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Protein

Serum albumin

Gene

ALB

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

Functioni

Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27CopperBy similarity1
Metal bindingi91Zinc1
Metal bindingi123Zinc1
Sitei223Aspirin-acetylated lysine1
Binding sitei264Bilirubin1
Metal bindingi271Zinc1
Metal bindingi273Zinc1

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB
  • chaperone binding Source: BHF-UCL
  • copper ion binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • drug binding Source: UniProtKB
  • fatty acid binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • pyridoxal phosphate binding Source: UniProtKB
  • toxic substance binding Source: UniProtKB

GO - Biological processi

  • bile acid and bile salt transport Source: Reactome
  • cellular response to starvation Source: UniProtKB
  • hemolysis by symbiont of host erythrocytes Source: UniProtKB
  • lipoprotein metabolic process Source: Reactome
  • maintenance of mitochondrion location Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of programmed cell death Source: UniProtKB
  • platelet degranulation Source: Reactome
  • receptor-mediated endocytosis Source: Reactome
  • retina homeostasis Source: UniProtKB
  • sodium-independent organic anion transport Source: Reactome
  • transport Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Copper, Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163631-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-159418. Recycling of bile acids and salts.
R-HSA-194223. HDL-mediated lipid transport.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-5619058. Defective SLCO1B3 causes hyperbilirubinemia, Rotor type (HBLRR).
R-HSA-5619110. Defective SLCO1B1 causes hyperbilirubinemia, Rotor type (HBLRR).
R-HSA-879518. Transport of organic anions.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum albumin
Gene namesi
Name:ALB
ORF Names:GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:399. ALB.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • endoplasmic reticulum Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: HPA
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • platelet alpha granule lumen Source: Reactome
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hyperthyroxinemia, familial dysalbuminemic (FDAH)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615999
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01301190L → P in FDAH. 1 PublicationCorresponds to variant rs77892378dbSNPEnsembl.1
Natural variantiVAR_000514242R → H in FDAH. 3 PublicationsCorresponds to variant rs75002628dbSNPEnsembl.1
Natural variantiVAR_013013242R → P in FDAH. Corresponds to variant rs75002628dbSNPEnsembl.1
Analbuminemia (ANALBA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:616000

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi213.
MalaCardsiALB.
MIMi615999. phenotype.
616000. phenotype.
OpenTargetsiENSG00000163631.
Orphaneti86816. Congenital analbuminemia.
276271. Familial dysalbuminemic hyperthyroxinemia.
PharmGKBiPA24690.

Protein family/group databases

Allergomei763. Hom s HSA.

Chemistry databases

ChEMBLiCHEMBL3253.
DrugBankiDB05812. Abiraterone.
DB01418. Acenocoumarol.
DB01614. Acepromazine.
DB00945. Acetylsalicylic acid.
DB00459. Acitretin.
DB00802. Alfentanil.
DB00321. Amitriptyline.
DB00415. Ampicillin.
DB00995. Auranofin.
DB01294. Bismuth Subsalicylate.
DB08907. Canagliflozin.
DB01197. Captopril.
DB00456. Cefalotin.
DB01327. Cefazolin.
DB00274. Cefmetazole.
DB01328. Cefonicid.
DB01329. Cefoperazone.
DB00493. Cefotaxime.
DB01330. Cefotetan.
DB00430. Cefpiramide.
DB01212. Ceftriaxone.
DB00482. Celecoxib.
DB00567. Cephalexin.
DB00477. Chlorpromazine.
DB01242. Clomipramine.
DB01068. Clonazepam.
DB01147. Cloxacillin.
DB01189. Desflurane.
DB00829. Diazepam.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB01396. Digitoxin.
DB04855. Dronedarone.
DB00228. Enflurane.
DB08899. Enzalutamide.
DB00530. Erlotinib.
DB00199. Erythromycin.
DB00783. Estradiol.
DB00655. Estrone.
DB04574. Estropipate.
DB00903. Ethacrynic acid.
DB00749. Etodolac.
DB00573. Fenoprofen.
DB00544. Fluorouracil.
DB00472. Fluoxetine.
DB00712. Flurbiprofen.
DB01320. Fosphenytoin.
DB06716. Fospropofol.
DB00695. Furosemide.
DB00743. Gadobenate Dimeglumine.
DB06705. Gadofosveset trisodium.
DB01044. Gatifloxacin.
DB00317. Gefitinib.
DB01120. Gliclazide.
DB01016. Glyburide.
DB01159. Halothane.
DB00070. Hyaluronidase.
DB06205. Hyaluronidase (Human Recombinant).
DB01050. Ibuprofen.
DB00619. Imatinib.
DB00328. Indomethacin.
DB01307. Insulin Detemir.
DB04711. Iodipamide.
DB00762. Irinotecan.
DB00753. Isoflurane.
DB08820. Ivacaftor.
DB01587. Ketazolam.
DB01009. Ketoprofen.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.
DB00678. Losartan.
DB08932. MACITENTAN.
DB01397. Magnesium salicylate.
DB00931. Methacycline.
DB00563. Methotrexate.
DB06710. Methyltestosterone.
DB08893. Mirabegron.
DB00688. Mycophenolate mofetil.
DB01183. Naloxone.
DB00788. Naproxen.
DB00731. Nateglinide.
DB00717. Norethisterone.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB04224. Oleic Acid.
DB00776. Oxcarbazepine.
DB06412. Oxymetholone.
DB00454. Pethidine.
DB00946. Phenprocoumon.
DB00252. Phenytoin.
DB01621. Pipotiazine.
DB00554. Piroxicam.
DB08860. Pitavastatin.
DB06209. Prasugrel.
DB00635. Prednisone.
DB01032. Probenecid.
DB00818. Propofol.
DB00912. Repaglinide.
DB01045. Rifampicin.
DB08931. Riociguat.
DB00412. Rosiglitazone.
DB01098. Rosuvastatin.
DB06201. Rufinamide.
DB00936. Salicylic acid.
DB01232. Saquinavir.
DB01236. Sevoflurane.
DB06290. Simeprevir.
DB00815. Sodium lauryl sulfate.
DB00364. Sucralfate.
DB01581. Sulfamerazine.
DB01582. Sulfamethazine.
DB00576. Sulfamethizole.
DB01015. Sulfamethoxazole.
DB00605. Sulindac.
DB00864. Tacrolimus.
DB05521. Telaprevir.
DB00624. Testosterone.
DB00759. Tetracycline.
DB01622. Thioproperazine.
DB01623. Thiothixene.
DB01056. Tocainide.
DB08895. Tofacitinib.
DB08867. Ulipristal.
DB00177. Valsartan.
DB00512. Vancomycin.
DB05294. Vandetanib.
DB08881. Vemurafenib.
DB08828. Vismodegib.
DB00682. Warfarin.
DB00137. Xanthophyll.
DB00495. Zidovudine.

Polymorphism and mutation databases

BioMutaiALB.
DMDMi113576.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
PropeptideiPRO_000000106719 – 246
ChainiPRO_000000106825 – 609Serum albuminAdd BLAST585

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29Phosphoserine; by FAM20C1 Publication1
Glycosylationi36N-linked (Glc) (glycation)Curated1
Glycosylationi75N-linked (Glc) (glycation); in vitro1
Disulfide bondi77 ↔ 86PROSITE-ProRule annotation1 Publication
Modified residuei82Phosphoserine; by FAM20CCombined sources1 Publication1
Modified residuei89Phosphoserine; by FAM20CCombined sources1 Publication1
Disulfide bondi99 ↔ 115PROSITE-ProRule annotation1 Publication
Modified residuei107Phosphothreonine; by FAM20C1 Publication1
Disulfide bondi114 ↔ 125PROSITE-ProRule annotation1 Publication
Disulfide bondi148 ↔ 193PROSITE-ProRule annotation1 Publication
Glycosylationi161N-linked (Glc) (glycation); in vitro1
Glycosylationi186N-linked (Glc) (glycation); in vitro1
Disulfide bondi192 ↔ 201PROSITE-ProRule annotation1 Publication
Glycosylationi223N-linked (Glc) (glycation); in vitro1
Disulfide bondi224 ↔ 270PROSITE-ProRule annotation1 Publication
Modified residuei229N6-succinyllysineBy similarity1
Glycosylationi249N-linked (Glc) (glycation); in vitro1
Glycosylationi257N-linked (Glc) (glycation)Curated1
Disulfide bondi269 ↔ 277PROSITE-ProRule annotation1 Publication
Disulfide bondi289 ↔ 303PROSITE-ProRule annotation1 Publication
Modified residuei297PhosphoserineBy similarity1
Glycosylationi300N-linked (Glc) (glycation); in vitro1
Disulfide bondi302 ↔ 313PROSITE-ProRule annotation1 Publication
Glycosylationi305N-linked (Glc) (glycation)1
Glycosylationi337N-linked (Glc) (glycation); in vitro1
Disulfide bondi340 ↔ 385PROSITE-ProRule annotation1 Publication
Glycosylationi341N-linked (Glc) (glycation)Curated1
GlycosylationiCAR_000226342N-linked (GlcNAc...); in variant Redhill1
Glycosylationi347N-linked (Glc) (glycation); in vitro1
Glycosylationi375N-linked (Glc) (glycation)Curated1
Disulfide bondi384 ↔ 393PROSITE-ProRule annotation1 Publication
Glycosylationi402N-linked (Glc) (glycation); in vitro1
Disulfide bondi416 ↔ 462PROSITE-ProRule annotation1 Publication
Glycosylationi437N-linked (Glc) (glycation); in vitro1
Modified residuei443PhosphoserineCombined sources1
Modified residuei444PhosphothreonineCombined sources1
Modified residuei446PhosphothreonineCombined sources1
Modified residuei460N6-succinyllysineBy similarity1
Disulfide bondi461 ↔ 472PROSITE-ProRule annotation1 Publication
Glycosylationi463N-linked (Glc) (glycation)1
Glycosylationi468N-linked (Glc) (glycation); in vitro1
Disulfide bondi485 ↔ 501PROSITE-ProRule annotation1 Publication
Disulfide bondi500 ↔ 511PROSITE-ProRule annotation1 Publication
Modified residuei513PhosphoserineCombined sources1
GlycosylationiCAR_000069518N-linked (GlcNAc...); in variant Casebrook1
Disulfide bondi538 ↔ 583PROSITE-ProRule annotation1 Publication
Modified residuei543N6-succinyllysineBy similarity1
Glycosylationi549N-linked (Glc) (glycation)1
Modified residuei558N6-methyllysine; alternateCombined sources1
Glycosylationi558N-linked (Glc) (glycation); alternateCurated1
Glycosylationi560N-linked (Glc) (glycation); in vitro1
Glycosylationi569N-linked (Glc) (glycation); in vitro1
Disulfide bondi582 ↔ 591PROSITE-ProRule annotation1 Publication
Modified residuei588N6-succinyllysineBy similarity1
Glycosylationi597N-linked (Glc) (glycation); in vitro1

Post-translational modificationi

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.1 Publication
Acetylated on Lys-223 by acetylsalicylic acid.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei28Not glycated1
Sitei44Not glycated1
Sitei65Not glycated1
Sitei88Not glycated1
Sitei97Not glycated1
Sitei117Not glycated1
Sitei130Not glycated1
Sitei160Not glycated1
Sitei183Not glycated1
Sitei198Not glycated1
Sitei205Not glycated1
Sitei214Not glycated1
Sitei219Not glycated1
Sitei229Not glycated1
Sitei236Not glycated1
Sitei264Not glycated1
Sitei286Not glycated1
Sitei298Not glycated1
Sitei310Not glycated1
Sitei383Not glycated1
Sitei396Not glycated1
Sitei413Not glycated1
Sitei426Not glycated1
Sitei438Not glycated1
Sitei456Not glycated1
Sitei460Not glycated1
Sitei490Not glycated1
Sitei499Not glycated1
Sitei524Not glycated1
Sitei543Not glycated1
Sitei548Not glycated1
Sitei562Not glycated1
Sitei565Not glycated1
Sitei581Not glycated1
Sitei584Not glycated1
Sitei588Not glycated1
Sitei598Not glycated1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02768.
PeptideAtlasiP02768.
PRIDEiP02768.

2D gel databases

DOSAC-COBS-2DPAGEP02768.
OGPiP02768.
REPRODUCTION-2DPAGEIPI00384697.
IPI00745872.
P02768.
SWISS-2DPAGEP02768.
UCD-2DPAGEP02768.

PTM databases

iPTMnetiP02768.
PhosphoSitePlusiP02768.
SwissPalmiP02768.
UniCarbKBiP02768.

Miscellaneous databases

PMAP-CutDBP02768.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000163631.
ExpressionAtlasiP02768. baseline and differential.
GenevisibleiP02768. HS.

Organism-specific databases

HPAiCAB006262.
HPA031024.
HPA031025.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-714423,EBI-714423
TFRCP027862EBI-714423,EBI-355727

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi106715. 182 interactors.
DIPiDIP-29902N.
IntActiP02768. 170 interactors.
MINTiMINT-3004222.
STRINGi9606.ENSP00000295897.

Chemistry databases

BindingDBiP02768.

Structurei

Secondary structure

1609
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 38Combined sources9
Helixi40 – 54Combined sources15
Beta strandi55 – 58Combined sources4
Helixi60 – 79Combined sources20
Turni84 – 87Combined sources4
Helixi90 – 99Combined sources10
Turni101 – 103Combined sources3
Helixi104 – 108Combined sources5
Helixi109 – 116Combined sources8
Helixi119 – 128Combined sources10
Beta strandi130 – 132Combined sources3
Helixi144 – 153Combined sources10
Helixi155 – 169Combined sources15
Beta strandi171 – 173Combined sources3
Helixi175 – 192Combined sources18
Beta strandi195 – 197Combined sources3
Helixi198 – 230Combined sources33
Helixi232 – 246Combined sources15
Beta strandi248 – 250Combined sources3
Helixi252 – 271Combined sources20
Helixi274 – 289Combined sources16
Helixi290 – 294Combined sources5
Helixi297 – 299Combined sources3
Helixi300 – 303Combined sources4
Helixi307 – 315Combined sources9
Helixi330 – 333Combined sources4
Beta strandi336 – 338Combined sources3
Helixi339 – 345Combined sources7
Helixi347 – 360Combined sources14
Beta strandi363 – 365Combined sources3
Helixi367 – 384Combined sources18
Beta strandi387 – 389Combined sources3
Helixi390 – 394Combined sources5
Helixi397 – 422Combined sources26
Helixi424 – 438Combined sources15
Beta strandi440 – 442Combined sources3
Helixi444 – 461Combined sources18
Beta strandi462 – 464Combined sources3
Helixi466 – 488Combined sources23
Beta strandi489 – 491Combined sources3
Helixi495 – 502Combined sources8
Turni505 – 507Combined sources3
Helixi508 – 513Combined sources6
Beta strandi519 – 521Combined sources3
Helixi529 – 531Combined sources3
Helixi535 – 538Combined sources4
Helixi542 – 559Combined sources18
Beta strandi561 – 563Combined sources3
Helixi565 – 583Combined sources19
Beta strandi584 – 587Combined sources4
Helixi588 – 590Combined sources3
Turni591 – 593Combined sources3
Helixi594 – 606Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AO6X-ray2.50A/B25-609[»]
1BJ5X-ray2.50A25-609[»]
1BKEX-ray3.15A28-608[»]
1BM0X-ray2.50A/B25-609[»]
1E78X-ray2.60A/B25-609[»]
1E7AX-ray2.20A/B25-609[»]
1E7BX-ray2.38A/B25-609[»]
1E7CX-ray2.40A25-609[»]
1E7EX-ray2.50A25-609[»]
1E7FX-ray2.43A25-609[»]
1E7GX-ray2.50A25-609[»]
1E7HX-ray2.43A25-609[»]
1E7IX-ray2.70A25-609[»]
1GNIX-ray2.40A25-609[»]
1GNJX-ray2.60A25-609[»]
1H9ZX-ray2.50A25-609[»]
1HA2X-ray2.50A25-609[»]
1HK1X-ray2.65A25-609[»]
1HK2X-ray2.80A25-609[»]
1HK3X-ray2.80A25-609[»]
1HK4X-ray2.40A25-609[»]
1HK5X-ray2.70A25-609[»]
1N5UX-ray1.90A25-609[»]
1O9XX-ray3.20A25-609[»]
1TF0X-ray2.70A25-596[»]
1UORX-ray2.80A25-609[»]
1YSXNMR-A409-609[»]
2BX8X-ray2.70A/B25-609[»]
2BXAX-ray2.35A/B25-609[»]
2BXBX-ray3.20A/B25-609[»]
2BXCX-ray3.10A/B25-609[»]
2BXDX-ray3.05A/B25-609[»]
2BXEX-ray2.95A/B25-609[»]
2BXFX-ray2.95A/B25-609[»]
2BXGX-ray2.70A/B25-609[»]
2BXHX-ray2.25A/B25-609[»]
2BXIX-ray2.50A25-609[»]
2BXKX-ray2.40A25-609[»]
2BXLX-ray2.60A25-609[»]
2BXMX-ray2.50A25-609[»]
2BXNX-ray2.65A25-609[»]
2BXOX-ray2.60A25-609[»]
2BXPX-ray2.30A25-609[»]
2BXQX-ray2.60A25-609[»]
2ESGX-ray-C25-609[»]
2I2ZX-ray2.70A25-609[»]
2I30X-ray2.90A25-609[»]
2N0XNMR-A432-447[»]
2VDBX-ray2.52A30-608[»]
2VUEX-ray2.42A/B25-609[»]
2VUFX-ray3.05A/B25-609[»]
2XSIX-ray2.70A25-609[»]
2XVQX-ray2.90A/B25-609[»]
2XVUX-ray2.60A/B25-609[»]
2XVVX-ray2.40A25-609[»]
2XVWX-ray2.65A25-609[»]
2XW0X-ray2.40A/B25-609[»]
2XW1X-ray2.50A/B25-609[»]
2YDFX-ray2.75A/B25-609[»]
3A73X-ray2.19A/B25-609[»]
3B9LX-ray2.60A25-609[»]
3B9MX-ray2.70A25-609[»]
3CX9X-ray2.80A27-608[»]
3JQZX-ray3.30A/B25-609[»]
3JRYX-ray2.30A/B25-609[»]
3LU6X-ray2.70A/B25-609[»]
3LU7X-ray2.80A/B25-609[»]
3LU8X-ray2.60A/B25-609[»]
3SQJX-ray2.05A/B27-608[»]
3TDLX-ray2.60A25-609[»]
3UIVX-ray2.20A/H25-609[»]
4BKEX-ray2.35A1-609[»]
4E99X-ray2.30A25-609[»]
4EMXX-ray2.30A/B25-609[»]
4G03X-ray2.22A/B25-609[»]
4G04X-ray2.30A/B25-609[»]
4HGKX-ray3.04A/B25-609[»]
4HGMX-ray2.34B25-609[»]
4IW1X-ray2.56A25-609[»]
4IW2X-ray2.41A25-609[»]
4K2CX-ray3.23A/B25-609[»]
4K71X-ray2.40A/D25-609[»]
4L8UX-ray2.01A25-609[»]
4L9KX-ray2.40A/B25-609[»]
4L9QX-ray2.70A/B25-609[»]
4LA0X-ray2.40A/B25-609[»]
4LB2X-ray2.80A/B25-609[»]
4LB9X-ray2.70A25-609[»]
4N0FX-ray3.02D/G/J/M25-609[»]
4N0UX-ray3.80D27-609[»]
4S1YX-ray3.16A25-609[»]
4Z69X-ray2.19A/I25-609[»]
5FUOX-ray3.60A25-609[»]
5ID7X-ray2.26A/B25-609[»]
5IFOX-ray3.20A25-609[»]
5IJFX-ray2.65A25-609[»]
DisProtiDP00515.
ProteinModelPortaliP02768.
SMRiP02768.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02768.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 210Albumin 1PROSITE-ProRule annotationAdd BLAST192
Domaini211 – 403Albumin 2PROSITE-ProRule annotationAdd BLAST193
Domaini404 – 601Albumin 3PROSITE-ProRule annotationAdd BLAST198

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
Contains 3 albumin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IIRZ. Eukaryota.
ENOG410Z40H. LUCA.
GeneTreeiENSGT00390000000113.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02768.
KOiK16141.
OMAiEPERNEC.
OrthoDBiEOG091G0F5F.
PhylomeDBiP02768.
TreeFamiTF335561.

Family and domain databases

CDDicd00015. ALBUMIN. 3 hits.
InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P02768-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA
60 70 80 90 100
FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT
110 120 130 140 150
VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA
160 170 180 190 200
FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA
210 220 230 240 250
CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA
260 270 280 290 300
EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK
310 320 330 340 350
ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF
360 370 380 390 400
LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE
410 420 430 440 450
FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV
460 470 480 490 500
SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC
510 520 530 540 550
CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ
560 570 580 590 600
TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV

AASQAALGL
Length:609
Mass (Da):69,367
Last modified:April 1, 1990 - v2
Checksum:iF88FF61DD242E818
GO
Isoform 2 (identifier: P02768-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-234: Missing.

Show »
Length:417
Mass (Da):47,360
Checksum:i16E764833EEF4E8D
GO
Isoform 3 (identifier: P02768-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     164-376: Missing.

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):45,160
Checksum:i756519C096463A9B
GO

Sequence cautioni

The sequence AAF22034 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF69644 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG35503 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55L → P in CAH18185 (PubMed:17974005).Curated1
Sequence conflicti122R → S in AAF01333 (Ref. 4) Curated1
Sequence conflicti155E → Q AA sequence (PubMed:1225573).Curated1
Sequence conflicti174Y → L AA sequence (PubMed:3087352).Curated1
Sequence conflicti174Y → L AA sequence (PubMed:2437111).Curated1
Sequence conflicti194Q → E AA sequence (PubMed:1225573).Curated1
Sequence conflicti327 – 332PSLAAD → MFVLLC in AAF71067 (PubMed:11483580).Curated6
Sequence conflicti405V → A in AAF71067 (PubMed:11483580).Curated1
Sequence conflicti409Q → E in AAH14308 (PubMed:15489334).Curated1
Sequence conflicti441Q → E in CAA23753 (PubMed:6275391).Curated1
Sequence conflicti466E → G in AAF01333 (Ref. 4) Curated1
Sequence conflicti488 – 489HE → EH AA sequence (PubMed:1225573).Curated2
Sequence conflicti490K → R in CAH18185 (PubMed:17974005).Curated1
Sequence conflicti525E → Q AA sequence (PubMed:1225573).Curated1
Sequence conflicti551T → A in CAH18185 (PubMed:17974005).Curated1
Sequence conflicti560K → R in CAH18185 (PubMed:17974005).Curated1
Sequence conflicti604Q → R in AAN17825 (Ref. 5) Curated1

Polymorphismi

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.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00049923R → C in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill. 1 PublicationCorresponds to variant rs80008208dbSNPEnsembl.1
Natural variantiVAR_00050023R → H in Fukuoka-2/Lille/Taipei/Varese/Komagome-3. 3 PublicationsCorresponds to variant rs72552709dbSNPEnsembl.1
Natural variantiVAR_00050124R → L in Jaffna. Corresponds to variant rs74821926dbSNPEnsembl.1
Natural variantiVAR_00050224R → P in Takefu/Honolulu-1. 1 PublicationCorresponds to variant rs74821926dbSNPEnsembl.1
Natural variantiVAR_00050324R → Q in Christchurch/Honolulu-2. 3 PublicationsCorresponds to variant rs74821926dbSNPEnsembl.1
Natural variantiVAR_00050425D → V in Bleinheim/Iowa city-2. 1 PublicationCorresponds to variant rs75353611dbSNPEnsembl.1
Natural variantiVAR_00050527H → Q in Nagasaki-3. Corresponds to variant rs76285851dbSNPEnsembl.1
Natural variantiVAR_00050627H → Y in Larino. 2 PublicationsCorresponds to variant rs141733599dbSNPEnsembl.1
Natural variantiVAR_01065773F → Y.1 Publication1
Natural variantiVAR_00050784E → K in Torino. 1 PublicationCorresponds to variant rs77050410dbSNPEnsembl.1
Natural variantiVAR_00050887D → N in Malmo-95/Dalakarlia. 1 PublicationCorresponds to variant rs78574148dbSNPEnsembl.1
Natural variantiVAR_01301190L → P in FDAH. 1 PublicationCorresponds to variant rs77892378dbSNPEnsembl.1
Natural variantiVAR_000509106E → K in Vibo Valentia. 1 PublicationCorresponds to variant rs80296402dbSNPEnsembl.1
Natural variantiVAR_014290121E → G.1 Publication1
Natural variantiVAR_000510138R → G in Yanomama-2. Corresponds to variant rs77238412dbSNPEnsembl.1
Natural variantiVAR_000511143E → K in Nagoya. 1 PublicationCorresponds to variant rs75522063dbSNPEnsembl.1
Natural variantiVAR_013012146V → E in Tregasio. Corresponds to variant rs77752336dbSNPEnsembl.1
Natural variantiVAR_000512152H → R in Komagome-2. 1 PublicationCorresponds to variant rs80095457dbSNPEnsembl.1
Natural variantiVAR_000513201C → F in Hawkes bay. 1 PublicationCorresponds to variant rs77656691dbSNPEnsembl.1
Natural variantiVAR_014291215A → T.Corresponds to variant rs3210154dbSNPEnsembl.1
Natural variantiVAR_014292215A → V.Corresponds to variant rs3204504dbSNPEnsembl.1
Natural variantiVAR_014293220Q → L.Corresponds to variant rs3210163dbSNPEnsembl.1
Natural variantiVAR_000514242R → H in FDAH. 3 PublicationsCorresponds to variant rs75002628dbSNPEnsembl.1
Natural variantiVAR_013013242R → P in FDAH. Corresponds to variant rs75002628dbSNPEnsembl.1
Natural variantiVAR_000515249K → Q in Tradate-2. 1 PublicationCorresponds to variant rs79804069dbSNPEnsembl.1
Natural variantiVAR_000516264K → E in Herborn. 1 PublicationCorresponds to variant rs79377490dbSNPEnsembl.1
Natural variantiVAR_000517292Q → R in Malmo-10. 1 PublicationCorresponds to variant rs80002911dbSNPEnsembl.1
Natural variantiVAR_000518293D → G in Nagasaki-1. 1 PublicationCorresponds to variant rs79744198dbSNPEnsembl.1
Natural variantiVAR_000519300K → N in Caserta. 1 PublicationCorresponds to variant rs74718349dbSNPEnsembl.1
Natural variantiVAR_000520337K → N in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown. 3 PublicationsCorresponds to variant rs72552710dbSNPEnsembl.1
Natural variantiVAR_013014338D → G in Bergamo. Corresponds to variant rs76242087dbSNPEnsembl.1
Natural variantiVAR_013015338D → V in Brest. Corresponds to variant rs76242087dbSNPEnsembl.1
Natural variantiVAR_000521342N → K in Malmo-47. 1 PublicationCorresponds to variant rs77544362dbSNPEnsembl.1
Natural variantiVAR_000522344A → T in Redhill; associated with C-23. Corresponds to variant rs78953271dbSNPEnsembl.1
Natural variantiVAR_000523345E → K in Roma. Corresponds to variant rs72552711dbSNPEnsembl.1
Natural variantiVAR_000524357E → K in Sondrio. 1 PublicationCorresponds to variant rs77354753dbSNPEnsembl.1
Natural variantiVAR_000525378E → K in Hiroshima-1. 2 PublicationsCorresponds to variant rs76593094dbSNPEnsembl.1
Natural variantiVAR_000526382E → K in Coari I/Porto Alegre. Corresponds to variant rs75791663dbSNPEnsembl.1
Natural variantiVAR_013016383K → N in Trieste. Corresponds to variant rs75069738dbSNPEnsembl.1
Natural variantiVAR_000527389D → H in Parklands. Corresponds to variant rs77187142dbSNPEnsembl.1
Natural variantiVAR_000528389D → V in Iowa city-1. 1 PublicationCorresponds to variant rs78538497dbSNPEnsembl.1
Natural variantiVAR_000529396K → E in Naskapi/Mersin/Komagome-1. 3 PublicationsCorresponds to variant rs78166690dbSNPEnsembl.1
Natural variantiVAR_000530399D → N in Nagasaki-2. 1 PublicationCorresponds to variant rs77514449dbSNPEnsembl.1
Natural variantiVAR_000531400E → K in Tochigi. 1 PublicationCorresponds to variant rs79047363dbSNPEnsembl.1
Natural variantiVAR_000532400E → Q in Malmo-5. 1 PublicationCorresponds to variant rs79047363dbSNPEnsembl.1
Natural variantiVAR_000533406E → K in Hiroshima-2. 1 PublicationCorresponds to variant rs76483862dbSNPEnsembl.1
Natural variantiVAR_014294420E → K.1 Publication1
Natural variantiVAR_013017434R → C in Liprizzi. Corresponds to variant rs78575701dbSNPEnsembl.1
Natural variantiVAR_014295490K → E.Corresponds to variant rs1063469dbSNPEnsembl.1
Natural variantiVAR_000534503E → K in Dublin. Corresponds to variant rs80259813dbSNPEnsembl.1
Natural variantiVAR_000535518D → N in Casebrook. 1 PublicationCorresponds to variant rs75920790dbSNPEnsembl.1
Natural variantiVAR_000536525E → K in Manaus-1/Adana/Lambadi/Vancouver. 1 PublicationCorresponds to variant rs75523493dbSNPEnsembl.1
Natural variantiVAR_000537529E → K in Ortonovo. 1 PublicationCorresponds to variant rs74826639dbSNPEnsembl.1
Natural variantiVAR_013018557V → M in Maddaloni. Corresponds to variant rs78284052dbSNPEnsembl.1
Natural variantiVAR_000538560K → E in Castel di Sangro. Corresponds to variant rs77645174dbSNPEnsembl.1
Natural variantiVAR_000539565K → E in Maku. 1 PublicationCorresponds to variant rs80345158dbSNPEnsembl.1
Natural variantiVAR_000541574D → A in Malmo-61. 1 PublicationCorresponds to variant rs79738788dbSNPEnsembl.1
Natural variantiVAR_000540574D → G in Mexico. 1 PublicationCorresponds to variant rs79738788dbSNPEnsembl.1
Natural variantiVAR_013019584K → E in Church bay. Corresponds to variant rs76671808dbSNPEnsembl.1
Natural variantiVAR_000542587D → N in Fukuoka-1/Paris-2. 2 PublicationsCorresponds to variant rs76587671dbSNPEnsembl.1
Natural variantiVAR_000543589E → K in Osaka-1. 1 PublicationCorresponds to variant rs75709682dbSNPEnsembl.1
Natural variantiVAR_000544594E → K in Osaka-2/Phnom Phen/albumin B/Verona. 3 PublicationsCorresponds to variant rs79228041dbSNPEnsembl.1
Natural variantiVAR_000547596 – 609GKKLV…AALGL → PTMRIRERK in Venezia. Add BLAST14
Natural variantiVAR_000545597K → E in Gent/Milano Fast. Corresponds to variant rs80106970dbSNPEnsembl.1
Natural variantiVAR_000546598K → N in Vanves. Corresponds to variant rs75738598dbSNPEnsembl.1
Natural variantiVAR_012981599 – 609LVAASQAALGL → TCCCKSSCLRLITSHLKASQ PTMRIRERK in Kenitra. Add BLAST11

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02127543 – 234Missing in isoform 2. 2 PublicationsAdd BLAST192
Alternative sequenceiVSP_057389164 – 376Missing in isoform 3. 1 PublicationAdd BLAST213

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00494 mRNA. Translation: CAA23753.1.
V00495 mRNA. Translation: CAA23754.1.
M12523 Genomic DNA. Translation: AAA98797.1.
M12523 Genomic DNA. Translation: AAA98798.1.
AF190168 mRNA. Translation: AAF01333.1.
AF542069 mRNA. Translation: AAN17825.1.
A06977 mRNA. Translation: CAA00606.1.
AY728024 mRNA. Translation: AAU21642.1.
DQ986150 mRNA. Translation: ABJ16448.1.
AY544124 mRNA. Translation: AAT11155.1.
AY550967 mRNA. Translation: AAT52213.1.
AF116645 mRNA. Translation: AAF71067.1.
AF118090 mRNA. Translation: AAF22034.1. Different initiation.
AF119840 mRNA. Translation: AAF69594.1.
AF119890 mRNA. Translation: AAF69644.1. Different initiation.
AF130077 mRNA. Translation: AAG35503.1. Different initiation.
CR749331 mRNA. Translation: CAH18185.1.
EF649953 Genomic DNA. Translation: ABS29264.1.
AC108157 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05676.1.
BC014308 mRNA. Translation: AAH14308.1.
BC034023 mRNA. Translation: AAH34023.1.
BC035969 mRNA. Translation: AAH35969.1.
BC036003 mRNA. Translation: AAH36003.1.
BC041789 mRNA. Translation: AAH41789.1.
U22961 mRNA. Translation: AAA64922.1.
AY358313 mRNA. Translation: AAQ89947.1.
AH002596 Genomic DNA. Translation: AAA51688.1.
CCDSiCCDS3555.1. [P02768-1]
PIRiA93743. ABHUS.
RefSeqiNP_000468.1. NM_000477.6. [P02768-1]
UniGeneiHs.418167.
Hs.592379.

Genome annotation databases

EnsembliENST00000295897; ENSP00000295897; ENSG00000163631. [P02768-1]
ENST00000621085; ENSP00000483421; ENSG00000163631. [P02768-3]
GeneIDi213.
KEGGihsa:213.
UCSCiuc003hgs.5. human. [P02768-1]
uc062xfr.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Albumin Website
Wikipedia

Serum albumin entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00494 mRNA. Translation: CAA23753.1.
V00495 mRNA. Translation: CAA23754.1.
M12523 Genomic DNA. Translation: AAA98797.1.
M12523 Genomic DNA. Translation: AAA98798.1.
AF190168 mRNA. Translation: AAF01333.1.
AF542069 mRNA. Translation: AAN17825.1.
A06977 mRNA. Translation: CAA00606.1.
AY728024 mRNA. Translation: AAU21642.1.
DQ986150 mRNA. Translation: ABJ16448.1.
AY544124 mRNA. Translation: AAT11155.1.
AY550967 mRNA. Translation: AAT52213.1.
AF116645 mRNA. Translation: AAF71067.1.
AF118090 mRNA. Translation: AAF22034.1. Different initiation.
AF119840 mRNA. Translation: AAF69594.1.
AF119890 mRNA. Translation: AAF69644.1. Different initiation.
AF130077 mRNA. Translation: AAG35503.1. Different initiation.
CR749331 mRNA. Translation: CAH18185.1.
EF649953 Genomic DNA. Translation: ABS29264.1.
AC108157 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05676.1.
BC014308 mRNA. Translation: AAH14308.1.
BC034023 mRNA. Translation: AAH34023.1.
BC035969 mRNA. Translation: AAH35969.1.
BC036003 mRNA. Translation: AAH36003.1.
BC041789 mRNA. Translation: AAH41789.1.
U22961 mRNA. Translation: AAA64922.1.
AY358313 mRNA. Translation: AAQ89947.1.
AH002596 Genomic DNA. Translation: AAA51688.1.
CCDSiCCDS3555.1. [P02768-1]
PIRiA93743. ABHUS.
RefSeqiNP_000468.1. NM_000477.6. [P02768-1]
UniGeneiHs.418167.
Hs.592379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AO6X-ray2.50A/B25-609[»]
1BJ5X-ray2.50A25-609[»]
1BKEX-ray3.15A28-608[»]
1BM0X-ray2.50A/B25-609[»]
1E78X-ray2.60A/B25-609[»]
1E7AX-ray2.20A/B25-609[»]
1E7BX-ray2.38A/B25-609[»]
1E7CX-ray2.40A25-609[»]
1E7EX-ray2.50A25-609[»]
1E7FX-ray2.43A25-609[»]
1E7GX-ray2.50A25-609[»]
1E7HX-ray2.43A25-609[»]
1E7IX-ray2.70A25-609[»]
1GNIX-ray2.40A25-609[»]
1GNJX-ray2.60A25-609[»]
1H9ZX-ray2.50A25-609[»]
1HA2X-ray2.50A25-609[»]
1HK1X-ray2.65A25-609[»]
1HK2X-ray2.80A25-609[»]
1HK3X-ray2.80A25-609[»]
1HK4X-ray2.40A25-609[»]
1HK5X-ray2.70A25-609[»]
1N5UX-ray1.90A25-609[»]
1O9XX-ray3.20A25-609[»]
1TF0X-ray2.70A25-596[»]
1UORX-ray2.80A25-609[»]
1YSXNMR-A409-609[»]
2BX8X-ray2.70A/B25-609[»]
2BXAX-ray2.35A/B25-609[»]
2BXBX-ray3.20A/B25-609[»]
2BXCX-ray3.10A/B25-609[»]
2BXDX-ray3.05A/B25-609[»]
2BXEX-ray2.95A/B25-609[»]
2BXFX-ray2.95A/B25-609[»]
2BXGX-ray2.70A/B25-609[»]
2BXHX-ray2.25A/B25-609[»]
2BXIX-ray2.50A25-609[»]
2BXKX-ray2.40A25-609[»]
2BXLX-ray2.60A25-609[»]
2BXMX-ray2.50A25-609[»]
2BXNX-ray2.65A25-609[»]
2BXOX-ray2.60A25-609[»]
2BXPX-ray2.30A25-609[»]
2BXQX-ray2.60A25-609[»]
2ESGX-ray-C25-609[»]
2I2ZX-ray2.70A25-609[»]
2I30X-ray2.90A25-609[»]
2N0XNMR-A432-447[»]
2VDBX-ray2.52A30-608[»]
2VUEX-ray2.42A/B25-609[»]
2VUFX-ray3.05A/B25-609[»]
2XSIX-ray2.70A25-609[»]
2XVQX-ray2.90A/B25-609[»]
2XVUX-ray2.60A/B25-609[»]
2XVVX-ray2.40A25-609[»]
2XVWX-ray2.65A25-609[»]
2XW0X-ray2.40A/B25-609[»]
2XW1X-ray2.50A/B25-609[»]
2YDFX-ray2.75A/B25-609[»]
3A73X-ray2.19A/B25-609[»]
3B9LX-ray2.60A25-609[»]
3B9MX-ray2.70A25-609[»]
3CX9X-ray2.80A27-608[»]
3JQZX-ray3.30A/B25-609[»]
3JRYX-ray2.30A/B25-609[»]
3LU6X-ray2.70A/B25-609[»]
3LU7X-ray2.80A/B25-609[»]
3LU8X-ray2.60A/B25-609[»]
3SQJX-ray2.05A/B27-608[»]
3TDLX-ray2.60A25-609[»]
3UIVX-ray2.20A/H25-609[»]
4BKEX-ray2.35A1-609[»]
4E99X-ray2.30A25-609[»]
4EMXX-ray2.30A/B25-609[»]
4G03X-ray2.22A/B25-609[»]
4G04X-ray2.30A/B25-609[»]
4HGKX-ray3.04A/B25-609[»]
4HGMX-ray2.34B25-609[»]
4IW1X-ray2.56A25-609[»]
4IW2X-ray2.41A25-609[»]
4K2CX-ray3.23A/B25-609[»]
4K71X-ray2.40A/D25-609[»]
4L8UX-ray2.01A25-609[»]
4L9KX-ray2.40A/B25-609[»]
4L9QX-ray2.70A/B25-609[»]
4LA0X-ray2.40A/B25-609[»]
4LB2X-ray2.80A/B25-609[»]
4LB9X-ray2.70A25-609[»]
4N0FX-ray3.02D/G/J/M25-609[»]
4N0UX-ray3.80D27-609[»]
4S1YX-ray3.16A25-609[»]
4Z69X-ray2.19A/I25-609[»]
5FUOX-ray3.60A25-609[»]
5ID7X-ray2.26A/B25-609[»]
5IFOX-ray3.20A25-609[»]
5IJFX-ray2.65A25-609[»]
DisProtiDP00515.
ProteinModelPortaliP02768.
SMRiP02768.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106715. 182 interactors.
DIPiDIP-29902N.
IntActiP02768. 170 interactors.
MINTiMINT-3004222.
STRINGi9606.ENSP00000295897.

Chemistry databases

BindingDBiP02768.
ChEMBLiCHEMBL3253.
DrugBankiDB05812. Abiraterone.
DB01418. Acenocoumarol.
DB01614. Acepromazine.
DB00945. Acetylsalicylic acid.
DB00459. Acitretin.
DB00802. Alfentanil.
DB00321. Amitriptyline.
DB00415. Ampicillin.
DB00995. Auranofin.
DB01294. Bismuth Subsalicylate.
DB08907. Canagliflozin.
DB01197. Captopril.
DB00456. Cefalotin.
DB01327. Cefazolin.
DB00274. Cefmetazole.
DB01328. Cefonicid.
DB01329. Cefoperazone.
DB00493. Cefotaxime.
DB01330. Cefotetan.
DB00430. Cefpiramide.
DB01212. Ceftriaxone.
DB00482. Celecoxib.
DB00567. Cephalexin.
DB00477. Chlorpromazine.
DB01242. Clomipramine.
DB01068. Clonazepam.
DB01147. Cloxacillin.
DB01189. Desflurane.
DB00829. Diazepam.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB01396. Digitoxin.
DB04855. Dronedarone.
DB00228. Enflurane.
DB08899. Enzalutamide.
DB00530. Erlotinib.
DB00199. Erythromycin.
DB00783. Estradiol.
DB00655. Estrone.
DB04574. Estropipate.
DB00903. Ethacrynic acid.
DB00749. Etodolac.
DB00573. Fenoprofen.
DB00544. Fluorouracil.
DB00472. Fluoxetine.
DB00712. Flurbiprofen.
DB01320. Fosphenytoin.
DB06716. Fospropofol.
DB00695. Furosemide.
DB00743. Gadobenate Dimeglumine.
DB06705. Gadofosveset trisodium.
DB01044. Gatifloxacin.
DB00317. Gefitinib.
DB01120. Gliclazide.
DB01016. Glyburide.
DB01159. Halothane.
DB00070. Hyaluronidase.
DB06205. Hyaluronidase (Human Recombinant).
DB01050. Ibuprofen.
DB00619. Imatinib.
DB00328. Indomethacin.
DB01307. Insulin Detemir.
DB04711. Iodipamide.
DB00762. Irinotecan.
DB00753. Isoflurane.
DB08820. Ivacaftor.
DB01587. Ketazolam.
DB01009. Ketoprofen.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.
DB00678. Losartan.
DB08932. MACITENTAN.
DB01397. Magnesium salicylate.
DB00931. Methacycline.
DB00563. Methotrexate.
DB06710. Methyltestosterone.
DB08893. Mirabegron.
DB00688. Mycophenolate mofetil.
DB01183. Naloxone.
DB00788. Naproxen.
DB00731. Nateglinide.
DB00717. Norethisterone.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB04224. Oleic Acid.
DB00776. Oxcarbazepine.
DB06412. Oxymetholone.
DB00454. Pethidine.
DB00946. Phenprocoumon.
DB00252. Phenytoin.
DB01621. Pipotiazine.
DB00554. Piroxicam.
DB08860. Pitavastatin.
DB06209. Prasugrel.
DB00635. Prednisone.
DB01032. Probenecid.
DB00818. Propofol.
DB00912. Repaglinide.
DB01045. Rifampicin.
DB08931. Riociguat.
DB00412. Rosiglitazone.
DB01098. Rosuvastatin.
DB06201. Rufinamide.
DB00936. Salicylic acid.
DB01232. Saquinavir.
DB01236. Sevoflurane.
DB06290. Simeprevir.
DB00815. Sodium lauryl sulfate.
DB00364. Sucralfate.
DB01581. Sulfamerazine.
DB01582. Sulfamethazine.
DB00576. Sulfamethizole.
DB01015. Sulfamethoxazole.
DB00605. Sulindac.
DB00864. Tacrolimus.
DB05521. Telaprevir.
DB00624. Testosterone.
DB00759. Tetracycline.
DB01622. Thioproperazine.
DB01623. Thiothixene.
DB01056. Tocainide.
DB08895. Tofacitinib.
DB08867. Ulipristal.
DB00177. Valsartan.
DB00512. Vancomycin.
DB05294. Vandetanib.
DB08881. Vemurafenib.
DB08828. Vismodegib.
DB00682. Warfarin.
DB00137. Xanthophyll.
DB00495. Zidovudine.

Protein family/group databases

Allergomei763. Hom s HSA.

PTM databases

iPTMnetiP02768.
PhosphoSitePlusiP02768.
SwissPalmiP02768.
UniCarbKBiP02768.

Polymorphism and mutation databases

BioMutaiALB.
DMDMi113576.

2D gel databases

DOSAC-COBS-2DPAGEP02768.
OGPiP02768.
REPRODUCTION-2DPAGEIPI00384697.
IPI00745872.
P02768.
SWISS-2DPAGEP02768.
UCD-2DPAGEP02768.

Proteomic databases

PaxDbiP02768.
PeptideAtlasiP02768.
PRIDEiP02768.

Protocols and materials databases

DNASUi213.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295897; ENSP00000295897; ENSG00000163631. [P02768-1]
ENST00000621085; ENSP00000483421; ENSG00000163631. [P02768-3]
GeneIDi213.
KEGGihsa:213.
UCSCiuc003hgs.5. human. [P02768-1]
uc062xfr.1. human.

Organism-specific databases

CTDi213.
DisGeNETi213.
GeneCardsiALB.
HGNCiHGNC:399. ALB.
HPAiCAB006262.
HPA031024.
HPA031025.
MalaCardsiALB.
MIMi103600. gene.
615999. phenotype.
616000. phenotype.
neXtProtiNX_P02768.
OpenTargetsiENSG00000163631.
Orphaneti86816. Congenital analbuminemia.
276271. Familial dysalbuminemic hyperthyroxinemia.
PharmGKBiPA24690.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIRZ. Eukaryota.
ENOG410Z40H. LUCA.
GeneTreeiENSGT00390000000113.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02768.
KOiK16141.
OMAiEPERNEC.
OrthoDBiEOG091G0F5F.
PhylomeDBiP02768.
TreeFamiTF335561.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163631-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-159418. Recycling of bile acids and salts.
R-HSA-194223. HDL-mediated lipid transport.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-5619058. Defective SLCO1B3 causes hyperbilirubinemia, Rotor type (HBLRR).
R-HSA-5619110. Defective SLCO1B1 causes hyperbilirubinemia, Rotor type (HBLRR).
R-HSA-879518. Transport of organic anions.

Miscellaneous databases

ChiTaRSiALB. human.
EvolutionaryTraceiP02768.
GeneWikiiSerum_albumin.
GenomeRNAii213.
PMAP-CutDBP02768.
PROiP02768.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163631.
ExpressionAtlasiP02768. baseline and differential.
GenevisibleiP02768. HS.

Family and domain databases

CDDicd00015. ALBUMIN. 3 hits.
InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALBU_HUMAN
AccessioniPrimary (citable) accession number: P02768
Secondary accession number(s): E7ESS9
, O95574, P04277, Q13140, Q645G4, Q68DN5, Q6UXK4, Q86YG0, Q8IUK7, Q9P157, Q9P1I7, Q9UHS3, Q9UJZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 235 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

Caution

A peptide arising from positions 166 to 174 was originally (PubMed:3087352 and PubMed:2437111) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulate fat digestion, lipid absorption, and blood flow.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

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 one 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.