Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serum albumin

Gene

ALB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, Na+, K+, fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271CopperBy similarity
Metal bindingi91 – 911ZincBy similarity
Metal bindingi123 – 1231ZincBy similarity
Metal bindingi270 – 2701ZincBy similarity
Metal bindingi272 – 2721ZincBy similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. drug binding Source: UniProtKB
  3. fatty acid binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. oxygen binding Source: Ensembl
  6. pyridoxal phosphate binding Source: UniProtKB
  7. toxic substance binding Source: UniProtKB

GO - Biological processi

  1. cellular response to starvation Source: UniProtKB
  2. hemolysis by symbiont of host erythrocytes Source: UniProtKB
  3. maintenance of mitochondrion location Source: UniProtKB
  4. negative regulation of apoptotic process Source: UniProtKB
  5. retina homeostasis Source: Ensembl
  6. transport Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Copper, Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_272065. Platelet degranulation.
REACT_291733. Transport of organic anions.
REACT_298300. HDL-mediated lipid transport.
REACT_330039. Recycling of bile acids and salts.
REACT_335647. Scavenging of heme from plasma.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum albumin
Alternative name(s):
BSA
Allergen: Bos d 6
Gene namesi
Name:ALB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. cytoplasm Source: Ensembl
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: Ensembl
  5. nucleus Source: Ensembl
  6. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei165. Bos d 6.
3166. Bos d 6.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Propeptidei19 – 224PRO_0000001057
Chaini25 – 607583Serum albuminPRO_0000001058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 86PROSITE-ProRule annotation1 Publication
Modified residuei82 – 821PhosphoserineBy similarity
Modified residuei89 – 891PhosphoserineBy similarity
Disulfide bondi99 ↔ 115PROSITE-ProRule annotation1 Publication
Disulfide bondi114 ↔ 125PROSITE-ProRule annotation1 Publication
Disulfide bondi147 ↔ 192PROSITE-ProRule annotation1 Publication
Disulfide bondi191 ↔ 200PROSITE-ProRule annotation1 Publication
Disulfide bondi223 ↔ 269PROSITE-ProRule annotation1 Publication
Modified residuei228 – 2281N6-succinyllysineBy similarity
Disulfide bondi268 ↔ 276PROSITE-ProRule annotation1 Publication
Disulfide bondi288 ↔ 302PROSITE-ProRule annotation1 Publication
Disulfide bondi301 ↔ 312PROSITE-ProRule annotation1 Publication
Disulfide bondi339 ↔ 384PROSITE-ProRule annotation1 Publication
Disulfide bondi383 ↔ 392PROSITE-ProRule annotation1 Publication
Disulfide bondi415 ↔ 461PROSITE-ProRule annotation1 Publication
Modified residuei442 – 4421PhosphoserineBy similarity
Modified residuei443 – 4431PhosphothreonineBy similarity
Modified residuei445 – 4451PhosphothreonineBy similarity
Disulfide bondi460 ↔ 471PROSITE-ProRule annotation1 Publication
Disulfide bondi484 ↔ 500PROSITE-ProRule annotation1 Publication
Disulfide bondi499 ↔ 510PROSITE-ProRule annotation1 Publication
Modified residuei512 – 5121PhosphoserineBy similarity
Disulfide bondi537 ↔ 582PROSITE-ProRule annotation1 Publication
Disulfide bondi581 ↔ 590PROSITE-ProRule annotation1 Publication
Modified residuei587 – 5871N6-succinyllysineBy similarity

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP02769.
PRIDEiP02769.

Expressioni

Tissue specificityi

Plasma.

Interactioni

Protein-protein interaction databases

BioGridi158123. 5 interactions.
STRINGi9913.ENSBTAP00000022763.

Structurei

Secondary structure

1
607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 389Combined sources
Helixi40 – 5415Combined sources
Beta strandi56 – 583Combined sources
Helixi60 – 7920Combined sources
Turni84 – 874Combined sources
Helixi90 – 9910Combined sources
Helixi104 – 1085Combined sources
Helixi109 – 1168Combined sources
Helixi121 – 1277Combined sources
Helixi143 – 15210Combined sources
Helixi154 – 16815Combined sources
Helixi174 – 19118Combined sources
Beta strandi194 – 1963Combined sources
Helixi197 – 22933Combined sources
Helixi231 – 24515Combined sources
Helixi251 – 26919Combined sources
Helixi273 – 28816Combined sources
Helixi291 – 2944Combined sources
Helixi296 – 2983Combined sources
Helixi301 – 3033Combined sources
Helixi306 – 31510Combined sources
Helixi329 – 3324Combined sources
Helixi338 – 3447Combined sources
Helixi346 – 36015Combined sources
Helixi366 – 38520Combined sources
Beta strandi386 – 3883Combined sources
Helixi389 – 3935Combined sources
Helixi396 – 4038Combined sources
Turni404 – 4074Combined sources
Helixi408 – 43730Combined sources
Helixi443 – 46018Combined sources
Beta strandi461 – 4633Combined sources
Helixi465 – 48925Combined sources
Helixi494 – 5029Combined sources
Helixi507 – 5126Combined sources
Beta strandi518 – 5203Combined sources
Helixi527 – 5304Combined sources
Helixi534 – 5374Combined sources
Helixi541 – 55818Combined sources
Helixi564 – 58320Combined sources
Beta strandi584 – 5863Combined sources
Helixi587 – 60620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7UNMR-B148-154[»]
3V03X-ray2.70A/B25-607[»]
4F5SX-ray2.47A/B25-607[»]
4JK4X-ray2.65A/B25-607[»]
4OR0X-ray2.58A/B25-607[»]
ProteinModelPortaliP02769.
SMRiP02769. Positions 29-584.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 209191Albumin 1PROSITE-ProRule annotationAdd
BLAST
Domaini210 – 402193Albumin 2PROSITE-ProRule annotationAdd
BLAST
Domaini403 – 600198Albumin 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
Contains 3 albumin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG45992.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02769.
KOiK16141.
OrthoDBiEOG7S4X5C.
TreeFamiTF335561.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA
60 70 80 90 100
FSQYLQQCPF DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK
110 120 130 140 150
VASLRETYGD MADCCEKQEP ERNECFLSHK DDSPDLPKLK PDPNTLCDEF
160 170 180 190 200
KADEKKFWGK YLYEIARRHP YFYAPELLYY ANKYNGVFQE CCQAEDKGAC
210 220 230 240 250
LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA RLSQKFPKAE
260 270 280 290 300
FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE
310 320 330 340 350
CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL
360 370 380 390 400
GSFLYEYSRR HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL
410 420 430 440 450
KHLVDEPQNL IKQNCDQFEK LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS
460 470 480 490 500
RSLGKVGTRC CTKPESERMP CTEDYLSLIL NRLCVLHEKT PVSEKVTKCC
510 520 530 540 550
TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP DTEKQIKKQT
560 570 580 590 600
ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV

STQTALA
Length:607
Mass (Da):69,293
Last modified:January 31, 1996 - v4
Checksum:i39167DFE768585D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581Missing AA sequence (PubMed:2379503).Curated
Sequence conflicti116 – 1161E → A in AAI02743 (Ref. 5) Curated
Sequence conflicti173 – 1731Y → L AA sequence (PubMed:2437111).Curated
Sequence conflicti302 – 3021C → K AA sequence (Ref. 9) Curated
Sequence conflicti304 – 3052KP → PC AA sequence (Ref. 9) Curated
Sequence conflicti324 – 3241N → D AA sequence (Ref. 9) Curated
Sequence conflicti394 – 3952ST → TS AA sequence (Ref. 9) Curated
Sequence conflicti429 – 4291A → E in AAI02743 (Ref. 5) Curated
Sequence conflicti437 – 4371K → R AA sequence (Ref. 16) Curated
Sequence conflicti472 – 4721T → A in AAI02743 (Ref. 5) Curated
Sequence conflicti493 – 4942SE → ES AA sequence (Ref. 9) Curated
Sequence conflicti579 – 5791D → G in AAI02743 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141A → T.4 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73993 mRNA. Translation: AAA51411.1.
X58989 mRNA. Translation: CAA41735.1.
Y17769 mRNA. Translation: CAA76847.1.
AF542068 mRNA. Translation: AAN17824.1.
BC102742 mRNA. Translation: AAI02743.1.
BC142272 mRNA. Translation: AAI42273.1.
PIRiA38885. ABBOS.
RefSeqiNP_851335.1. NM_180992.2.
UniGeneiBt.106669.

Genome annotation databases

GeneIDi280717.
KEGGibta:280717.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73993 mRNA. Translation: AAA51411.1.
X58989 mRNA. Translation: CAA41735.1.
Y17769 mRNA. Translation: CAA76847.1.
AF542068 mRNA. Translation: AAN17824.1.
BC102742 mRNA. Translation: AAI02743.1.
BC142272 mRNA. Translation: AAI42273.1.
PIRiA38885. ABBOS.
RefSeqiNP_851335.1. NM_180992.2.
UniGeneiBt.106669.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7UNMR-B148-154[»]
3V03X-ray2.70A/B25-607[»]
4F5SX-ray2.47A/B25-607[»]
4JK4X-ray2.65A/B25-607[»]
4OR0X-ray2.58A/B25-607[»]
ProteinModelPortaliP02769.
SMRiP02769. Positions 29-584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158123. 5 interactions.
STRINGi9913.ENSBTAP00000022763.

Chemistry

BindingDBiP02769.
ChEMBLiCHEMBL3728.

Protein family/group databases

Allergomei165. Bos d 6.
3166. Bos d 6.0101.

Proteomic databases

PaxDbiP02769.
PRIDEiP02769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280717.
KEGGibta:280717.

Organism-specific databases

CTDi213.

Phylogenomic databases

eggNOGiNOG45992.
HOGENOMiHOG000293137.
HOVERGENiHBG004207.
InParanoidiP02769.
KOiK16141.
OrthoDBiEOG7S4X5C.
TreeFamiTF335561.

Enzyme and pathway databases

ReactomeiREACT_272065. Platelet degranulation.
REACT_291733. Transport of organic anions.
REACT_298300. HDL-mediated lipid transport.
REACT_330039. Recycling of bile acids and salts.
REACT_335647. Scavenging of heme from plasma.

Miscellaneous databases

NextBioi20804896.

Family and domain databases

InterProiIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP/Afamin.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamiPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFiPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSiPR00803. AFETOPROTEIN.
PR00802. SERUMALBUMIN.
SMARTiSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 3 hits.
PROSITEiPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bovine serum albumin: cDNA sequence and expression."
    Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.
    Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The bovine serum albumin mRNA."
    Barry T., Power S., Gannon F.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-214.
    Tissue: Liver.
  3. "Differential binding of IgG and IgA antibodies to antigenic determinants of bovine serum albumin."
    Hilger C., Grigioni F., De Beaufort C., Michel G., Freilinger J., Hentges F.
    Clin. Exp. Immunol. 123:387-394(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "The complete cDNA sequence of bovine serum albumin."
    Wu H.T., Huang M.C.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-214.
  5. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-214.
    Strain: Hereford.
    Tissue: Fetal liver and Testis.
  6. "Biosynthesis of bovine plasma proteins in a cell-free system. Amino-terminal sequence of preproalbumin."
    McGillivray R.T.A., Chung D.W., Davie E.W.
    Eur. J. Biochem. 98:477-485(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-32.
  7. "Bovine microsomal albumin: amino terminal sequence of bovine proalbumin."
    Patterson J.E., Geller D.M.
    Biochem. Biophys. Res. Commun. 74:1220-1226(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-28.
  8. "Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and Frit-FAB LC/MS."
    Hirayama K., Akashi S., Furuya M., Fukuhara K.
    Biochem. Biophys. Res. Commun. 173:639-646(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SEQUENCE REVISION TO 118-119 AND 180.
  9. "Structure of bovine serum albumin."
    Brown J.R.
    Fed. Proc. 34:591-591(1974)
    Cited for: PROTEIN SEQUENCE OF 25-424 AND 429-607, VARIANT THR-214.
  10. Brown J.R.
    Submitted (MAR-1975) to the PIR data bank
    Cited for: SEQUENCE REVISION TO 190-195.
  11. "Tooth 'enamelins' identified mainly as serum proteins. Major 'enamelin' is albumin."
    Strawich E., Glimcher M.J.
    Eur. J. Biochem. 191:47-56(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-64.
  12. "Electroblotting onto glass-fiber filter from an analytical isoelectrofocusing gel: a preparative method for isolating proteins for N-terminal microsequencing."
    Hsieh J.C., Lin F.P., Tam M.F.
    Anal. Biochem. 170:1-8(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-41.
  13. "Structures of histamine-releasing peptides formed by the action of acid proteases on mammalian albumin(s)."
    Carraway R.E., Cochrane D.E., Boucher W., Mitra S.P.
    J. Immunol. 143:1680-1684(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 163-172.
  14. "Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s)."
    Carraway R.E., Mitra S.P., Cochrane D.E.
    J. Biol. Chem. 262:5968-5973(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 165-173.
    Tissue: Plasma.
  15. "Sequence of residues 400-403 of bovine serum albumin."
    Reed R.G., Putnam F.W., Peters T. Jr.
    Biochem. J. 191:867-868(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 402-433.
  16. Vilbois F.
    Submitted (JUL-1998) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 437-451.
  17. "Structure of serum albumin: disulfide bridges."
    Brown J.R.
    Fed. Proc. 33:1389-1389(1973)
    Cited for: DISULFIDE BONDS.

Entry informationi

Entry nameiALBU_BOVIN
AccessioniPrimary (citable) accession number: P02769
Secondary accession number(s): A5PJX3
, O02787, P04277, Q3SZR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: January 31, 1996
Last modified: March 31, 2015
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

A peptide arising from positions 165 to 173 was originally termed neurotensin-related peptide (NRP) and was thought to regulate fat digestion, lipid absorption, and blood flow.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.