Skip Header

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

P02769

- ALBU_BOVIN

UniProt

P02769 - ALBU_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serum albumin

Gene

ALB

Organism
Bos taurus (Bovine)
Status
Reviewed - 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_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. 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 ↔ 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

        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: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

« 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 (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 29, 2014
This is version 139 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