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P02769

- ALBU_BOVIN

UniProt

P02769 - ALBU_BOVIN

Protein

Serum albumin

Gene

ALB

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 4 (01 Feb 1996)
      Previous versions | rss
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    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. transport Source: InterPro

    Keywords - Ligandi

    Copper, Lipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196231. Advanced glycosylation endproduct receptor signaling.
    REACT_216574. Transport of organic anions.
    REACT_219679. Scavenging of heme from plasma.
    REACT_222480. HDL-mediated lipid transport.
    REACT_223874. Recycling of bile acids and salts.

    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: Chromosome 6

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: Ensembl
    4. extracellular vesicular exosome Source: Ensembl
    5. protein complex Source: UniProtKB

    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 ↔ 861 PublicationPROSITE-ProRule annotation
    Modified residuei82 – 821PhosphoserineBy similarity
    Disulfide bondi99 ↔ 1151 PublicationPROSITE-ProRule annotation
    Disulfide bondi114 ↔ 1251 PublicationPROSITE-ProRule annotation
    Disulfide bondi147 ↔ 1921 PublicationPROSITE-ProRule annotation
    Disulfide bondi191 ↔ 2001 PublicationPROSITE-ProRule annotation
    Disulfide bondi223 ↔ 2691 PublicationPROSITE-ProRule annotation
    Modified residuei228 – 2281N6-succinyllysineBy similarity
    Disulfide bondi268 ↔ 2761 PublicationPROSITE-ProRule annotation
    Disulfide bondi288 ↔ 3021 PublicationPROSITE-ProRule annotation
    Disulfide bondi301 ↔ 3121 PublicationPROSITE-ProRule annotation
    Disulfide bondi339 ↔ 3841 PublicationPROSITE-ProRule annotation
    Disulfide bondi383 ↔ 3921 PublicationPROSITE-ProRule annotation
    Disulfide bondi415 ↔ 4611 PublicationPROSITE-ProRule annotation
    Modified residuei442 – 4421PhosphoserineBy similarity
    Modified residuei443 – 4431PhosphothreonineBy similarity
    Modified residuei445 – 4451PhosphothreonineBy similarity
    Disulfide bondi460 ↔ 4711 PublicationPROSITE-ProRule annotation
    Disulfide bondi484 ↔ 5001 PublicationPROSITE-ProRule annotation
    Disulfide bondi499 ↔ 5101 PublicationPROSITE-ProRule annotation
    Disulfide bondi537 ↔ 5821 PublicationPROSITE-ProRule annotation
    Disulfide bondi581 ↔ 5901 PublicationPROSITE-ProRule annotation
    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.
    ProMEXiP02769.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00390000000113.
    HOGENOMiHOG000293137.
    HOVERGENiHBG004207.
    InParanoidiP02769.
    KOiK16141.
    OrthoDBiEOG7S4X5C.
    TreeFamiTF335561.

    Family and domain databases

    InterProiIPR000264. ALB/AFP/VDB.
    IPR001703. Alpha-fetoprotein.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    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

    MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA    50
    FSQYLQQCPF DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK 100
    VASLRETYGD MADCCEKQEP ERNECFLSHK DDSPDLPKLK PDPNTLCDEF 150
    KADEKKFWGK YLYEIARRHP YFYAPELLYY ANKYNGVFQE CCQAEDKGAC 200
    LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA RLSQKFPKAE 250
    FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE 300
    CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL 350
    GSFLYEYSRR HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL 400
    KHLVDEPQNL IKQNCDQFEK LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS 450
    RSLGKVGTRC CTKPESERMP CTEDYLSLIL NRLCVLHEKT PVSEKVTKCC 500
    TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP DTEKQIKKQT 550
    ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV 600
    STQTALA 607
    Length:607
    Mass (Da):69,293
    Last modified:February 1, 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. 1 PublicationCurated
    Sequence conflicti173 – 1731Y → L AA sequence (PubMed:2437111)Curated
    Sequence conflicti302 – 3021C → K AA sequence 1 PublicationCurated
    Sequence conflicti304 – 3052KP → PC AA sequence 1 PublicationCurated
    Sequence conflicti324 – 3241N → D AA sequence 1 PublicationCurated
    Sequence conflicti394 – 3952ST → TS AA sequence 1 PublicationCurated
    Sequence conflicti429 – 4291A → E in AAI02743. 1 PublicationCurated
    Sequence conflicti437 – 4371K → R AA sequence 1 PublicationCurated
    Sequence conflicti472 – 4721T → A in AAI02743. 1 PublicationCurated
    Sequence conflicti493 – 4942SE → ES AA sequence 1 PublicationCurated
    Sequence conflicti579 – 5791D → G in AAI02743. 1 PublicationCurated

    Natural variant

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENSBTAT00000022763; ENSBTAP00000022763; ENSBTAG00000017121.
    GeneIDi280717.
    KEGGibta:280717.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A38885. ABBOS.
    RefSeqi NP_851335.1. NM_180992.2.
    UniGenei Bt.106669.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L7U NMR - B 148-154 [» ]
    3V03 X-ray 2.70 A/B 25-607 [» ]
    4F5S X-ray 2.47 A/B 25-607 [» ]
    4JK4 X-ray 2.65 A/B 25-607 [» ]
    4OR0 X-ray 2.58 A/B 25-607 [» ]
    ProteinModelPortali P02769.
    SMRi P02769. Positions 29-584.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 158123. 5 interactions.
    STRINGi 9913.ENSBTAP00000022763.

    Chemistry

    BindingDBi P02769.
    ChEMBLi CHEMBL3728.

    Protein family/group databases

    Allergomei 165. Bos d 6.
    3166. Bos d 6.0101.

    Proteomic databases

    PaxDbi P02769.
    PRIDEi P02769.
    ProMEXi P02769.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000022763 ; ENSBTAP00000022763 ; ENSBTAG00000017121 .
    GeneIDi 280717.
    KEGGi bta:280717.

    Organism-specific databases

    CTDi 213.

    Phylogenomic databases

    eggNOGi NOG45992.
    GeneTreei ENSGT00390000000113.
    HOGENOMi HOG000293137.
    HOVERGENi HBG004207.
    InParanoidi P02769.
    KOi K16141.
    OrthoDBi EOG7S4X5C.
    TreeFami TF335561.

    Enzyme and pathway databases

    Reactomei REACT_196231. Advanced glycosylation endproduct receptor signaling.
    REACT_216574. Transport of organic anions.
    REACT_219679. Scavenging of heme from plasma.
    REACT_222480. HDL-mediated lipid transport.
    REACT_223874. Recycling of bile acids and salts.

    Miscellaneous databases

    NextBioi 20804896.

    Family and domain databases

    InterProi IPR000264. ALB/AFP/VDB.
    IPR001703. Alpha-fetoprotein.
    IPR020858. Serum_albumin-like.
    IPR021177. Serum_albumin/AFP.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    [Graphical view ]
    Pfami PF00273. Serum_albumin. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF002520. Serum_albumin_subgroup. 1 hit.
    PRINTSi PR00803. AFETOPROTEIN.
    PR00802. SERUMALBUMIN.
    SMARTi SM00103. ALBUMIN. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48552. SSF48552. 3 hits.
    PROSITEi PS00212. ALBUMIN_1. 3 hits.
    PS51438. ALBUMIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Bovine serum albumin: cDNA sequence and expression."
      Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.
      Submitted (AUG-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 (JUL-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(2001) [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 (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-214.
    5. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-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(1979) [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(1977) [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(1990) [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(1975)
      Cited for: PROTEIN SEQUENCE OF 25-424 AND 429-607, VARIANT THR-214.
    10. Brown J.R.
      Submitted (APR-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(1990) [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(1988) [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(1989) [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(1987) [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(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 402-433.
    16. Vilbois F.
      Submitted (AUG-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(1974)
      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 21, 1986
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 138 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