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Reviewed, UniProtKB/Swiss-Prot P02768 (ALBU_HUMAN)

Last modified November 25, 2008. Version 139. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Serum albumin
Gene names
Name: ALB
ORF Names: GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords

   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   LigandCopper
Lipid-binding
Metal-binding
   PTMCleavage on pair of basic residues
Glycation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processcellular 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 componentextracellular space

Inferred from electronic annotation. Source: InterPro

platelet alpha granule lumen

Inferred from Experiment. Source: Reactome

protein complex

Inferred from direct assay. Source: UniProtKB

   Molecular functionDNA 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...

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 246
PRO_0000001067
Chain25 – 609585Serum albumin
PRO_0000001068

Regions

Domain25 – 205181Albumin 1
Domain212 – 397186Albumin 2
Domain404 – 595192Albumin 3

Sites

Metal binding271Copper By similarity
Binding site2641Bilirubin Potential
Site281Not glycated
Site441Not glycated
Site651Not glycated
Site881Not glycated
Site971Not glycated
Site1171Not glycated
Site1301Not glycated
Site1601Not glycated
Site1831Not glycated
Site1981Not glycated
Site2051Not glycated
Site2141Not glycated
Site2191Not glycated
Site2231Aspirin-acetylated lysine
Site2291Not glycated
Site2361Not glycated
Site2641Not glycated
Site2861Not glycated
Site2981Not glycated
Site3101Not glycated
Site3831Not glycated
Site3961Not glycated
Site4131Not glycated
Site4261Not glycated
Site4381Not glycated
Site4561Not glycated
Site4601Not glycated
Site4901Not glycated
Site4991Not glycated
Site5241Not glycated
Site5431Not glycated
Site5481Not glycated
Site5621Not glycated
Site5651Not glycated
Site5811Not glycated
Site5841Not glycated
Site5881Not glycated
Site5981Not glycated

Amino acid modifications

Modified residue821Phosphoserine
Modified residue1081Phosphotyrosine
Modified residue1641Phosphotyrosine
Glycosylation361N-linked (Glc) (glycation) Probable
Glycosylation751N-linked (Glc) (glycation); in vitro
Glycosylation1611N-linked (Glc) (glycation); in vitro
Glycosylation1861N-linked (Glc) (glycation); in vitro
Glycosylation2231N-linked (Glc) (glycation); in vitro
Glycosylation2491N-linked (Glc) (glycation); in vitro
Glycosylation2571N-linked (Glc) (glycation) Probable
Glycosylation3001N-linked (Glc) (glycation); in vitro
Glycosylation3051N-linked (Glc) (glycation)
Glycosylation3371N-linked (Glc) (glycation); in vitro
Glycosylation3411N-linked (Glc) (glycation) Probable
Glycosylation3421N-linked (GlcNAc...); in variant Redhill
CAR_000226
Glycosylation3471N-linked (Glc) (glycation); in vitro
Glycosylation3751N-linked (Glc) (glycation) Probable
Glycosylation4021N-linked (Glc) (glycation); in vitro
Glycosylation4371N-linked (Glc) (glycation); in vitro
Glycosylation4631N-linked (Glc) (glycation)
Glycosylation4681N-linked (Glc) (glycation); in vitro
Glycosylation5181N-linked (GlcNAc...); in variant Casebrook
CAR_000069
Glycosylation5491N-linked (Glc) (glycation)
Glycosylation5581N-linked (Glc) (glycation) Probable
Glycosylation5601N-linked (Glc) (glycation); in vitro
Glycosylation5691N-linked (Glc) (glycation); in vitro
Glycosylation5971N-linked (Glc) (glycation); in vitro
Disulfide bond77 ↔ 86
Disulfide bond99 ↔ 115
Disulfide bond114 ↔ 125
Disulfide bond148 ↔ 193
Disulfide bond192 ↔ 201
Disulfide bond224 ↔ 270
Disulfide bond269 ↔ 277
Disulfide bond289 ↔ 303
Disulfide bond302 ↔ 313
Disulfide bond340 ↔ 385
Disulfide bond384 ↔ 393
Disulfide bond416 ↔ 462
Disulfide bond461 ↔ 472
Disulfide bond485 ↔ 501
Disulfide bond500 ↔ 511
Disulfide bond538 ↔ 583
Disulfide bond582 ↔ 591

Natural variations

Alternative sequence43 – 234192Missing in isoform 2.
VSP_021275
Natural variant231R → C in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill.
VAR_000499
Natural variant231R → H in Fukuoka-2/Lille/Taipei/Varese/Komagome-3.
VAR_000500
Natural variant241R → L in Jaffna.
VAR_000501
Natural variant241R → P in Takefu/Honolulu-1.
VAR_000502
Natural variant241R → Q in Christchurch/Honolulu-2.
VAR_000503
Natural variant251D → V in Bleinheim/Iowa city-2.
VAR_000504
Natural variant271H → Q in Nagasaki-3.
VAR_000505
Natural variant271H → Y in Larino.
VAR_000506
Natural variant731F → Y