ALB albumin [Bos taurus] - Gene

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Summary

Symbol: ALB
Full Name: albumin
Primary source: BGD:BT11285
Locus tag: BOS_6773
See related: Ensembl:ENSBTAG00000017121
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as: MGC179277

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Genomic context

Location :: chromosome: 6

Sequence :: Chromosome: 6; AC_000163.1 (90232762..90251122)

See ALB in MapViewer

Chromosome 6 - AC_000163.1 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

The results showed that the riboflavin could efficiently bind to BSA in aqueous solution.
Title: Spectrometry researches on interaction and sonodynamic damage of riboflavin (RF) to bovine serum albumin (BSA).
The unfolding and refolding of BSA appear to proceed through intermediates and both the processes are sequential in nature.
Title: Protein unfolding and subsequent refolding: a spectroscopic investigation.
The results indicated that the binding abilities of vitamin B12 to BSA in the acidic and basic pH regions (pH 2.5, 3.5, 5.0, and 9.0) were lower than that at simulating physiological condition (pH 7.4).
Title: Effect of pH on the interaction of vitamin B12 with bovine serum albumin by spectroscopic approaches.
new insights on bovine serum albumin self-assembly process
Title: Bovine Serum Albumin protofibril-like aggregates formation: solo but not simple mechanism.
Data indicate that CD spectroscopy of the HSA and BSA released in solution after desorption from the matrices shows that, while both proteins partially regain their helical structure, they show a distinct behaviour in their tertiary structure.
Title: Conformational modifications of serum albumins adsorbed on different kinds of biomimetic hydroxyapatite nanocrystals.
Data show that the fluorescence quenching process may occur through energy transfer from singlet excited state of tryptophan in BSA to the corresponding level of ASP.
Title: Interaction of bovine serum albumin and albumin-gold nanoconjugates with l-aspartic acid. A spectroscopic approach.
L-Arginine does not prevent amyloid-like fibril formation by BSA.
Title: L-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin.
Our data suggest that the efficacy of this detoxication system is based on the high concentration of albumin in plasma (and in the rest of the body), and not on the catalytic efficacy itself, which is low for albumin.
Title: Serum albumins and detoxication of anti-cholinesterase agents.
The shortest binding distance and energy transfer efficiencies between donor BSA and acceptor methyl pheophorbide-a were obtained by Forster's nonradiative energy transfer mechanism.
Title: [Study on the interaction of methyl pheophorbide-a and bovine serum albumins by fluorescence].
Data show that the apparent complexation constant of Pb2 x BSA is lgK = 11.61, and the nitrogen in BSA could coordinate with lead in Pb2-BSA.
Title: [Study on the interaction of Pb2+ and bovine serum albumin by fluorescence].

Submit: New GeneRIF Correction See all (34)

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description
BioGRID:158123	BioGRID:110216	LRP2		BioGRID	PubMed	Reconstituted Complex

Function	Evidence Code	Pubs
DNA binding	ISS Inferred from Sequence or Structural Similarity more info
drug binding	ISS Inferred from Sequence or Structural Similarity more info
fatty acid binding	ISS Inferred from Sequence or Structural Similarity more info
metal ion binding	IEA Inferred from Electronic Annotation more info
contributes_to oxygen binding	ISS Inferred from Sequence or Structural Similarity more info
pyridoxal phosphate binding	ISS Inferred from Sequence or Structural Similarity more info
toxin binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
cellular response to starvation	ISS Inferred from Sequence or Structural Similarity more info
hemolysis by symbiont of host erythrocytes	ISS Inferred from Sequence or Structural Similarity more info
maintenance of mitochondrion location	ISS Inferred from Sequence or Structural Similarity more info
negative regulation of apoptotic process	ISS Inferred from Sequence or Structural Similarity more info
transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
extracellular region	TAS Traceable Author Statement more info
extracellular space	IEA Inferred from Electronic Annotation more info
protein complex	ISS Inferred from Sequence or Structural Similarity more info

General protein information

Preferred Names: serum albumin

Names: serum albumin; BSA

NP_851335.1

EC 6.1.1.16

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NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_180992.2 → NP_851335.1 serum albumin precursor

Status: PROVISIONAL

Source sequence(s)

X58989

UniProtKB/Swiss-Prot

P02769

Related

ENSBTAP00000022763, ENSBTAT00000022763

Conserved Domains (1) summary

cd00015
Location:220 – 400
Blast Score: 458

ALBUMIN; Albumin domain, contains five or six internal disulphide bonds; albuminoid superfamily includes alpha-fetoprotein which binds various cations, fatty acids and bilirubin; vitamin D-binding protein which binds to vitamin D, its metabolites, and fatty acids; ...

RefSeqs of Annotated Genomes: Build 6.1

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference Bos_taurus_UMD_3.1 Primary Assembly

Genomic

AC_000163.1 Reference Bos_taurus_UMD_3.1 Primary Assembly

Range

90232762..90251122

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate Btau_4.6.1

Genomic

NC_007304.5 Alternate Btau_4.6.1

Range

91410140..91428507

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein	Strain
Heading	Accession and Version	Protein	Strain
genomic	GJ060968.1	DAA28523.1	Hereford
mRNA	AF542068.1	AAN17824.1
mRNA	BC102742.1	AAI02743.1	Hereford
mRNA	BC142272.1	AAI42273.1	Hereford
mRNA	BC151546.1	AAI51547.1	mixed
mRNA	M73993.1	AAA51411.1
mRNA	X58989.1	CAA41735.1
mRNA	Y17769.1	CAA76847.1