Reviewed, UniProtKB/Swiss-Prot P02768 (ALBU_HUMAN)

Names and origin

Protein names

Recommended name:
    Serum albumin

Gene names

Name:	ALB
ORF Names:	GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood.
Subcellular location	Secreted.
Tissue specificity	Plasma.
Post-translational modification	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.
Polymorphism	The sequence shown is that of variant albumin A.
Involvement in disease	Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population. A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood [MIM:194470].
Miscellaneous	Acetylated on Lys-223 by acetylsalicylic acid.
Sequence similarities	Belongs to the ALB/AFP/VDB family. Contains 3 albumin domains.
Caution	A peptide arising from positions 166 to 174 was originally (Ref.23 and Ref.24) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulates fat digestion, lipid absorption, and blood flow.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
Ligand	Copper Lipid-binding Metal-binding
PTM	Cleavage on pair of basic residues Glycation Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to starvation Inferred from direct assay. Source: UniProtKB hemolysis by symbiont of host red blood cells Inferred from direct assay. Source: UniProtKB maintenance of mitochondrion location Inferred from direct assay. Source: UniProtKB negative regulation of apoptosis Inferred from direct assay. Source: UniProtKB negative regulation of non-apoptotic programmed cell death Non-traceable author statement. Source: UniProtKB transport Traceable author statement. Source: UniProtKB
Cellular component	extracellular region Non-traceable author statement. Source: UniProtKB platelet alpha granule lumen Inferred from Experiment. Source: Reactome protein complex Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from direct assay. Source: UniProtKB antioxidant activity Non-traceable author statement. Source: UniProtKB copper ion binding Non-traceable author statement. Source: UniProtKB drug binding Ref.40 Inferred from direct assay. Source: UniProtKB fatty acid binding Ref.38 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB pyridoxal phosphate binding Inferred from direct assay. Source: UniProtKB toxin binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P02768-1)

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.

Isoform 2 (identifier: P02768-2)

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

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 18	18
	Propeptide	19 – 24	6
	Chain	25 – 609	585	Serum albumin
Regions
	Domain	25 – 205	181	Albumin 1
	Domain	212 – 397	186	Albumin 2
	Domain	404 – 595	192	Albumin 3
Sites
	Metal binding	27	1	Copper By similarity
	Binding site	264	1	Bilirubin Potential
	Site	28	1	Not glycated
	Site	44	1	Not glycated
	Site	65	1	Not glycated
	Site	88	1	Not glycated
	Site	97	1	Not glycated
	Site	117	1	Not glycated
	Site	130	1	Not glycated
	Site	160	1	Not glycated
	Site	183	1	Not glycated
	Site	198	1	Not glycated
	Site	205	1	Not glycated
	Site	214	1	Not glycated
	Site	219	1	Not glycated
	Site	223	1	Aspirin-acetylated lysine
	Site	229	1	Not glycated
	Site	236	1	Not glycated
	Site	264	1	Not glycated
	Site	286	1	Not glycated
	Site	298	1	Not glycated
	Site	310	1	Not glycated
	Site	383	1	Not glycated
	Site	396	1	Not glycated
	Site	413	1	Not glycated
	Site	426	1	Not glycated
	Site	438	1	Not glycated
	Site	456	1	Not glycated
	Site	460	1	Not glycated
	Site	490	1	Not glycated
	Site	499	1	Not glycated
	Site	524	1	Not glycated
	Site	543	1	Not glycated
	Site	548	1	Not glycated
	Site	562	1	Not glycated
	Site	565	1	Not glycated
	Site	581	1	Not glycated
	Site	584	1	Not glycated
	Site	588	1	Not glycated
	Site	598	1	Not glycated
Amino acid modifications
	Modified residue	82	1	Phosphoserine
	Modified residue	108	1	Phosphotyrosine
	Modified residue	164	1	Phosphotyrosine
	Glycosylation	36	1	N-linked (Glc) (glycation) Probable
	Glycosylation	75	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	161	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	186	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	223	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	249	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	257	1	N-linked (Glc) (glycation) Probable
	Glycosylation	300	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	305	1	N-linked (Glc) (glycation)
	Glycosylation	337	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	341	1	N-linked (Glc) (glycation) Probable
	Glycosylation	342	1	N-linked (GlcNAc...); in variant Redhill
	Glycosylation	347	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	375	1	N-linked (Glc) (glycation) Probable
	Glycosylation	402	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	437	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	463	1	N-linked (Glc) (glycation)
	Glycosylation	468	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	518	1	N-linked (GlcNAc...); in variant Casebrook
	Glycosylation	549	1	N-linked (Glc) (glycation)
	Glycosylation	558	1	N-linked (Glc) (glycation) Probable
	Glycosylation	560	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	569	1	N-linked (Glc) (glycation); in vitro
	Glycosylation	597	1	N-linked (Glc) (glycation); in vitro
	Disulfide bond	77 ↔ 86
	Disulfide bond	99 ↔ 115
	Disulfide bond	114 ↔ 125
	Disulfide bond	148 ↔ 193
	Disulfide bond	192 ↔ 201
	Disulfide bond	224 ↔ 270
	Disulfide bond	269 ↔ 277
	Disulfide bond	289 ↔ 303
	Disulfide bond	302 ↔ 313
	Disulfide bond	340 ↔ 385
	Disulfide bond	384 ↔ 393
	Disulfide bond	416 ↔ 462
	Disulfide bond	461 ↔ 472
	Disulfide bond	485 ↔ 501
	Disulfide bond	500 ↔ 511
	Disulfide bond	538 ↔ 583
	Disulfide bond	582 ↔ 591
Natural variations
	Alternative sequence	43 – 234	192	Missing in isoform 2.
	Natural variant	23	1	R → C in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill.
	Natural variant	23	1	R → H in Fukuoka-2/Lille/Taipei/Varese/Komagome-3.
	Natural variant	24	1	R → L in Jaffna.
	Natural variant	24	1	R → P in Takefu/Honolulu-1.
	Natural variant	24	1	R → Q in Christchurch/Honolulu-2.
	Natural variant	25	1	D → V in Bleinheim/Iowa city-2.
	Natural variant	27	1	H → Q in Nagasaki-3.
	Natural variant	27	1	H → Y in Larino.
	Natural variant	73	1	F → Y
	Natural variant