Human serum albumin

blood albumin
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AO6, 1BJ5, 1BKE, 1BM0, 1E78, 1E7A, 1E7B, 1E7C, 1E7E, 1E7F, 1E7G, 1E7H, 1E7I, 1GNI, 1GNJ, 1H9Z, 1HA2, 1HK1, 1HK2, 1HK3, 1HK4, 1HK5, 1N5U, 1O9X, 1TF0, 1UOR, 1YSX, 2BX8, 2BXA, 2BXB, 2BXC, 2BXD, 2BXF, 2BXG, 2BXH, 2BXI, 2BXK, 2BXL, 2BXM, 2BXN, 2BXO, 2BXP, 2BXQ, 2I2Z, 2I30, 2VDB, 2VUE, 2VUF, 2XSI, 2XVQ, 2XVU, 2XVV, 2XVW, 2XW0, 2XW1, 2YDF, 3A73, 3B9L, 3B9M, 3CX9, 3JQZ, 3JRY, 3LU6, 3LU7, 3LU8, 3SQJ, 3TDL, 3UIV, 4E99, 4EMX, 4G03, 4G04, 4HGK, 4HGM, 4IW1, 4IW2, 4K2C, 4L8U, 4L9K, 4L9Q, 4LA0, 4LB9, 4LB2, 2N0X, 2ESG, 4S1Y, 4N0F, 4Z69, 4N0U, 4K71, 2BXE, 4BKE, 5IJF, 5ID7, 5IFO, 5FUO
Identifiers
Aliases	ALB, ANALBA, FDAH, PRO0883, PRO0903, PRO1341, albumin, HSA, FDAHT, serum albumin
External IDs	OMIM: 103600; MGI: 87991; HomoloGene: 405; GeneCards: ALB; OMA:ALB - orthologs
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q13.3 Start 73,397,114 bp[1] End 73,421,482 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 E1|5 44.7 cM Start 90,608,756 bp[2] End 90,624,461 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in liver right lobe of liver body of pancreas kidney tubule islet of Langerhans human kidney epithelium of colon glomerulus metanephric glomerulus testicle Top expressed in gallbladder left lobe of liver fetal liver hematopoietic progenitor cell human fetus atrioventricular valve abdominal wall sexually immature organism upper lip white adipose tissue muscle of thorax More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding oxygen binding chaperone binding metal ion binding antioxidant activity protein binding identical protein binding pyridoxal phosphate binding copper ion binding lipid binding toxic substance binding fatty acid binding exogenous protein binding Cellular component cytoplasm Golgi apparatus blood microparticle myelin sheath extracellular region endoplasmic reticulum extracellular exosome platelet alpha granule lumen nucleus extracellular space endoplasmic reticulum lumen protein-containing complex Biological process sodium-independent organic anion transport hemolysis by symbiont of host erythrocytes cellular response to starvation platelet degranulation negative regulation of apoptotic process receptor-mediated endocytosis maintenance of mitochondrion location retina homeostasis bile acid and bile salt transport negative regulation of programmed cell death cellular oxidant detoxification high-density lipoprotein particle remodeling post-translational protein modification transport negative regulation of protein oligomerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 213 11657 Ensembl ENSG00000163631 ENSMUSG00000029368 UniProt P02768 P07724 RefSeq (mRNA) NM_000477 NM_009654 RefSeq (protein) NP_000468 NP_033784 Location (UCSC) Chr 4: 73.4 – 73.42 Mb Chr 5: 90.61 – 90.62 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma; it constitutes about half of serum protein. It is produced in the liver. It is soluble in water, and it is monomeric.^{[citation needed]}

Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains oncotic pressure, among other functions.

Albumin is synthesized in the liver as preproalbumin, which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi apparatus to produce the secreted albumin.

The reference range for albumin concentrations in serum is approximately 35–50 g/L (3.5–5.0 g/dL).^[5] It has a serum half-life of approximately 21 days.^[6] It has a molecular mass of 66.5 kDa.

The gene for albumin is located on chromosome 4 in locus 4q13.3 and mutations in this gene can result in anomalous proteins. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly(A) addition site. It is split into 15 exons that are symmetrically placed within the 3 domains thought to have arisen by triplication of a single primordial domain.

Human serum albumin (HSA) is a highly water-soluble globular monomeric plasma protein with a relative molecular weight of 67 KDa, consisting of 585 amino acid residues, one sulfhydryl group and 17 disulfide bridges. Among nanoparticulate carriers, HSA nanoparticles have long been the center of attention in the pharmaceutical industry due to their ability to bind to various drug molecules, great stability during storage and in vivo usage, no toxicity and antigenicity, biodegradability, reproducibility, scale up of the production process and a better control over release properties. In addition, significant amounts of drug can be incorporated into the particle matrix because of the large number of drug binding sites on the albumin molecule.^[7]