):c.71G>C (p.Arg24Pro)Pathogenic
18187NM_000477.7(ALB):c.74A>T (p.Asp25Val)Pathogenic
18203NM_000477.7(ALB):c.1693A>G (p.Lys565Glu)Pathogenic
18207NM_000477.7(ALB):c.1780G>A (p.Glu594Lys)Pathogenic
18210NM_000477.7(ALB):c.714-2A>GPathogenic
18224NM_000477.7(ALB):c.872dup (p.Asn291fs)Pathogenic
18238NM_000477.7(ALB):c.725G>C (p.Arg242Pro)Pathogenic
18239NM_000477.7(ALB):c.269T>C (p.Leu90Pro)Pathogenic
18240NM_000477.7(ALB):c.79+1G>APathogenic
2788444NM_000477.7(ALB):c.1378A>T (p.Lys460Ter)Pathogenic
4682120NM_000477.7(ALB):c.724C>A (p.Arg242Ser)Pathogenic
4696783NM_000477.7(ALB):c.1020C>A (p.Cys340Ter)Pathogenic
4720501NM_000477.7(ALB):c.70C>T (p.Arg24Ter)Pathogenic
4755693NM_000477.7(ALB):c.1225C>T (p.Gln409Ter)Pathogenic
636260NM_000477.7(ALB):c.1098dup (p.Val367fs)Pathogenic
2442164NM_000477.7(ALB):c.656_659del (p.Lys219fs)Likely pathogenic

SpliceAI

0 predictions. Top by Δscore:

AlphaMissense

4030 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
4:73410366:T:AC224S0.997
4:73410367:G:CC224S0.997
4:73412012:A:CS244R0.996
4:73412014:C:AS244R0.996
4:73412014:C:GS244R0.996
4:73418113:G:AC485Y0.996
4:73410366:T:CC224R0.995
4:73412090:T:AC270S0.995
4:73412091:G:CC270S0.995
4:73418112:T:AC485S0.995
4:73418113:G:CC485S0.995
4:73418160:T:AC501S0.995
4:73418161:G:CC501S0.995
4:73408618:T:AC99S0.994
4:73408619:G:CC99S0.994
4:73408713:A:CK130N0.994
4:73408713:A:TK130N0.994
4:73412091:G:AC270Y0.994
4:73417622:T:AC461S0.994
4:73417623:G:CC461S0.994
4:73418112:T:CC485R0.994
4:73418114:T:GC485W0.994
4:73418161:G:AC501Y0.994
4:73418162:C:GC501W0.994
4:73406721:G:AC77Y0.993
4:73406722:T:GC77W0.993
4:73408619:G:AC99Y0.993
4:73408765:T:AC148S0.993
4:73408766:G:CC148S0.993
4:73412090:T:CC270R0.993

dbSNP variants (sampled 300 via entrez): RS1000236315 (4:73418918 C>T), RS10002897 (4:73404707 A>G), RS1000474352 (4:73420822 T>C), RS1000589905 (4:73420506 A>G), RS1000932485 (4:73407561 G>A), RS1000987701 (4:73419702 G>A,C), RS1001030097 (4:73406429 A>T), RS1001066991 (4:73407146 C>A), RS1001127206 (4:73419916 T>G), RS1001229515 (4:73418978 G>C), RS1001405633 (4:73407090 GTATT>G,GTATTTATT), RS1002104967 (4:73407121 A>G,T), RS1002158644 (4:73406903 T>G), RS1002161396 (4:73420333 T>G), RS10022167 (4:73413092 G>A,C)

Disease associations

OMIM: gene MIM:103600 | disease phenotypes: MIM:615999

GenCC curated gene-disease

DiseaseClassificationInheritance
congenital analbuminemiaDefinitiveAutosomal recessive
hyperthyroxinemia, familial dysalbuminemicStrongAutosomal dominant

ClinGen Gene-Disease Validity (2)

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

DiseaseClassificationInheritance
hyperthyroxinemia, familial dysalbuminemicModerateAD
congenital analbuminemiaDefinitiveAR

Mondo (4): hyperthyroxinemia, familial dysalbuminemic (MONDO:0014448), Ehlers-Danlos syndrome, arthrochalasia type (MONDO:0007525), hyperthyroidism (MONDO:0004425), congenital analbuminemia (MONDO:0014449)

Orphanet (5): Congenital analbuminemia (Orphanet:86816), Arthrochalasia Ehlers-Danlos syndrome (Orphanet:1899), OBSOLETE: Ehlers-Danlos syndrome type 7A (Orphanet:99875), OBSOLETE: Ehlers-Danlos syndrome type 7B (Orphanet:99876), NON RARE IN EUROPE: Familial dysalbuminemic hyperthyroxinemia (Orphanet:276271)

HPO phenotypes

31 total (30 of 31 shown, HPO-id order):

HPOTerm
HP:0000006Autosomal dominant inheritance
HP:0000007Autosomal recessive inheritance
HP:0000282Facial edema
HP:0000939Osteoporosis
HP:0000969Edema
HP:0001263Global developmental delay
HP:0001513Obesity
HP:0001518Small for gestational age
HP:0001562Oligohydramnios
HP:0001622Premature birth
HP:0001643Patent ductus arteriosus
HP:0002615Hypotension
HP:0002783Recurrent lower respiratory tract infections
HP:0003073Hypoalbuminemia
HP:0003075Hypoproteinemia
HP:0003077Hyperlipidemia
HP:0003124Hypercholesterolemia
HP:0003141Increased LDL cholesterol concentration
HP:0005268Miscarriage
HP:0005413Elevated circulating alpha-globulin concentration
HP:0008247Euthyroid hyperthyroxinemia
HP:0009125Lipodystrophy
HP:0010702Increased circulating immunoglobulin concentration
HP:0010741Pedal edema
HP:0011342Mild global developmental delay
HP:0012378Fatigue
HP:0030851Low pulse pressure
HP:0031097Abnormal thyroid-stimulating hormone level
HP:0032386Elevated circulating transferrin concentration
HP:0033076Abnormal circulating free T4 concentration

GWAS associations

0 associations (top):

MeSH disease descriptors (3)

DescriptorNameTree numbers
D006980HyperthyroidismC19.874.397
D050010Hyperthyroxinemia, Familial DysalbuminemicC16.320.427; C19.874.410.249
C562625Ehlers-Danlos Syndrome, Type VII, Autosomal Dominant (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL3253 (SINGLE PROTEIN)

Molecules with ChEMBL bioactivity

36 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 942,122 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL12DIAZEPAM492,281
CHEMBL1200712EVANS BLUE424,260
CHEMBL129ZIDOVUDINE44,996
CHEMBL1380ABACAVIR430,419
CHEMBL139DICLOFENAC4125,009
CHEMBL141LAMIVUDINE412,250
CHEMBL1434MINOCYCLINE462,058
CHEMBL1447LINCOMYCIN433,659
CHEMBL1460DIDANOSINE489,412
CHEMBL1464WARFARIN469,797
CHEMBL1730CEFOTAXIME4480
CHEMBL2103837TAFAMIDIS4672
CHEMBL262777VANCOMYCIN4100,538
CHEMBL36506NOVOBIOCIN411,401
CHEMBL374478RIFAMPIN493,834
CHEMBL374975FUSIDIC ACID447,850
CHEMBL388590BENZBROMARONE48,245
CHEMBL3940890ACORAMIDIS4576
CHEMBL4OFLOXACIN447,798
CHEMBL409BICALUTAMIDE486,587
CHEMBL4301898BRILLIANT BLUE G FREE ACID4
CHEMBL473417VISMODEGIB4
CHEMBL521IBUPROFEN4
CHEMBL532ERYTHROMYCIN4
CHEMBL54349ALPIDEM4
CHEMBL568OXAZEPAM4
CHEMBL6INDOMETHACIN4
CHEMBL71CHLORPROMAZINE4
CHEMBL782TOLBUTAMIDE4
CHEMBL853ZALCITABINE4

PharmGKB: 1 entry (VIP=true, CPIC=false)

ChEMBL bioactivities

144 potent at pChembl≥5 of 200 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
8.08Ki8.27nMCHEMBL5199978
7.82Kd15nMCHEMBL5270477
7.70Kd20nMCHEMBL4874500
7.52Kd30nMCHEMBL4875916
7.52Kd30nMCHEMBL3394540
7.52Kd30nMCHEMBL5567878
7.52Kd30nMCHEMBL5559833
7.52Kd30nMCHEMBL5550030
7.52Kd30nMCHEMBL5563477
7.41Kd39nMCHEMBL5205331
7.41Kd39nMCHEMBL5204039
7.41Kd39nMCHEMBL5270284
7.30Ki49.7nMCHEMBL5436933
7.16Kd70nMCHEMBL4852232
7.05Kd89.3nMPYROPHEOPHORBIDE A
7.05Kd90nMCHEMBL81444
7.00Kd99nMCHEMBL3260990
6.97Kd108nMCHEMBL5287247
6.93Kd118nMCHEMBL5172861
6.92Kd119nMCHEMBL5203652
6.79Kd164nMCHEMBL5204199
6.78Kd168nMCHEMBL5183937
6.78Kd168nMCHEMBL5275396
6.77Kd170nMCHEMBL4845813
6.68Kd210nMCHEMBL4870031
6.66Kd220nMCHEMBL4866037
6.64Kd230nMCHEMBL3260990
6.64Kd230nMCHEMBL5082399
6.57Kd270nMCHEMBL4866759
6.55Kd280nMCHEMBL337637
6.54Kd290nMCHEMBL4877313
6.51Kd310nMCHEMBL4856339
6.50Kd320nMBRILLIANT BLUE G FREE ACID
6.49Kd321nMCHEMBL2180871
6.48Kd330nMCHEMBL5287247
6.47Kd340nMCHEMBL5091083
6.44Ki360nMCHEMBL3417694
6.44Kd363nMCHEMBL4850435
6.44Kd360nMCHEMBL5093073
6.42Kd382nMRESVERATROL HEXANOIC ACID
6.41Kd390nMCHEMBL249022
6.41Kd390nMCHEMBL4869829
6.40Ki400nMCHEMBL2314198
6.38Kd420nMCHEMBL249990
6.37Kd430nMCHEMBL4879282
6.33Kd467nMCHEMBL5267643
6.28Kd520nMCHEMBL6170858
6.24Kd580nMCHEMBL4873867
6.23Kd593nMBETULINIC ACID
6.18Kd660nMCHEMBL77613

PubChem BioAssay actives

135 with measured affinity, of 2691 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
N-[[2-((18F)fluoromethoxy)phenyl]methyl]-N-(4-phenoxy-3-pyridinyl)acetamide1992575: Binding affinity to human serum albumin by fluorescence polarization assayki0.0083uM
(4S)-4-[[(2S)-2-[[(2S)-2-acetamido-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-5-carbamimidamido-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[2-[[2-[[(2S,3R)-1-[(2S)-2-carbamoylpyrrolidin-1-yl]-3-hydroxy-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-5-oxopentanoic acid1940746: Binding affinity to human albumin assessed as dissociation constantkd0.0150uM
(2S)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-(3-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.0200uM
(2S)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-naphthalen-2-ylpropanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.0300uM
7-[(2-hydroxy-5-nitrophenyl)methylamino]-4-methylchromen-2-one2074276: Reversible binding affinity to human serum albuminkd0.0300uM
7-(2-methylphenyl)-3-(3-naphthalen-1-yloxypropyl)-1H-indole-2-carboxylic acid1200464: Displacement of probe S1 from recombinant human serum albumin domain 3 after 5 mins by fluorescence polarization assayki0.0300uM
7-[(2-hydroxyphenyl)methylamino]-4-methylchromen-2-one2074276: Reversible binding affinity to human serum albuminkd0.0300uM
7-[(3,5-dichloro-2-hydroxyphenyl)methylamino]-4-methylchromen-2-one2074276: Reversible binding affinity to human serum albuminkd0.0300uM
7-[(3,5-dibromo-2-hydroxyphenyl)methylamino]-4-methylchromen-2-one2074276: Reversible binding affinity to human serum albuminkd0.0300uM
7-[(2-hydroxy-3,5-diiodophenyl)methylamino]-4-methylchromen-2-one2074276: Reversible binding affinity to human serum albuminkd0.0300uM
(2S)-2-[[(3R,6S,9S,12S,15S,18S,21S)-6-[3-(diaminomethylideneamino)propyl]-15-[(4-hydroxyphenyl)methyl]-9-methyl-12,18-bis(2-methylpropyl)-5,8,11,14,17,20,25-heptaoxo-21-[[(2S)-pyrrolidine-2-carbonyl]amino]-1,23-dithia-4,7,10,13,16,19-hexazacyclohexacosane-3-carbonyl]amino]-3-hydroxypropanoic acid1884314: Binding affinity to human serum albumin by fluorescence polarization assaykd0.0390uM
(3S,6S,9S,12S,15R,23R,26S)-15-[(2-aminoacetyl)amino]-6-(3-amino-3-oxopropyl)-9-[3-(diaminomethylideneamino)propyl]-12-[(1R)-1-hydroxyethyl]-3-[(4-hydroxyphenyl)methyl]-2,5,8,11,14,19,25-heptaoxo-17,21-dithia-1,4,7,10,13,24-hexazabicyclo[24.3.0]nonacosane-23-carboxylic acid1884314: Binding affinity to human serum albumin by fluorescence polarization assaykd0.0390uM
(4S)-5-amino-4-[[(2S)-2-[[(2S)-4-carboxy-2-[[(2S)-2-[[(2S)-4-carboxy-2-[[(2S)-2-[[(2S)-4-carboxy-2-[[2-[2-[2-[(3’,6’-dihydroxy-3-oxospiro[2-benzofuran-1,9’-xanthene]-5-carbonyl)amino]ethoxy]ethoxy]acetyl]amino]butanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]butanoyl]amino]-6-(hexadecanoylamino)hexanoyl]amino]butanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-5-oxopentanoic acid1940738: Binding affinity to human albumin by fluorescence polarization assaykd0.0390uM
[1-[4-(1H-benzimidazol-2-yl)benzoyl]piperidin-4-yl] N-[3-[2-[2-(2-aminoethoxy)ethoxy]ethylcarbamoyl]phenyl]carbamate1973690: Binding affinity to human serum albumin by fluorescence polarization assayki0.0497uM
(2S)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-(4-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.0700uM
3-[(21S,22S)-16-ethenyl-11-ethyl-4-hydroxy-12,17,21,26-tetramethyl-7,23,24,25-tetrazahexacyclo[18.2.1.15,8.110,13.115,18.02,6]hexacosa-1,4,6,8(26),9,11,13(25),14,16,18(24),19-undecaen-22-yl]propanoic acid1758625: Binding affinity to human serum albumin assessed as dissociation constant by fluorescence emission spectrophotometric analysiskd0.0893uM
7-(8-carboxy-1,6,7-trihydroxy-3-methyl-5-propan-2-ylnaphthalen-2-yl)-2,3,8-trihydroxy-6-methyl-4-propan-2-ylnaphthalene-1-carboxylic acid203631: Compound was tested for binding activity to human serum albumin (HSA)kd0.0900uM
(1E)-2-(5-tert-butyl-1,2-oxazol-3-yl)-N-(3-chloroanilino)-2-oxoethanimidoyl cyanide1598740: Displacement of dansylated phenylalanine from human serum albumin by fluorescence assaykd0.0990uM
5-[[(1R)-1-carboxy-5-[4-(4-iodophenyl)butanoylamino]pentyl]carbamoyl]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid1940748: Binding affinity to human albumin assessed as dissociation constant by fluorescence polarization assaykd0.1080uM
5-[2-[2-[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[2-[2-[2-[[(3S,6S,9S,12S,15R,23R,26S)-6-(3-amino-3-oxopropyl)-9-(3-carbamimidamidopropyl)-23-carbamoyl-12-[(1R)-1-hydroxyethyl]-3-[(4-hydroxyphenyl)methyl]-2,5,8,11,14,19,25-heptaoxo-17,21-dithia-1,4,7,10,13,24-hexazabicyclo[24.3.0]nonacosan-15-yl]amino]-2-oxoethoxy]ethoxy]ethylamino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-6-(hexadecanoylamino)-1-oxohexan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-2-oxoethoxy]ethoxy]ethylcarbamoyl]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid1884314: Binding affinity to human serum albumin by fluorescence polarization assaykd0.1180uM
5-[2-[2-[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[2-[2-[2-[[(5S)-5-[[2-[[(3S,6S,9S,12S,15R,23R,26S)-15-[(2-aminoacetyl)amino]-6-(3-amino-3-oxopropyl)-9-(3-carbamimidamidopropyl)-12-[(1R)-1-hydroxyethyl]-3-[(4-hydroxyphenyl)methyl]-2,5,8,11,14,19,25-heptaoxo-17,21-dithia-1,4,7,10,13,24-hexazabicyclo[24.3.0]nonacosane-23-carbonyl]amino]acetyl]amino]-6-[(2-amino-2-oxoethyl)amino]-6-oxohexyl]amino]-2-oxoethoxy]ethoxy]ethylamino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-6-(hexadecanoylamino)-1-oxohexan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-2-oxoethoxy]ethoxy]ethylcarbamoyl]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid1884314: Binding affinity to human serum albumin by fluorescence polarization assaykd0.1190uM
5-[2-[2-[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[2-[2-[2-[[(5S)-6-[(2-amino-2-oxoethyl)amino]-5-[[2-[[(3R,6S,9S,12S,15S,18S,21R)-6-(3-carbamimidamidopropyl)-15-[(4-hydroxyphenyl)methyl]-9-methyl-12,18-bis(2-methylpropyl)-5,8,11,14,17,20,25-heptaoxo-21-[[(2S)-pyrrolidine-2-carbonyl]amino]-1,23-dithia-4,7,10,13,16,19-hexazacyclohexacosane-3-carbonyl]amino]acetyl]amino]-6-oxohexyl]amino]-2-oxoethoxy]ethoxy]ethylamino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-6-(hexadecanoylamino)-1-oxohexan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-2-oxoethoxy]ethoxy]ethylcarbamoyl]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid1884314: Binding affinity to human serum albumin by fluorescence polarization assaykd0.1640uM
5-[2-[2-[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[2-[2-[2-[(2S)-2-[[(3R,6S,9S,12S,15S,18S,21R)-3-[[(2S)-1-amino-3-hydroxy-1-oxopropan-2-yl]carbamoyl]-6-(3-carbamimidamidopropyl)-15-[(4-hydroxyphenyl)methyl]-9-methyl-12,18-bis(2-methylpropyl)-5,8,11,14,17,20,25-heptaoxo-1,23-dithia-4,7,10,13,16,19-hexazacyclohexacos-21-yl]carbamoyl]pyrrolidin-1-yl]-2-oxoethoxy]ethoxy]ethylamino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-6-(hexadecanoylamino)-1-oxohexan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-2-oxoethoxy]ethoxy]ethylcarbamoyl]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid1884314: Binding affinity to human serum albumin by fluorescence polarization assaykd0.1680uM
(4S)-4-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-4-carboxybutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-carboxybutanoyl]amino]-6-(pentadecanoylamino)hexanoyl]amino]-5-[[(2S)-1-[[(2S)-4-carboxy-1-oxo-1-[[(2S)-1-oxo-1-[[(7R,10S,13S,19S,25S,28R,31S,34S,37S,40S,43S,46S,49R)-19,25,43-tris(3-carbamimidamidopropyl)-37-(2-carboxyethyl)-31-(carboxymethyl)-7-(carboxymethylcarbamoyl)-13,46-bis(hydroxymethyl)-40-[(4-hydroxyphenyl)methyl]-10-methyl-9,12,15,18,21,24,27,30,33,36,39,42,45,48-tetradecaoxo-34-propan-2-yl-5,51,56-trithia-8,11,14,17,20,23,26,29,32,35,38,41,44,47-tetradecazatricyclo[26.26.3.13,53]octapentaconta-1(54),2,53(58)-trien-49-yl]amino]propan-2-yl]amino]butan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid1940738: Binding affinity to human albumin by fluorescence polarization assaykd0.1680uM
(2S)-2-[(6-fluoro-1H-indole-2-carbonyl)amino]-3-(4-hydroxy-3-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.1700uM
(2S)-2-[(7-fluoro-1H-indole-2-carbonyl)amino]-3-(4-hydroxy-3-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.2100uM
(2R)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-(4-hydroxy-3-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.2200uM
4-[[(1R)-1-carboxy-5-[4-(4-iodophenyl)butanoylamino]pentyl]carbamoyl]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid1821156: Binding affinity to human serum albumin assessed as dissociation constant using N-alpha-(6-FAM)-N-epsilon-(4-Iodophenylbutanoyl)-D-lysine as substrate and measured after 5 mins by fluorescence based competition assaykd0.2300uM
(2S)-2-[(5-fluoro-1H-indole-2-carbonyl)amino]-3-(4-hydroxy-3-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.2700uM
2-[2-oxo-2-[3-[(E)-2-(4-propan-2-yl-1,3-thiazol-2-yl)ethenyl]anilino]ethyl]benzoic acid203632: Protein binding affinity for human serum albumin was measuredkd0.2800uM
(2S)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-(4-hydroxy-3-iodophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.2900uM
(2S)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-(4-hydroxy-3-nitrophenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.3100uM
(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(3S,6R,11R,17S,20S,23S)-6-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-1-(4-azidobutylamino)-1-oxohexan-2-yl]amino]-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-4-carboxybutanoyl]amino]-3-carboxypropanoyl]amino]-3-methylpentanoyl]amino]-20-(3-carbamimidamidopropyl)-17-(1H-indol-3-ylmethyl)-3-(2-methylpropyl)-2,5,13,16,19,22-hexaoxo-8,9-dithia-1,4,12,15,18,21-hexazabicyclo[21.3.0]hexacosane-11-carbonyl]amino]-4-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-carboxybutanoyl]amino]-3-carboxypropanoyl]amino]butanedioic acid709576: Binding affinity to human serum albumin by fluorescence polarization assaykd0.3210uM
(2S)-2-[(4-ethynylbenzoyl)amino]-6-[4-(4-iodophenyl)butanoylamino]hexanoic acid1821155: Binding affinity to human serum albumin assessed as dissociation constant and measured after 5 mins by fluorescence based competition assaykd0.3400uM
(2S)-2-[(4-azidobenzoyl)amino]-6-[4-(4-iodophenyl)butanoylamino]hexanoic acid1821155: Binding affinity to human serum albumin assessed as dissociation constant and measured after 5 mins by fluorescence based competition assaykd0.3600uM
7-(2-methylphenyl)-1-(2-morpholin-4-ylethyl)-3-(3-naphthalen-1-yloxypropyl)indole-2-carboxylic acid1200464: Displacement of probe S1 from recombinant human serum albumin domain 3 after 5 mins by fluorescence polarization assayki0.3600uM
(2S)-6-amino-2-[[(2R)-6-amino-2-[[(2R)-2-[[(2S)-2-[[(2R)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2R)-2-[[(2S)-6-amino-2-[[(2S)-2-[[2-[[2-[3-[(21S,22S)-16-ethenyl-11-ethyl-12,17,21,26-tetramethyl-4-oxo-7,23,24,25-tetrazahexacyclo[18.2.1.15,8.110,13.115,18.02,6]hexacosa-1,5,8(26),9,11,13(25),14,16,18,20(23)-decaen-22-yl]propanoylamino]acetyl]amino]acetyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]-N-[(2S)-1-[[(2S)-1-[[(2R)-6-amino-1-[[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]hexanamide1758625: Binding affinity to human serum albumin assessed as dissociation constant by fluorescence emission spectrophotometric analysiskd0.3630uM
6-[4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]phenoxy]hexanoic acid404515: Binding affinity to human serum albumin at 4 uM by UV-vis measurementkd0.3820uM
5-cyano-2-[(E)-2-(1-methylindol-2-yl)ethenyl]benzoic acid308402: Binding affinity at human serum albuminkd0.3900uM
(2S)-3-(4-hydroxy-3-iodophenyl)-2-(1H-indole-2-carbonylamino)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.3900uM
3-(3-naphthalen-1-yloxypropyl)-1H-indole-2-carboxylic acid1200464: Displacement of probe S1 from recombinant human serum albumin domain 3 after 5 mins by fluorescence polarization assayki0.4000uM
(2S)-3-[4-[3-[[2-(cyclopropylamino)-3,4-dioxocyclobuten-1-yl]amino]phenyl]phenyl]-2-[(2,4,6-trimethylphenyl)sulfonylamino]propanoic acid310225: Binding affinity to human serum albumin by equilibrium dialysiskd0.4200uM
(2S)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]-3-(4-methoxyphenyl)propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.4300uM
(4S)-4-[[(2S)-2-[[(2S)-2-[[(3S,6R,10R,16S,18S,21S)-6-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-acetamido-5-carbamimidamidopentanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-4-carboxybutanoyl]amino]-3-carboxypropanoyl]amino]-3-methylpentanoyl]amino]-18-(3-carbamimidamidopropyl)-16-(1H-indol-3-ylmethyl)-3-(2-methylpropyl)-2,5,12,15,17,20-hexaoxo-8-thia-1,4,11,14,19-pentazabicyclo[19.3.0]tetracosane-10-carbonyl]amino]-4-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-[[(2S)-1-[[(2S)-1-amino-3-carboxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-5-oxopentanoic acid1940751: Binding affinity to human albumin assessed as dissociation constant by surface plasmon resonance assaykd0.4670uM
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[(4-fluoro-1H-indole-2-carbonyl)amino]propanoic acid1774672: Binding affinity to human serum albumin by fluorescence polarization assaykd0.5800uM
(1R,3aS,5aR,5bR,7aR,9S,11aR,11bR,13aR,13bR)-9-hydroxy-5a,5b,8,8,11a-pentamethyl-1-prop-1-en-2-yl-1,2,3,4,5,6,7,7a,9,10,11,11b,12,13,13a,13b-hexadecahydrocyclopenta[a]chrysene-3a-carboxylic acid1238544: Binding affinity to human serum albumin with excitation at 285 nm by fluorescence emission spectroscopic analysiskd0.5930uM
2,3-dihydroxy-6-methyl-4-propan-2-ylnaphthalene-1-carbaldehyde203631: Compound was tested for binding activity to human serum albumin (HSA)kd0.6600uM
5-cyano-2-[[6-[3-(2-methoxyethoxy)propylsulfanyl]pyridine-3-carbonyl]amino]benzoic acid295540: Binding affinity to human serum albuminkd0.7000uM
Indomethacin1450923: Binding affinity to human serum albuminkd0.7000uM
(2S)-3-[4-[3-(cyclopropylcarbamoylamino)phenyl]phenyl]-2-[(2,4,6-trimethylphenyl)sulfonylamino]propanoic acid310225: Binding affinity to human serum albumin by equilibrium dialysiskd0.7400uM

CTD chemical–gene interactions

430 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
Acetaminophendecreases reaction, increases abundance, increases activity, affects cotreatment, decreases expression (+1 more)9
Copperaffects binding, decreases reaction, increases oxidation, affects cotreatment8
quinonedecreases reaction, affects binding, increases reaction7
Warfarinaffects binding, decreases reaction7
Toluene 2,4-Diisocyanateaffects binding, decreases reaction, increases expression, affects reaction, increases phosphorylation6
Acetohexamideaffects binding5
Fenoprofenaffects binding, decreases reaction5
Mustard Gasaffects binding, increases alkylation5
Cyclosporineaffects reaction, increases uptake, decreases expression, increases expression, affects cotreatment5
bisphenol Aaffects cotreatment, increases expression, affects expression, affects binding, affects folding4
sodium arsenitedecreases reaction, affects methylation, increases expression, decreases expression4
perfluorooctanoic aciddecreases folding, affects folding, affects binding4
benzene oxideaffects binding, increases reaction4
Aspirinaffects transport, decreases reaction, decreases secretion, increases secretion, increases reaction (+1 more)4
Benzeneincreases chemical synthesis, decreases reaction, increases reaction, affects binding4
Doxorubicinaffects binding, increases cleavage, affects expression, decreases expression4
Glucosedecreases uptake, increases metabolic processing, decreases reaction, affects cotreatment, increases glycation4
Tolbutamideaffects binding4
Tretinoindecreases reaction, decreases expression, decreases secretion, affects binding4
Valproic Acidaffects binding, decreases reaction, decreases expression, decreases methylation, increases expression4
Oleic Acidaffects binding, decreases reduction, affects cotreatment, decreases reaction, increases expression (+4 more)4
Palmitic Acidaffects binding, increases reaction, increases reduction, increases oxidation, decreases reduction (+3 more)4
pimagedineaffects cotreatment, decreases reaction, increases glycation3
O,O-diethyl O-3,5,6-trichloro-2-pyridyl phosphatedecreases response to substance, decreases activity, increases hydrolysis, affects binding3
prodanaffects binding, decreases reaction3
Atazanavir Sulfateaffects binding, affects cotreatment, decreases expression3
Resveratrolaffects binding, affects folding, increases stability, decreases reaction, increases activity (+2 more)3
Vehicle Emissionsdecreases abundance, decreases expression, increases abundance, affects cotreatment, increases expression3
Benzo(a)pyreneaffects binding, decreases expression, decreases methylation3
Cadmiumaffects binding, increases expression3

ChEMBL screening assays

953 unique, capped per target: 767 admet, 168 binding, 18 functional

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1000711BindingBinding affinity to human plasma albumin by ultracentrifugationStudies on the interaction of caffeine with bovine hemoglobin. — Eur J Med Chem
CHEMBL1007341ADMETBinding affinity to human serum albumin at 289 kelvin by fluorescence quenching measurementA concise approach to 1,11-didechloro-6-methyl-4’-O-demethyl rebeccamycin and its binding to human serum albumin: fluorescence spectroscopy and molecular modeling method. — Bioorg Med Chem
CHEMBL644481FunctionalWarfarin (80 uM) response( between early and middle) on first day of human serum albumin (HSA) immobilizationBiosensor analysis of the interaction between immobilized human serum albumin and drug compounds for prediction of human serum albumin binding levels. — J Med Chem

Cellosaurus cell lines

5 cell lines: 2 transformed cell line, 1 finite cell line, 1 spontaneously immortalized cell line, 1 cancer cell line

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_5U21GM06248Finite cell lineFemale
CVCL_B6JCC-HAlbSpontaneously immortalized cell lineFemale
CVCL_E1L0HyCyte Hep-G2 KO-hALBCancer cell lineMale
CVCL_JZ95CHO-ADLETransformed cell lineFemale
CVCL_JZ96CHO-AFLETransformed cell lineFemale

Clinical trials (associated diseases)

76 trials via MONDO — disease-level, not drug-specific.

TrialPhaseStatusTitle
NCT00946296PHASE4COMPLETEDImpact of SSKI Pre-Treatment on Blood Loss in Thyroidectomy for Graves Disease
NCT03379181PHASE4COMPLETEDThermogenesis in Hyperthyroidism and Effect of Anti-Adrenergic Therapy
NCT03393728PHASE4COMPLETEDHeart Rate Variability and Hyperthyroidism: Evaluation of the Short-term Effects of Propanolol
NCT05512715PHASE4COMPLETEDLIthium as Bridging thErapy Prior to Radioactiveiodine in hyperThYroidism
NCT03303053PHASE3UNKNOWNEfficacy and Safety of Cholestyramine and Prednisolone as Adjunctive Therapy in Treatment of Overt Hyperthyroidism
NCT04856488PHASE3RECRUITINGPreoperative Lugol’s Solution in Graves’ Disease and Toxic Nodular Goiter
NCT05118542PHASE3COMPLETEDEffect of Hyperthyroidism and Its Treatment in Graves’ Disease to Early Marker of Atherosclerosis
NCT02203682PHASE2UNKNOWNDoxycycline Treatment in Mild Thyroid-Associated Ophthalmopathy
NCT07369063PHASE2RECRUITINGImpact of Vitamin D Therapy on Thyroid Function and Antibody Levels in Pediatric Graves’ Disease
NCT04346901PHASE1COMPLETEDComparative Study of mMASI Before and After Hyperthyroid Therapy in Hyperthyroid Subjects With Melasma
NCT01727973PHASE1/PHASE2COMPLETEDEfficacy of Subantimicrobial Dose Doxycycline for Moderate to Severe and Active Graves’ Orbitopathy
NCT00001159Not specifiedRECRUITINGNatural History of Thyroid Function Disorders
NCT00151723Not specifiedUNKNOWNDoes Radioiodine Treatment Prevent Atrial Fibrillation and Bone Loss in Endogenous Subclinical Hyperthyroidism?
NCT00437931Not specifiedCOMPLETEDColor Flow Doppler Ultrasound in Subclinical Thyroid Dysfunction
NCT00471458Not specifiedCOMPLETEDFollow-up Study of the RAI-Treated Hyperthyroid Patients
NCT00525122Not specifiedUNKNOWNTreatment of M.Graves With Radioactive Iodine: Follow-up Study
NCT00796913Not specifiedCOMPLETEDRemission Induction and Sustenance in Graves’ Disease 2
NCT00822289Not specifiedUNKNOWNThe Effect of Radioactive Iodine Administration for Thyroid Diseases on H.Pylori Eradication
NCT01095341Not specifiedCOMPLETEDPostoperative Hyperthyroidism
NCT01105923Not specifiedUNKNOWNStudy of an Intervention to Improve Problem List Accuracy and Use
NCT01145040Not specifiedUNKNOWNNOMOTHETICOS: Nonlinear Modelling of Thyroid Hormones’ Effect on Thyrotropin Incretion in Confirmed Open-loop Situation
NCT01306916Not specifiedCOMPLETEDCoexisting Thyroid Disease and Hyperparathyroidism
NCT01376648Not specifiedUNKNOWNThyroid Hormones Effect on Brown Adipose Tissue
NCT01945229Not specifiedTERMINATEDThumb-ECG Ambulant Screening for Atrial Fibrillation in Patients Treated for Hyperthyroidism (TAMBOURINE)
NCT02005250Not specifiedCOMPLETEDBone Structure and Strength Evaluated by Extreme-CT Scan Before and After Treatment of Hyper- and Hypothyroidism
NCT02107794Not specifiedCOMPLETEDShared Decision Making in Graves Disease - Graves Disease (GD) Choice
NCT02133040Not specifiedUNKNOWNEffects of Hyperthyroidism on Amount and Activity of Brown Adipose Tissue
NCT02190214Not specifiedCOMPLETEDThyroid Disorders in Malaysia: A Nationwide Multicentre Study
NCT02375451Not specifiedCOMPLETEDEffect of Childhood Radioiodine Therapy on Salivary Function
NCT02499471Not specifiedCOMPLETEDBrown Adipose Tissue Activity and Thyroid Hormone
NCT02514187Not specifiedCOMPLETEDA Blinded Study Evaluating the Accuracy and Safety of Cyclotron-produced 99mTc in Adult Patients
NCT02710799Not specifiedCOMPLETEDEvaluation of the Effects of Teleconsultations on a Endocrinology Referral List
NCT02772705Not specifiedUNKNOWNComparison of SUV Using SPECT/CT Between Grave’s Disease Patients and Normal Humans
NCT02812888Not specifiedUNKNOWNSerum Betatrophin Levels and Its Influencing Factors in Patients With Hyperthyroidism
NCT03064542Not specifiedCOMPLETEDThe Role of Thyroid Status in Regulating Brown Adipose Tissue Activity, White Adipose Tissue Partitioning and Resting Energy Expenditure
NCT03434067Not specifiedUNKNOWNThe Application of Rapid PTH Test Paper in Operation of Hyperparathyroidism
NCT03444246Not specifiedUNKNOWNA Trial for the Evaluation of the Treatment and Outcome of Hyperthyroidism With Iodized Salt and Non Iodized Salt
NCT03612908Not specifiedCOMPLETEDTSHβX1 and D2 THR92ALA in Pregnancy
NCT03823859Not specifiedCOMPLETEDMetabolomics of Thyroid Hormones
NCT03951532Not specifiedCOMPLETEDMorbidity and Mortality Associated With the Care Journey in Children and Adolescents With Hyperthyroidism