ALB albumin [Bos taurus (domestic cattle)] - Gene

Summary

Official Symbol: ALBprovided by VGNC
Official Full Name: albuminprovided by VGNC
Primary source: VGNC:VGNC:53687
See related: BGD:BT11285; Ensembl:ENSBTAG00000017121
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 6

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_12	current	ARS-UCD2.0 (GCF_002263795.3)	6	NC_037333.1 (88484961..88503330)

Chromosome 6 - NC_037333.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_037333.1 Chromosome 6 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Dominette sequence data
BioProject: PRJNA294306
Analysis date: Tue Dec 17 08:57:05 2024

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The binding constant and quenching constant values suggest that tamoxifen dislodges neratinib from its serum albumin (SA)complex whereas neratinib doesn't affect the interaction between SA and tamoxifen.
Title: Evaluation of competitive binding interaction of neratinib and tamoxifen to serum albumin in multidrug therapy.
Data show that the fluorescence intensity of bovine serum albumin (BSA) constantly decreased upon increasing concentration of bixin and crocin with fluorescence emission spectra.
Title: Structural insights into the binding mode and conformational changes of BSA induced by bixin and crocin.
High glucose concentrations inhibited megalin expression and megalin-mediated albumin endocytosis after 48 h of incubation.
Title: High glucose reduces megalin-mediated albumin endocytosis in renal proximal tubule cells through protein kinase B O-GlcNAcylation.
The interaction of DRV with bovine serum albumin (BSA), a major carrier protein, has been studied under simulated physiological conditions (pH7.4) by multi-spectroscopic techniques in combination with molecular modeling.
Title: Multi-spectroscopic and molecular modeling approaches to elucidate the binding interaction between bovine serum albumin and darunavir, a HIV protease inhibitor.
hese obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins.
Title: A multispectroscopic and molecular docking investigation of the binding interaction between serum albumins and acid orange dye.
that thiamine hydrochloride (TA) is located in site I of bovine serum albumin (BSA).
Title: Multi-spectroscopic and voltammetric evidences for binding, conformational changes of bovine serum albumin with thiamine.
The molecular dynamics results show how the negatively charged BSA at pH7 adsorbs to the negatively charged silica surface, and reveal a unique orientation with preserved secondary and tertiary structure. The experiments then show that the protein forms complete monolayers at approximately pH6, just above the protein's isoelectric point (pH5.1).
Title: Bovine Serum Albumin Adsorption at a Silica Surface Explored by Simulation and Experiment.
Molecular dynamics (MD) simulation results demonstrate that the "hard protein" lysozyme retains much of its secondary structure during adsorption, whereas BSA loses it almost completely. BSA has a considerably larger adsorption energy compared to that of lysozyme, which does not scale with chain length. Desorption simulations are carried out using classical steered MD.
Title: Forced Desorption of Bovine Serum Albumin and Lysozyme from Graphite: Insights from Molecular Dynamics Simulation.
identified a total of 125 carbonylated residues in bovine serum albumin after extensive in vitro metal ion-catalysed oxidation
Title: A biotin enrichment strategy identifies novel carbonylated amino acids in proteins from human plasma.
Degradation of BSA by serine proteases was monitored with Fourier transform infrared (FT-IR) and ultraviolet circular dichroism (UV-CD). alpha-Helical structure of BSA was converted into unordered structure upon digestion.
Title: Proteolytically-induced changes of secondary structural protein conformation of bovine serum albumin monitored by Fourier transform infrared (FT-IR) and UV-circular dichroism spectroscopy.

Submit: New GeneRIF Correction See all GeneRIFs (56)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RefSeq

Process	Evidence Code	Pubs
involved_in transport	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in blood microparticle	IEA Inferred from Electronic Annotation more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info	PubMed
located_in extracellular space	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: albumin

Names: BSA; serum albumin

NP_851335.1

EC 6.1.1.16

NCBI Reference Sequences (RefSeq)

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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.